##gff-version 3 Q15831 UniProtKB Chain 1 430 . . . ID=PRO_0000086699;Note=Serine/threonine-protein kinase STK11 Q15831 UniProtKB Propeptide 431 433 . . . ID=PRO_0000422300;Note=Removed in mature form;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q15831 UniProtKB Domain 49 309 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q15831 UniProtKB Region 45 90 . . . Note=Sufficient for interaction with SIRT1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Region 312 331 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15831 UniProtKB Region 397 433 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q15831 UniProtKB Active site 176 176 . . . Note=Proton acceptor Q15831 UniProtKB Binding site 55 63 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 Q15831 UniProtKB Binding site 78 78 . . . Ontology_term=ECO:0000305;evidence=ECO:0000305 Q15831 UniProtKB Modified residue 31 31 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q15831 UniProtKB Modified residue 44 44 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 48 48 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 96 96 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 97 97 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 189 189 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11430832;Dbxref=PMID:11430832 Q15831 UniProtKB Modified residue 296 296 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 311 311 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 325 325 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q9WTK7 Q15831 UniProtKB Modified residue 336 336 . . . Note=Phosphothreonine%3B by autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12805220;Dbxref=PMID:12805220 Q15831 UniProtKB Modified residue 363 363 . . . Note=Phosphothreonine%3B by ATM and autocatalysis;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12805220;Dbxref=PMID:12805220 Q15831 UniProtKB Modified residue 401 401 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 Q15831 UniProtKB Modified residue 416 416 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 423 423 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Modified residue 428 428 . . . Note=Phosphoserine%3B by autocatalysis%2C PKA%2C PKC/PRKCZ and RPS6KA1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18854309;Dbxref=PMID:18854309 Q15831 UniProtKB Modified residue 430 430 . . . Note=Cysteine methyl ester;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q15831 UniProtKB Modified residue 431 431 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Lipidation 418 418 . . . Note=S-palmitoyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q15831 UniProtKB Lipidation 430 430 . . . Note=S-farnesyl cysteine;Ontology_term=ECO:0000250;evidence=ECO:0000250 Q15831 UniProtKB Alternative sequence 371 433 . . . ID=VSP_041746;Note=In isoform 2. QVPEEEASHNGQRRGLPKAVCMNGTEAAQLSTKSRAEGRAPNPARKACSASSKIRRLSACKQQ->GEEASEAGLRAERGLQKSEGSDLSGEEASRPAPQ;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q15831 UniProtKB Natural variant 14 14 . . . ID=VAR_065627;Note=In cervical cancer%3B somatic mutation. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12533684;Dbxref=PMID:12533684 Q15831 UniProtKB Natural variant 16 16 . . . ID=VAR_065628;Note=In PJS. E->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21411391;Dbxref=PMID:21411391 Q15831 UniProtKB Natural variant 49 49 . . . ID=VAR_033138;Note=In melanoma%3B sporadic malignant%3B somatic mutation. Y->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10201537;Dbxref=dbSNP:rs137853080,PMID:10201537 Q15831 UniProtKB Natural variant 50 53 . . . ID=VAR_071057;Note=In PJS. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9837816;Dbxref=PMID:9837816 Q15831 UniProtKB Natural variant 66 66 . . . ID=VAR_065629;Note=In cervical carcinoma%3B somatic mutation. V->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12533684,ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs1599915144,PMID:12533684,PMID:19892943 Q15831 UniProtKB Natural variant 67 67 . . . ID=VAR_006202;Note=In PJS%3B abolishes kinase activity%2C leading to loss of autophosphorylation. L->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:9428765,ECO:0000269|PubMed:9837816;Dbxref=dbSNP:rs137853077,PMID:9428765,PMID:9837816 Q15831 UniProtKB Natural variant 86 86 . . . ID=VAR_065630;Note=In sporadic cancer%3B somatic mutation%3B no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs1057520039,PMID:19892943 Q15831 UniProtKB Natural variant 87 87 . . . ID=VAR_041139;Note=In a metastatic melanoma sample%3B somatic mutation. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17344846;Dbxref=dbSNP:rs1568690463,PMID:17344846 Q15831 UniProtKB Natural variant 123 123 . . . ID=VAR_065631;Note=In sporadic cancer%3B somatic mutation%3B no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. Q->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs764449808,PMID:19892943 Q15831 UniProtKB Natural variant 135 135 . . . ID=VAR_033139;Note=In melanoma%3B sporadic malignant%3B somatic mutation. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10201537;Dbxref=dbSNP:rs137853081,PMID:10201537 Q15831 UniProtKB Natural variant 157 157 . . . ID=VAR_065632;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. F->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 160 160 . . . ID=VAR_065633;Note=In cervical cancer%3B somatic mutation. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12533684;Dbxref=PMID:12533684 Q15831 UniProtKB Natural variant 162 164 . . . ID=VAR_007920;Note=In PJS. DGL->NDM;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10408777;Dbxref=PMID:10408777 Q15831 UniProtKB Natural variant 163 163 . . . ID=VAR_033140;Note=In TGCT%3B a tumor with seminoma and teratoma components%3B somatic mutation%3B severely impaired but detectable kinase activity%3B impairs heterotrimeric complex assembly with STRADA and CAB39%3B predominantly nuclear localization. G->D;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19892943,ECO:0000269|PubMed:9605748,ECO:0000269|PubMed:9887330;Dbxref=dbSNP:rs137853078,PMID:19892943,PMID:9605748,PMID:9887330 Q15831 UniProtKB Natural variant 170 170 . . . ID=VAR_065634;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. Q->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 171 171 . . . ID=VAR_065635;Note=In colorectal cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19892943,ECO:0000269|PubMed:9731485;Dbxref=dbSNP:rs1599926499,PMID:19892943,PMID:9731485 Q15831 UniProtKB Natural variant 174 174 . . . ID=VAR_065636;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 176 176 . . . ID=VAR_071058;Note=In PJS%3B loss of kinase activity%2C leading to greatly reduced autophosphorylation%3B fails to phosphorylate PTEN in vitro%3B no significant effect on nucleocytoplasmic localization. D->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15987703,ECO:0000269|PubMed:9837816;Dbxref=dbSNP:rs730881979,PMID:15987703,PMID:9837816 Q15831 UniProtKB Natural variant 176 176 . . . ID=VAR_065637;Note=In sporadic cancer%3B somatic mutation%3B Loss of kinase activity. D->Y;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12805220,ECO:0000269|PubMed:19892943;Dbxref=PMID:12805220,PMID:19892943 Q15831 UniProtKB Natural variant 177 177 . . . ID=VAR_065638;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. I->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs1057520041,PMID:19892943 Q15831 UniProtKB Natural variant 181 181 . . . ID=VAR_065639;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39%3B requires 2 nucleotide substitutions. N->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs1568707668,PMID:19892943 Q15831 UniProtKB Natural variant 194 194 . . . ID=VAR_007921;Note=In PJS. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10408777;Dbxref=dbSNP:rs121913315,PMID:10408777 Q15831 UniProtKB Natural variant 194 194 . . . ID=VAR_065640;Note=In lung cancer%3B somatic mutation. D->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10079245;Dbxref=dbSNP:rs121913316,PMID:10079245 Q15831 UniProtKB Natural variant 194 194 . . . ID=VAR_033141;Note=In melanoma%3B sporadic malignant%3B somatic mutation. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10208439;Dbxref=dbSNP:rs121913315,PMID:10208439 Q15831 UniProtKB Natural variant 199 199 . . . ID=VAR_065641;Note=In colorectal cancer%3B somatic mutation%3B impaired kinase activity. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9731485;Dbxref=dbSNP:rs121913317,PMID:9731485 Q15831 UniProtKB Natural variant 199 199 . . . ID=VAR_065642;Note=In sporadic cancer%3B somatic mutation%3B does not affect kinase activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 205 205 . . . ID=VAR_065643;Note=In sporadic cancer%3B somatic mutation%3B no effect heterotrimeric complex assembly with STRADA and CAB39. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs730881981,PMID:19892943 Q15831 UniProtKB Natural variant 208 208 . . . ID=VAR_065644;Note=In colorectal cancer%3B somatic mutation%3B no effect heterotrimeric complex assembly with STRADA and CAB39. D->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9731485;Dbxref=dbSNP:rs1555738372,PMID:9731485 Q15831 UniProtKB Natural variant 215 215 . . . ID=VAR_065645;Note=In colorectal cancer%3B somatic mutation. G->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9731485;Dbxref=dbSNP:rs1057520038,PMID:9731485 Q15831 UniProtKB Natural variant 216 216 . . . ID=VAR_065646;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. S->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs1057520017,PMID:19892943 Q15831 UniProtKB Natural variant 223 223 . . . ID=VAR_065647;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. E->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 230 230 . . . ID=VAR_065648;Note=In sporadic cancer%3B somatic mutation%3B no effect heterotrimeric complex assembly with STRADA and CAB39. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 231 231 . . . ID=VAR_065649;Note=In cervical cancer%3B somatic mutation. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12533684;Dbxref=dbSNP:rs929783669,PMID:12533684 Q15831 UniProtKB Natural variant 232 232 . . . ID=VAR_065650;Note=In sporadic cancer%3B somatic mutation%3B no effect heterotrimeric complex assembly with STRADA and CAB39. S->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 239 239 . . . ID=VAR_033142;Note=In PJS%3B late onset suggests reduced penetrance. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12372054;Dbxref=dbSNP:rs137853082,PMID:12372054 Q15831 UniProtKB Natural variant 245 245 . . . ID=VAR_065651;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. L->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 247 247 . . . ID=VAR_006203;Note=In PJS. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9760200;Dbxref=PMID:9760200 Q15831 UniProtKB Natural variant 250 250 . . . ID=VAR_065652;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 272 272 . . . ID=VAR_065653;Note=In sporadic cancer%3B somatic mutation%3B no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. Y->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 277 277 . . . ID=VAR_065654;Note=In sporadic cancer%3B somatic mutation%3B no effect on kinase activity nor in heterotrimeric complex assembly with STRADA and CAB39. D->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 281 281 . . . ID=VAR_065655;Note=In ovarian carcinoma%3B somatic mutation. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10429654;Dbxref=dbSNP:rs121913322,PMID:10429654 Q15831 UniProtKB Natural variant 285 285 . . . ID=VAR_065656;Note=In sporadic cancer%3B somatic mutation%3B impairs heterotrimeric complex assembly with STRADA and CAB39. L->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Natural variant 297 297 . . . ID=VAR_007922;Note=In PJS. R->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10408777;Dbxref=dbSNP:rs1568710381,PMID:10408777 Q15831 UniProtKB Natural variant 303 306 . . . ID=VAR_033143;Note=In PJS. IRQH->N Q15831 UniProtKB Natural variant 308 308 . . . ID=VAR_071059;Note=In PJS%3B abolishes kinase activity%2C leading to loss of autophosphorylation. W->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9837816;Dbxref=dbSNP:rs1057520042,PMID:9837816 Q15831 UniProtKB Natural variant 314 314 . . . ID=VAR_065657;Note=In colorectal cancer%3B no effect heterotrimeric complex assembly with STRADA and CAB39. P->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9809980;Dbxref=PMID:9809980 Q15831 UniProtKB Natural variant 315 315 . . . ID=VAR_033144;Note=In PJS%3B uncertain significance%3B no effect heterotrimeric complex assembly with STRADA and CAB39. P->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12372054,ECO:0000269|PubMed:19892943;Dbxref=dbSNP:rs786202431,PMID:12372054,PMID:19892943 Q15831 UniProtKB Natural variant 324 324 . . . ID=VAR_065658;Note=In gastric carcinoma%3B no effect heterotrimeric complex assembly with STRADA and CAB39. P->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9683800;Dbxref=dbSNP:rs367807476,PMID:9683800 Q15831 UniProtKB Natural variant 354 354 . . . ID=VAR_065659;Note=In colorectal cancer%3B somatic mutation. F->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9731485;Dbxref=dbSNP:rs59912467,PMID:9731485 Q15831 UniProtKB Natural variant 367 367 . . . ID=VAR_065660;Note=In colorectal cancer%3B somatic mutation. T->M;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:9731485;Dbxref=dbSNP:rs587782835,PMID:9731485 Q15831 UniProtKB Mutagenesis 44 44 . . . Note=No effect on kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Mutagenesis 48 48 . . . Note=No effect on basal nucleocytoplasmic localization%2C but fails to translocate to the cytoplasm when coexpressed with SIRT1. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Mutagenesis 48 48 . . . Note=Enhanced phosphorylation at Thr-336 and Ser-428%2C enhanced cytoplasmic localization and increased kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Mutagenesis 74 74 . . . Note=Impaired formation of a heterotrimeric complex with STRADA and CAB39%3B when associated with A-204. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Mutagenesis 78 78 . . . Note=Loss of kinase activity%2C leading to greatly reduced autophosphorylation. K->I;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11430832,ECO:0000269|PubMed:9837816;Dbxref=PMID:11430832,PMID:9837816 Q15831 UniProtKB Mutagenesis 78 78 . . . Note=Loss of kinase activity%2C leading to reduced autophosphorylation and acting as a dominant-negative mutant. K->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:11430832,ECO:0000269|PubMed:9837816;Dbxref=PMID:11430832,PMID:9837816 Q15831 UniProtKB Mutagenesis 96 96 . . . Note=No effect on kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Mutagenesis 97 97 . . . Note=No effect on kinase activity. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18687677;Dbxref=PMID:18687677 Q15831 UniProtKB Mutagenesis 189 189 . . . Note=Reduced phosphorylation. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11430832;Dbxref=PMID:11430832 Q15831 UniProtKB Mutagenesis 194 194 . . . Note=Loss of kinase activity. D->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14517248,ECO:0000269|PubMed:14976552,ECO:0000269|PubMed:19892943;Dbxref=PMID:14517248,PMID:14976552,PMID:19892943 Q15831 UniProtKB Mutagenesis 204 204 . . . Note=No effect. Impaired formation of a heterotrimeric complex with STRADA and CAB39%3B when associated with A-74. F->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19892943;Dbxref=PMID:19892943 Q15831 UniProtKB Mutagenesis 428 428 . . . Note=No effect on kinase activity. S->A%2CE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:18854309;Dbxref=PMID:18854309 Q15831 UniProtKB Beta strand 54 57 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 62 68 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Turn 69 71 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 74 80 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 82 87 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 91 102 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 113 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 125 130 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 133 135 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 136 142 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 150 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 179 181 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 182 184 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 190 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 217 219 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 222 225 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 231 233 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 234 250 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 260 269 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Beta strand 276 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 280 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Turn 294 296 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 300 305 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 307 310 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Helix 334 336 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4ZDR Q15831 UniProtKB Helix 339 341 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2WTK Q15831 UniProtKB Modified residue 399 399 . . . Note=Phosphoserine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23612973;Dbxref=PMID:23612973