##gff-version 3 P31749 UniProtKB Chain 1 480 . . . ID=PRO_0000085605;Note=RAC-alpha serine/threonine-protein kinase P31749 UniProtKB Domain 5 108 . . . Note=PH;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00145 P31749 UniProtKB Domain 150 408 . . . Note=Protein kinase;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P31749 UniProtKB Domain 409 480 . . . Note=AGC-kinase C-terminal;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00618 P31749 UniProtKB Region 113 138 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P31749 UniProtKB Region 450 480 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P31749 UniProtKB Active site 274 274 . . . Note=Proton acceptor;Ontology_term=ECO:0000255,ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159,ECO:0000255|PROSITE-ProRule:PRU10027 P31749 UniProtKB Binding site 14 19 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:12964941;Dbxref=PMID:12176338,PMID:12964941 P31749 UniProtKB Binding site 23 25 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:12964941;Dbxref=PMID:12176338,PMID:12964941 P31749 UniProtKB Binding site 53 53 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:12964941;Dbxref=PMID:12176338,PMID:12964941 P31749 UniProtKB Binding site 86 86 . . . Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:12964941;Dbxref=PMID:12176338,PMID:12964941 P31749 UniProtKB Binding site 156 164 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P31749 UniProtKB Binding site 179 179 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00159 P31749 UniProtKB Site 462 462 . . . Note=Cleavage%3B by caspase-3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31750 P31749 UniProtKB Modified residue 14 14 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 P31749 UniProtKB Modified residue 20 20 . . . Note=N6-acetyllysine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 P31749 UniProtKB Modified residue 124 124 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 P31749 UniProtKB Modified residue 126 126 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:18669648;Dbxref=PMID:18669648 P31749 UniProtKB Modified residue 129 129 . . . Note=Phosphoserine%3B alternate;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:17081983,ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:23186163;Dbxref=PMID:17081983,PMID:18669648,PMID:23186163 P31749 UniProtKB Modified residue 176 176 . . . Note=Phosphotyrosine%3B by TNK2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 P31749 UniProtKB Modified residue 308 308 . . . Note=Phosphothreonine%3B by IKKE%2C PDPK1 and TBK1;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:15718470,ECO:0000269|PubMed:18456494,ECO:0000269|PubMed:20333297,ECO:0000269|PubMed:20481595,ECO:0000269|PubMed:21464307,ECO:0000269|PubMed:8978681,ECO:0000269|PubMed:9512493;Dbxref=PMID:15718470,PMID:18456494,PMID:20333297,PMID:20481595,PMID:21464307,PMID:8978681,PMID:9512493 P31749 UniProtKB Modified residue 448 448 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P31749 UniProtKB Modified residue 450 450 . . . Note=Phosphothreonine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:24275569;Dbxref=PMID:24275569 P31749 UniProtKB Modified residue 473 473 . . . Note=Phosphoserine%3B by IKKE%2C MTOR and TBK1%3B alternate;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:14761976,ECO:0000269|PubMed:15047712,ECO:0000269|PubMed:15718470,ECO:0000269|PubMed:16266983,ECO:0000269|PubMed:17013611,ECO:0000269|PubMed:20333297,ECO:0000269|PubMed:20978158,ECO:0000269|PubMed:21464307,ECO:0000269|PubMed:23799035,ECO:0000269|PubMed:8978681,ECO:0000269|PubMed:9736715;Dbxref=PMID:14761976,PMID:15047712,PMID:15718470,PMID:16266983,PMID:17013611,PMID:20333297,PMID:20978158,PMID:21464307,PMID:23799035,PMID:8978681,PMID:9736715 P31749 UniProtKB Modified residue 474 474 . . . Note=Phosphotyrosine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12149249;Dbxref=PMID:12149249 P31749 UniProtKB Glycosylation 126 126 . . . Note=O-linked (GlcNAc) serine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Glycosylation 129 129 . . . Note=O-linked (GlcNAc) serine%3B alternate;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Glycosylation 305 305 . . . Note=O-linked (GlcNAc) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Glycosylation 312 312 . . . Note=O-linked (GlcNAc) threonine;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Glycosylation 473 473 . . . Note=O-linked (GlcNAc) serine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31750 P31749 UniProtKB Disulfide bond 60 77 . . . Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20886116;Dbxref=PMID:20886116 P31749 UniProtKB Disulfide bond 296 310 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P31751 P31749 UniProtKB Cross-link 284 284 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin);Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22410793;Dbxref=PMID:22410793 P31749 UniProtKB Alternative sequence 1 62 . . . ID=VSP_056180;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P31749 UniProtKB Natural variant 17 17 . . . ID=VAR_055422;Note=In PROTEUSS and breast cancer%3B also detected in colorectal and ovarian cancer%3B somatic mutation%3B results in increased phosphorylation at T-308 and higher basal ubiquitination%3B the mutant protein is more efficiently recruited to the plasma membrane%3B alters phosphatidylinositiol phosphates lipid specificity of the AKT1 PH domain. E->K;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:17611497,ECO:0000269|PubMed:18954143,ECO:0000269|PubMed:19713527,ECO:0000269|PubMed:21793738;Dbxref=dbSNP:rs121434592,PMID:17611497,PMID:18954143,PMID:19713527,PMID:21793738 P31749 UniProtKB Natural variant 25 25 . . . ID=VAR_069791;Note=In CWS6. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514644,PMID:23246288 P31749 UniProtKB Natural variant 167 167 . . . ID=VAR_051617;Note=V->A;Dbxref=dbSNP:rs11555433 P31749 UniProtKB Natural variant 435 435 . . . ID=VAR_069792;Note=In CWS6. T->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:23246288;Dbxref=dbSNP:rs397514645,PMID:23246288 P31749 UniProtKB Mutagenesis 8 8 . . . Note=Substantial reduction of ubiquitination%2C phosphorylation at T-308 and S-473%2C AKT activation as well as IGF1-induced membrane recruitment. Decrease in ubiquitination and phosphorylation at T-308 as well as impaired association with the membrane%3B when associated with K-17. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19713527;Dbxref=PMID:19713527 P31749 UniProtKB Mutagenesis 14 14 . . . Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. K->A;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:19713527,ECO:0000269|PubMed:21775285;Dbxref=PMID:12176338,PMID:19713527,PMID:21775285 P31749 UniProtKB Mutagenesis 14 14 . . . Note=Substantial reduction of phosphorylation at T-308 and S-473%2C loss of AKT activation%2C and loss of binding to PIP3 as well as IGF1-induced membrane recruitment. K->Q;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:19713527,ECO:0000269|PubMed:21775285;Dbxref=PMID:12176338,PMID:19713527,PMID:21775285 P31749 UniProtKB Mutagenesis 14 14 . . . Note=Substantial reduction of ubiquitination%2C phosphorylation at T-308 and S-473%2C AKT activation%2C loss of binding to PIP3 as well as IGF1-induced membrane recruitment. K->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12176338,ECO:0000269|PubMed:19713527,ECO:0000269|PubMed:21775285;Dbxref=PMID:12176338,PMID:19713527,PMID:21775285 P31749 UniProtKB Mutagenesis 17 17 . . . Note=No effect on membrane localization. Loss of membrane localization%3B when associated with Q-20. E->K;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 P31749 UniProtKB Mutagenesis 20 20 . . . Note=Substantial reduction of phosphorylation at T-308 and S-473%2C reduced AKT activation%2C and reduced binding to PIP3 as well as IGF1-induced membrane recruitment. Loss of membrane localization%3B when associated with K-17. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 P31749 UniProtKB Mutagenesis 20 20 . . . Note=Slight increase of phosphorylation at T-308 and S-473. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21775285;Dbxref=PMID:21775285 P31749 UniProtKB Mutagenesis 25 25 . . . Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A%2CC;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 P31749 UniProtKB Mutagenesis 86 86 . . . Note=Impairs interaction with PtdIns(3%2C4%2C5)P3 and PtdIns(3%2C4)P2. R->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12176338;Dbxref=PMID:12176338 P31749 UniProtKB Mutagenesis 176 176 . . . Note=Significant loss of interaction with TNK2. Loss of membrane localization. Significant reduction in phosphorylation on Ser-473. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20333297;Dbxref=PMID:20333297 P31749 UniProtKB Mutagenesis 179 179 . . . Note=Abolished serine/threonine-protein kinase activity. K->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12172553,ECO:0000269|PubMed:33594058;Dbxref=PMID:12172553,PMID:33594058 P31749 UniProtKB Mutagenesis 305 305 . . . Note=Reduces O-GlcNAc levels%3B Reduces O-GlcNAc levels even more%3B when associated with A-312. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Mutagenesis 305 305 . . . Note=Abolishes phosphorylation at Thr-308. T->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Mutagenesis 308 308 . . . Note=5-fold activation and 18-fold activation%3B when associated with D-473. T->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12244301,ECO:0000269|PubMed:8978681;Dbxref=PMID:12244301,PMID:8978681 P31749 UniProtKB Mutagenesis 312 312 . . . Note=Reduces O-GlcNAc levels%3B Reduces O-GlcNAc levels even more%3B when associated with A-305. T->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Mutagenesis 312 312 . . . Note=Abolishes phosphorylation at Thr-308. T->Y;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:22629392;Dbxref=PMID:22629392 P31749 UniProtKB Mutagenesis 473 473 . . . Note=7-fold activation and 25-fold activation%3B when associated with D-308. S->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:12244301,ECO:0000269|PubMed:8978681;Dbxref=PMID:12244301,PMID:8978681 P31749 UniProtKB Mutagenesis 474 474 . . . Note=55%25 inhibition of activation. Y->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12149249;Dbxref=PMID:12149249 P31749 UniProtKB Sequence conflict 173 174 . . . Note=GR->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 202 202 . . . Note=L->Q;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 212 212 . . . Note=A->R;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 246 246 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 409 409 . . . Note=A->T;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 476 476 . . . Note=A->P;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 478 478 . . . Note=G->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Sequence conflict 478 478 . . . Note=G->S;Ontology_term=ECO:0000305;evidence=ECO:0000305 P31749 UniProtKB Helix 2 4 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 6 15 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 17 19 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 22 30 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 33 40 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Helix 42 44 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7APJ P31749 UniProtKB Helix 45 48 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 52 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 61 65 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 67 69 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 72 79 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Beta strand 82 89 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Helix 93 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1UNQ P31749 UniProtKB Helix 147 149 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 150 158 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 160 169 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Turn 170 172 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 175 182 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 183 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 192 204 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 213 218 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 220 227 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 235 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 247 268 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 277 279 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 284 286 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4EJN P31749 UniProtKB Beta strand 288 290 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 309 311 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MVH P31749 UniProtKB Helix 313 315 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 318 322 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 330 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 354 363 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 374 383 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 388 390 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Turn 396 398 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 399 403 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 406 408 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Helix 413 417 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 430 433 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:3MVH P31749 UniProtKB Turn 436 438 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7NH5 P31749 UniProtKB Helix 440 443 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 464 466 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1 P31749 UniProtKB Beta strand 473 475 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:4GV1