##gff-version 3 Q8K387 UniProtKB Chain 1 813 . . . ID=PRO_0000280562;Note=Ubiquitin carboxyl-terminal hydrolase 45 Q8K387 UniProtKB Domain 191 812 . . . Note=USP Q8K387 UniProtKB Zinc finger 36 153 . . . Note=UBP-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Region 1 62 . . . Note=Interaction with ERCC1;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:25538220;Dbxref=PMID:25538220 Q8K387 UniProtKB Region 1 27 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K387 UniProtKB Region 405 552 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K387 UniProtKB Compositional bias 411 428 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K387 UniProtKB Compositional bias 429 462 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K387 UniProtKB Compositional bias 463 489 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q8K387 UniProtKB Active site 200 200 . . . Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 Q8K387 UniProtKB Active site 745 745 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093 Q8K387 UniProtKB Binding site 38 38 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 40 40 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 62 62 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 65 65 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 85 85 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 88 88 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 93 93 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 101 101 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 105 105 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 114 114 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 127 127 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Binding site 130 130 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00502 Q8K387 UniProtKB Modified residue 28 28 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8K387 UniProtKB Modified residue 29 29 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8K387 UniProtKB Modified residue 507 507 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8K387 UniProtKB Modified residue 525 525 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079 Q8K387 UniProtKB Alternative sequence 390 437 . . . ID=VSP_023794;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:16141072;Dbxref=PMID:16141072 Q8K387 UniProtKB Sequence conflict 595 595 . . . Note=R->G;Ontology_term=ECO:0000305;evidence=ECO:0000305