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Q9P0J1

- PDP1_HUMAN

UniProt

Q9P0J1 - PDP1_HUMAN

Protein

[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial

Gene

PDP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (25 Oct 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex.By similarity

    Catalytic activityi

    [Pyruvate dehydrogenase (acetyl-transferring)] phosphate + H2O = [pyruvate dehydrogenase (acetyl-transferring)] + phosphate.

    Cofactori

    Binds 2 magnesium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi144 – 1441Magnesium 1By similarity
    Metal bindingi144 – 1441Magnesium 2By similarity
    Metal bindingi145 – 1451Magnesium 1; via carbonyl oxygenBy similarity
    Metal bindingi418 – 4181Magnesium 2By similarity
    Metal bindingi516 – 5161Magnesium 1By similarity

    GO - Molecular functioni

    1. [pyruvate dehydrogenase (lipoamide)] phosphatase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW
    3. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial (EC:3.1.3.43)
    Short name:
    PDP 1
    Alternative name(s):
    Protein phosphatase 2C
    Pyruvate dehydrogenase phosphatase catalytic subunit 1
    Short name:
    PDPC 1
    Gene namesi
    Name:PDP1
    Synonyms:PDP, PPM2C
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9279. PDP1.

    Subcellular locationi

    Mitochondrion matrix By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Pyruvate dehydrogenase phosphatase deficiency (PDP deficiency) [MIM:608782]: Results in lactic acidosis leading to neurological dysfunction.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti284 – 2841Missing in PDP deficiency; low activity. 1 Publication
    VAR_029882

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi608782. phenotype.
    Orphaneti79246. Pyruvate dehydrogenase phosphatase deficiency.
    PharmGKBiPA33607.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7171MitochondrionBy similarityAdd
    BLAST
    Chaini72 – 537466[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrialPRO_0000025419Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei202 – 2021N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9P0J1.
    PaxDbiQ9P0J1.
    PRIDEiQ9P0J1.

    PTM databases

    PhosphoSiteiQ9P0J1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9P0J1.
    BgeeiQ9P0J1.
    CleanExiHS_PPM2C.
    GenevestigatoriQ9P0J1.

    Organism-specific databases

    HPAiHPA018483.
    HPA019081.
    HPA021152.

    Interactioni

    Subunit structurei

    Heterodimer of a catalytic (PDP1) and a regulatory (PDPR) subunit.By similarity

    Protein-protein interaction databases

    BioGridi120103. 3 interactions.
    IntActiQ9P0J1. 2 interactions.
    MINTiMINT-4831562.
    STRINGi9606.ENSP00000297598.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P0J1.
    SMRiQ9P0J1. Positions 80-537.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000220821.
    HOVERGENiHBG008162.
    InParanoidiQ9P0J1.
    KOiK01102.
    OMAiHNAQNER.
    OrthoDBiEOG7KQ219.
    PhylomeDBiQ9P0J1.
    TreeFamiTF313505.

    Family and domain databases

    Gene3Di3.60.40.10. 2 hits.
    InterProiIPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view]
    PANTHERiPTHR13832. PTHR13832. 1 hit.
    PfamiPF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 3 hits.
    PROSITEiPS01032. PP2C. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P0J1-1) [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

    MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSSSYIP QSRLRYTPHP    50
    AYATFCRPKE NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE 100
    FDGKNVSSIL GFDSNQLPAN APIEDRRSAA TCLQTRGMLL GVFDGHAGCA 150
    CSQAVSERLF YYIAVSLLPH ETLLEIENAV ESGRALLPIL QWHKHPNDYF 200
    SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF KRLDNDISLE 250
    AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE 300
    EDGSWSAVTL SNDHNAQNER ELERLKLEHP KSEAKSVVKQ DRLLGLLMPF 350
    RAFGDVKFKW SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE 400
    VTYHRLRPQD KFLVLATDGL WETMHRQDVV RIVGEYLTGM HHQQPIAVGG 450
    YKVTLGQMHG LLTERRTKMS SVFEDQNAAT HLIRHAVGNN EFGTVDHERL 500
    SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQE 537
    Length:537
    Mass (Da):61,054
    Last modified:October 25, 2005 - v3
    Checksum:i818B0064CA7961A0
    GO
    Isoform 2 (identifier: Q9P0J1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MCVCPGPRRIGIPVRSSSLPLFSDAM

    Note: No experimental confirmation available.

    Show »
    Length:562
    Mass (Da):63,695
    Checksum:i2A29F37D7121A093
    GO

    Sequence cautioni

    The sequence AAF67480.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 11612NVSSI…FDSNQ → MSVLSLDLTAIK in AAF67480. (PubMed:10931946)CuratedAdd
    BLAST
    Sequence conflicti151 – 1511C → W in AAF67480. (PubMed:10931946)Curated
    Sequence conflicti165 – 1651V → G in AAF67480. (PubMed:10931946)Curated
    Sequence conflicti168 – 1681L → V in AAF67480. (PubMed:10931946)Curated
    Sequence conflicti537 – 5371E → EK in AAF67480. (PubMed:10931946)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti284 – 2841Missing in PDP deficiency; low activity. 1 Publication
    VAR_029882

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MCVCPGPRRIGIPVRSSSLP LFSDAM in isoform 2. 1 PublicationVSP_046869

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155661 mRNA. Translation: AAF67480.1. Different initiation.
    AK126862 mRNA. Translation: BAG54383.1.
    DA769567 mRNA. No translation available.
    AC084346 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW91704.1.
    BC047619 mRNA. Translation: AAH47619.1.
    BC098343 mRNA. Translation: AAH98343.1.
    CCDSiCCDS55262.1. [Q9P0J1-2]
    CCDS6259.1. [Q9P0J1-1]
    RefSeqiNP_001155251.1. NM_001161779.1. [Q9P0J1-2]
    NP_001155252.1. NM_001161780.1. [Q9P0J1-2]
    NP_001155253.1. NM_001161781.1. [Q9P0J1-1]
    NP_060914.2. NM_018444.3. [Q9P0J1-1]
    UniGeneiHs.22265.

    Genome annotation databases

    EnsembliENST00000297598; ENSP00000297598; ENSG00000164951. [Q9P0J1-1]
    ENST00000396200; ENSP00000379503; ENSG00000164951. [Q9P0J1-2]
    ENST00000517764; ENSP00000430380; ENSG00000164951. [Q9P0J1-1]
    ENST00000520728; ENSP00000428317; ENSG00000164951. [Q9P0J1-1]
    GeneIDi54704.
    KEGGihsa:54704.
    UCSCiuc003yge.3. human. [Q9P0J1-1]

    Polymorphism databases

    DMDMi78099789.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF155661 mRNA. Translation: AAF67480.1 . Different initiation.
    AK126862 mRNA. Translation: BAG54383.1 .
    DA769567 mRNA. No translation available.
    AC084346 Genomic DNA. No translation available.
    CH471060 Genomic DNA. Translation: EAW91704.1 .
    BC047619 mRNA. Translation: AAH47619.1 .
    BC098343 mRNA. Translation: AAH98343.1 .
    CCDSi CCDS55262.1. [Q9P0J1-2 ]
    CCDS6259.1. [Q9P0J1-1 ]
    RefSeqi NP_001155251.1. NM_001161779.1. [Q9P0J1-2 ]
    NP_001155252.1. NM_001161780.1. [Q9P0J1-2 ]
    NP_001155253.1. NM_001161781.1. [Q9P0J1-1 ]
    NP_060914.2. NM_018444.3. [Q9P0J1-1 ]
    UniGenei Hs.22265.

    3D structure databases

    ProteinModelPortali Q9P0J1.
    SMRi Q9P0J1. Positions 80-537.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120103. 3 interactions.
    IntActi Q9P0J1. 2 interactions.
    MINTi MINT-4831562.
    STRINGi 9606.ENSP00000297598.

    PTM databases

    PhosphoSitei Q9P0J1.

    Polymorphism databases

    DMDMi 78099789.

    Proteomic databases

    MaxQBi Q9P0J1.
    PaxDbi Q9P0J1.
    PRIDEi Q9P0J1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297598 ; ENSP00000297598 ; ENSG00000164951 . [Q9P0J1-1 ]
    ENST00000396200 ; ENSP00000379503 ; ENSG00000164951 . [Q9P0J1-2 ]
    ENST00000517764 ; ENSP00000430380 ; ENSG00000164951 . [Q9P0J1-1 ]
    ENST00000520728 ; ENSP00000428317 ; ENSG00000164951 . [Q9P0J1-1 ]
    GeneIDi 54704.
    KEGGi hsa:54704.
    UCSCi uc003yge.3. human. [Q9P0J1-1 ]

    Organism-specific databases

    CTDi 54704.
    GeneCardsi GC08P094870.
    HGNCi HGNC:9279. PDP1.
    HPAi HPA018483.
    HPA019081.
    HPA021152.
    MIMi 605993. gene.
    608782. phenotype.
    neXtProti NX_Q9P0J1.
    Orphaneti 79246. Pyruvate dehydrogenase phosphatase deficiency.
    PharmGKBi PA33607.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000220821.
    HOVERGENi HBG008162.
    InParanoidi Q9P0J1.
    KOi K01102.
    OMAi HNAQNER.
    OrthoDBi EOG7KQ219.
    PhylomeDBi Q9P0J1.
    TreeFami TF313505.

    Enzyme and pathway databases

    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

    Miscellaneous databases

    ChiTaRSi PDP1. human.
    GeneWikii Pyruvate_dehydrogenase_phosphatase.
    GenomeRNAii 54704.
    NextBioi 35535205.
    PROi Q9P0J1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P0J1.
    Bgeei Q9P0J1.
    CleanExi HS_PPM2C.
    Genevestigatori Q9P0J1.

    Family and domain databases

    Gene3Di 3.60.40.10. 2 hits.
    InterProi IPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view ]
    PANTHERi PTHR13832. PTHR13832. 1 hit.
    Pfami PF00481. PP2C. 1 hit.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 3 hits.
    PROSITEi PS01032. PP2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-101 (ISOFORM 2).
      Tissue: Amygdala and Fetal brain.
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Testis.
    6. "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-202, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Pyruvate dehydrogenase phosphatase deficiency: identification of the first mutation in two brothers and restoration of activity by protein complementation."
      Maj M.C., MacKay N., Levandovskiy V., Addis J., Baumgartner E.R., Baumgartner M.R., Robinson B.H., Cameron J.M.
      J. Clin. Endocrinol. Metab. 90:4101-4107(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PDP DEFICIENCY LEU-284 DEL, CHARACTERIZATION OF VARIANT PDP DEFICIENCY LEU-284 DEL.

    Entry informationi

    Entry nameiPDP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9P0J1
    Secondary accession number(s): B3KX71, J3KPU0, Q5U5K1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: October 25, 2005
    Last modified: October 1, 2014
    This is version 129 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3