##gff-version 3
A2VDM8	UniProtKB	Chain	1	711	.	.	.	ID=PRO_0000395816;Note=Ubiquitin carboxyl-terminal hydrolase BAP1	
A2VDM8	UniProtKB	Region	255	337	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Region	354	420	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Region	446	506	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Region	557	605	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Region	578	703	.	.	.	Note=Interaction with BRCA1;Ontology_term=ECO:0000250;evidence=ECO:0000250	
A2VDM8	UniProtKB	Region	685	711	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Coiled coil	612	643	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
A2VDM8	UniProtKB	Motif	345	348	.	.	.	Note=HBM-like motif;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Motif	699	704	.	.	.	Note=Nuclear localization signal;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Compositional bias	255	288	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Compositional bias	558	579	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Compositional bias	583	597	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Compositional bias	686	711	.	.	.	Note=Basic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
A2VDM8	UniProtKB	Active site	91	91	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Active site	169	169	.	.	.	Note=Proton donor;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09936	
A2VDM8	UniProtKB	Site	184	184	.	.	.	Note=Important for enzyme activity;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P09936	
A2VDM8	UniProtKB	Modified residue	274	274	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Modified residue	351	351	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Modified residue	377	377	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q99PU7	
A2VDM8	UniProtKB	Modified residue	475	475	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Modified residue	503	503	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Modified residue	519	519	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Modified residue	567	567	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560	
A2VDM8	UniProtKB	Modified residue	579	579	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q92560