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UniProtKB/Swiss-Prot entry P08559

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ODPA_HUMAN
Primary accession number P08559
Secondary accession numbers Q9NP12 Q9UBJ8 Q9UBU0 Q9UNG4 Q9UNG5
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on May 1, 1992 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 113)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial [Precursor]
Synonyms EC 1.2.4.1
PDHE1-A type I
Gene name
Name: PDHA1
Synonyms: PHE1A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
DOI=10.1016/0378-1119(90)90241-I; PubMed=2227443 [NCBI, ExPASy, EBI, Israel, Japan]
Koike K., Urata Y., Matsuo S., Koike M.;
"Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit.";
Gene 93:307-311(1990).
[2]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2748588 [NCBI, ExPASy, EBI, Israel, Japan]
Ho L., Wexler I.D., Liu T.C., Thekkumkara T.J., Patel M.S.;
"Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit.";
Proc. Natl. Acad. Sci. U.S.A. 86:5330-5334(1989).
[3]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain, and Liver;
Huh T.L., Chi Y.T., Casazza J.P., Veech R.L., Song B.J.;
Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3034892 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl H.-H.M., Hunt S.M., Hutchison W.M., Brown G.K.;
"The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA.";
J. Biol. Chem. 262:7398-7403(1987).
[5]
 SEQUENCE REVISION.
PubMed=2745444 [NCBI, ExPASy, EBI, Israel, Japan]
Maragos C., Hutchinson W.M., Hayasaki K., Brown G.K., Dahl H.-H.M.;
"Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex.";
J. Biol. Chem. 264:12294-12298(1989).
[6]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2828359 [NCBI, ExPASy, EBI, Israel, Japan]
de Meirleir L., MacKay N., Wah A.M.L.H., Robinson B.H.;
"Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex.";
J. Biol. Chem. 263:1991-1995(1988).
[7]
 NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3422424 [NCBI, ExPASy, EBI, Israel, Japan]
Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.;
"Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988).
[8]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-336, AND VARIANT LEU-282.
DOI=10.1073/pnas.96.6.3320; PubMed=10077682 [NCBI, ExPASy, EBI, Israel, Japan]
Harris E.E., Hey J.;
"X chromosome evidence for ancient human histories.";
Proc. Natl. Acad. Sci. U.S.A. 96:3320-3324(1999).
[10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASS SPECTROMETRY.
DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan]
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line.";
Electrophoresis 28:2027-2034(2007).
[13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-293, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[14]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293; SER-295 AND SER-300, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[15]
 X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THIAMINE PYROPHOSPHATE.
DOI=10.1074/jbc.M300339200; PubMed=12651851 [NCBI, ExPASy, EBI, Israel, Japan]
Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.;
"Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase.";
J. Biol. Chem. 278:21240-21246(2003).
[16]
 REVIEW ON VARIANTS.
PubMed=1301207 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl H.-H.M., Brown G.K., Brown R.M., Hansen L.L., Kerr D.S., Wexler I.D., Patel M.S., de Meirleir L., Lissens W., Chun K., McKay N., Robinson B.H.;
"Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene.";
Hum. Mutat. 1:97-102(1992).
[17]
 VARIANT PDHE1 DEFICIENCY LYS-313 DEL, AND VARIANT LS HIS-378.
DOI=10.1007/BF01800586; PubMed=1909401 [NCBI, ExPASy, EBI, Israel, Japan]
Hansen L.L., Brown G.K., Kirby D.M., Dahl H.-H.M.;
"Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency.";
J. Inherit. Metab. Dis. 14:140-151(1991).
[18]
 VARIANT PDHE1 DEFICIENCY ASP-SER-TYR-ARG-THR-ARG-GLU-305 INS.
DOI=10.1007/BF02265291; PubMed=1551669 [NCBI, ExPASy, EBI, Israel, Japan]
De Meirleir L., Lissens W., Vamos E., Liebaers I.;
"Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit.";
Hum. Genet. 88:649-652(1992).
[19]
 VARIANT PDHE1 DEFICIENCY CYS-302.
DOI=10.1007/BF01800219; PubMed=1293379 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl H.-H.M., Hansen L.L., Brown R.M., Danks D.M., Rogers J.G., Brown G.K.;
"X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation.";
J. Inherit. Metab. Dis. 15:835-847(1992).
[20]
 INVOLVEMENT IN PDHE1 DEFICIENCY.
DOI=10.1007/BF01800220; PubMed=1338114 [NCBI, ExPASy, EBI, Israel, Japan]
Ito M., Huq A.H., Naito E., Saijo T., Takeda E., Kuroda Y.;
"Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein.";
J. Inherit. Metab. Dis. 15:848-856(1992).
[21]
 VARIANT LS ALA-258.
PubMed=8498846 [NCBI, ExPASy, EBI, Israel, Japan]
Matthews P.M., Marchington D.R., Squier M., Land J., Brown R.M., Brown G.K.;
"Molecular genetic characterization of an X-linked form of Leigh's syndrome.";
Ann. Neurol. 33:652-655(1993).
[22]
 VARIANTS PDHE1 DEFICIENCY MET-167; THR-199; ALA-231; GLY-263 AND LEU-292.
DOI=10.1093/hmg/2.4.449; PubMed=8504306 [NCBI, ExPASy, EBI, Israel, Japan]
Chun K., McKay N., Petrova-Benedict R., Robinson B.H.;
"Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex.";
Hum. Mol. Genet. 2:449-454(1993).
[23]
 VARIANTS PDHE1 DEFICIENCY ASN-243; ASN-315 AND HIS-378, AND VARIANT LEU-282.
DOI=10.1093/brain/117.3.435; PubMed=8032855 [NCBI, ExPASy, EBI, Israel, Japan]
Matthews P.M., Brown R.M., Otero L.J., Marchington D.R., LeGris M., Howes R., Meadows L.S., Shevell M., Scriver C.R., Brown G.K.;
"Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients.";
Brain 117:435-443(1994).
[24]
 VARIANT PDHE1 DEFICIENCY PRO-PRO-HIS-SER-TYR-ARG-THR-ARG-GLU-GLU-ILE-307 INS.
DOI=10.1093/hmg/3.6.1021; PubMed=7545958 [NCBI, ExPASy, EBI, Israel, Japan]
Hansen L.L., Horn N., Dahl H.H., Kruse T.A.;
"Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit.";
Hum. Mol. Genet. 3:1021-1022(1994).
[25]
 VARIANT LS LEU-205.
PubMed=8199595 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl H.-H.M., Brown G.K.;
"Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit.";
Hum. Mutat. 3:152-155(1994).
[26]
 VARIANT PDHE1 DEFICIENCY GLN-263.
DOI=10.1007/BF00711616; PubMed=7967473 [NCBI, ExPASy, EBI, Israel, Japan]
Awata H., Endo F., Tanoue A., Kitano A., Matsuda I.;
"Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia.";
J. Inherit. Metab. Dis. 17:189-195(1994).
[27]
 VARIANTS PDHE1 DEFICIENCY CYS-72; GLY-263 AND ARG-311 DEL, AND VARIANTS LS LEU-205 AND HIS-378.
PubMed=7887409 [NCBI, ExPASy, EBI, Israel, Japan]
Chun K., MacKay N., Petrova-Benedict R., Federico A., Fois A., Cole D.E.C., Robertson E., Robinson B.H.;
"Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex.";
Am. J. Hum. Genet. 56:558-569(1995).
[28]
 VARIANT PDHE1 DEFICIENCY PRO-10.
PubMed=7573035 [NCBI, ExPASy, EBI, Israel, Japan]
Takakubo F., Cartwright P., Hoogenraad N., Thorburn D.R., Collins F., Lithgow T., Dahl H.H.;
"An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein.";
Am. J. Hum. Genet. 57:772-780(1995).
[29]
 VARIANT PDHE1 DEFICIENCY LEU-217.
DOI=10.1093/hmg/4.2.315; PubMed=7757088 [NCBI, ExPASy, EBI, Israel, Japan]
Hemalatha S.G., Kerr D.S., Wexler I.D., Lusk M.M., Kaung M., Du Y., Kolli M., Schelper R.L., Patel M.S.;
"Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit.";
Hum. Mol. Genet. 4:315-318(1995).
[30]
 VARIANTS PDHE1 DEFICIENCY CYS-72; ASP-113; ARG-162; GLY-263; HIS-288 AND CYS-302.
DOI=10.1002/(SICI)1098-1004(1996)7:1<46::AID-HUMU6>3.3.CO;2-2; PubMed=8664900 [NCBI, ExPASy, EBI, Israel, Japan]
Lissens W., de Meirleir L., Seneca S., Benelli C., Marsac C., Poll-The B.T., Briones P., Ruitenbeek W., van Diggelen O., Chaigne D., Ramaekers V., Liebaers I.;
"Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency.";
Hum. Mutat. 7:46-51(1996).
[31]
 VARIANTS PDHE1 DEFICIENCY VAL-210 AND ARG-311 DEL.
DOI=10.1002/(SICI)1098-1004(1996)8:2<180::AID-HUMU11>3.3.CO;2-O; PubMed=8844217 [NCBI, ExPASy, EBI, Israel, Japan]
Tripatara A., Kerr D.S., Lusk M.M., Kolli M., Tan J., Patel M.S.;
"Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS).";
Hum. Mutat. 8:180-182(1996).
[32]
 VARIANT LS GLY-263.
DOI=10.1023/A:1005305614374; PubMed=9266390 [NCBI, ExPASy, EBI, Israel, Japan]
Naito E., Ito M., Yokota I., Saijo T., Matsuda J., Osaka H., Kimura S., Kuroda Y.;
"Biochemical and molecular analysis of an X-linked case of Leigh syndrome associated with thiamin-responsive pyruvate dehydrogenase deficiency.";
J. Inherit. Metab. Dis. 20:539-548(1997).
[33]
 VARIANTS PDHE1 DEFICIENCY CYS-302 AND HIS-302.
DOI=10.1002/(SICI)1098-1004(1998)12:2<114::AID-HUMU6>3.0.CO;2-#; PubMed=9671272 [NCBI, ExPASy, EBI, Israel, Japan]
Otero L.J., Brown R.M., Brown G.K.;
"Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity.";
Hum. Mutat. 12:114-121(1998).
Comments
  • FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
  • CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
  • COFACTOR: Thiamine pyrophosphate.
  • ENZYME REGULATION: E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.
  • SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
  • INTERACTION:
    P52429:DGKE; NbExp=1; IntAct=EBI-715747, EBI-1057499;
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • TISSUE SPECIFICITY: Ubiquitous.
  • DISEASE: Defects in PDHA1 are a cause of pyruvate decarboxylase E1 component deficiency (PDHE1 deficiency) [MIM:312170]. PDHE1 deficiency is the most common enzyme defect in patients with primary lactic acidosis. It is associated with variable clinical phenotypes ranging from neonatal death to prolonged survival complicated by developmental delay, seizures, ataxia, apnea, and in some cases to an X-linked form of Leigh syndrome (LS) (Leigh encephalomyelopathy).
  • DISEASE: Defects in PDHA1 are the cause of X-linked Leigh syndrome (LS) [MIM:308930]. LS is an early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes.
  • SEQUENCE CAUTION:
    • Sequence=AAB59581.1; Type=Frameshift; Positions=106, 175;
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=PDHA1";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D90084; BAA14121.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24848; AAA36533.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52709; CAA36933.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X52710; CAA36934.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27257; AAA60051.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29155; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29156; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29157; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29158; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29159; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29160; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29161; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29162; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29163; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M29164; AAA60051.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L13318; AAA60227.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03503; AAA60055.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03575; AAA60050.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L48690; AAB59581.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002406; AAH02406.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125053; AAD23841.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125054; AAD23842.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125055; AAD23843.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125056; AAD23844.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125057; AAD23845.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125058; AAD23846.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125059; AAD23847.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125060; AAD23848.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125061; AAD23849.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125062; AAD23850.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125063; AAD23851.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125064; AAD23852.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125065; AAD23853.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125066; AAD23854.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125067; AAD23855.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125068; AAD23856.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125069; AAD23857.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125070; AAD23858.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125071; AAD23859.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125072; AAD23860.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125073; AAD23861.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125074; AAD23862.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125075; AAD23863.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125076; AAD23864.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125078; AAD23866.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125079; AAD23867.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125080; AAD23868.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125081; AAD23869.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125082; AAD23870.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125083; AAD23871.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125084; AAD23872.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125085; AAD23873.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125086; AAD23874.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125087; AAD23875.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125088; AAD23876.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JQ0770; DEHUPA.
RefSeq NP_000275.1; -.
UniGene Hs.530331
3D structure databases
PDB
1NI4; X-ray; 1.95 A; A/C=30-390.[ExPASy / RCSB / EBI]
2OZL; X-ray; 1.90 A; A/C=29-390.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1NI4; -.
2OZL; -.
ModBase P08559.
Protein-protein interaction databases
IntAct P08559; -.
PTM databases
PhosphoSite P08559; -.
Enzyme and pathway databases
Reactome REACT_1046; Pyruvate metabolism and TCA cycle.
2D gel databases
REPRODUCTION-2DPAGE IPI00306301; -.
Organism-specific databases
H-InvDB HIX0016687; -.
HGNC HGNC:8806; PDHA1.
GenAtlas PDHA1.
MIM 300502; gene. [NCBI / EBI]
308930; phenotype. [NCBI / EBI]
312170; phenotype. [NCBI / EBI]
Orphanet 506; Leigh syndrome.
2597; Mitochondrial myopathy - lactic acidosis.
765; Pyruvate dehydrogenase deficiency.
PharmGKB PA33150; -.
GeneCards P08559.
Gene expression databases
ArrayExpress P08559; -.
CleanEx HS_PDHA1; -.
GermOnline ENSG00000131828; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001017; DHase_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.
Graphical view of domain structure.
Pfam PF00676; E1_dh; 1.
Pfam graphical view of domain structure.
BLOCKS P08559.
Proteomic databases
PeptideAtlas P08559; -.
Genome annotation databases
Ensembl ENSG00000131828; Homo sapiens. [Contig view]
GeneID 5160; -.
KEGG hsa:5160; -.
Phylogenomic databases
HOGENOM P08559; -.
HOVERGEN P08559; -.
Other
DrugBank DB00157; NADH.
LinkHub P08559; -.
SOURCE PDHA1; Homo sapiens.
ProtoNet P08559.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Disease mutation; Glycolysis; Leigh syndrome; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    29  29     Mitochondrion. 
CHAIN   30   390  361     Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial. PRO_0000020440
MOD_RES   232   232        Phosphoserine. 
MOD_RES   289   289        Phosphotyrosine (By similarity). 
MOD_RES   293   293        Phosphoserine. 
MOD_RES   295   295        Phosphoserine. 
MOD_RES   300   300        Phosphoserine. 
MOD_RES   301   301        Phosphotyrosine (By similarity). 
VARIANT   10    10  1     R -> P (in PDHE1 deficiency; affects mitochondrial import of precursor protein). VAR_010238 
VARIANT   72    72  1     R -> C (in PDHE1 deficiency). VAR_004949 [3D]
VARIANT   113   113  1     H -> D (in PDHE1 deficiency). VAR_004950 [3D]
VARIANT   162   162  1     G -> R (in PDHE1 deficiency). VAR_004951 [3D]
VARIANT   167   167  1     V -> M (in PDHE1 deficiency). VAR_004952 [3D]
VARIANT   199   199  1     A -> T (in PDHE1 deficiency). VAR_004953 [3D]
VARIANT   205   205  1     F -> L (in LS; PDHE1 deficiency). VAR_004954 [3D]
VARIANT   210   210  1     M -> V (in PDHE1 deficiency). VAR_004955 [3D]
VARIANT   217   217  1     P -> L (in PDHE1 deficiency). VAR_004956 [3D]
VARIANT   231   231  1     T -> A (in PDHE1 deficiency). VAR_004957 [3D]
VARIANT   243   243  1     Y -> N (in PDHE1 deficiency). VAR_021053 [3D]
VARIANT   258   258  1     D -> A (in LS; PDHE1 deficiency). VAR_004958 [3D]
VARIANT   263   263  1     R -> G (in PDHE1 deficiency and LS). VAR_004959 [3D]
VARIANT   263   263  1     R -> Q (in PDHE1 deficiency). VAR_004960 [3D]
VARIANT   282   282  1     M -> L (in dbSNP:rs3810710 [NCBI]). VAR_021054 [3D]
VARIANT   288   288  1     R -> H (in PDHE1 deficiency). VAR_021055 [3D]
VARIANT   292   292  1     H -> L (in PDHE1 deficiency). VAR_004961 [3D]
VARIANT   302   302  1     R -> C (in PDHE1 deficiency; loss of activity; common mutation). VAR_004962 [3D]
VARIANT   302   302  1     R -> H (in PDHE1 deficiency). VAR_004963 [3D]
VARIANT   305   305  1     E -> EDSYRTRE (in PDHE1 deficiency). VAR_020908
VARIANT   307   307  1     I -> IPPHSYRTREEI (in PDHE1 deficiency). VAR_020909
VARIANT   311   311  1     Missing (in PDHE1 deficiency). VAR_004964
VARIANT   313   313