##gff-version 3
Q8CFH6	UniProtKB	Chain	1	931	.	.	.	ID=PRO_0000086663;Note=Serine/threonine-protein kinase SIK2	
Q8CFH6	UniProtKB	Domain	20	271	.	.	.	Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159	
Q8CFH6	UniProtKB	Domain	295	335	.	.	.	Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212	
Q8CFH6	UniProtKB	Region	565	586	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFH6	UniProtKB	Region	595	624	.	.	.	Note=RK-rich region%3B required for cAMP responsiveness;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Region	631	662	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFH6	UniProtKB	Region	744	768	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFH6	UniProtKB	Region	798	842	.	.	.	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFH6	UniProtKB	Compositional bias	801	838	.	.	.	Note=Pro residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite	
Q8CFH6	UniProtKB	Active site	142	142	.	.	.	Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q13131,ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027	
Q8CFH6	UniProtKB	Binding site	26	34	.	.	.	Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:Q13131,ECO:0000255|PROSITE-ProRule:PRU00159	
Q8CFH6	UniProtKB	Binding site	49	49	.	.	.	Ontology_term=ECO:0000255,ECO:0000269;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000269|PubMed:12624099;Dbxref=PMID:12624099	
Q8CFH6	UniProtKB	Modified residue	25	25	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H0K1	
Q8CFH6	UniProtKB	Modified residue	53	53	.	.	.	Note=N6-acetyllysine%3B by EP300;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9H0K1	
Q8CFH6	UniProtKB	Modified residue	175	175	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16817901;Dbxref=PMID:16817901	
Q8CFH6	UniProtKB	Modified residue	358	358	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Modified residue	484	484	.	.	.	Note=Phosphothreonine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Modified residue	532	532	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFH6	UniProtKB	Modified residue	534	534	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFH6	UniProtKB	Modified residue	587	587	.	.	.	Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:21183079;Dbxref=PMID:21183079	
Q8CFH6	UniProtKB	Mutagenesis	49	49	.	.	.	Note=Loss of kinase activity. K->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12624099,ECO:0000269|PubMed:16817901;Dbxref=PMID:12624099,PMID:16817901	
Q8CFH6	UniProtKB	Mutagenesis	175	175	.	.	.	Note=Reduced inhibitory activity towards TORCs in presence and absence of cAMP signaling. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16817901;Dbxref=PMID:16817901	
Q8CFH6	UniProtKB	Mutagenesis	175	175	.	.	.	Note=Low levels of constitutive activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16817901;Dbxref=PMID:16817901	
Q8CFH6	UniProtKB	Mutagenesis	343	343	.	.	.	Note=Reduced interaction with 14-3-3 proteins in response to cAMP signaling and%2C thus%2C still able to inhibit TORC activity. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Mutagenesis	358	358	.	.	.	Note=Reduced interaction with 14-3-3 proteins in response to cAMP signaling and%2C thus%2C still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and%2C thus%2C still able to inhibit TORC activity%3B when associated with A-484 and A-587. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Mutagenesis	484	484	.	.	.	Note=Reduced interaction with 14-3-3 proteins in response to cAMP signaling and%2C thus%2C still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and%2C thus%2C still able to inhibit TORC activity%3B when associated with A-358 and A-587. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Mutagenesis	587	587	.	.	.	Note=Reduced interaction with 14-3-3 proteins in response to cAMP signaling and%2C thus%2C still able to inhibit TORC activity. Resistant to inhibition by cAMP signaling and%2C thus%2C still able to inhibit TORC activity%3B when associated with A-358 and A-484. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348	
Q8CFH6	UniProtKB	Mutagenesis	595	624	.	.	.	Note=Reduced 14-3-3 interaction. Reduced inactivation following cAMP signaling. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348