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O00330

- ODPX_HUMAN

UniProt

O00330 - ODPX_HUMAN

Protein

Pyruvate dehydrogenase protein X component, mitochondrial

Gene

PDHX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (24 Jan 2001)
      Previous versions | rss
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    Functioni

    Required for anchoring dihydrolipoamide dehydrogenase (E3) to the dihydrolipoamide transacetylase (E2) core of the pyruvate dehydrogenase complexes of eukaryotes. This specific binding is essential for a functional PDH complex.

    GO - Molecular functioni

    1. transferase activity, transferring acyl groups Source: InterPro

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. pyruvate metabolic process Source: Reactome
    3. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
    4. small molecule metabolic process Source: Reactome

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000110435-MONOMER.
    ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_2071. Pyruvate metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase protein X component, mitochondrial
    Alternative name(s):
    Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
    E3-binding protein
    Short name:
    E3BP
    Lipoyl-containing pyruvate dehydrogenase complex component X
    proX
    Gene namesi
    Name:PDHX
    Synonyms:PDX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:21350. PDHX.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Pyruvate dehydrogenase E3-binding protein deficiency (PDHXD) [MIM:245349]: A metabolic disorder characterized by decreased activity of the pyruvate dehydrogenase complex without observable reduction in the activities of enzymes E1, E2, or E3. Clinical features include hypotonia and psychomotor retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi183 – 1831R → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi185 – 1851S → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi186 – 1861P → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi187 – 1871A → M: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi189 – 1891R → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi190 – 1901N → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi193 – 1931E → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi208 – 2081R → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi210 – 2101I → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi213 – 2131K → A: Strongly decreased DLD binding. 1 Publication
    Mutagenesisi214 – 2141E → A: Strongly decreased DLD binding. 1 Publication

    Organism-specific databases

    MIMi245349. phenotype.
    Orphaneti255182. Pyruvate dehydrogenase E3-binding protein deficiency.
    PharmGKBiPA134976445.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionBy similarityAdd
    BLAST
    Chaini54 – 501448Pyruvate dehydrogenase protein X component, mitochondrialPRO_0000020484Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei97 – 971N6-lipoyllysineBy similarity
    Modified residuei194 – 1941N6-acetyllysine1 Publication
    Modified residuei394 – 3941N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO00330.
    PaxDbiO00330.
    PeptideAtlasiO00330.
    PRIDEiO00330.

    PTM databases

    PhosphoSiteiO00330.

    Expressioni

    Gene expression databases

    ArrayExpressiO00330.
    BgeeiO00330.
    CleanExiHS_PDHX.
    HS_PDX1.
    GenevestigatoriO00330.

    Organism-specific databases

    HPAiHPA038484.
    HPA038485.

    Interactioni

    Subunit structurei

    Part of the inner core of the multimeric pyruvate dehydrogenase complex that is composed of about 48 DLAT and 12 PDHX molecules. This core binds multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3).3 Publications

    Protein-protein interaction databases

    BioGridi113737. 13 interactions.
    DIPiDIP-29026N.
    IntActiO00330. 5 interactions.
    MINTiMINT-1482590.
    STRINGi9606.ENSP00000227868.

    Structurei

    Secondary structure

    1
    501
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi57 – 604
    Beta strandi69 – 713
    Beta strandi73 – 786
    Beta strandi88 – 947
    Beta strandi99 – 1035
    Beta strandi108 – 1125
    Beta strandi122 – 1254
    Beta strandi127 – 1326
    Helixi180 – 1834
    Helixi186 – 1949
    Helixi199 – 2013
    Helixi207 – 2093
    Helixi213 – 22816

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZY8X-ray2.59K/L/M/N/O54-274[»]
    2DNCNMR-A57-141[»]
    2F5ZX-ray2.18K/L/M/N/O173-228[»]
    2F60X-ray1.55K173-228[»]
    ProteinModelPortaliO00330.
    SMRiO00330. Positions 57-144, 183-225, 266-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00330.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini57 – 13175Lipoyl-bindingAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni183 – 21432Interaction with DLDAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi149 – 17022Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the 2-oxoacid dehydrogenase family.Curated
    Contains 1 lipoyl-binding domain.Curated

    Keywords - Domaini

    Lipoyl, Transit peptide

    Phylogenomic databases

    eggNOGiCOG0508.
    HOGENOMiHOG000281566.
    HOVERGENiHBG005063.
    InParanoidiO00330.
    KOiK13997.
    OMAiSWRLGCD.
    PhylomeDBiO00330.
    TreeFamiTF332256.

    Family and domain databases

    Gene3Di3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProiIPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view]
    SUPFAMiSSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEiPS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view]

    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: O00330-1) [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

    MAASWRLGCD PRLLRYLVGF PGRRSVGLVK GALGWSVSRG ANWRWFHSTQ    50
    WLRGDPIKIL MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV 100
    TLDASDDGIL AKIVVEEGSK NIRLGSLIGL IVEEGEDWKH VEIPKDVGPP 150
    PPVSKPSEPR PSPEPQISIP VKKEHIPGTL RFRLSPAARN ILEKHSLDAS 200
    QGTATGPRGI FTKEDALKLV QLKQTGKITE SRPTPAPTAT PTAPSPLQAT 250
    AGPSYPRPVI PPVSTPGQPN AVGTFTEIPA SNIRRVIAKR LTESKSTVPH 300
    AYATADCDLG AVLKVRQDLV KDDIKVSVND FIIKAAAVTL KQMPDVNVSW 350
    DGEGPKQLPF IDISVAVATD KGLLTPIIKD AAAKGIQEIA DSVKALSKKA 400
    RDGKLLPEEY QGGSFSISNL GMFGIDEFTA VINPPQACIL AVGRFRPVLK 450
    LTEDEEGNAK LQQRQLITVT MSSDSRVVDD ELATRFLKSF KANLENPIRL 500
    A 501
    Length:501
    Mass (Da):54,122
    Last modified:January 24, 2001 - v3
    Checksum:i9CF0C1DAE9E12EF9
    GO
    Isoform 2 (identifier: O00330-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         115-341: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:274
    Mass (Da):29,906
    Checksum:i7657F43CA5F9B61D
    GO
    Isoform 3 (identifier: O00330-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-53: AASWRLGCDP...RWFHSTQWLR → QSGGAEGSPG...ISSGAPDFPG

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:486
    Mass (Da):51,460
    Checksum:iC0682D60CAC5BDF5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti41 – 411A → R in AAC39661. (PubMed:9467010)Curated
    Sequence conflicti251 – 2511A → S in AAB66315. (PubMed:9242632)Curated
    Sequence conflicti251 – 2511A → S in CAA73606. (PubMed:9399911)Curated
    Sequence conflicti344 – 3441P → S in BAG62924. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231R → C.1 Publication
    Corresponds to variant rs1049306 [ dbSNP | Ensembl ].
    VAR_046619
    Natural varianti101 – 1011T → A.
    Corresponds to variant rs11539202 [ dbSNP | Ensembl ].
    VAR_046620
    Natural varianti370 – 3701D → V.1 Publication
    Corresponds to variant rs17850649 [ dbSNP | Ensembl ].
    VAR_046621

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 5352AASWR…TQWLR → QSGGAEGSPGAGRTGRGPGS GKAPPAEISSGAPDFPG in isoform 3. CuratedVSP_053817Add
    BLAST
    Alternative sequencei115 – 341227Missing in isoform 2. CuratedVSP_045271Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001437 mRNA. Translation: AAB66315.1.
    Y13145 mRNA. Translation: CAA73606.1.
    U82328 mRNA. Translation: AAC39661.1.
    AJ298105 Genomic DNA. Translation: CAC18649.1.
    AK301384 mRNA. Translation: BAG62924.1.
    AC107928 Genomic DNA. No translation available.
    AL138810 Genomic DNA. No translation available.
    AL356215 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68158.1.
    CH471064 Genomic DNA. Translation: EAW68160.1.
    BC010389 mRNA. Translation: AAH10389.1.
    U79296 mRNA. Translation: AAB50223.1.
    CCDSiCCDS44569.1. [O00330-3]
    CCDS53616.1. [O00330-2]
    CCDS7896.1. [O00330-1]
    RefSeqiNP_001128496.1. NM_001135024.1. [O00330-3]
    NP_001159630.1. NM_001166158.1. [O00330-2]
    NP_003468.2. NM_003477.2. [O00330-1]
    UniGeneiHs.502315.

    Genome annotation databases

    EnsembliENST00000227868; ENSP00000227868; ENSG00000110435. [O00330-1]
    ENST00000430469; ENSP00000415695; ENSG00000110435. [O00330-2]
    ENST00000448838; ENSP00000389404; ENSG00000110435. [O00330-3]
    GeneIDi8050.
    KEGGihsa:8050.
    UCSCiuc001mvt.3. human. [O00330-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF001437 mRNA. Translation: AAB66315.1 .
    Y13145 mRNA. Translation: CAA73606.1 .
    U82328 mRNA. Translation: AAC39661.1 .
    AJ298105 Genomic DNA. Translation: CAC18649.1 .
    AK301384 mRNA. Translation: BAG62924.1 .
    AC107928 Genomic DNA. No translation available.
    AL138810 Genomic DNA. No translation available.
    AL356215 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW68158.1 .
    CH471064 Genomic DNA. Translation: EAW68160.1 .
    BC010389 mRNA. Translation: AAH10389.1 .
    U79296 mRNA. Translation: AAB50223.1 .
    CCDSi CCDS44569.1. [O00330-3 ]
    CCDS53616.1. [O00330-2 ]
    CCDS7896.1. [O00330-1 ]
    RefSeqi NP_001128496.1. NM_001135024.1. [O00330-3 ]
    NP_001159630.1. NM_001166158.1. [O00330-2 ]
    NP_003468.2. NM_003477.2. [O00330-1 ]
    UniGenei Hs.502315.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZY8 X-ray 2.59 K/L/M/N/O 54-274 [» ]
    2DNC NMR - A 57-141 [» ]
    2F5Z X-ray 2.18 K/L/M/N/O 173-228 [» ]
    2F60 X-ray 1.55 K 173-228 [» ]
    ProteinModelPortali O00330.
    SMRi O00330. Positions 57-144, 183-225, 266-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113737. 13 interactions.
    DIPi DIP-29026N.
    IntActi O00330. 5 interactions.
    MINTi MINT-1482590.
    STRINGi 9606.ENSP00000227868.

    PTM databases

    PhosphoSitei O00330.

    Proteomic databases

    MaxQBi O00330.
    PaxDbi O00330.
    PeptideAtlasi O00330.
    PRIDEi O00330.

    Protocols and materials databases

    DNASUi 8050.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227868 ; ENSP00000227868 ; ENSG00000110435 . [O00330-1 ]
    ENST00000430469 ; ENSP00000415695 ; ENSG00000110435 . [O00330-2 ]
    ENST00000448838 ; ENSP00000389404 ; ENSG00000110435 . [O00330-3 ]
    GeneIDi 8050.
    KEGGi hsa:8050.
    UCSCi uc001mvt.3. human. [O00330-1 ]

    Organism-specific databases

    CTDi 8050.
    GeneCardsi GC11P034894.
    HGNCi HGNC:21350. PDHX.
    HPAi HPA038484.
    HPA038485.
    MIMi 245349. phenotype.
    608769. gene.
    neXtProti NX_O00330.
    Orphaneti 255182. Pyruvate dehydrogenase E3-binding protein deficiency.
    PharmGKBi PA134976445.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0508.
    HOGENOMi HOG000281566.
    HOVERGENi HBG005063.
    InParanoidi O00330.
    KOi K13997.
    OMAi SWRLGCD.
    PhylomeDBi O00330.
    TreeFami TF332256.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000110435-MONOMER.
    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
    REACT_2071. Pyruvate metabolism.

    Miscellaneous databases

    EvolutionaryTracei O00330.
    GeneWikii E3_binding_protein.
    GenomeRNAii 8050.
    NextBioi 30644.
    PROi O00330.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00330.
    Bgeei O00330.
    CleanExi HS_PDHX.
    HS_PDX1.
    Genevestigatori O00330.

    Family and domain databases

    Gene3Di 3.30.559.10. 1 hit.
    4.10.320.10. 1 hit.
    InterProi IPR003016. 2-oxoA_DH_lipoyl-BS.
    IPR001078. 2-oxoacid_DH_actylTfrase.
    IPR000089. Biotin_lipoyl.
    IPR023213. CAT-like_dom.
    IPR004167. E3-bd.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF00198. 2-oxoacid_dh. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF02817. E3_binding. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47005. SSF47005. 1 hit.
    SSF51230. SSF51230. 1 hit.
    PROSITEi PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00189. LIPOYL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex."
      Harris R.A., Bowker-Kinley M.M., Wu P., Jeng J., Popov K.M.
      J. Biol. Chem. 272:19746-19751(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CYS-23.
    2. "Mutations in PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital lactic acidosis."
      Aral B., Benelli C., Ait-Ghezala G., Amessou M., Fouque F., Maunoury C., Creau N., Kamoun P., Marsac C.
      Am. J. Hum. Genet. 61:1318-1326(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN PDHXD.
      Tissue: Liver.
    3. "Detection of a homozygous four base pair deletion in the protein X gene in a case of pyruvate dehydrogenase complex deficiency."
      Ling M., McEachern G., Seyda A., Mackay N., Scherer S.W., Bratinova S., Beatty B., Giovannucci-Uzielli M.L., Robinson B.H.
      Hum. Mol. Genet. 7:501-505(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Human gene sequence for PDX1, the human lipoyl-containing component X of the pyruvate dehydrogenase complex."
      Aral B., Dey R., Marsac C.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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].
      Tissue: Synovium.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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), VARIANT VAL-370.
      Tissue: Brain.
    9. "Large-scale concatenation cDNA sequencing."
      Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
      Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-501 (ISOFORM 1).
      Tissue: Brain.
    10. "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.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex."
      Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K., Korotchkina L.G., Patel M.S.
      J. Biol. Chem. 281:648-655(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 54-274 IN COMPLEX WITH DLD.
    14. "Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex."
      Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R., Chuang D.T.
      Structure 14:611-621(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 174-230 IN COMPLEX WITH DLD, MUTAGENESIS OF ARG-183; SER-185; PRO-186; ALA-187; ARG-189; ASN-190; GLU-193; ARG-208; ILE-210; LYS-213 AND GLU-214.
    15. "Solution structure of RSGI RUH-054, a lipoyl domain from human 2-oxoacid dehydrogenase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 57-141.

    Entry informationi

    Entry nameiODPX_HUMAN
    AccessioniPrimary (citable) accession number: O00330
    Secondary accession number(s): B4DW62
    , D3DR11, E9PB14, E9PBP7, O60221, Q96FV8, Q99783
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 146 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, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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