##gff-version 3
O94972	UniProtKB	Chain	1	964	.	.	.	ID=PRO_0000056254;Note=E3 ubiquitin-protein ligase TRIM37	
O94972	UniProtKB	Domain	276	403	.	.	.	Note=MATH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00129	
O94972	UniProtKB	Zinc finger	15	55	.	.	.	Note=RING-type%3B degenerate;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00175	
O94972	UniProtKB	Zinc finger	90	132	.	.	.	Note=B box-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
O94972	UniProtKB	Region	477	513	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Region	530	554	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Region	640	663	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Region	752	812	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Region	891	964	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Coiled coil	132	234	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O94972	UniProtKB	Coiled coil	419	450	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O94972	UniProtKB	Coiled coil	673	700	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255	
O94972	UniProtKB	Compositional bias	490	513	.	.	.	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Compositional bias	530	546	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Compositional bias	752	767	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Compositional bias	785	810	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
O94972	UniProtKB	Binding site	95	95	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
O94972	UniProtKB	Binding site	98	98	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
O94972	UniProtKB	Binding site	117	117	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
O94972	UniProtKB	Binding site	124	124	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00024	
O94972	UniProtKB	Modified residue	1	1	.	.	.	Note=N-acetylmethionine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:22814378;Dbxref=PMID:22814378	
O94972	UniProtKB	Modified residue	454	454	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
O94972	UniProtKB	Alternative sequence	1	122	.	.	.	ID=VSP_011919;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17974005;Dbxref=PMID:17974005	
O94972	UniProtKB	Alternative sequence	8	41	.	.	.	ID=VSP_057468;Note=In isoform 3. Missing	
O94972	UniProtKB	Alternative sequence	899	937	.	.	.	ID=VSP_011920;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:17974005;Dbxref=PMID:17974005	
O94972	UniProtKB	Natural variant	76	76	.	.	.	ID=VAR_060217;Note=In MUL%3B decreased ubiquitination and abolishes the formation of perinuclear aggregates. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15885686;Dbxref=dbSNP:rs386834004,PMID:15885686	
O94972	UniProtKB	Natural variant	108	108	.	.	.	ID=VAR_060218;Note=T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15489334;Dbxref=dbSNP:rs17853504,PMID:15489334	
O94972	UniProtKB	Natural variant	109	109	.	.	.	ID=VAR_060219;Note=In MUL%3B no effect on E3 ubiquitin-protein ligase activity. C->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17100991;Dbxref=dbSNP:rs121908391,PMID:17100991	
O94972	UniProtKB	Natural variant	322	322	.	.	.	ID=VAR_060220;Note=In MUL%3B no effect on ubiquitination but affects subcellular localization. G->V;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15108285,ECO:0000269|PubMed:15885686;Dbxref=dbSNP:rs386834009,PMID:15108285,PMID:15885686	
O94972	UniProtKB	Natural variant	432	432	.	.	.	ID=VAR_075470;Note=Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26697951;Dbxref=dbSNP:rs1458302547,PMID:26697951	
O94972	UniProtKB	Natural variant	838	838	.	.	.	ID=VAR_052142;Note=V->I;Dbxref=dbSNP:rs7222388	
O94972	UniProtKB	Mutagenesis	18	18	.	.	.	Note=Abolishes ability to monoubiquitinate 'Lys-119' of histone H2A (H2AK119Ub). C->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25470042;Dbxref=PMID:25470042	
O94972	UniProtKB	Mutagenesis	35	36	.	.	.	Note=Reduces ubiquitination and abolishes the formation of perinuclear aggregates. CC->SS;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:15885686;Dbxref=PMID:15885686	
O94972	UniProtKB	Sequence conflict	620	620	.	.	.	Note=I->M;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O94972	UniProtKB	Sequence conflict	624	624	.	.	.	Note=D->A;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O94972	UniProtKB	Sequence conflict	916	916	.	.	.	Note=E->G;Ontology_term=ECO:0000305;evidence=ECO:0000305	
O94972	UniProtKB	Helix	1	12	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Turn	16	18	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Beta strand	23	27	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Turn	29	31	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Beta strand	34	36	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Helix	37	46	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Turn	52	54	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Helix	60	62	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ	
O94972	UniProtKB	Helix	69	79	.	.	.	Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3LRQ