##gff-version 3
Q70EK9	UniProtKB	Chain	1	711	.	.	.	ID=PRO_0000080680;Note=Ubiquitin carboxyl-terminal hydrolase 51	
Q70EK9	UniProtKB	Domain	363	706	.	.	.	Note=USP	
Q70EK9	UniProtKB	Zinc finger	193	311	.	.	.	Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Region	1	174	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q70EK9	UniProtKB	Compositional bias	48	66	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q70EK9	UniProtKB	Compositional bias	119	145	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q70EK9	UniProtKB	Active site	372	372	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093,ECO:0000269|PubMed:27083998;Dbxref=PMID:27083998	
Q70EK9	UniProtKB	Active site	665	665	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093,ECO:0000269|PubMed:27083998;Dbxref=PMID:27083998	
Q70EK9	UniProtKB	Binding site	195	195	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	197	197	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	236	236	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	239	239	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	249	249	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	252	252	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	257	257	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	262	262	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	266	266	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	272	272	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	285	285	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Binding site	288	288	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
Q70EK9	UniProtKB	Mutagenesis	372	372	.	.	.	Note=Abolishes ability to deubiquitinate histone H2A%3B when associated with 665-R. No decrease of total H2AK15ub levels following ionizing radiation%3B when associated with 665-R. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27083998;Dbxref=PMID:27083998	
Q70EK9	UniProtKB	Mutagenesis	665	665	.	.	.	Note=Abolishes ability to deubiquitinate histone H2A%3B when associated with 665-R. Suppresses ionizing radiation-induced H2AK13%2C15Ub%3B when associated with 372-R. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27083998;Dbxref=PMID:27083998