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PDHX pyruvate dehydrogenase complex component X [ Homo sapiens (human) ]

Gene ID: 8050, updated on 7-Feb-2016
Official Symbol
PDHXprovided by HGNC
Official Full Name
pyruvate dehydrogenase complex component Xprovided by HGNC
Primary source
HGNC:HGNC:21350
See related
Ensembl:ENSG00000110435; HPRD:02002; MIM:608769; Vega:OTTHUMG00000166491
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
E3BP; OPDX; PDX1; proX; DLDBP
Summary
The pyruvate dehydrogenase (PDH) complex is located in the mitochondrial matrix and catalyzes the conversion of pyruvate to acetyl coenzyme A. The PDH complex thereby links glycolysis to Krebs cycle. The PDH complex contains three catalytic subunits, E1, E2, and E3, two regulatory subunits, E1 kinase and E1 phosphatase, and a non-catalytic subunit, E3 binding protein (E3BP). This gene encodes the E3 binding protein subunit; also known as component X of the pyruvate dehydrogenase complex. This protein tethers E3 dimers to the E2 core of the PDH complex. Defects in this gene are a cause of pyruvate dehydrogenase deficiency which results in neurological dysfunction and lactic acidosis in infancy and early childhood. This protein is also a minor antigen for antimitochondrial antibodies. These autoantibodies are present in nearly 95% of patients with the autoimmune liver disease primary biliary cirrhosis (PBC). In PBC, activated T lymphocytes attack and destroy epithelial cells in the bile duct where this protein is abnormally distributed and overexpressed. PBC eventually leads to cirrhosis and liver failure. Alternative splicing results in multiple transcript variants encoding distinct isoforms.[provided by RefSeq, Oct 2009]
Orthologs
See PDHX in Epigenomics, MapViewer
Location:
11p13
Exon count:
12
Annotation release Status Assembly Chr Location
107 current GRCh38.p2 (GCF_000001405.28) 11 NC_000011.10 (34915829..34996128)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 11 NC_000011.9 (34937677..35017675)

Chromosome 11 - NC_000011.10Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC102723568 Neighboring gene uncharacterized LOC105376625 Neighboring gene uncharacterized LOC105376624 Neighboring gene APAF1 interacting protein Neighboring gene microRNA 1343 Neighboring gene uncharacterized LOC105376626 Neighboring gene uncharacterized LOC105376627

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

  • Glycolysis and Gluconeogenesis, organism-specific biosystem (from WikiPathways)
    Glycolysis and Gluconeogenesis, organism-specific biosystem
    Glycolysis and Gluconeogenesis
  • Glyoxylate metabolism and glycine degradation, organism-specific biosystem (from REACTOME)
    Glyoxylate metabolism and glycine degradation, organism-specific biosystemGlyoxylate is generated in the course of glycine and hydroxyproline catabolism and can be converted to oxalate. In humans, this process takes place in the liver. Defects in two enzymes of glyoxylate ...
  • Metabolic pathways, organism-specific biosystem (from KEGG)
    Metabolic pathways, organism-specific biosystem
    Metabolic pathways
  • Metabolism, organism-specific biosystem (from REACTOME)
    Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
  • Metabolism of amino acids and derivatives, organism-specific biosystem (from REACTOME)
    Metabolism of amino acids and derivatives, organism-specific biosystemThis group of reactions is responsible for: 1) the breakdown of amino acids; 2) the synthesis of urea from ammonia and amino groups generated by amino acid breakdown; 3) the synthesis of the ten amin...
  • Pyruvate metabolism, organism-specific biosystem (from REACTOME)
    Pyruvate metabolism, organism-specific biosystemPyruvate sits at an intersection of key pathways of energy metabolism. It is the end product of glycolysis and the starting point for gluconeogenesis, and can be generated by transamination of alanin...
  • Pyruvate metabolism and Citric Acid (TCA) cycle, organism-specific biosystem (from REACTOME)
    Pyruvate metabolism and Citric Acid (TCA) cycle, organism-specific biosystemPyruvate metabolism and the citric acid (TCA) cycle together link the processes of energy metabolism in a human cell with one another and with key biosynthetic reactions. Pyruvate, derived from the r...
  • Regulation of pyruvate dehydrogenase (PDH) complex, organism-specific biosystem (from REACTOME)
    Regulation of pyruvate dehydrogenase (PDH) complex, organism-specific biosystemThe mitochondrial pyruvate dehydrogenase (PDH) complex catalyzes the oxidative decarboxylation of pyruvate, linking glycolysis to the tricarboxylic acid cycle and fatty acid synthesis. PDH inactivati...
  • Signal Transduction, organism-specific biosystem (from REACTOME)
    Signal Transduction, organism-specific biosystemSignal transduction is a process in which extracellular signals elicit changes in cell state and activity. Transmembrane receptors sense changes in the cellular environment by binding ligands, such a...
  • Signaling by Retinoic Acid, organism-specific biosystem (from REACTOME)
    Signaling by Retinoic Acid, organism-specific biosystemVitamin A (retinol) can be metabolised into active retinoid metabolites that function either as a chromophore in vision or in regulating gene expression transcriptionally and post-transcriptionally. ...
  • The citric acid (TCA) cycle and respiratory electron transport, organism-specific biosystem (from REACTOME)
    The citric acid (TCA) cycle and respiratory electron transport, organism-specific biosystemThe metabolism of pyruvate provides one source of acetyl-CoA which enters the citric acid (TCA, tricarboxylic acid) cycle to generate energy and the reducing equivalent NADH. These reducing equivalen...
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
contributes_to pyruvate dehydrogenase (NAD+) activity IDA
Inferred from Direct Assay
more info
PubMed 
transferase activity, transferring acyl groups IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
mitochondrial matrix TAS
Traceable Author Statement
more info
 
pyruvate dehydrogenase complex IDA
Inferred from Direct Assay
more info
PubMed 
Preferred Names
pyruvate dehydrogenase protein X component, mitochondrial
Names
dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex
lipoyl-containing pyruvate dehydrogenase complex component X
pyruvate dehydrogenase complex, E3-binding protein subunit
pyruvate dehydrogenase complex, component X
pyruvate dehydrogenase complex, lipoyl-containing component X

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_013368.1 RefSeqGene

    Range
    5001..84999
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001135024.1NP_001128496.1  pyruvate dehydrogenase protein X component, mitochondrial isoform 2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) lacks a segment in the 5' region, resulting in upstream in-frame AUG start codon, as compared to variant 1. The resulting isoform (2) has a shorter and distinct N-terminus, as compared to isoform 1.
    Source sequence(s)
    AA282215, BI915296, DA573433, U79296
    Consensus CDS
    CCDS44569.1
    UniProtKB/Swiss-Prot
    O00330
    Related
    ENSP00000389404, OTTHUMP00000233038, ENST00000448838, OTTHUMT00000390016
    Conserved Domains (4) summary
    cd06849
    Location:42116
    lipoyl_domain; Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid ...
    pfam00198
    Location:276485
    2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
    pfam02817
    Location:166203
    E3_binding; e3 binding domain
    TIGR01349
    Location:43485
    PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form
  2. NM_001166158.1NP_001159630.1  pyruvate dehydrogenase protein X component, mitochondrial isoform 3 precursor

    See identical proteins and their annotated locations for NP_001159630.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) lacks multiple in-frame exons in the central coding region, compared to variant 1, resulting in a protein (isoform 3) that lacks 227 aa, compared to isoform 1.
    Source sequence(s)
    AA282215, AC107928, AF001437, BC010389
    Consensus CDS
    CCDS53616.1
    UniProtKB/Swiss-Prot
    O00330
    Conserved Domains (3) summary
    cd06849
    Location:57114
    lipoyl_domain; Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid ...
    PRK11856
    Location:56273
    PRK11856; branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
    pfam00198
    Location:109273
    2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
  3. NM_003477.2NP_003468.2  pyruvate dehydrogenase protein X component, mitochondrial isoform 1 precursor

    See identical proteins and their annotated locations for NP_003468.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) encodes the longest isoform (1).
    Source sequence(s)
    AA282215, AC107928, AF001437, BC010389
    Consensus CDS
    CCDS7896.1
    UniProtKB/Swiss-Prot
    O00330
    Related
    ENSP00000227868, OTTHUMP00000233039, ENST00000227868, OTTHUMT00000390017
    Conserved Domains (4) summary
    cd06849
    Location:57131
    lipoyl_domain; Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid ...
    pfam00198
    Location:291500
    2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
    pfam02817
    Location:181218
    E3_binding; e3 binding domain
    TIGR01349
    Location:58500
    PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 107

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p2 Primary Assembly

Genomic

  1. NC_000011.10 Reference GRCh38.p2 Primary Assembly

    Range
    34915829..34996128
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011520390.1XP_011518692.1  

    Conserved Domains (4) summary
    cd06849
    Location:171
    lipoyl_domain; Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid ...
    pfam00198
    Location:231440
    2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
    pfam02817
    Location:121158
    E3_binding; e3 binding domain
    TIGR01349
    Location:1440
    PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form

Alternate CHM1_1.1

Genomic

  1. NC_018922.2 Alternate CHM1_1.1

    Range
    34935934..35015929
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)