##gff-version 3 P62873 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0000269|Ref.9,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:25944712;Dbxref=PMID:19413330,PMID:22223895,PMID:25944712 P62873 UniProtKB Chain 2 340 . . . ID=PRO_0000127687;Note=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 P62873 UniProtKB Repeat 53 83 . . . Note=WD 1 P62873 UniProtKB Repeat 95 125 . . . Note=WD 2 P62873 UniProtKB Repeat 141 170 . . . Note=WD 3 P62873 UniProtKB Repeat 182 212 . . . Note=WD 4 P62873 UniProtKB Repeat 224 254 . . . Note=WD 5 P62873 UniProtKB Repeat 268 298 . . . Note=WD 6 P62873 UniProtKB Repeat 310 340 . . . Note=WD 7 P62873 UniProtKB Modified residue 2 2 . . . Note=N-acetylserine;Ontology_term=ECO:0000269,ECO:0000269,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0000269|Ref.8,ECO:0000269|Ref.9,ECO:0007744|PubMed:19413330,ECO:0007744|PubMed:22223895,ECO:0007744|PubMed:25944712;Dbxref=PMID:19413330,PMID:22223895,PMID:25944712 P62873 UniProtKB Modified residue 2 2 . . . Note=Phosphoserine;Ontology_term=ECO:0007744;evidence=ECO:0007744|PubMed:23186163;Dbxref=PMID:23186163 P62873 UniProtKB Modified residue 266 266 . . . Note=Phosphohistidine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P62871 P62873 UniProtKB Alternative sequence 329 340 . . . ID=VSP_055232;Note=In isoform 2. TGSWDSFLKIWN->SVLG;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:15489334;Dbxref=PMID:15489334 P62873 UniProtKB Natural variant 30 30 . . . ID=VAR_078279;Note=In MRD42%3B uncertain significance%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit%3B no effect on trimer formation with alpha and gamma subunits%3B no effect on receptor-driven G protein activation. L->F;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=dbSNP:rs764997309,PMID:28087732 P62873 UniProtKB Natural variant 52 52 . . . ID=VAR_078280;Note=In MRD42%3B decreases receptor-driven G protein activation%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit%3B decreases trimer formation with alpha and gamma subunit. R->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 64 64 . . . ID=VAR_078281;Note=In MRD42%3B decreases receptor-driven G protein activation%3B decreases protein abundance%3B decreases complex formation with gamma subunit%3B decreases trimer formation with alpha and gamma subunit. G->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 76 76 . . . ID=VAR_076644;Note=In MRD42. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs869312822,PMID:27108799 P62873 UniProtKB Natural variant 76 76 . . . ID=VAR_076643;Note=In MRD42. D->G;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs869312821,PMID:27108799 P62873 UniProtKB Natural variant 77 77 . . . ID=VAR_076645;Note=In MRD42. G->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs758432471,PMID:27108799 P62873 UniProtKB Natural variant 78 78 . . . ID=VAR_076646;Note=In MRD42. K->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs869312823,PMID:27108799 P62873 UniProtKB Natural variant 80 80 . . . ID=VAR_076647;Note=In MRD42%3B also found in patients with acute lymphoblastic T-cell leukemia%3B reduces interaction with GNAI2%2C GNAI3%2C GNA13 and GNA11%3B induces activation of PI3K-AKT-mTOR and MAPK pathways. I->N;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25485910,ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs752746786,PMID:25485910,PMID:27108799 P62873 UniProtKB Natural variant 80 80 . . . ID=VAR_076648;Note=In MRD42%3B also found in patient with hematologic malignancies%3B reduces interaction with GNAI2%2C GNAI3%2C GNA13 and GNA11%3B induces activation of PI3K-AKT-mTOR and MAPK pathways. I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:25485910,ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs752746786,PMID:25485910,PMID:27108799 P62873 UniProtKB Natural variant 91 91 . . . ID=VAR_078282;Note=In MRD42%3B uncertain significance%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit%3B no effect on trimer formation with apha and gamma subunits%3B no effect on receptor-driven G protein activation. H->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 92 92 . . . ID=VAR_078283;Note=In MRD42%3B decreases receptor-driven G protein activation%3B increases trimer formation with alpha and gamma subunits%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 94 94 . . . ID=VAR_078284;Note=In MRD42%3B decreases receptor-driven G protein activation%3B decreases trimer formation with alpha and gamma subunit%3B no effect on protein abundance%3Bno effect on complex formation with gamma subunit. P->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 95 95 . . . ID=VAR_076649;Note=In MRD42. L->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs869312824,PMID:27108799 P62873 UniProtKB Natural variant 96 96 . . . ID=VAR_078285;Note=In MRD42%3B decreases receptor-driven G protein activation%3B decreases trimer formation with alpha and gamma subunit%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit. R->L;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 101 101 . . . ID=VAR_076650;Note=In MRD42. M->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs869312825,PMID:27108799 P62873 UniProtKB Natural variant 106 106 . . . ID=VAR_078286;Note=In MRD42%3B decreases receptor-driven G protein activation%3B decreases complex formation with gamma subunit%3B decreases trimer formation with alpha and gamma subunit%3B no effect on protein abundance. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Natural variant 118 118 . . . ID=VAR_078287;Note=In MRD42%3B decreases receptor-driven G protein activation%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit%3B no effect on trimer formation with alpha and gamma subunits. D->G;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:27668284,ECO:0000269|PubMed:28087732;Dbxref=dbSNP:rs1553194162,PMID:27668284,PMID:28087732 P62873 UniProtKB Natural variant 326 326 . . . ID=VAR_076651;Note=In MRD42. A->T;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27108799;Dbxref=dbSNP:rs869312826,PMID:27108799 P62873 UniProtKB Natural variant 337 337 . . . ID=VAR_078288;Note=In MRD42%3B uncertain significance%3B no effect on protein abundance%3B no effect on complex formation with gamma subunit%3B no effect on trimer formation with alpha and gamma subunits%3B no effect on receptor-driven G protein activation. K->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:28087732;Dbxref=PMID:28087732 P62873 UniProtKB Helix 3 25 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Helix 30 33 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 34 36 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6CRK P62873 UniProtKB Beta strand 46 52 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 54 56 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8HQN P62873 UniProtKB Beta strand 58 63 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 67 74 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 75 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 78 83 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 84 86 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 89 94 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 96 98 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 100 105 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 109 116 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 117 119 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7Y66 P62873 UniProtKB Beta strand 121 126 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 129 131 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0J P62873 UniProtKB Beta strand 134 139 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 146 161 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 162 164 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7S8M P62873 UniProtKB Beta strand 166 170 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 171 174 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 175 180 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 187 192 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 196 203 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 206 212 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 213 215 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 218 223 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 229 234 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 238 245 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 246 248 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8IOD P62873 UniProtKB Beta strand 250 254 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 255 258 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 259 264 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 273 278 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 280 289 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 290 292 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8JR9 P62873 UniProtKB Beta strand 294 298 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Turn 299 301 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 304 308 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 315 320 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 322 325 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:6WZG P62873 UniProtKB Beta strand 327 331 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K P62873 UniProtKB Beta strand 334 340 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:8F0K