##gff-version 3
Q9NQC1	UniProtKB	Chain	1	790	.	.	.	ID=PRO_0000059308;Note=E3 ubiquitin-protein ligase Jade-2	
Q9NQC1	UniProtKB	Zinc finger	199	249	.	.	.	Note=PHD-type 1;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00146	
Q9NQC1	UniProtKB	Zinc finger	251	285	.	.	.	Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146	
Q9NQC1	UniProtKB	Zinc finger	309	365	.	.	.	Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU01146	
Q9NQC1	UniProtKB	Region	1	52	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NQC1	UniProtKB	Region	111	130	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NQC1	UniProtKB	Region	361	386	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NQC1	UniProtKB	Region	578	777	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NQC1	UniProtKB	Compositional bias	13	43	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9NQC1	UniProtKB	Modified residue	9	9	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163	
Q9NQC1	UniProtKB	Modified residue	15	15	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569	
Q9NQC1	UniProtKB	Modified residue	32	32	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
Q9NQC1	UniProtKB	Modified residue	38	38	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
Q9NQC1	UniProtKB	Modified residue	117	117	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q6ZQF7	
Q9NQC1	UniProtKB	Modified residue	298	298	.	.	.	Note=N6-acetyllysine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:19608861;Dbxref=PMID:19608861	
Q9NQC1	UniProtKB	Alternative sequence	518	790	.	.	.	ID=VSP_021050;Note=In isoform 3. GLSTSFPIDGTFFNSWLAQSVQITAENMAMSEWPLNNGHREDPAPGLLSEELLQDEETLLSFMRDPSLRPGDPARKARGRTRLPAKKKPPPPPPQDGPGSRTTPDKAPKKTWGQDAGSGKGGQGPPTRKPPRRTSSHLPSSPAAGDCPILATPESPPPLAPETPDEAASVAADSDVQVPGPAASPKPLGRLRPPRESKVTRRLPGARPDAGMGPPSAVAERPKVSLHFDTETDGYFSDGEMSDSDVEAEDGGVQRGPREAGAEEVVRMGVLAS->ERSGRRAKGKKSDSKRKGCEGSKGSTEKKEKVKAGPDSVLGQLGE;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:12693554;Dbxref=PMID:12693554	
Q9NQC1	UniProtKB	Alternative sequence	518	518	.	.	.	ID=VSP_021051;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:15489334,ECO:0000303|PubMed:9039502;Dbxref=PMID:15489334,PMID:9039502	
Q9NQC1	UniProtKB	Natural variant	581	581	.	.	.	ID=VAR_053778;Note=R->G;Dbxref=dbSNP:rs34200923	
Q9NQC1	UniProtKB	Mutagenesis	202	202	.	.	.	Note=Loss of E3 ubiquitin-protein ligase activity on KDM1A. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25018020;Dbxref=PMID:25018020	
Q9NQC1	UniProtKB	Mutagenesis	243	243	.	.	.	Note=Loss of E3 ubiquitin-protein ligase activity on KDM1A. C->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25018020;Dbxref=PMID:25018020	
Q9NQC1	UniProtKB	Sequence conflict	331	331	.	.	.	Note=T->I;Ontology_term=ECO:0000305;evidence=ECO:0000305