##gff-version 3
Q9QZS2	UniProtKB	Chain	1	194	.	.	.	ID=PRO_0000056044;Note=E3 ubiquitin-protein ligase RNF4	
Q9QZS2	UniProtKB	Zinc finger	136	181	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
Q9QZS2	UniProtKB	Region	1	39	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9QZS2	UniProtKB	Region	1	20	.	.	.	Note=Required for ubiquitination activity;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12885770;Dbxref=PMID:12885770	
Q9QZS2	UniProtKB	Region	6	65	.	.	.	Note=Mediates interaction with TRPS1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12885770;Dbxref=PMID:12885770	
Q9QZS2	UniProtKB	Region	110	130	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9QZS2	UniProtKB	Motif	40	43	.	.	.	Note=SUMO interaction motif 1%3B mediates the binding to polysumoylated substrates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P78317	
Q9QZS2	UniProtKB	Motif	50	53	.	.	.	Note=SUMO interaction motif 2%3B mediates the binding to polysumoylated substrates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P78317	
Q9QZS2	UniProtKB	Motif	61	63	.	.	.	Note=SUMO interaction motif 3%3B mediates the binding to polysumoylated substrates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P78317	
Q9QZS2	UniProtKB	Motif	71	74	.	.	.	Note=SUMO interaction motif 4%3B mediates the binding to polysumoylated substrates;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P78317	
Q9QZS2	UniProtKB	Compositional bias	1	35	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9QZS2	UniProtKB	Binding site	136	136	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	139	139	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	158	158	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	160	160	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	163	163	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	166	166	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	177	177	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Binding site	180	180	.	.	.	Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88846	
Q9QZS2	UniProtKB	Modified residue	98	98	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17242355,ECO:0007744|PubMed:21183079;Dbxref=PMID:17242355,PMID:21183079	
Q9QZS2	UniProtKB	Modified residue	99	99	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q9QZS2	UniProtKB	Mutagenesis	134	134	.	.	.	Note=Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. V->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20681948;Dbxref=PMID:20681948	
Q9QZS2	UniProtKB	Mutagenesis	155	155	.	.	.	Note=No effect. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20681948;Dbxref=PMID:20681948	
Q9QZS2	UniProtKB	Mutagenesis	155	155	.	.	.	Note=Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20681948;Dbxref=PMID:20681948	
Q9QZS2	UniProtKB	Mutagenesis	161	161	.	.	.	Note=Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20681948;Dbxref=PMID:20681948	
Q9QZS2	UniProtKB	Mutagenesis	193	193	.	.	.	Note=Abolishes homodimerization. Loss of E3 ubiquitin ligase activity. Y->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20681948;Dbxref=PMID:20681948