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P11177

- ODPB_HUMAN

UniProt

P11177 - ODPB_HUMAN

Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

PDHB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 3 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle.2 Publications

    Catalytic activityi

    Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.1 Publication

    Cofactori

    Thiamine pyrophosphate.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891Thiamine pyrophosphate1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. pyruvate dehydrogenase (acetyl-transferring) activity Source: ProtInc
    3. pyruvate dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    2. cellular metabolic process Source: Reactome
    3. glucose metabolic process Source: UniProtKB-KW
    4. pyruvate metabolic process Source: Reactome
    5. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. tricarboxylic acid cycle Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09727-MONOMER.
    ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_2071. Pyruvate metabolism.
    SABIO-RKP11177.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1)
    Short name:
    PDHE1-B
    Gene namesi
    Name:PDHB
    Synonyms:PHE1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:8808. PDHB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome
    3. nucleus Source: UniProt
    4. pyruvate dehydrogenase complex Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:614111]: An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321Y → C in PDHBD. 1 Publication
    Corresponds to variant rs28935769 [ dbSNP | Ensembl ].
    VAR_030954
    Natural varianti344 – 3441P → S in PDHBD. 1 Publication
    Corresponds to variant rs28933391 [ dbSNP | Ensembl ].
    VAR_021058

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614111. phenotype.
    Orphaneti255138. Pyruvate dehydrogenase E1-beta deficiency.
    PharmGKBiPA33152.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030Mitochondrion2 PublicationsAdd
    BLAST
    Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020457Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671PhosphotyrosineBy similarity
    Modified residuei354 – 3541N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11177.
    PaxDbiP11177.
    PRIDEiP11177.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00549885.
    SWISS-2DPAGEP11177.
    UCD-2DPAGEP11177.

    PTM databases

    PhosphoSiteiP11177.

    Expressioni

    Gene expression databases

    ArrayExpressiP11177.
    BgeeiP11177.
    CleanExiHS_PDHB.
    GenevestigatoriP11177.

    Organism-specific databases

    HPAiHPA036744.

    Interactioni

    Subunit structurei

    Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DLATP105157EBI-1035872,EBI-2959723

    Protein-protein interaction databases

    BioGridi111188. 35 interactions.
    DIPiDIP-37651N.
    IntActiP11177. 15 interactions.
    MINTiMINT-3007546.
    STRINGi9606.ENSP00000307241.

    Structurei

    Secondary structure

    1
    359
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 343
    Helixi35 – 4915
    Beta strandi53 – 575
    Turni58 – 614
    Turni69 – 724
    Helixi73 – 775
    Turni79 – 813
    Beta strandi82 – 843
    Helixi89 – 10113
    Beta strandi105 – 1095
    Helixi113 – 1197
    Helixi120 – 1245
    Turni125 – 1295
    Helixi130 – 1334
    Turni134 – 1363
    Beta strandi143 – 1475
    Helixi156 – 1583
    Helixi163 – 1675
    Beta strandi173 – 1753
    Helixi180 – 19213
    Beta strandi193 – 1953
    Beta strandi197 – 2015
    Turni203 – 2075
    Beta strandi209 – 2113
    Helixi214 – 2174
    Beta strandi229 – 2324
    Beta strandi235 – 2417
    Helixi245 – 25713
    Turni258 – 2603
    Beta strandi263 – 2675
    Beta strandi270 – 2723
    Helixi276 – 28611
    Beta strandi289 – 2924
    Helixi301 – 31111
    Helixi315 – 3173
    Beta strandi323 – 3253
    Beta strandi329 – 3313
    Helixi336 – 3405
    Helixi346 – 35712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NI4X-ray1.95B/D31-359[»]
    2OZLX-ray1.90B/D32-359[»]
    3EXEX-ray1.98B/D/F/H31-359[»]
    3EXFX-ray3.00B/D/F/H31-359[»]
    3EXGX-ray3.012/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z31-359[»]
    3EXHX-ray2.44B/D/F/H31-359[»]
    3EXIX-ray2.20B31-359[»]
    ProteinModelPortaliP11177.
    SMRiP11177. Positions 30-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11177.

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0022.
    HOGENOMiHOG000281450.
    HOVERGENiHBG000917.
    InParanoidiP11177.
    KOiK00162.
    OMAiDPKVFVM.
    OrthoDBiEOG7KSX8S.
    PhylomeDBiP11177.
    TreeFamiTF105674.

    Family and domain databases

    Gene3Di3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProiIPR027110. PDHB.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view]
    PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
    PfamiPF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    [Graphical view]
    SMARTiSM00861. Transket_pyr. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.
    SSF52922. SSF52922. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11177-1) [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

    MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD    50
    EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA 100
    MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSGGLQPV PIVFRGPNGA 150
    SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVVL 200
    ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV SHSRPVGHCL 250
    EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 300
    VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII 350
    FAIKKTLNI 359
    Length:359
    Mass (Da):39,233
    Last modified:March 6, 2007 - v3
    Checksum:iAB459B1259FBDBD3
    GO
    Isoform 2 (identifier: P11177-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-33: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:341
    Mass (Da):37,200
    Checksum:iB4F137127819BB38
    GO
    Isoform 3 (identifier: P11177-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         135-152: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:341
    Mass (Da):37,514
    Checksum:i89F0A32D89507E9D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 135RRPLR → AETPS(PubMed:3422424)Curated
    Sequence conflicti43 – 431M → G AA sequence (PubMed:7895732)Curated
    Sequence conflicti160 – 1601Q → G(PubMed:3422424)Curated
    Sequence conflicti213 – 2219PPEAQSKDF → LRKLSQKIL(PubMed:3422424)Curated
    Sequence conflicti213 – 2131P → L in AAA88097. (PubMed:2377599)Curated
    Sequence conflicti213 – 2131P → L in BAA14123. (PubMed:2377599)Curated
    Sequence conflicti310 – 3123MEG → NGS(PubMed:3422424)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti31 – 311L → V.2 Publications
    VAR_004967
    Natural varianti132 – 1321Y → C in PDHBD. 1 Publication
    Corresponds to variant rs28935769 [ dbSNP | Ensembl ].
    VAR_030954
    Natural varianti344 – 3441P → S in PDHBD. 1 Publication
    Corresponds to variant rs28933391 [ dbSNP | Ensembl ].
    VAR_021058

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei16 – 3318Missing in isoform 2. 1 PublicationVSP_012675Add
    BLAST
    Alternative sequencei135 – 15218Missing in isoform 3. 1 PublicationVSP_043364Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34479 mRNA. Translation: AAA36428.1.
    M19123 mRNA. Translation: AAA60052.1. Sequence problems.
    M54788 mRNA. Translation: AAA60053.1.
    M34055 mRNA. Translation: AAA60233.1.
    M34056 mRNA. Translation: AAA60054.1.
    D90086 Genomic DNA. Translation: BAA14123.1.
    J03576 mRNA. Translation: AAA88097.1.
    AL117618 mRNA. Translation: CAB56017.1.
    CR541911 mRNA. Translation: CAG46709.1.
    AK293153 mRNA. Translation: BAG56698.1.
    AK313022 mRNA. Translation: BAG35857.1.
    AC135507 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65371.1.
    BC000439 mRNA. Translation: AAH00439.1.
    BC001924 mRNA. Translation: AAH01924.1.
    X57778 mRNA. Translation: CAA40924.1.
    CCDSiCCDS2890.1. [P11177-1]
    CCDS54602.1. [P11177-3]
    PIRiJU0145. DEHUPB.
    RefSeqiNP_000916.2. NM_000925.3. [P11177-1]
    NP_001166939.1. NM_001173468.1. [P11177-3]
    UniGeneiHs.161357.

    Genome annotation databases

    EnsembliENST00000302746; ENSP00000307241; ENSG00000168291. [P11177-1]
    ENST00000383714; ENSP00000373220; ENSG00000168291. [P11177-2]
    ENST00000485460; ENSP00000417267; ENSG00000168291. [P11177-3]
    GeneIDi5162.
    KEGGihsa:5162.
    UCSCiuc003dke.4. human. [P11177-1]
    uc003dkg.4. human. [P11177-2]
    uc011bff.2. human. [P11177-3]

    Polymorphism databases

    DMDMi134044259.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34479 mRNA. Translation: AAA36428.1 .
    M19123 mRNA. Translation: AAA60052.1 . Sequence problems.
    M54788 mRNA. Translation: AAA60053.1 .
    M34055 mRNA. Translation: AAA60233.1 .
    M34056 mRNA. Translation: AAA60054.1 .
    D90086 Genomic DNA. Translation: BAA14123.1 .
    J03576 mRNA. Translation: AAA88097.1 .
    AL117618 mRNA. Translation: CAB56017.1 .
    CR541911 mRNA. Translation: CAG46709.1 .
    AK293153 mRNA. Translation: BAG56698.1 .
    AK313022 mRNA. Translation: BAG35857.1 .
    AC135507 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW65371.1 .
    BC000439 mRNA. Translation: AAH00439.1 .
    BC001924 mRNA. Translation: AAH01924.1 .
    X57778 mRNA. Translation: CAA40924.1 .
    CCDSi CCDS2890.1. [P11177-1 ]
    CCDS54602.1. [P11177-3 ]
    PIRi JU0145. DEHUPB.
    RefSeqi NP_000916.2. NM_000925.3. [P11177-1 ]
    NP_001166939.1. NM_001173468.1. [P11177-3 ]
    UniGenei Hs.161357.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NI4 X-ray 1.95 B/D 31-359 [» ]
    2OZL X-ray 1.90 B/D 32-359 [» ]
    3EXE X-ray 1.98 B/D/F/H 31-359 [» ]
    3EXF X-ray 3.00 B/D/F/H 31-359 [» ]
    3EXG X-ray 3.01 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z 31-359 [» ]
    3EXH X-ray 2.44 B/D/F/H 31-359 [» ]
    3EXI X-ray 2.20 B 31-359 [» ]
    ProteinModelPortali P11177.
    SMRi P11177. Positions 30-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111188. 35 interactions.
    DIPi DIP-37651N.
    IntActi P11177. 15 interactions.
    MINTi MINT-3007546.
    STRINGi 9606.ENSP00000307241.

    Chemistry

    DrugBanki DB00157. NADH.
    DB00119. Pyruvic acid.

    PTM databases

    PhosphoSitei P11177.

    Polymorphism databases

    DMDMi 134044259.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00549885.
    SWISS-2DPAGE P11177.
    UCD-2DPAGE P11177.

    Proteomic databases

    MaxQBi P11177.
    PaxDbi P11177.
    PRIDEi P11177.

    Protocols and materials databases

    DNASUi 5162.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000302746 ; ENSP00000307241 ; ENSG00000168291 . [P11177-1 ]
    ENST00000383714 ; ENSP00000373220 ; ENSG00000168291 . [P11177-2 ]
    ENST00000485460 ; ENSP00000417267 ; ENSG00000168291 . [P11177-3 ]
    GeneIDi 5162.
    KEGGi hsa:5162.
    UCSCi uc003dke.4. human. [P11177-1 ]
    uc003dkg.4. human. [P11177-2 ]
    uc011bff.2. human. [P11177-3 ]

    Organism-specific databases

    CTDi 5162.
    GeneCardsi GC03M058388.
    HGNCi HGNC:8808. PDHB.
    HPAi HPA036744.
    MIMi 179060. gene.
    614111. phenotype.
    neXtProti NX_P11177.
    Orphaneti 255138. Pyruvate dehydrogenase E1-beta deficiency.
    PharmGKBi PA33152.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0022.
    HOGENOMi HOG000281450.
    HOVERGENi HBG000917.
    InParanoidi P11177.
    KOi K00162.
    OMAi DPKVFVM.
    OrthoDBi EOG7KSX8S.
    PhylomeDBi P11177.
    TreeFami TF105674.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09727-MONOMER.
    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_2071. Pyruvate metabolism.
    SABIO-RK P11177.

    Miscellaneous databases

    ChiTaRSi PDHB. human.
    EvolutionaryTracei P11177.
    GeneWikii Pyruvate_dehydrogenase_(lipoamide)_beta.
    GenomeRNAii 5162.
    NextBioi 19970.
    PROi P11177.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11177.
    Bgeei P11177.
    CleanExi HS_PDHB.
    Genevestigatori P11177.

    Family and domain databases

    Gene3Di 3.40.50.920. 1 hit.
    3.40.50.970. 1 hit.
    InterProi IPR027110. PDHB.
    IPR029061. THDP-binding.
    IPR009014. Transketo_C/Pyr-ferredox_oxred.
    IPR005475. Transketolase-like_Pyr-bd.
    IPR005476. Transketolase_C.
    [Graphical view ]
    PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
    Pfami PF02779. Transket_pyr. 1 hit.
    PF02780. Transketolase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00861. Transket_pyr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    SSF52922. SSF52922. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex."
      Ho L., Patel M.S.
      Gene 86:297-302(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Isolation, characterization and chromosomal localization of cDNA clones for the E1 beta subunit of the pyruvate dehydrogenase complex."
      Chun K., MacKay N., Willard H.F., Robinson B.H.
      Eur. J. Biochem. 194:587-592(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast."
      Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J.
      J. Biol. Chem. 265:13320-13326(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-31.
    4. "Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene."
      Koike K., Urata Y., Koike M.
      Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    5. "Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase."
      Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.
      Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-31.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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] (ISOFORMS 1 AND 3).
      Tissue: Brain cortex.
    9. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Lung.
    12. "Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex."
      Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.
      Biochem. Biophys. Res. Commun. 150:904-908(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
    13. "The human myocardial two-dimensional gel protein database: update 1994."
      Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.
      Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-43.
      Tissue: Heart.
    14. "Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis."
      Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y., Namihisa T.
      Hepatology 11:16-23(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 31-55.
    15. "Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."
      Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.
      J. Biol. Chem. 279:6921-6933(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase."
      Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.
      J. Biol. Chem. 278:21240-21246(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH THIAMINE PYROPHOSPHATE, COFACTOR.
    18. "Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex."
      Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.
      Biochemistry 46:6277-6287(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-359, SUBUNIT, FUNCTION.
    19. "Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops."
      Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J., Chuang D.T.
      Structure 16:1849-1859(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 31-359, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, FUNCTION.
    20. "Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency."
      Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H., Brown G.K.
      Hum. Genet. 115:123-127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PDHBD CYS-132 AND SER-344.

    Entry informationi

    Entry nameiODPB_HUMAN
    AccessioniPrimary (citable) accession number: P11177
    Secondary accession number(s): B2R7L0
    , B4DDD7, Q6FH45, Q9BQ27, Q9UFK3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 173 of the entry and version 3 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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

    External Data

    Dasty 3