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P35487

- ODPAT_MOUSE

UniProt

P35487 - ODPAT_MOUSE

Protein

Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial

Gene

Pdha2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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

    Enzyme regulationi

    Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation.By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. glucose metabolic process Source: UniProtKB-KW
    2. glycolytic process Source: InterPro
    3. pyruvate metabolic process Source: UniProtKB
    4. tricarboxylic acid cycle Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

    Keywords - Ligandi

    Pyruvate, Thiamine pyrophosphate

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial (EC:1.2.4.1)
    Alternative name(s):
    PDHE1-A type II
    Gene namesi
    Name:Pdha2
    Synonyms:Pdha-2, Pdhal
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:97533. Pdha2.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3030MitochondrionBy similarityAdd
    BLAST
    Chaini31 – 391361Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrialPRO_0000020448Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei294 – 2941Phosphoserine; by PDK1, PDK2, PDK3 and PDK4By similarity
    Modified residuei301 – 3011Phosphoserine; by PDK3By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP35487.
    PRIDEiP35487.

    2D gel databases

    REPRODUCTION-2DPAGEP35487.

    PTM databases

    PhosphoSiteiP35487.

    Expressioni

    Tissue specificityi

    Testis.

    Gene expression databases

    BgeeiP35487.
    CleanExiMM_PDHA2.
    GenevestigatoriP35487.

    Interactioni

    Subunit structurei

    Heterotetramer of two PDHA2 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

    Structurei

    3D structure databases

    ProteinModelPortaliP35487.
    SMRiP35487. Positions 31-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1071.
    GeneTreeiENSGT00530000063174.
    HOGENOMiHOG000281336.
    HOVERGENiHBG001863.
    InParanoidiQ497M8.
    KOiK00161.
    OMAiTSNERSA.
    OrthoDBiEOG73JKVQ.
    PhylomeDBiP35487.
    TreeFamiTF300742.

    Family and domain databases

    Gene3Di3.40.50.970. 1 hit.
    InterProiIPR001017. DH_E1.
    IPR017597. Pyrv_DH_E1_asu_subgrp-y.
    IPR029061. THDP-binding.
    [Graphical view]
    PfamiPF00676. E1_dh. 1 hit.
    [Graphical view]
    SUPFAMiSSF52518. SSF52518. 1 hit.
    TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P35487-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRKMLTAVLS HVFSGMVQKP ALRGLLSSLK FSNDATCDIK KCDLYRLEEG    50
    PPTSTVLTRA EALKYYRTMQ VIRRMELKAD QLYKQKFIRG FCHLCDGQEA 100
    CCVGLEAGIN PTDHVITSYR AHGFCYTRGL SVKSILAELT GRKGGCAKGK 150
    GGSMHMYGKN FYGGNGIVGA QVPLGAGVAF ACKYLKNGQV CLALYGDGAA 200
    NQGQVFEAYN MSALWKLPCV FICENNLYGM GTSNERSAAS TDYHKKGFII 250
    PGLRVNGMDI LCVREATKFA ADHCRSGKGP IVMELQTYRY HGHSMSDPGI 300
    SYRSREEVHN VRSKSDPIML LRERIISNNL SNIEELKEID ADVKKEVEDA 350
    AQFATTDPEP AVEDIANYLY HQDPPFEVRG AHKWLKYKSH S 391
    Length:391
    Mass (Da):43,413
    Last modified:June 1, 1994 - v1
    Checksum:iA2DE823362485977
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76728 mRNA. Translation: AAA53047.1.
    AK076791 mRNA. Translation: BAC36482.1.
    BC100460 mRNA. Translation: AAI00461.1.
    CCDSiCCDS17872.1.
    PIRiS23507.
    RefSeqiNP_032837.1. NM_008811.2.
    UniGeneiMm.4223.

    Genome annotation databases

    EnsembliENSMUST00000057860; ENSMUSP00000060774; ENSMUSG00000047674.
    GeneIDi18598.
    KEGGimmu:18598.
    UCSCiuc008rob.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M76728 mRNA. Translation: AAA53047.1 .
    AK076791 mRNA. Translation: BAC36482.1 .
    BC100460 mRNA. Translation: AAI00461.1 .
    CCDSi CCDS17872.1.
    PIRi S23507.
    RefSeqi NP_032837.1. NM_008811.2.
    UniGenei Mm.4223.

    3D structure databases

    ProteinModelPortali P35487.
    SMRi P35487. Positions 31-391.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P35487.

    2D gel databases

    REPRODUCTION-2DPAGE P35487.

    Proteomic databases

    PaxDbi P35487.
    PRIDEi P35487.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000057860 ; ENSMUSP00000060774 ; ENSMUSG00000047674 .
    GeneIDi 18598.
    KEGGi mmu:18598.
    UCSCi uc008rob.1. mouse.

    Organism-specific databases

    CTDi 5161.
    MGIi MGI:97533. Pdha2.

    Phylogenomic databases

    eggNOGi COG1071.
    GeneTreei ENSGT00530000063174.
    HOGENOMi HOG000281336.
    HOVERGENi HBG001863.
    InParanoidi Q497M8.
    KOi K00161.
    OMAi TSNERSA.
    OrthoDBi EOG73JKVQ.
    PhylomeDBi P35487.
    TreeFami TF300742.

    Miscellaneous databases

    NextBioi 294494.
    PROi P35487.
    SOURCEi Search...

    Gene expression databases

    Bgeei P35487.
    CleanExi MM_PDHA2.
    Genevestigatori P35487.

    Family and domain databases

    Gene3Di 3.40.50.970. 1 hit.
    InterProi IPR001017. DH_E1.
    IPR017597. Pyrv_DH_E1_asu_subgrp-y.
    IPR029061. THDP-binding.
    [Graphical view ]
    Pfami PF00676. E1_dh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52518. SSF52518. 1 hit.
    TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterisation of the mouse pyruvate dehydrogenase E1 alpha genes."
      Fitzgerald G.F., Hutchison W.M., Dahl H.-H.M.
      Biochim. Biophys. Acta 1131:83-90(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Testis.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.

    Entry informationi

    Entry nameiODPAT_MOUSE
    AccessioniPrimary (citable) accession number: P35487
    Secondary accession number(s): Q497M8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 116 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, Reference proteome

    Documents

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

    External Data

    Dasty 3