{"metadata":{"accession":"IPR030849","entry_id":null,"type":"family","go_terms":[{"identifier":"GO:0004843","name":"cysteine-type deubiquitinase activity","category":{"code":"F","name":"molecular_function"}},{"identifier":"GO:0010468","name":"regulation of gene expression","category":{"code":"P","name":"biological_process"}},{"identifier":"GO:0051726","name":"regulation of cell cycle","category":{"code":"P","name":"biological_process"}}],"source_database":"interpro","member_databases":{"hamap":{"MF_03062":"Ubiquitin carboxyl-terminal hydrolase 16 [USP16]"}},"integrated":null,"hierarchy":{"accession":"IPR050164","name":"Ubiquitin carboxyl-terminal hydrolases","type":"Family","children":[{"accession":"IPR030849","name":"Ubiquitin carboxyl-terminal hydrolase 16","type":"Family","children":[]}]},"name":{"name":"Ubiquitin carboxyl-terminal hydrolase 16","short":"UBP16"},"description":[{"text":"<p>Ubiquitin carboxyl-terminal hydrolase 16 (UBP16 or Ubp-M), also known as ubiquitin-specific protease 16 (USP16), is a histone H2A deubiquitinase required for cell cycle M phase progression. It also regulates gene expression in G1/S phase. In Xenopus embryos, it regulates embryonic anterior-posterior patterning through the regulation of Hox gene expression [[cite:PUB00074123]]. USP16 is a critical regulator of DNA damage response that fine-tunes DNA damage-induced histone ubiquitin foci formation [[cite:PUB00074272]].</p>","llm":false,"checked":false,"updated":false}],"wikipedia":null,"literature":{"PUB00074123":{"PMID":17914355,"ISBN":null,"volume":"449","issue":"7165","year":2007,"title":"Regulation of cell cycle progression and gene expression by H2A deubiquitination.","URL":null,"raw_pages":"1068-72","medline_journal":"Nature","ISO_journal":"Nature","authors":["Joo HY","Zhai L","Yang C","Nie S","Erdjument-Bromage H","Tempst P","Chang C","Wang H."],"DOI_URL":"http://dx.doi.org/10.1038/nature06256"},"PUB00074272":{"PMID":25305019,"ISBN":null,"volume":"289","issue":"47","year":2014,"title":"The histone H2A deubiquitinase USP16 interacts with HERC2 and fine-tunes cellular response to DNA damage.","URL":null,"raw_pages":"32883-94","medline_journal":"J Biol Chem","ISO_journal":"J. Biol. Chem.","authors":["Zhang Z","Yang H","Wang H."],"DOI_URL":"http://dx.doi.org/10.1074/jbc.M114.599605"}},"set_info":null,"overlaps_with":[{"accession":"IPR038765","name":"Papain-like cysteine peptidase superfamily","type":"homologous_superfamily"}],"counters":{"subfamilies":0,"domain_architectures":0,"interactions":0,"matches":612,"pathways":5,"proteins":612,"proteomes":291,"sets":0,"structural_models":{"alphafold":560,"bfvd":0},"structures":1,"taxa":1043},"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}}