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Q9P0J1

- PDP1_HUMAN

UniProt

Q9P0J1 - PDP1_HUMAN

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Protein
[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
Gene
PDP1, PDP, PPM2C
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi144 – 1441Magnesium 2 By similarity
Metal bindingi145 – 1451Magnesium 1; via carbonyl oxygen By similarity
Metal bindingi418 – 4181Magnesium 2 By similarity
Metal bindingi516 – 5161Magnesium 1 By 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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

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.
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 – 7171Mitochondrion By similarity
Add
BLAST
Chaini72 – 537466[Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 1, mitochondrial
PRO_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.

Family & Domainsi

Sequence similaritiesi

Belongs to the PP2C family.

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.

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.
VSP_046869

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 11612NVSSI…FDSNQ → MSVLSLDLTAIK in AAF67480. 1 Publication
Add
BLAST
Sequence conflicti151 – 1511C → W in AAF67480. 1 Publication
Sequence conflicti165 – 1651V → G in AAF67480. 1 Publication
Sequence conflicti168 – 1681L → V in AAF67480. 1 Publication
Sequence conflicti537 – 5371E → EK in AAF67480. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 128 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

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