##gff-version 3
E1BMF7	UniProtKB	Chain	1	863	.	.	.	ID=PRO_0000418010;Note=Ubiquitin carboxyl-terminal hydrolase 13	
E1BMF7	UniProtKB	Domain	336	861	.	.	.	Note=USP	
E1BMF7	UniProtKB	Domain	652	693	.	.	.	Note=UBA 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
E1BMF7	UniProtKB	Domain	727	767	.	.	.	Note=UBA 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
E1BMF7	UniProtKB	Zinc finger	187	295	.	.	.	Note=UBP-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
E1BMF7	UniProtKB	Active site	345	345	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
E1BMF7	UniProtKB	Active site	823	823	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
E1BMF7	UniProtKB	Binding site	211	211	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
E1BMF7	UniProtKB	Binding site	214	214	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
E1BMF7	UniProtKB	Binding site	231	231	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
E1BMF7	UniProtKB	Binding site	244	244	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502	
E1BMF7	UniProtKB	Modified residue	114	114	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92995	
E1BMF7	UniProtKB	Modified residue	122	122	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92995	
E1BMF7	UniProtKB	Cross-link	311	311	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92995	
E1BMF7	UniProtKB	Cross-link	405	405	.	.	.	Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92995