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P29803

- ODPAT_HUMAN

UniProt

P29803 - ODPAT_HUMAN

Protein

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

Gene

PDHA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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.1 Publication

    Catalytic activityi

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

    Cofactori

    Thiamine pyrophosphate.

    Enzyme regulationi

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

    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:PDHAL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8807. PDHA2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: UniProtKB-SubCell
    2. nucleus Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi230 – 2301S → A: Slightly reduces enzyme activity. 1 Publication
    Mutagenesisi291 – 2911S → A: Strongly reduces enzyme activity. 1 Publication
    Mutagenesisi291 – 2911S → E: Abolishes enzyme activity. 1 Publication
    Mutagenesisi298 – 2981S → A: Slightly reduces enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33151.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2727MitochondrionBy similarityAdd
    BLAST
    Chaini28 – 388361Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrialPRO_0000020447Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei291 – 2911Phosphoserine; by PDK1, PDK2, PDK3 and PDK41 Publication
    Modified residuei298 – 2981Phosphoserine; by PDK31 Publication

    Post-translational modificationi

    Phosphorylation at Ser-205, Ser-266 and Ser-273 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-266 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-205, Ser-266 and Ser-273, is required for reactivation.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP29803.
    PaxDbiP29803.
    PRIDEiP29803.

    PTM databases

    PhosphoSiteiP29803.

    Expressioni

    Tissue specificityi

    Testis. Expressed in postmeiotic spermatogenic cells.1 Publication

    Gene expression databases

    BgeeiP29803.
    CleanExiHS_PDHA2.
    GenevestigatoriP29803.

    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.1 Publication

    Protein-protein interaction databases

    BioGridi111187. 8 interactions.
    IntActiP29803. 1 interaction.
    STRINGi9606.ENSP00000295266.

    Structurei

    3D structure databases

    ProteinModelPortaliP29803.
    SMRiP29803. Positions 29-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1071.
    HOGENOMiHOG000281336.
    HOVERGENiHBG001863.
    InParanoidiP29803.
    KOiK00161.
    OMAiIANGPIV.
    OrthoDBiEOG73JKVQ.
    PhylomeDBiP29803.
    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.

    P29803-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLAAFISRVL RRVAQKSARR VLVASRNSSN DATFEIKKCD LYLLEEGPPV    50
    TTVLTRAEGL KYYRMMLTVR RMELKADQLY KQKFIRGFCH LCDGQEACCV 100
    GLEAGINPSD HVITSYRAHG VCYTRGLSVR SILAELTGRR GGCAKGKGGS 150
    MHMYTKNFYG GNGIVGAQGP LGAGIALACK YKGNDEICLT LYGDGAANQG 200
    QIAEAFNMAA LWKLPCVFIC ENNLYGMGTS TERAAASPDY YKRGNFIPGL 250
    KVDGMDVLCV REATKFAANY CRSGKGPILM ELQTYRYHGH SMSDPGVSYR 300
    TREEIQEVRS KRDPIIILQD RMVNSKLATV EELKEIGAEV RKEIDDAAQF 350
    ATTDPEPHLE ELGHHIYSSD SSFEVRGANP WIKFKSVS 388
    Length:388
    Mass (Da):42,933
    Last modified:April 1, 1993 - v1
    Checksum:i075B6CFF6DC73CC5
    GO

    Sequence cautioni

    The sequence AAH94760.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti127 – 1271L → P in AAH66953. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti280 – 2801M → L.
    Corresponds to variant rs2229137 [ dbSNP | Ensembl ].
    VAR_034358
    Natural varianti376 – 3761R → G.
    Corresponds to variant rs17024795 [ dbSNP | Ensembl ].
    VAR_034359

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86808 Genomic DNA. Translation: AAA60232.1.
    AK313872 mRNA. Translation: BAG36600.1.
    BC030697 mRNA. Translation: AAH30697.3.
    BC066953 mRNA. Translation: AAH66953.2.
    BC094760 mRNA. Translation: AAH94760.1. Different initiation.
    BC119656 mRNA. Translation: AAI19657.1.
    BC119657 mRNA. Translation: AAI19658.1.
    BC127637 mRNA. Translation: AAI27638.1.
    BC127638 mRNA. Translation: AAI27639.1.
    CCDSiCCDS3644.1.
    PIRiA37104. DEHUPT.
    RefSeqiNP_005381.1. NM_005390.4.
    UniGeneiHs.131361.

    Genome annotation databases

    EnsembliENST00000295266; ENSP00000295266; ENSG00000163114.
    GeneIDi5161.
    KEGGihsa:5161.
    UCSCiuc003htr.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86808 Genomic DNA. Translation: AAA60232.1 .
    AK313872 mRNA. Translation: BAG36600.1 .
    BC030697 mRNA. Translation: AAH30697.3 .
    BC066953 mRNA. Translation: AAH66953.2 .
    BC094760 mRNA. Translation: AAH94760.1 . Different initiation.
    BC119656 mRNA. Translation: AAI19657.1 .
    BC119657 mRNA. Translation: AAI19658.1 .
    BC127637 mRNA. Translation: AAI27638.1 .
    BC127638 mRNA. Translation: AAI27639.1 .
    CCDSi CCDS3644.1.
    PIRi A37104. DEHUPT.
    RefSeqi NP_005381.1. NM_005390.4.
    UniGenei Hs.131361.

    3D structure databases

    ProteinModelPortali P29803.
    SMRi P29803. Positions 29-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111187. 8 interactions.
    IntActi P29803. 1 interaction.
    STRINGi 9606.ENSP00000295266.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P29803.

    Proteomic databases

    MaxQBi P29803.
    PaxDbi P29803.
    PRIDEi P29803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000295266 ; ENSP00000295266 ; ENSG00000163114 .
    GeneIDi 5161.
    KEGGi hsa:5161.
    UCSCi uc003htr.4. human.

    Organism-specific databases

    CTDi 5161.
    GeneCardsi GC04P096761.
    HGNCi HGNC:8807. PDHA2.
    MIMi 179061. gene.
    neXtProti NX_P29803.
    PharmGKBi PA33151.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1071.
    HOGENOMi HOG000281336.
    HOVERGENi HBG001863.
    InParanoidi P29803.
    KOi K00161.
    OMAi IANGPIV.
    OrthoDBi EOG73JKVQ.
    PhylomeDBi P29803.
    TreeFami TF300742.

    Miscellaneous databases

    ChiTaRSi PDHA2. human.
    GeneWikii Pyruvate_dehydrogenase_(lipoamide)_alpha_2.
    GenomeRNAii 5161.
    NextBioi 19966.
    PROi P29803.
    SOURCEi Search...

    Gene expression databases

    Bgeei P29803.
    CleanExi HS_PDHA2.
    Genevestigatori P29803.

    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. "A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4."
      Dahl H.-H.M., Brown R.M., Hutchison W.M., Maragos C., Brown G.K.
      Genomics 8:225-232(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Testis.
    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].
      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.
    4. "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.
    5. "Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase."
      Korotchkina L.G., Sidhu S., Patel M.S.
      J. Biol. Chem. 281:9688-9696(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION AT SER-291 AND SER-298, MUTAGENESIS OF SER-230; SER-291 AND SER-298.
    6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Pyruvate dehydrogenase complex: mRNA and protein expression patterns of E1alpha subunit genes in human spermatogenesis."
      Pinheiro A., Silva M.J., Graca I., Silva J., Sa R., Sousa M., Barros A., Tavares de Almeida I., Rivera I.
      Gene 506:173-178(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiODPAT_HUMAN
    AccessioniPrimary (citable) accession number: P29803
    Secondary accession number(s): B2R9Q3
    , Q0VDI5, Q4VC02, Q6NXQ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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

    External Data

    Dasty 3