##gff-version 3
Q4VSI4	UniProtKB	Chain	1	1103	.	.	.	ID=PRO_0000268007;Note=Ubiquitin C-terminal hydrolase 7	
Q4VSI4	UniProtKB	Domain	69	196	.	.	.	Note=MATH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00129	
Q4VSI4	UniProtKB	Domain	215	522	.	.	.	Note=USP	
Q4VSI4	UniProtKB	Region	1	209	.	.	.	Note=Interaction with TSPYL5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Region	1	40	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q4VSI4	UniProtKB	Region	54	209	.	.	.	Note=Interaction with p53/TP53 and MDM2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Region	71	206	.	.	.	Note=Necessary for nuclear localization;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Compositional bias	1	11	.	.	.	Note=Low complexity;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q4VSI4	UniProtKB	Compositional bias	20	32	.	.	.	Note=Acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q4VSI4	UniProtKB	Active site	224	224	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255,ECO:0000269,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093,ECO:0000269|PubMed:16111684,ECO:0000269|PubMed:16328052;Dbxref=PMID:16111684,PMID:16328052	
Q4VSI4	UniProtKB	Active site	465	465	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
Q4VSI4	UniProtKB	Modified residue	19	19	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q4VSI4	UniProtKB	Modified residue	50	50	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6A4J8	
Q4VSI4	UniProtKB	Modified residue	54	54	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6A4J8	
Q4VSI4	UniProtKB	Modified residue	870	870	.	.	.	Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Modified residue	964	964	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Modified residue	1085	1085	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Modified residue	1097	1097	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Cross-link	870	870	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Cross-link	870	870	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Cross-link	883	883	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q93009	
Q4VSI4	UniProtKB	Mutagenesis	224	224	.	.	.	Note=Loss of p53/TP53-deubiquitinating activity. C->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16111684,ECO:0000269|PubMed:16328052;Dbxref=PMID:16111684,PMID:16328052