##gff-version 3 Q9WTK7 UniProtKB Chain 1 433 . . . ID=PRO_0000260032;Note=Serine/threonine-protein kinase STK11 Q9WTK7 UniProtKB Propeptide 434 436 . . . ID=PRO_0000422301;Note=Removed in mature form Q9WTK7 UniProtKB Domain 49 309 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q9WTK7 UniProtKB Region 45 90 . . . Note=Sufficient for interaction with SIRT1;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q9WTK7 UniProtKB Region 397 421 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9WTK7 UniProtKB Active site 176 176 . . . Note=Proton acceptor;Ontology_term=ECO:0000250,ECO:0000255,ECO:0000255;evidence=ECO:0000250|UniProtKB:P28523,ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 Q9WTK7 UniProtKB Binding site 55 63 . . . Ontology_term=ECO:0000250,ECO:0000255;evidence=ECO:0000250|UniProtKB:P28523,ECO:0000255|PROSITE-ProRule:PRU00159 Q9WTK7 UniProtKB Binding site 78 78 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9WTK7 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:11853558,ECO:0007744|PubMed:21183079;Dbxref=PMID:11853558,PMID:21183079 Q9WTK7 UniProtKB Modified residue 44 44 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 48 48 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 96 96 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 97 97 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 189 189 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 296 296 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 311 311 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Modified residue 336 336 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Modified residue 366 366 . . . Note=Phosphothreonine%3B by ATM and autocatalysis;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11853558,ECO:0000269|PubMed:12234250,ECO:0000269|PubMed:20864035,ECO:0000269|PubMed:25329316;Dbxref=PMID:11853558,PMID:12234250,PMID:20864035,PMID:25329316 Q9WTK7 UniProtKB Modified residue 403 403 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 420 420 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 426 426 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Modified residue 431 431 . . . Note=Phosphoserine%3B by autocatalysis%2C PKA%2C PKC/PRKCZ and RPS6KA1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642527,ECO:0000269|PubMed:11297520,ECO:0000269|PubMed:17482548,ECO:0000269|PubMed:17482549;Dbxref=PMID:10642527,PMID:11297520,PMID:17482548,PMID:17482549 Q9WTK7 UniProtKB Modified residue 433 433 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Modified residue 434 434 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q15831 Q9WTK7 UniProtKB Lipidation 422 422 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10642527;Dbxref=PMID:10642527 Q9WTK7 UniProtKB Lipidation 433 433 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642527,ECO:0000269|PubMed:11297520,ECO:0000269|PubMed:11853558;Dbxref=PMID:10642527,PMID:11297520,PMID:11853558 Q9WTK7 UniProtKB Alternative sequence 98 232 . . . ID=VSP_060609;Note=In isoform 3. EIQLLRRLRHRNVIQLVDVLYNEEKQKMYMVMEYCVCGMQEMLDSVPEKRFPVCQAHGYFRQLIDGLEYLHSQGIVHKDIKPGNLLLTTNGTLKISDLGVAEALHPFAVDDTCRTSQGSPAFQPPEIANGLDTFS->PCTLSLWMTPAGQARAPRPSSLLRLPMDWTPFQVSRWTSGQLGSHFTTSPRACTHLRGTISTSSLRTLGEETSPSLVTAAHHSLTYSEGCWSMSRPRGSPSDRLGSTAGSGRNTLWLRRSYLSHQAQTLRTAGAV;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29777910;Dbxref=PMID:29777910 Q9WTK7 UniProtKB Alternative sequence 233 436 . . . ID=VSP_060610;Note=In isoform 3. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:29777910;Dbxref=PMID:29777910 Q9WTK7 UniProtKB Alternative sequence 374 415 . . . ID=VSP_052222;Note=In isoform 2. QVLEEEVGQNGQSHSLPKAVCVNGTEPQLSSKVKPEGRPGTA->VEEAAEAGLSEDACDTCMWKSQGAGLPGEEPEEGFGALV;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:16141072,ECO:0000303|Ref.6;Dbxref=PMID:16141072 Q9WTK7 UniProtKB Alternative sequence 416 436 . . . ID=VSP_052223;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:16141072,ECO:0000303|Ref.6;Dbxref=PMID:16141072 Q9WTK7 UniProtKB Mutagenesis 31 31 . . . Note=No change in kinase activity%3B when associated with A-325%3B A-336 and A-366. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Mutagenesis 78 78 . . . Note=Loss of kinase activity. K->I Q9WTK7 UniProtKB Mutagenesis 194 194 . . . Note=Loss of kinase activity and descreased phosphorylation. D->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Mutagenesis 325 325 . . . Note=No change in kinase activity%3B when associated with A-31%3B A-336 and A-366. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Mutagenesis 336 336 . . . Note=Abolishes ability to suppress cell growth. Decreased phosphorylation%3B when associated with A-366. No change in kinase activity%3B when associated with A-31%3B A-325 and A-366. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11853558;Dbxref=PMID:11853558 Q9WTK7 UniProtKB Mutagenesis 366 366 . . . Note=Diminished interaction with CDKN1A and impaired ability to repair UV-induced DNA damage by affecting CDKN1AUV-induced degradation. Decreased phosphorylation%3B when associated with A-336. No change in kinase activity%3B when associated with A-31%3B A-325 and A-336. T->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11853558,ECO:0000269|PubMed:12234250,ECO:0000269|PubMed:20864035,ECO:0000269|PubMed:25329316;Dbxref=PMID:11853558,PMID:12234250,PMID:20864035,PMID:25329316 Q9WTK7 UniProtKB Mutagenesis 431 431 . . . Note=Does not prevent S-farnesylation. Defects in neuron polarization. S->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642527,ECO:0000269|PubMed:11297520,ECO:0000269|PubMed:17482548,ECO:0000269|PubMed:17482549;Dbxref=PMID:10642527,PMID:11297520,PMID:17482548,PMID:17482549 Q9WTK7 UniProtKB Mutagenesis 433 433 . . . Note=Does not affect nuclear localization. Does not prevent phosphorylation at S-431. C->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10642527,ECO:0000269|PubMed:11297520,ECO:0000269|PubMed:11853558;Dbxref=PMID:10642527,PMID:11297520,PMID:11853558 Q9WTK7 UniProtKB Sequence conflict 95 95 . . . Note=V->L;Ontology_term=ECO:0000305;evidence=ECO:0000305