{"metadata":{"accession":"PF12057","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021925","hierarchy":null,"name":{"name":"BCL2-associated athanogene 6","short":"BAG6"},"description":[{"text":"<p>This domain is found in large proline-rich protein BAG6 protein. It has a conserved SDL sequence motif. Human BAG6 is an ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins [[cite:PUB00086005]]. It functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation [[cite:PUB00086005],[cite:PUB00086006],[cite:PUB00086007],[cite:PUB00086008]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00086006":{"PMID":20516149,"ISBN":null,"volume":"123","issue":"Pt 13","year":2010,"title":"Bat3 promotes the membrane integration of tail-anchored proteins.","URL":null,"raw_pages":"2170-8","medline_journal":"J Cell Sci","ISO_journal":"J. Cell. Sci.","authors":["Leznicki P","Clancy A","Schwappach B","High S."],"DOI_URL":"https://doi.org/10.1242/jcs.066738"},"PUB00086008":{"PMID":28104892,"ISBN":null,"volume":"355","issue":"6322","year":2017,"title":"Mechanistic basis for a molecular triage reaction.","URL":null,"raw_pages":"298-302","medline_journal":"Science","ISO_journal":"Science","authors":["Shao S","Rodrigo-Brenni MC","Kivlen MH","Hegde RS."],"DOI_URL":"https://doi.org/10.1126/science.aah6130"},"PUB00086007":{"PMID":21743475,"ISBN":null,"volume":"475","issue":"7356","year":2011,"title":"Protein targeting and degradation are coupled for elimination of mislocalized proteins.","URL":null,"raw_pages":"394-7","medline_journal":"Nature","ISO_journal":"Nature","authors":["Hessa T","Sharma A","Mariappan M","Eshleman HD","Gutierrez E","Hegde RS."],"DOI_URL":"https://doi.org/10.1038/nature10181"},"PUB00086005":{"PMID":21636303,"ISBN":null,"volume":"42","issue":"6","year":2011,"title":"A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation.","URL":null,"raw_pages":"758-70","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Wang Q","Liu Y","Soetandyo N","Baek K","Hegde R","Ye Y."],"DOI_URL":"https://doi.org/10.1016/j.molcel.2011.05.010"}},"set_info":null,"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":23,"interactions":0,"matches":2442,"pathways":0,"proteins":2436,"proteomes":725,"sets":0,"structural_models":{"alphafold":1779},"structures":0,"taxa":2709},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":14,"alignment:full":1678},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}