##gff-version 3
Q9Y463	UniProtKB	Chain	1	629	.	.	.	ID=PRO_0000085934;Note=Dual specificity tyrosine-phosphorylation-regulated kinase 1B	
Q9Y463	UniProtKB	Domain	111	431	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q9Y463	UniProtKB	Region	67	89	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9Y463	UniProtKB	Region	380	399	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9Y463	UniProtKB	Region	436	629	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9Y463	UniProtKB	Region	480	520	.	.	.	Note=Interaction with RANBP9;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14500717;Dbxref=PMID:14500717	
Q9Y463	UniProtKB	Motif	69	86	.	.	.	Note=Bipartite nuclear localization signal;Ontology_term=ECO:0000255;evidence=ECO:0000255	
Q9Y463	UniProtKB	Compositional bias	439	485	.	.	.	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9Y463	UniProtKB	Compositional bias	546	562	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q9Y463	UniProtKB	Active site	239	239	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q9Y463	UniProtKB	Binding site	117	125	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q9Y463	UniProtKB	Binding site	140	140	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q9Y463	UniProtKB	Binding site	190	193	.	.	.	Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q9Y463	UniProtKB	Modified residue	63	63	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Modified residue	92	92	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Modified residue	111	111	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Modified residue	129	129	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Modified residue	171	171	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q63470	
Q9Y463	UniProtKB	Modified residue	262	262	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Modified residue	271	271	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910078;Dbxref=PMID:10910078	
Q9Y463	UniProtKB	Modified residue	273	273	.	.	.	Note=Phosphotyrosine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910078;Dbxref=PMID:10910078	
Q9Y463	UniProtKB	Modified residue	401	401	.	.	.	Note=Phosphotyrosine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Modified residue	624	624	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q13627	
Q9Y463	UniProtKB	Alternative sequence	366	405	.	.	.	ID=VSP_004925;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9918863;Dbxref=PMID:9918863	
Q9Y463	UniProtKB	Alternative sequence	378	405	.	.	.	ID=VSP_004926;Note=In isoform 3. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:9918863;Dbxref=PMID:9918863	
Q9Y463	UniProtKB	Natural variant	28	28	.	.	.	ID=VAR_040454;Note=L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs34587974,PMID:17344846	
Q9Y463	UniProtKB	Natural variant	90	90	.	.	.	ID=VAR_071773;Note=In AOMS3%3B expression of glucose-6-phosphatase is significantly higher than wild-type. H->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24827035;Dbxref=dbSNP:rs587777380,PMID:24827035	
Q9Y463	UniProtKB	Natural variant	102	102	.	.	.	ID=VAR_071774;Note=In AOMS3%3B accumulation of intracellular lipid is significantly greater than with wild-type protein%3B cells expressing the variant are able to transform into mature adipocytes without requiring adipogenic medium%3B expression levels of CEBPA%2C PPARG forms 1 and 2 and PPARGC1A are higher and those of GLI1 and CDKN1B are lower in cells transfected with the mutant protein compared to wild-type%3B WNT1 signaling activity is lower in mutant cells compared to wild-type. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:24827035;Dbxref=dbSNP:rs367643250,PMID:24827035	
Q9Y463	UniProtKB	Natural variant	102	102	.	.	.	ID=VAR_040455;Note=R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs55687541,PMID:17344846	
Q9Y463	UniProtKB	Natural variant	234	234	.	.	.	ID=VAR_040456;Note=S->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35858874,PMID:17344846	
Q9Y463	UniProtKB	Natural variant	275	275	.	.	.	ID=VAR_040457;Note=In a metastatic melanoma sample%3B somatic mutation. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846	
Q9Y463	UniProtKB	Mutagenesis	140	140	.	.	.	Note=Abolishes kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910078;Dbxref=PMID:10910078	
Q9Y463	UniProtKB	Mutagenesis	239	239	.	.	.	Note=Abolishes kinase activity. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:32611815;Dbxref=PMID:32611815	
Q9Y463	UniProtKB	Mutagenesis	271	271	.	.	.	Note=Abolishes kinase activity%3B when associated with F-273. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910078;Dbxref=PMID:10910078	
Q9Y463	UniProtKB	Mutagenesis	273	273	.	.	.	Note=Abolishes kinase activity%3B when associated with F-271. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10910078;Dbxref=PMID:10910078