##gff-version 3
Q9UPQ4	UniProtKB	Chain	1	493	.	.	.	ID=PRO_0000056250;Note=E3 ubiquitin-protein ligase TRIM35	
Q9UPQ4	UniProtKB	Domain	284	487	.	.	.	Note=B30.2/SPRY;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00548	
Q9UPQ4	UniProtKB	Zinc finger	21	61	.	.	.	Note=RING-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
Q9UPQ4	UniProtKB	Zinc finger	96	137	.	.	.	Note=B box-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
Q9UPQ4	UniProtKB	Coiled coil	210	251	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9UPQ4	UniProtKB	Binding site	101	101	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
Q9UPQ4	UniProtKB	Binding site	104	104	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
Q9UPQ4	UniProtKB	Binding site	123	123	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
Q9UPQ4	UniProtKB	Binding site	129	129	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
Q9UPQ4	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692	
Q9UPQ4	UniProtKB	Modified residue	4	4	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:21406692,PMID:23186163	
Q9UPQ4	UniProtKB	Modified residue	8	8	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21406692;Dbxref=PMID:21406692	
Q9UPQ4	UniProtKB	Alternative sequence	146	206	.	.	.	ID=VSP_012061;Note=In isoform 2. AKCRNMEHALREKAKAFWAMRRSYEAIAKHNQVEAAWLEGRIRQEFDKLREFLRVEEQAIL->VRSLIAEERRNFLPTHQWIVTKTRLQTSSPNLQSRRQGQVQEHGACTAGEGQGLLGHAALL;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334