##gff-version 3
B2GUZ1	UniProtKB	Chain	1	961	.	.	.	ID=PRO_0000396806;Note=Ubiquitin carboxyl-terminal hydrolase 4	
B2GUZ1	UniProtKB	Domain	11	122	.	.	.	Note=DUSP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00613	
B2GUZ1	UniProtKB	Domain	142	226	.	.	.	Note=Ubiquitin-like 1;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B2GUZ1	UniProtKB	Domain	302	921	.	.	.	Note=USP;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01035	
B2GUZ1	UniProtKB	Domain	483	571	.	.	.	Note=Ubiquitin-like 2;Ontology_term=ECO:0000255;evidence=ECO:0000255	
B2GUZ1	UniProtKB	Region	27	216	.	.	.	Note=Necessary for interaction with SART3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Region	219	257	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B2GUZ1	UniProtKB	Region	229	295	.	.	.	Note=Required for USP4 activation by providing conformational flexibility between the DUSP and catalytic domains;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Region	384	386	.	.	.	Note=Regulates ubiquitin dissociation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Region	405	407	.	.	.	Note=Necessary for interaction with RBL2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35123	
B2GUZ1	UniProtKB	Region	459	463	.	.	.	Note=Necessary for interaction with RB1 and RBL2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35123	
B2GUZ1	UniProtKB	Region	485	773	.	.	.	Note=Interacts with DUSP and ubiquitin-like 1 domains and is required for USP4 activation;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Region	641	700	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B2GUZ1	UniProtKB	Region	924	961	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B2GUZ1	UniProtKB	Motif	133	141	.	.	.	Note=Nuclear export signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35123	
B2GUZ1	UniProtKB	Motif	765	770	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35123	
B2GUZ1	UniProtKB	Compositional bias	221	257	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
B2GUZ1	UniProtKB	Active site	311	311	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01035	
B2GUZ1	UniProtKB	Active site	879	879	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01035	
B2GUZ1	UniProtKB	Binding site	461	461	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Binding site	464	464	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Binding site	797	797	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Binding site	800	800	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Modified residue	445	445	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13107	
B2GUZ1	UniProtKB	Modified residue	655	655	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
B2GUZ1	UniProtKB	Modified residue	674	674	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
B2GUZ1	UniProtKB	Modified residue	679	679	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P35123