{"metadata":{"accession":"PF11816","entry_id":null,"type":"domain","go_terms":null,"source_database":"pfam","member_databases":null,"integrated":"IPR021772","hierarchy":null,"name":{"name":"WDR48/Bun107, ubiquitin-like domain","short":"Ubl_WDR48-Bun107"},"description":[{"text":"<p>This entry represents the ubiquitin-like domain of WDR48 and its homologues. WDR48 (also known as UAF1) is a regulator of deubiquitinating complexes [[cite:PUB00092494],[cite:PUB00092495],[cite:PUB00092496]]. Bun107 is required for the Ubp9 recruitment to septa and cell tips but also for its enzymatic activity at these specific locations [[cite:PUB00057398]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00092494":{"PMID":18082604,"ISBN":null,"volume":"28","issue":"5","year":2007,"title":"A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway.","URL":null,"raw_pages":"786-97","medline_journal":"Mol Cell","ISO_journal":"Mol. Cell","authors":["Cohn MA","Kowal P","Yang K","Haas W","Huang TT","Gygi SP","D'Andrea AD."],"DOI_URL":"https://doi.org/10.1016/j.molcel.2007.09.031"},"PUB00092496":{"PMID":26388029,"ISBN":null,"volume":"23","issue":"11","year":2015,"title":"Structural Insights into WD-Repeat 48 Activation of Ubiquitin-Specific Protease 46.","URL":null,"raw_pages":"2043-54","medline_journal":"Structure","ISO_journal":"Structure","authors":["Yin J","Schoeffler AJ","Wickliffe K","Newton K","Starovasnik MA","Dueber EC","Harris SF."],"DOI_URL":"https://doi.org/10.1016/j.str.2015.08.010"},"PUB00092495":{"PMID":19075014,"ISBN":null,"volume":"284","issue":"8","year":2009,"title":"UAF1 is a subunit of multiple deubiquitinating enzyme complexes.","URL":null,"raw_pages":"5343-51","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Cohn MA","Kee Y","Haas W","Gygi SP","D'Andrea AD."],"DOI_URL":"https://doi.org/10.1074/jbc.M808430200"},"PUB00057398":{"PMID":20838651,"ISBN":null,"volume":"8","issue":"9","year":2010,"title":"A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity.","URL":null,"raw_pages":null,"medline_journal":"PLoS Biol","ISO_journal":"PLoS Biol.","authors":["Kouranti I","McLean JR","Feoktistova A","Liang P","Johnson AE","Roberts-Galbraith RH","Gould KL."],"DOI_URL":null}},"set_info":{"accession":"CL0072","name":"Ubiquitin"},"overlaps_with":null,"counters":{"subfamilies":0,"domain_architectures":138,"interactions":0,"matches":4519,"pathways":0,"proteins":4442,"proteomes":3062,"sets":1,"structural_models":{"alphafold":3587},"structures":14,"taxa":8139},"entry_annotations":{"hmm":0,"logo":0,"alignment:seed":65,"alignment:full":3438},"cross_references":{},"is_llm":false,"is_reviewed_llm":false,"is_updated_llm":false,"representative_structure":null}}