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Q9D051

- ODPB_MOUSE

UniProt

Q9D051 - ODPB_MOUSE

Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

Pdhb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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.By similarity

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891Thiamine pyrophosphateBy similarity

    GO - Molecular functioni

    1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
    2. pyruvate dehydrogenase activity Source: UniProtKB

    GO - Biological processi

    1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    2. glucose metabolic process Source: UniProtKB-KW
    3. 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

    ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1915513. Pdhb.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI
    3. pyruvate dehydrogenase complex Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030MitochondrionBy similarityAdd
    BLAST
    Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020458Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei67 – 671Phosphotyrosine1 Publication
    Modified residuei354 – 3541N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9D051.
    PaxDbiQ9D051.
    PRIDEiQ9D051.

    2D gel databases

    REPRODUCTION-2DPAGEQ9D051.
    UCD-2DPAGEQ9D051.

    PTM databases

    PhosphoSiteiQ9D051.

    Expressioni

    Gene expression databases

    BgeeiQ9D051.
    CleanExiMM_PDHB.
    GenevestigatoriQ9D051.

    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 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi212768. 2 interactions.
    IntActiQ9D051. 9 interactions.
    MINTiMINT-1860720.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D051.
    SMRiQ9D051. Positions 30-359.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0022.
    GeneTreeiENSGT00530000063423.
    HOGENOMiHOG000281450.
    HOVERGENiHBG000917.
    InParanoidiQ9D051.
    KOiK00162.
    OMAiYASWYAH.
    OrthoDBiEOG7KSX8S.
    PhylomeDBiQ9D051.
    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.

    Sequencei

    Sequence statusi: Complete.

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

    Q9D051-1 [UniParc]FASTAAdd to Basket

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    MAVVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD    50
    EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA 100
    MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSAGLQPV PIVFRGPNGA 150
    SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVML 200
    ENELMYGVAF ELPAEAQSKD FLIPIGKAKI ERQGTHITVV AHSRPVGHCL 250
    EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG 300
    VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKVLED NSVPQVKDII 350
    FAVKKTLNI 359
    Length:359
    Mass (Da):38,937
    Last modified:June 1, 2001 - v1
    Checksum:iF5CD2A186DF58DDE
    GO

    Sequence cautioni

    The sequence AAH02188.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti237 – 2371I → M in BAE38906. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011810 mRNA. Translation: BAB27855.1.
    AK153058 mRNA. Translation: BAE31684.1.
    AK166631 mRNA. Translation: BAE38906.1.
    BC002188 mRNA. Translation: AAH02188.1. Different initiation.
    BC019512 mRNA. Translation: AAH19512.1.
    BC094468 mRNA. Translation: AAH94468.1.
    CCDSiCCDS36800.1.
    PIRiPT0096.
    RefSeqiNP_077183.1. NM_024221.3.
    UniGeneiMm.301527.

    Genome annotation databases

    EnsembliENSMUST00000022268; ENSMUSP00000022268; ENSMUSG00000021748.
    GeneIDi68263.
    KEGGimmu:68263.
    UCSCiuc007sev.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK011810 mRNA. Translation: BAB27855.1 .
    AK153058 mRNA. Translation: BAE31684.1 .
    AK166631 mRNA. Translation: BAE38906.1 .
    BC002188 mRNA. Translation: AAH02188.1 . Different initiation.
    BC019512 mRNA. Translation: AAH19512.1 .
    BC094468 mRNA. Translation: AAH94468.1 .
    CCDSi CCDS36800.1.
    PIRi PT0096.
    RefSeqi NP_077183.1. NM_024221.3.
    UniGenei Mm.301527.

    3D structure databases

    ProteinModelPortali Q9D051.
    SMRi Q9D051. Positions 30-359.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212768. 2 interactions.
    IntActi Q9D051. 9 interactions.
    MINTi MINT-1860720.

    PTM databases

    PhosphoSitei Q9D051.

    2D gel databases

    REPRODUCTION-2DPAGE Q9D051.
    UCD-2DPAGE Q9D051.

    Proteomic databases

    MaxQBi Q9D051.
    PaxDbi Q9D051.
    PRIDEi Q9D051.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022268 ; ENSMUSP00000022268 ; ENSMUSG00000021748 .
    GeneIDi 68263.
    KEGGi mmu:68263.
    UCSCi uc007sev.1. mouse.

    Organism-specific databases

    CTDi 5162.
    MGIi MGI:1915513. Pdhb.

    Phylogenomic databases

    eggNOGi COG0022.
    GeneTreei ENSGT00530000063423.
    HOGENOMi HOG000281450.
    HOVERGENi HBG000917.
    InParanoidi Q9D051.
    KOi K00162.
    OMAi YASWYAH.
    OrthoDBi EOG7KSX8S.
    PhylomeDBi Q9D051.
    TreeFami TF105674.

    Enzyme and pathway databases

    Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

    Miscellaneous databases

    ChiTaRSi PDHB. mouse.
    NextBioi 326854.
    PROi Q9D051.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D051.
    CleanExi MM_PDHB.
    Genevestigatori Q9D051.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow and Embryo.
    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].
      Strain: FVB/N-3.
      Tissue: Liver and Mammary tumor.
    3. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 309-324, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    4. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiODPB_MOUSE
    AccessioniPrimary (citable) accession number: Q9D051
    Secondary accession number(s): Q3TL86, Q505N8, Q99LW9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

    External Data

    Dasty 3