##gff-version 3
Q6J1Y9	UniProtKB	Chain	1	1357	.	.	.	ID=PRO_0000295158;Note=Ubiquitin carboxyl-terminal hydrolase 19	
Q6J1Y9	UniProtKB	Topological domain	1	1330	.	.	.	Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q6J1Y9	UniProtKB	Transmembrane	1331	1351	.	.	.	Note=Helical;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q6J1Y9	UniProtKB	Topological domain	1352	1357	.	.	.	Note=Lumenal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q6J1Y9	UniProtKB	Domain	51	140	.	.	.	Note=CS 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547	
Q6J1Y9	UniProtKB	Domain	321	423	.	.	.	Note=CS 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00547	
Q6J1Y9	UniProtKB	Domain	536	1253	.	.	.	Note=USP	
Q6J1Y9	UniProtKB	Zinc finger	830	872	.	.	.	Note=MYND-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Region	1	52	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Region	162	239	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Region	275	296	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Region	432	479	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Region	962	981	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Region	1259	1278	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Region	1292	1320	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Compositional bias	17	52	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Compositional bias	172	186	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Compositional bias	460	477	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Compositional bias	1302	1316	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q6J1Y9	UniProtKB	Active site	545	545	.	.	.	Note=Nucleophile;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
Q6J1Y9	UniProtKB	Active site	1204	1204	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU10092,ECO:0000255|PROSITE-ProRule:PRU10093	
Q6J1Y9	UniProtKB	Binding site	830	830	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	833	833	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	847	847	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	850	850	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	856	856	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	860	860	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	868	868	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Binding site	872	872	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00134	
Q6J1Y9	UniProtKB	Modified residue	221	221	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q3UJD6	
Q6J1Y9	UniProtKB	Modified residue	283	283	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22673903;Dbxref=PMID:22673903	
Q6J1Y9	UniProtKB	Mutagenesis	545	545	.	.	.	Note=Has a destabilizing effect on RNF123. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19015242;Dbxref=PMID:19015242