Seroatlas · Human Serome Atlas

PDP1

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

Also known as: PDH, PDP, PDP1_HUMAN, PPM2A, PPM2C

Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene

Protein identityUniProt · HPA

UniProt accession
Q9P0J1
Gene
PDP1
Ensembl
ENSG00000164951
Chromosome
8
Canonical length
537 aa
Protein class
Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Plasma proteins, Potential drug targets, Predicted intracellular proteins
Subcellular location
Nucleoplasm,Mitochondria,Cytosol

OverviewNCBI Gene

Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvate dehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvate dehydrogenase kinases. Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits. Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle and another one is is much more abundant in the liver. The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily. Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial matrix. Mutation in this gene causes pyruvate dehydrogenase phosphatase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been identified.[provided by RefSeq, Jun 2009]

Canonical amino-acid sequenceUniProt

537 residues, UniProt reviewed canonical sequence.

>Q9P0J1|PDP1
     1  MPAPTQLFFP LIRNCELSRI YGTACYCHHK HLCCSSSYIP QSRLRYTPHP AYATFCRPKE
    61  NWWQYTQGRR YASTPQKFYL TPPQVNSILK ANEYSFKVPE FDGKNVSSIL GFDSNQLPAN
   121  APIEDRRSAA TCLQTRGMLL GVFDGHAGCA CSQAVSERLF YYIAVSLLPH ETLLEIENAV
   181  ESGRALLPIL QWHKHPNDYF SKEASKLYFN SLRTYWQELI DLNTGESTDI DVKEALINAF
   241  KRLDNDISLE AQVGDPNSFL NYLVLRVAFS GATACVAHVD GVDLHVANTG DSRAMLGVQE
   301  EDGSWSAVTL SNDHNAQNER ELERLKLEHP KSEAKSVVKQ DRLLGLLMPF RAFGDVKFKW
   361  SIDLQKRVIE SGPDQLNDNE YTKFIPPNYH TPPYLTAEPE VTYHRLRPQD KFLVLATDGL
   421  WETMHRQDVV RIVGEYLTGM HHQQPIAVGG YKVTLGQMHG LLTERRTKMS SVFEDQNAAT
   481  HLIRHAVGNN EFGTVDHERL SKMLSLPEEL ARMYRDDITI IVVQFNSHVV GAYQNQE

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against PDP1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability
Intracellular
Secreted
No
Transmembrane segments
0
Mean surface accessibility (rSASA)
0.32
Highest tissue expression
68 nTPM

Expression across tissuesHPA

Tissue

  • skeletal muscle: 68 nTPM
  • adrenal gland: 59 nTPM
  • heart muscle: 46 nTPM
  • cerebral cortex: 43 nTPM
  • parathyroid gland: 28 nTPM
  • testis: 25 nTPM

Single-cell type

  • early spermatids: 178 nCPM
  • adrenal cortex cells: 165 nCPM
  • cardiomyocytes: 107 nCPM
  • salivary duct cells: 95 nCPM
  • endometrial glandular cells: 93 nCPM
  • ocular epithelial cells: 91 nCPM

Immune cell

  • non-classical monocyte: 41 nTPM
  • T-reg: 35 nTPM
  • classical monocyte: 28 nTPM
  • intermediate monocyte: 25 nTPM
  • myeloid DC: 23 nTPM
  • naive B-cell: 18 nTPM

Brain region

  • cerebral cortex: 170 nTPM
  • white matter: 120 nTPM
  • basal ganglia: 105 nTPM
  • thalamus: 75 nTPM
  • hippocampal formation: 68 nTPM
  • choroid plexus: 64 nTPM

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about PDP1.

Disease | AllUniProt

Conditions PDP1 is implicated in, by any mechanism.

  • Pyruvate dehydrogenase phosphatase deficiency (PDP deficiency) MIM:608782

Disease | GeneticClinVar

6 pathogenic / likely-pathogenic of 205 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)
0.49
gnomAD pLI
0.45
gnomAD missense Z
1.62
DepMap mean gene effect
0.03
DepMap dependency class
none

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 10% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

Molecular functions

Cellular components

Protein domainsUniProt · Pfam · InterPro

KeywordsUniProt

Antibody and autoantibody relevanceSeroatlas analysis

Seroatlas reads PDP1 as an antibody target. Whether an autoantibody or antibody against PDP1 could matter depends on whether native PDP1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.

PDP1 is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.

Annotation status

The present source text does not explicitly label PDP1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.

Canonical record: https://seroatlas.com/gene/PDP1. Study-independent annotations aggregated from UniProt, Human Protein Atlas, PubMed, IEDB, Pfam, InterPro, Gene Ontology, AlphaFold, gnomAD, DepMap, ClinVar, TCGA. Catalog release seroatlas-reviewed-human-uniprot-20260313.

Seroatlas is the reference for exploring autoantibody and antibody serology at the human-protein level: the autoreactome and human serome, multiplex serology (HuProt, HuScan, VirScan, PhIP-Seq).

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