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P12694

- ODBA_HUMAN

UniProt

P12694 - ODBA_HUMAN

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Protein
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
Gene
BCKDHA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO2. It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).

Catalytic activityi

3-methyl-2-oxobutanoate + [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] lipoyllysine = [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine + CO2.

Cofactori

Thiamine pyrophosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi206 – 2061Potassium
Metal bindingi211 – 2111Potassium
Metal bindingi212 – 2121Potassium

GO - Molecular functioni

  1. 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity Source: ProtInc
  2. alpha-ketoacid dehydrogenase activity Source: HGNC
  3. carboxy-lyase activity Source: HGNC
  4. metal ion binding Source: UniProtKB-KW
  5. protein binding Source: IntAct

GO - Biological processi

  1. branched-chain amino acid catabolic process Source: HGNC
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Metal-binding, Potassium, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12005.
ReactomeiREACT_197. Branched-chain amino acid catabolism.
SABIO-RKP12694.

Names & Taxonomyi

Protein namesi
Recommended name:
2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial (EC:1.2.4.4)
Alternative name(s):
Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain
Short name:
BCKDE1A
Short name:
BCKDH E1-alpha
Gene namesi
Name:BCKDHA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:986. BCKDHA.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial alpha-ketoglutarate dehydrogenase complex Source: HGNC
  2. mitochondrial matrix Source: Reactome
  3. mitochondrion Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Maple syrup urine disease 1A (MSUD1A) [MIM:248600]: A metabolic disorder due to an enzyme defect in the catabolic pathway of the branched-chain amino acids leucine, isoleucine, and valine. Accumulation of these 3 amino acids and their corresponding keto acids leads to encephalopathy and progressive neurodegeneration. Clinical features include mental and physical retardation, feeding problems, and a maple syrup odor to the urine. The keto acids of the branched-chain amino acids are present in the urine. If untreated, maple syrup urine disease can lead to seizures, coma, and death. The disease is often classified by its pattern of signs and symptoms. The most common and severe form of the disease is the classic type, which becomes apparent soon after birth. Variant forms of the disorder become apparent later in infancy or childhood and are typically milder, but they still involve developmental delay and other medical problems if not treated.
Note: The disease is caused by mutations affecting the gene represented in this entry.9 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti159 – 1591R → W in MSUD1A. 1 Publication
VAR_004968
Natural varianti190 – 1901Q → K in MSUD1A. 1 Publication
VAR_004969
Natural varianti211 – 2111T → M in MSUD1A. 1 Publication
VAR_069748
Natural varianti220 – 2201A → V in MSUD1A. 1 Publication
VAR_069749
Natural varianti253 – 2531A → T in MSUD1A. 1 Publication
VAR_004970
Natural varianti290 – 2901G → R in MSUD1A. 1 Publication
VAR_015101
Natural varianti326 – 3261I → T in MSUD1A. 1 Publication
VAR_004971
Natural varianti346 – 3461R → C in MSUD1A. 1 Publication
VAR_069750
Natural varianti403 – 4031P → PKP in MSUD1A.
VAR_069751
Natural varianti409 – 4091F → C in MSUD1A. 1 Publication
VAR_015102
Natural varianti413 – 4131Y → C in MSUD1A. 1 Publication
VAR_004972
Natural varianti427 – 4282LA → P in MSUD1A.
VAR_069752
Natural varianti438 – 4381Y → N in MSUD1A; impedes assembly of the E1 component. 5 Publications
VAR_004973

Keywords - Diseasei

Disease mutation, Maple syrup urine disease

Organism-specific databases

MIMi248600. phenotype.
Orphaneti268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBiPA25297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545Mitochondrion1 Publication
Add
BLAST
Chaini46 – 4454002-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
PRO_0000020465Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei337 – 3371Phosphoserine2 Publications
Modified residuei347 – 3471Phosphoserine4 Publications
Modified residuei356 – 3561N6-acetyllysine; alternate By similarity
Modified residuei356 – 3561N6-succinyllysine; alternate By similarity
Modified residuei380 – 3801N6-succinyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP12694.
PaxDbiP12694.
PRIDEiP12694.

PTM databases

PhosphoSiteiP12694.

Expressioni

Gene expression databases

BgeeiP12694.
CleanExiHS_BCKDHA.
GenevestigatoriP12694.

Organism-specific databases

HPAiHPA036640.

Interactioni

Subunit structurei

Heterotetramer of alpha and beta chains.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCKDHBP2195314EBI-1029053,EBI-1029067

Protein-protein interaction databases

BioGridi107065. 3 interactions.
DIPiDIP-6146N.
IntActiP12694. 3 interactions.
MINTiMINT-271818.
STRINGi9606.ENSP00000269980.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi61 – 644
Beta strandi88 – 903
Helixi91 – 933
Helixi99 – 12426
Beta strandi127 – 1293
Turni135 – 1373
Helixi138 – 1469
Beta strandi152 – 1554
Helixi161 – 1666
Helixi171 – 1799
Turni185 – 1884
Turni198 – 2014
Turni209 – 2113
Helixi212 – 22615
Beta strandi232 – 2376
Helixi240 – 2423
Helixi244 – 25512
Beta strandi260 – 2667
Beta strandi268 – 2703
Helixi275 – 2773
Beta strandi280 – 2823
Helixi285 – 2873
Helixi289 – 2913
Beta strandi294 – 2996
Helixi303 – 32018
Beta strandi324 – 3296
Helixi342 – 3443
Helixi351 – 3577
Helixi360 – 3689
Turni369 – 3724
Helixi376 – 39924
Helixi405 – 4084
Turni409 – 4113
Beta strandi412 – 4154
Helixi418 – 43417
Helixi435 – 4373
Helixi440 – 4423

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DTWX-ray2.70A46-445[»]
1OLSX-ray1.85A46-445[»]
1OLUX-ray1.90A46-445[»]
1OLXX-ray2.25A46-445[»]
1U5BX-ray1.83A46-445[»]
1V11X-ray1.95A46-445[»]
1V16X-ray1.90A46-445[»]
1V1MX-ray2.00A46-445[»]
1V1RX-ray1.80A46-445[»]
1WCIX-ray1.84A46-445[»]
1X7WX-ray1.73A46-445[»]
1X7XX-ray2.10A46-445[»]
1X7YX-ray1.57A46-445[»]
1X7ZX-ray1.72A46-445[»]
1X80X-ray2.00A46-445[»]
2BEUX-ray1.89A46-445[»]
2BEVX-ray1.80A46-445[»]
2BEWX-ray1.79A46-445[»]
2BFBX-ray1.77A46-445[»]
2BFCX-ray1.64A46-445[»]
2BFDX-ray1.39A46-445[»]
2BFEX-ray1.69A46-445[»]
2BFFX-ray1.46A46-445[»]
2J9FX-ray1.88A/C46-445[»]
ProteinModelPortaliP12694.
SMRiP12694. Positions 20-445.

Miscellaneous databases

EvolutionaryTraceiP12694.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni157 – 1593Thiamine pyrophosphate binding

Sequence similaritiesi

Belongs to the BCKDHA family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOVERGENiHBG002459.
InParanoidiP12694.
KOiK00166.
OrthoDBiEOG7WT41H.
PhylomeDBiP12694.
TreeFamiTF300863.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P12694-1 [UniParc]FASTAAdd to Basket

« Hide

MAVAIAAARV WRLNRGLSQA ALLLLRQPGA RGLARSHPPR QQQQFSSLDD    50
KPQFPGASAE FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE 100
KVLKLYKSMT LLNTMDRILY ESQRQGRISF YMTNYGEEGT HVGSAAALDN 150
TDLVFGQYRE AGVLMYRDYP LELFMAQCYG NISDLGKGRQ MPVHYGCKER 200
HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA ASEGDAHAGF 250
NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG 300
NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE 350
VNYWDKQDHP ISRLRHYLLS QGWWDEEQEK AWRKQSRRKV MEAFEQAERK 400
PKPNPNLLFS DVYQEMPAQL RKQQESLARH LQTYGEHYPL DHFDK 445
Length:445
Mass (Da):50,471
Last modified:June 1, 1994 - v2
Checksum:i2B4DD658924DB0C3
GO

Sequence cautioni

The sequence AAB59549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti39 – 391P → H.
Corresponds to variant rs34589432 [ dbSNP | Ensembl ].
VAR_034360
Natural varianti151 – 1511T → M.
Corresponds to variant rs34442879 [ dbSNP | Ensembl ].
VAR_034361
Natural varianti159 – 1591R → W in MSUD1A. 1 Publication
VAR_004968
Natural varianti190 – 1901Q → K in MSUD1A. 1 Publication
VAR_004969
Natural varianti211 – 2111T → M in MSUD1A. 1 Publication
VAR_069748
Natural varianti220 – 2201A → V in MSUD1A. 1 Publication
VAR_069749
Natural varianti253 – 2531A → T in MSUD1A. 1 Publication
VAR_004970
Natural varianti290 – 2901G → R in MSUD1A. 1 Publication
VAR_015101
Natural varianti326 – 3261I → T in MSUD1A. 1 Publication
VAR_004971
Natural varianti346 – 3461R → C in MSUD1A. 1 Publication
VAR_069750
Natural varianti403 – 4031P → PKP in MSUD1A.
VAR_069751
Natural varianti409 – 4091F → C in MSUD1A. 1 Publication
VAR_015102
Natural varianti413 – 4131Y → C in MSUD1A. 1 Publication
VAR_004972
Natural varianti427 – 4282LA → P in MSUD1A.
VAR_069752
Natural varianti438 – 4381Y → N in MSUD1A; impedes assembly of the E1 component. 5 Publications
VAR_004973

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31V → G in AAB20222. 1 Publication
Sequence conflicti3 – 31V → G in AAB19268. 1 Publication
Sequence conflicti36 – 361S → A in AAB59549. 1 Publication
Sequence conflicti248 – 2481A → D in AAA35590. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z14093 mRNA. Translation: CAA78475.1.
BC007878 mRNA. Translation: AAH07878.1.
BC008933 mRNA. Translation: AAH08933.1.
BC023983 mRNA. Translation: AAH23983.1.
J04474 mRNA. Translation: AAB59549.1. Different initiation.
AH003771 Genomic DNA. Translation: AAB20222.2.
AH003707 Genomic DNA. Translation: AAB19268.2.
M22221 mRNA. Translation: AAA35590.1.
CCDSiCCDS12581.1.
PIRiS27156. DEHUXA.
RefSeqiNP_000700.1. NM_000709.3.
UniGeneiHs.433307.

Genome annotation databases

EnsembliENST00000269980; ENSP00000269980; ENSG00000248098.
GeneIDi593.
KEGGihsa:593.
UCSCiuc002oqp.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z14093 mRNA. Translation: CAA78475.1 .
BC007878 mRNA. Translation: AAH07878.1 .
BC008933 mRNA. Translation: AAH08933.1 .
BC023983 mRNA. Translation: AAH23983.1 .
J04474 mRNA. Translation: AAB59549.1 . Different initiation.
AH003771 Genomic DNA. Translation: AAB20222.2 .
AH003707 Genomic DNA. Translation: AAB19268.2 .
M22221 mRNA. Translation: AAA35590.1 .
CCDSi CCDS12581.1.
PIRi S27156. DEHUXA.
RefSeqi NP_000700.1. NM_000709.3.
UniGenei Hs.433307.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DTW X-ray 2.70 A 46-445 [» ]
1OLS X-ray 1.85 A 46-445 [» ]
1OLU X-ray 1.90 A 46-445 [» ]
1OLX X-ray 2.25 A 46-445 [» ]
1U5B X-ray 1.83 A 46-445 [» ]
1V11 X-ray 1.95 A 46-445 [» ]
1V16 X-ray 1.90 A 46-445 [» ]
1V1M X-ray 2.00 A 46-445 [» ]
1V1R X-ray 1.80 A 46-445 [» ]
1WCI X-ray 1.84 A 46-445 [» ]
1X7W X-ray 1.73 A 46-445 [» ]
1X7X X-ray 2.10 A 46-445 [» ]
1X7Y X-ray 1.57 A 46-445 [» ]
1X7Z X-ray 1.72 A 46-445 [» ]
1X80 X-ray 2.00 A 46-445 [» ]
2BEU X-ray 1.89 A 46-445 [» ]
2BEV X-ray 1.80 A 46-445 [» ]
2BEW X-ray 1.79 A 46-445 [» ]
2BFB X-ray 1.77 A 46-445 [» ]
2BFC X-ray 1.64 A 46-445 [» ]
2BFD X-ray 1.39 A 46-445 [» ]
2BFE X-ray 1.69 A 46-445 [» ]
2BFF X-ray 1.46 A 46-445 [» ]
2J9F X-ray 1.88 A/C 46-445 [» ]
ProteinModelPortali P12694.
SMRi P12694. Positions 20-445.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107065. 3 interactions.
DIPi DIP-6146N.
IntActi P12694. 3 interactions.
MINTi MINT-271818.
STRINGi 9606.ENSP00000269980.

PTM databases

PhosphoSitei P12694.

Proteomic databases

MaxQBi P12694.
PaxDbi P12694.
PRIDEi P12694.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269980 ; ENSP00000269980 ; ENSG00000248098 .
GeneIDi 593.
KEGGi hsa:593.
UCSCi uc002oqp.2. human.

Organism-specific databases

CTDi 593.
GeneCardsi GC19P041857.
GeneReviewsi BCKDHA.
HGNCi HGNC:986. BCKDHA.
HPAi HPA036640.
MIMi 248600. phenotype.
608348. gene.
neXtProti NX_P12694.
Orphaneti 268145. Classic maple syrup urine disease.
268162. Intermediate maple syrup urine disease.
268173. Intermittent maple syrup urine disease.
268184. Thiamine-responsive maple syrup urine disease.
PharmGKBi PA25297.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1071.
HOVERGENi HBG002459.
InParanoidi P12694.
KOi K00166.
OrthoDBi EOG7WT41H.
PhylomeDBi P12694.
TreeFami TF300863.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-12005.
Reactomei REACT_197. Branched-chain amino acid catabolism.
SABIO-RK P12694.

Miscellaneous databases

EvolutionaryTracei P12694.
GeneWikii BCKDHA.
GenomeRNAii 593.
NextBioi 2409.
PROi P12694.
SOURCEi Search...

Gene expression databases

Bgeei P12694.
CleanExi HS_BCKDHA.
Genevestigatori P12694.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the 5' end including the initiation codon of cDNA for the E1 alpha subunit of the human branched chain alpha-ketoacid dehydrogenase complex."
    McKean M.C., Winkeler K.A., Danner D.J.
    Biochim. Biophys. Acta 1171:109-112(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow and Lung.
  3. "Molecular phenotypes in cultured maple syrup urine disease cells. Complete E1 alpha cDNA sequence and mRNA and subunit contents of the human branched chain alpha-keto acid dehydrogenase complex."
    Fisher C.W., Chuang J.L., Griffin T.A., Lau K.S., Cox R.P., Chuang D.T.
    J. Biol. Chem. 264:3448-3453(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-445.
  4. "Structure of the gene encoding the entire mature E1 alpha subunit of human branched-chain alpha-keto acid dehydrogenase complex."
    Dariush N., Fisher C.W., Cox R.P., Chuang D.T.
    FEBS Lett. 284:34-38(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-445, VARIANT MSUD1A ASN-438.
  5. "Nucleotide and deduced amino acid sequence of the E1 alpha subunit of human liver branched-chain alpha-ketoacid dehydrogenase."
    Zhang B., Crabb D.W., Harris R.A.
    Gene 69:159-164(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-445.
    Tissue: Liver.
  6. "Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence."
    Wynn R.M., Kochi H., Cox R.P., Chuang D.T.
    Biochim. Biophys. Acta 1201:125-128(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 46-57.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND SER-347, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Crystal structure of human branched-chain alpha-ketoacid dehydrogenase and the molecular basis of multienzyme complex deficiency in maple syrup urine disease."
    Aevarsson A., Chuang J.L., Wynn R.M., Turley S., Chuang D.T., Hol W.G.J.
    Structure 8:277-291(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-445 IN COMPLEX WITH THIAMINE PYROPHOSPHATE AND POTASSIUM IONS, SUBUNIT STRUCTURE.
  16. "Molecular basis of maple syrup urine disease: novel mutations at the E1 alpha locus that impair E1(alpha 2 beta 2) assembly or decrease steady-state E1 alpha mRNA levels of branched-chain alpha-keto acid dehydrogenase complex."
    Chuang J.L., Fisher C.R., Cox R.P., Chuang D.T.
    Am. J. Hum. Genet. 55:297-304(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD1A CYS-413.
  17. "Evidence for both a regulatory mutation and a structural mutation in a family with maple syrup urine disease."
    Zhang B., Edenberg H.J., Crabb D.W., Harris R.A.
    J. Clin. Invest. 83:1425-1429(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD1A ASN-438.
  18. "A T-to-A substitution in the E1 alpha subunit gene of the branched-chain alpha-ketoacid dehydrogenase complex in two cell lines derived from Menonite maple syrup urine disease patients."
    Matsuda I., Nobukuni Y., Mitsubuchi H., Indo Y., Endo F., Asaka J., Harada A.
    Biochem. Biophys. Res. Commun. 172:646-651(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD1A ASN-438.
  19. "Occurrence of a Tyr393-->Asn (Y393N) mutation in the E1 alpha gene of the branched-chain alpha-keto acid dehydrogenase complex in maple syrup urine disease patients from a Mennonite population."
    Fisher C.R., Fisher C.W., Chuang D.T., Cox R.P.
    Am. J. Hum. Genet. 49:429-434(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD1A ASN-438.
  20. "Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1 alpha impedes assembly of the E1 component of branched-chain alpha-keto acid dehydrogenase complex."
    Fisher C.R., Chuang J.L., Cox R.P., Fisher C.W., Star R.A., Chuang D.T.
    J. Clin. Invest. 88:1034-1037(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MSUD1A ASN-438.
  21. "Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex."
    Nobukuni Y., Mitsubuchi H., Hayashida Y., Ohta K., Indo Y., Ichiba Y., Endo F., Matsuda I.
    Biochim. Biophys. Acta 1225:64-70(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MSUD1A TRP-159; LYS-190; THR-253 AND THR-326.
  22. "Molecular and biochemical basis of intermediate maple syrup urine disease: occurrence of homozygous G245R and F364C mutations at the E1-alpha locus of Hispanic-Mexican patients."
    Chuang J.L., Davie J.R., Chinsky J.M., Wynn R.M., Cox R.P., Chuang D.T.
    J. Clin. Invest. 95:954-963(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MSUD1A ARG-290 AND CYS-409.
  23. "Three Korean patients with maple syrup urine disease: four novel mutations in the BCKDHA gene."
    Park H.D., Lee D.H., Hong Y.H., Kang D.H., Lee Y.K., Song J., Lee S.Y., Kim J.W., Ki C.S., Lee Y.W.
    Ann. Clin. Lab. Sci. 41:167-173(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MSUD1A MET-211; VAL-220; CYS-346; LYS-PRO-403 INS AND 427-LEU-ALA-428 DELINS PRO.

Entry informationi

Entry nameiODBA_HUMAN
AccessioniPrimary (citable) accession number: P12694
Secondary accession number(s): Q16034, Q16472
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Bound potassium ions stabilize the protein structure.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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