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{
"metadata": {
"accession": "IPR038093",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cathgene3d": {
"G3DSA:2.30.29.180": "Ubiquitin carboxyl-terminal hydrolase 26/29/37, pleckstrin homology-like domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR038093",
"name": "Ubiquitin carboxyl-terminal hydrolase 37, pleckstrin homology-like domain superfamily",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "Ubiquitin carboxyl-terminal hydrolase 37, pleckstrin homology-like domain superfamily",
"short": "USP37-like_PH_sf"
},
"description": [
{
"text": "<p>This pleckstrin homology (PH)-like domain can be found at the N terminus of some ubiquitin carboxyl-terminal hydrolases, including USP26, USP29 and USP37. USP37 antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), resulting in promoting S phase entry [[cite:PUB00080587]]. USP26 is a regulator of androgen receptor (AR) signaling [[cite:PUB00080586]]. Both USP26 and USP37 are critical for double-strand breaks repair by homologous recombination [[cite:PUB00076470]]. USP29 plays a role in apoptosis and oxidative stress [[cite:PUB00078663]].</p>\r\n\r\n<p>PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner [[cite:PUB00080401]]. They share little sequence conservation, but all have a common fold, which is electrostatically polarized.</p>",
"llm": false,
"checked": false,
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}
],
"wikipedia": null,
"literature": {
"PUB00076470": {
"PMID": 26101254,
"ISBN": null,
"volume": "43",
"issue": "14",
"year": 2015,
"title": "The de-ubiquitylating enzymes USP26 and USP37 regulate homologous recombination by counteracting RAP80.",
"URL": null,
"raw_pages": "6919-33",
"medline_journal": "Nucleic Acids Res",
"ISO_journal": "Nucleic Acids Res.",
"authors": [
"Typas D",
"Luijsterburg MS",
"Wiegant WW",
"Diakatou M",
"Helfricht A",
"Thijssen PE",
"van de Broek B",
"Mullenders LH",
"van Attikum H."
],
"DOI_URL": "http://dx.doi.org/10.1093/nar/gkv613"
},
"PUB00080401": {
"PMID": 22728242,
"ISBN": null,
"volume": "586",
"issue": "17",
"year": 2012,
"title": "Pleckstrin homology (PH) like domains - versatile modules in protein-protein interaction platforms.",
"URL": null,
"raw_pages": "2662-73",
"medline_journal": "FEBS Lett",
"ISO_journal": "FEBS Lett.",
"authors": [
"Scheffzek K",
"Welti S."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.febslet.2012.06.006"
},
"PUB00080586": {
"PMID": 20501646,
"ISBN": null,
"volume": "8",
"issue": "6",
"year": 2010,
"title": "The deubiquitinating enzyme USP26 is a regulator of androgen receptor signaling.",
"URL": null,
"raw_pages": "844-54",
"medline_journal": "Mol Cancer Res",
"ISO_journal": "Mol. Cancer Res.",
"authors": [
"Dirac AM",
"Bernards R."
],
"DOI_URL": "http://dx.doi.org/10.1158/1541-7786.MCR-09-0424"
},
"PUB00080587": {
"PMID": 21596315,
"ISBN": null,
"volume": "42",
"issue": "4",
"year": 2011,
"title": "Deubiquitinase USP37 is activated by CDK2 to antagonize APC(CDH1) and promote S phase entry.",
"URL": null,
"raw_pages": "511-23",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol. Cell",
"authors": [
"Huang X",
"Summers MK",
"Pham V",
"Lill JR",
"Liu J",
"Lee G",
"Kirkpatrick DS",
"Jackson PK",
"Fang G",
"Dixit VM."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.molcel.2011.03.027"
},
"PUB00078663": {
"PMID": 21285945,
"ISBN": null,
"volume": "30",
"issue": "5",
"year": 2011,
"title": "JTV1 co-activates FBP to induce USP29 transcription and stabilize p53 in response to oxidative stress.",
"URL": null,
"raw_pages": "846-58",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Liu J",
"Chung HJ",
"Vogt M",
"Jin Y",
"Malide D",
"He L",
"Dundr M",
"Levens D."
],
"DOI_URL": "http://dx.doi.org/10.1038/emboj.2011.11"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR032069",
"name": "Ubiquitin carboxyl-terminal hydrolase 37, pleckstrin homology-like domain",
"type": "domain"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1406,
"pathways": 5,
"proteins": 1406,
"proteomes": 678,
"sets": 0,
"structural_models": {
"alphafold": 1293,
"bfvd": 0
},
"structures": 1,
"taxa": 2153
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.4.19.12",
"url": "https://enzyme.expasy.org/EC/3.4.19.12"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
