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P12694

- ODBA_HUMAN

UniProt

P12694 - ODBA_HUMAN

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
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    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

    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

    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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 PublicationAdd
    BLAST
    Chaini46 – 4454002-oxoisovalerate dehydrogenase subunit alpha, mitochondrialPRO_0000020465Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei337 – 3371Phosphoserine2 Publications
    Modified residuei347 – 3471Phosphoserine4 Publications
    Modified residuei356 – 3561N6-acetyllysine; alternateBy similarity
    Modified residuei356 – 3561N6-succinyllysine; alternateBy similarity
    Modified residuei380 – 3801N6-succinyllysineBy 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. 4 interactions.
    DIPiDIP-6146N.
    IntActiP12694. 3 interactions.
    MINTiMINT-271818.
    STRINGi9606.ENSP00000269980.

    Structurei

    Secondary structure

    1
    445
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12694.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Belongs to the BCKDHA family.Curated

    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.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12694-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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
    Isoform 2 (identifier: P12694-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-40: Missing.
         331-331: Y → YSSSPILPPDPHSREPTLTWGPLPLC

    Note: No experimental confirmation available.

    Show »
    Length:448
    Mass (Da):50,790
    Checksum:i25C9E70619832776
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31V → G in AAB20222. (PubMed:2060625)Curated
    Sequence conflicti3 – 31V → G in AAB19268. (PubMed:2060625)Curated
    Sequence conflicti36 – 361S → A in AAB59549. (PubMed:2914958)Curated
    Sequence conflicti248 – 2481A → D in AAA35590. (PubMed:3224821)Curated

    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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei19 – 4022Missing in isoform 2. 1 PublicationVSP_056156Add
    BLAST
    Alternative sequencei331 – 3311Y → YSSSPILPPDPHSREPTLTW GPLPLC in isoform 2. 1 PublicationVSP_056157

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14093 mRNA. Translation: CAA78475.1.
    AK298188 mRNA. Translation: BAG60459.1.
    AC011462 Genomic DNA. No translation available.
    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.
    ENST00000457836; ENSP00000416000; ENSG00000248098.
    GeneIDi593.
    KEGGihsa:593.
    UCSCiuc002oqp.2. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z14093 mRNA. Translation: CAA78475.1 .
    AK298188 mRNA. Translation: BAG60459.1 .
    AC011462 Genomic DNA. No translation available.
    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. 4 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 .
    ENST00000457836 ; ENSP00000416000 ; 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

    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] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Bone marrow and Lung.
    5. "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 (ISOFORM 1).
    6. "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.
    7. "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 (ISOFORM 1).
      Tissue: Liver.
    8. "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.
    9. "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.
    10. "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.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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.
    14. "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.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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].
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. "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): B4DP47
    , E7EW46, Q16034, Q16472
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 178 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