##gff-version 3 P12694 UniProtKB Transit peptide 1 45 . . . Note=Mitochondrion;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:7918575;Dbxref=PMID:7918575 P12694 UniProtKB Chain 46 445 . . . ID=PRO_0000020465;Note=2-oxoisovalerate dehydrogenase subunit alpha%2C mitochondrial P12694 UniProtKB Region 33 52 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P12694 UniProtKB Compositional bias 37 51 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite P12694 UniProtKB Binding site 158 158 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 159 159 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 206 206 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 207 207 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 208 208 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 211 211 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 212 212 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 238 238 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 239 239 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 240 240 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 265 265 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 267 267 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 269 269 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Binding site 336 336 . . . Ontology_term=ECO:0000269,ECO:0007744;evidence=ECO:0000269|PubMed:10745006,ECO:0007744|PDB:1DTW;Dbxref=PMID:10745006 P12694 UniProtKB Modified residue 337 337 . . . Note=Phosphoserine%3B by BCKDK;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19411760,ECO:0000269|PubMed:22589535;Dbxref=PMID:19411760,PMID:22589535 P12694 UniProtKB Modified residue 338 338 . . . Note=Phosphothreonine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50136 P12694 UniProtKB Modified residue 339 339 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50136 P12694 UniProtKB Modified residue 347 347 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50136 P12694 UniProtKB Modified residue 356 356 . . . Note=N6-acetyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50136 P12694 UniProtKB Modified residue 356 356 . . . Note=N6-succinyllysine%3B alternate;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50136 P12694 UniProtKB Modified residue 380 380 . . . Note=N6-succinyllysine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P50136 P12694 UniProtKB Alternative sequence 19 40 . . . ID=VSP_056156;Note=In isoform 2. Missing;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P12694 UniProtKB Alternative sequence 331 331 . . . ID=VSP_056157;Note=In isoform 2. Y->YSSSPILPPDPHSREPTLTWGPLPLC;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 P12694 UniProtKB Natural variant 39 39 . . . ID=VAR_034360;Note=P->H;Dbxref=dbSNP:rs11549936 P12694 UniProtKB Natural variant 151 151 . . . ID=VAR_034361;Note=T->M;Dbxref=dbSNP:rs34442879 P12694 UniProtKB Natural variant 159 159 . . . ID=VAR_004968;Note=In MSUD1A%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:8161368;Dbxref=dbSNP:rs769688327,PMID:10745006,PMID:8161368 P12694 UniProtKB Natural variant 190 190 . . . ID=VAR_004969;Note=In MSUD1A%3B decreased 3-methyl-2-oxobutanoate dehydrogenase activity. Q->K;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:8161368;Dbxref=PMID:10745006,PMID:8161368 P12694 UniProtKB Natural variant 211 211 . . . ID=VAR_069748;Note=In MSUD1A%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. T->M;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:21844576;Dbxref=dbSNP:rs398123503,PMID:10745006,PMID:21844576 P12694 UniProtKB Natural variant 220 220 . . . ID=VAR_069749;Note=In MSUD1A. A->V;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844576;Dbxref=dbSNP:rs375785084,PMID:21844576 P12694 UniProtKB Natural variant 249 249 . . . ID=VAR_088268;Note=In MSUD1A%3B no effect on solubility%3B no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. G->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs137852874,PMID:10745006,PMID:9582350 P12694 UniProtKB Natural variant 253 253 . . . ID=VAR_004970;Note=In MSUD1A%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. A->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:8161368;Dbxref=dbSNP:rs199599175,PMID:10745006,PMID:8161368 P12694 UniProtKB Natural variant 254 254 . . . ID=VAR_088269;Note=In MSUD1A%3B uncertain significance%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10745006;Dbxref=PMID:10745006 P12694 UniProtKB Natural variant 265 265 . . . ID=VAR_088270;Note=In MSUD1A%3B uncertain significance%3B no effect on solubility%3B no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. R->W;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs137852873,PMID:10745006,PMID:9582350 P12694 UniProtKB Natural variant 267 267 . . . ID=VAR_088271;Note=In MSUD1A%3B uncertain significance%3B no effect on solubility%3B no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B decreased affinity for the cofactor thiamine diphosphate%3B decreased 3-methyl-2-oxobutanoate dehydrogenase activity. N->S;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:9582350;Dbxref=PMID:10745006,PMID:9582350 P12694 UniProtKB Natural variant 285 285 . . . ID=VAR_088272;Note=In MSUD1A%3B no effect on solubility%3B no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. A->P;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs398123508,PMID:10745006,PMID:9582350 P12694 UniProtKB Natural variant 290 290 . . . ID=VAR_015101;Note=In MSUD1A%3B no effect on solubility%3B no effect on mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B decreased 3-methyl-2-oxobutanoate dehydrogenase activity. G->R;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:7883996,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs137852871,PMID:10745006,PMID:7883996,PMID:9582350 P12694 UniProtKB Natural variant 297 297 . . . ID=VAR_088273;Note=In MSUD1A%3B uncertain significance%3B decreased affinity for the cofactor thiamine diphosphate%3B decreased 3-methyl-2-oxobutanoate dehydrogenase activity. R->H;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:10745006;Dbxref=dbSNP:rs200137189,PMID:10745006 P12694 UniProtKB Natural variant 310 310 . . . ID=VAR_088274;Note=In MSUD1A%3B decreased solubility%3B changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. T->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs137852875,PMID:10745006,PMID:9582350 P12694 UniProtKB Natural variant 326 326 . . . ID=VAR_004971;Note=In MSUD1A%3B decreased 3-methyl-2-oxobutanoate dehydrogenase activity. I->T;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:8161368;Dbxref=PMID:10745006,PMID:8161368 P12694 UniProtKB Natural variant 346 346 . . . ID=VAR_069750;Note=In MSUD1A. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844576;Dbxref=dbSNP:rs182923857,PMID:21844576 P12694 UniProtKB Natural variant 403 403 . . . ID=VAR_069751;Note=In MSUD1A. P->PKP P12694 UniProtKB Natural variant 409 409 . . . ID=VAR_015102;Note=In MSUD1A%3B decreased solubility%3B loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. F->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:7883996,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs137852872,PMID:10745006,PMID:7883996,PMID:9582350 P12694 UniProtKB Natural variant 413 413 . . . ID=VAR_004972;Note=In MSUD1A%3B uncertain significance%3B decreased solubility%3B changed mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. Y->C;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:8037208,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs398123508,PMID:10745006,PMID:8037208,PMID:9582350 P12694 UniProtKB Natural variant 427 428 . . . ID=VAR_069752;Note=In MSUD1A. LA->P;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21844576;Dbxref=PMID:21844576 P12694 UniProtKB Natural variant 438 438 . . . ID=VAR_004973;Note=In MSUD1A%3B decreased solubility%3B loss of mitochondrial alpha-ketoglutarate dehydrogenase complex assembly%3B loss of 3-methyl-2-oxobutanoate dehydrogenase activity. Y->N;Ontology_term=ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:10745006,ECO:0000269|PubMed:1867199,ECO:0000269|PubMed:1885764,ECO:0000269|PubMed:2060625,ECO:0000269|PubMed:2241958,ECO:0000269|PubMed:2703538,ECO:0000269|PubMed:9582350;Dbxref=dbSNP:rs137852870,PMID:10745006,PMID:1867199,PMID:1885764,PMID:2060625,PMID:2241958,PMID:2703538,PMID:9582350 P12694 UniProtKB Mutagenesis 337 337 . . . Note=Substantially decreases the stability of the BCKD complex. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19411760;Dbxref=PMID:19411760 P12694 UniProtKB Mutagenesis 347 347 . . . Note=Does not affect the stability of the BCKD complex. S->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19411760;Dbxref=PMID:19411760 P12694 UniProtKB Sequence conflict 3 3 . . . Note=V->G;Ontology_term=ECO:0000305;evidence=ECO:0000305 P12694 UniProtKB Sequence conflict 36 36 . . . Note=S->A;Ontology_term=ECO:0000305;evidence=ECO:0000305 P12694 UniProtKB Sequence conflict 248 248 . . . Note=A->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 P12694 UniProtKB Beta strand 61 64 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2J9F P12694 UniProtKB Beta strand 88 90 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:1DTW P12694 UniProtKB Helix 91 93 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 99 124 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 127 129 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Turn 135 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFB P12694 UniProtKB Helix 138 146 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 152 155 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 161 166 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 171 179 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Turn 185 188 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Turn 198 201 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Turn 209 211 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 212 226 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 232 237 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 240 242 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 244 255 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 260 266 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 268 270 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 275 277 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 280 282 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 285 287 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 289 291 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 294 299 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 303 320 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Beta strand 324 329 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 342 344 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFF P12694 UniProtKB Helix 351 357 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFF P12694 UniProtKB Helix 360 368 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Turn 369 372 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 376 399 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 405 408 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Turn 409 411 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BEW P12694 UniProtKB Beta strand 412 415 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 418 434 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 435 437 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD P12694 UniProtKB Helix 440 442 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2BFD