##gff-version 3 P57059 UniProtKB Chain 1 783 . . . ID=PRO_0000086659;Note=Serine/threonine-protein kinase SIK1 P57059 UniProtKB Domain 27 278 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P57059 UniProtKB Domain 303 343 . . . Note=UBA;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00212 P57059 UniProtKB Region 353 377 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P57059 UniProtKB Region 449 477 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P57059 UniProtKB Region 583 612 . . . Note=RK-rich region%3B required for cAMP responsiveness and nuclear localization;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Region 619 643 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P57059 UniProtKB Compositional bias 457 477 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P57059 UniProtKB Active site 149 149 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P57059 UniProtKB Binding site 33 41 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P57059 UniProtKB Binding site 56 56 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 P57059 UniProtKB Modified residue 182 182 . . . Note=Phosphothreonine%3B by LKB1 and GSK3-beta;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14976552,ECO:0000269|PubMed:18348280;Dbxref=PMID:14976552,PMID:18348280 P57059 UniProtKB Modified residue 186 186 . . . Note=Phosphoserine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348280;Dbxref=PMID:18348280 P57059 UniProtKB Modified residue 322 322 . . . Note=Phosphothreonine%3B by CaMK1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9R1U5 P57059 UniProtKB Modified residue 473 473 . . . Note=Phosphothreonine%3B by PKA;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Modified residue 575 575 . . . Note=Phosphoserine%3B by PKA;Ontology_term=ECO:0000250,ECO:0000305;evidence=ECO:0000250|UniProtKB:Q60670,ECO:0000305|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Natural variant 15 15 . . . ID=VAR_041087;Note=G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs3746951,PMID:17344846 P57059 UniProtKB Natural variant 142 142 . . . ID=VAR_041088;Note=D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs45491503,PMID:17344846 P57059 UniProtKB Natural variant 211 211 . . . ID=VAR_041089;Note=In a glioblastoma multiforme sample%3B somatic mutation. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P57059 UniProtKB Natural variant 287 287 . . . ID=VAR_073701;Note=In DEE30%3B no change in subcellular location. P->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25839329;Dbxref=dbSNP:rs786205159,PMID:25839329 P57059 UniProtKB Natural variant 411 411 . . . ID=VAR_073702;Note=In DEE30%3B no change in subcellular location. S->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25839329;Dbxref=PMID:25839329 P57059 UniProtKB Natural variant 430 430 . . . ID=VAR_033910;Note=R->W;Dbxref=dbSNP:rs34164089 P57059 UniProtKB Natural variant 469 469 . . . ID=VAR_041090;Note=In a metastatic melanoma sample%3B somatic mutation. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=PMID:17344846 P57059 UniProtKB Natural variant 615 615 . . . ID=VAR_021255;Note=A->V;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14702039,ECO:0000269|PubMed:15489334,ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs430554,PMID:14702039,PMID:15489334,PMID:17344846 P57059 UniProtKB Natural variant 636 636 . . . ID=VAR_073703;Note=In DEE30%3B no change in subcellular location. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25839329;Dbxref=dbSNP:rs786205163,PMID:25839329 P57059 UniProtKB Natural variant 696 696 . . . ID=VAR_041091;Note=P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs56386767,PMID:17344846 P57059 UniProtKB Natural variant 725 725 . . . ID=VAR_041092;Note=A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs35596465,PMID:17344846 P57059 UniProtKB Mutagenesis 56 56 . . . Note=Loss of kinase activity. K->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:18348280,ECO:0000269|PubMed:19622832;Dbxref=PMID:18348280,PMID:19622832 P57059 UniProtKB Mutagenesis 135 135 . . . Note=Decreased kinase activity without affecting much autophosphorylation status. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348280;Dbxref=PMID:18348280 P57059 UniProtKB Mutagenesis 182 182 . . . Note=Prevents phosphorylation and activation by STK11/LKB1 complex. Reduced inhibition of CRTC3-mediated transcriptional activity. T->A;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14976552,ECO:0000269|PubMed:29211348;Dbxref=PMID:14976552,PMID:29211348 P57059 UniProtKB Mutagenesis 186 186 . . . Note=Impaired autophosphorylation and kinase activity. S->A%2CD%2CC%2CG;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348280;Dbxref=PMID:18348280 P57059 UniProtKB Mutagenesis 186 186 . . . Note=Does not autophosphorylation and kinase activity. S->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348280;Dbxref=PMID:18348280 P57059 UniProtKB Mutagenesis 209 209 . . . Note=Decreased kinase activity without affecting much autophosphorylation status. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348280;Dbxref=PMID:18348280 P57059 UniProtKB Mutagenesis 248 248 . . . Note=Decreased kinase activity without affecting much autophosphorylation status. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18348280;Dbxref=PMID:18348280 P57059 UniProtKB Mutagenesis 473 473 . . . Note=Reduced but still present 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-575. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Mutagenesis 473 473 . . . Note=Reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and%2C thus%2C still able to inhibit TORC activity. T->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Mutagenesis 575 575 . . . Note=Loss of 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-473. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Mutagenesis 575 575 . . . Note=Strongly reduced but still present interaction with 14-3-3 proteins in response to cAMP signaling and%2C thus%2C still able to inhibit TORC activity. S->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29211348;Dbxref=PMID:29211348 P57059 UniProtKB Sequence conflict 166 166 . . . Note=A->AGTE;Ontology_term=ECO:0000305;evidence=ECO:0000305 P57059 UniProtKB Sequence conflict 489 490 . . . Note=IV->KF;Ontology_term=ECO:0000305;evidence=ECO:0000305