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

    Gene ID: 8050, updated on 12-Oct-2019

    Summary

    Official Symbol
    PDHXprovided by HGNC
    Official Full Name
    pyruvate dehydrogenase complex component Xprovided by HGNC
    Primary source
    HGNC:HGNC:21350
    See related
    Ensembl:ENSG00000110435 MIM:608769
    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; PDHXD
    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]
    Expression
    Ubiquitous expression in heart (RPKM 24.7), testis (RPKM 13.6) and 25 other tissues See more
    Orthologs

    Genomic context

    See PDHX in Genome Data Viewer
    Location:
    11p13
    Exon count:
    12
    Annotation release Status Assembly Chr Location
    109.20190905 current GRCh38.p13 (GCF_000001405.39) 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

    Genomic regions, transcripts, and products

    Expression

    • Project title: HPA RNA-seq normal tissues
    • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
    • BioProject: PRJEB4337
    • Publication: PMID 24309898
    • Analysis date: Wed Apr 4 07:08:55 2018

    Bibliography

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?

    Pathways from BioSystems

    • Amino Acid metabolism, organism-specific biosystem (from WikiPathways)
      Amino Acid metabolism, organism-specific biosystemA complete overview of the metabolism of all 20 amino acids
    • Glycolysis and Gluconeogenesis, organism-specific biosystem (from WikiPathways)
      Glycolysis and Gluconeogenesis, organism-specific biosystemGlycolysis is the metabolic pathway that converts glucose C6H12O6, into pyruvate, CH3COCOO? + H+. The free energy released in this process is used to form the ATP and NADH. Gluconeogenesis is a metab...
    • 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...

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    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
     
    Process Evidence Code Pubs
    mitochondrial acetyl-CoA biosynthetic process from pyruvate IC
    Inferred by Curator
    more info
    PubMed 
    pyruvate metabolic process TAS
    Traceable Author Statement
    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 

    General protein information

    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, lipoyl-containing component X
    NP_001128496.1
    NP_001159630.1
    NP_003468.2
    XP_011518692.1

    NCBI Reference Sequences (RefSeq)

    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
      5489..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
      ENSP00000389404.2, ENST00000448838.7
      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 ...
      TIGR01349
      Location:43485
      PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form
      pfam00198
      Location:276485
      2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
      pfam02817
      Location:168200
      E3_binding; e3 binding domain
    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
      Related
      ENSP00000415695.2, ENST00000430469.6
      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_003477.3NP_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
      ENSP00000227868.4, ENST00000227868.9
      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 ...
      TIGR01349
      Location:58500
      PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form
      pfam00198
      Location:291500
      2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
      pfam02817
      Location:183215
      E3_binding; e3 binding domain

    RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109.20190905

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

    Reference GRCh38.p13 Primary Assembly

    Genomic

    1. NC_000011.10 Reference GRCh38.p13 Primary Assembly

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

    mRNA and Protein(s)

    1. XM_011520390.1XP_011518692.1  pyruvate dehydrogenase protein X component, mitochondrial isoform X1

      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 ...
      TIGR01349
      Location:1440
      PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form
      pfam00198
      Location:231440
      2-oxoacid_dh; 2-oxoacid dehydrogenases acyltransferase (catalytic domain)
      pfam02817
      Location:123155
      E3_binding; e3 binding domain
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