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P08559 (ODPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

EC=1.2.4.1
Alternative name(s):
PDHE1-A type I
Gene names
Name:PDHA1
Synonyms:PHE1A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle. Ref.16 Ref.31

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.16 Ref.30 Ref.31

Cofactor

Thiamine pyrophosphate. Ref.28 Ref.31

Enzyme regulation

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation. Ref.16 Ref.30 Ref.31

Subunit structure

Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Ref.18 Ref.31

Subcellular location

Mitochondrion matrix.

Tissue specificity

Ubiquitous.

Post-translational modification

Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.

Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 By similarity.

Involvement in disease

Pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:312170]: An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47

Leigh syndrome, X-linked (X-LS) [MIM:308930]: A X-linked form of Leigh syndrome, an early-onset progressive neurodegenerative disorder characterized by the presence 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 and include psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, dysphagia, and lactic acidosis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32 Ref.35 Ref.39 Ref.41 Ref.46

Sequence caution

The sequence AAA60055.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAB59581.1 differs from that shown. Reason: Frameshift at positions 106 and 175.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Tricarboxylic acid cycle
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Leigh syndrome
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetyl-CoA biosynthetic process from pyruvate

Inferred from direct assay Ref.31. Source: UniProtKB

cellular metabolic process

Traceable author statement. Source: Reactome

glycolysis

Inferred from electronic annotation. Source: InterPro

pyruvate metabolic process

Traceable author statement. Source: Reactome

regulation of acetyl-CoA biosynthetic process from pyruvate

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

tricarboxylic acid cycle

Inferred from direct assay Ref.31. Source: UniProtKB

   Cellular_componentintracellular membrane-bounded organelle

Inferred from electronic annotation. Source: InterPro

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay PubMed 20833797. Source: UniProt

pyruvate dehydrogenase complex

Inferred from direct assay Ref.31. Source: UniProtKB

   Molecular_functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

pyruvate dehydrogenase activity

Inferred from direct assay Ref.31. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P08559-1)

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.
Isoform 2 (identifier: P08559-2)

The sequence of this isoform differs from the canonical sequence as follows:
     96-96: G → GQFLLPLT
Note: No experimental confirmation available.
Isoform 3 (identifier: P08559-3)

The sequence of this isoform differs from the canonical sequence as follows:
     170-200: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P08559-4)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: P → PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLKTRQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion
Chain30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000020440

Amino acid modifications

Modified residue631N6-acetyllysine; alternate By similarity
Modified residue631N6-succinyllysine; alternate By similarity
Modified residue2321Phosphoserine; by PDK1 Ref.17 Ref.25 Ref.27
Modified residue2441N6-acetyllysine; alternate By similarity
Modified residue2441N6-succinyllysine; alternate By similarity
Modified residue2771N6-succinyllysine By similarity
Modified residue2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.17 Ref.30 Ref.31
Modified residue2951Phosphoserine By similarity
Modified residue3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.17 Ref.31
Modified residue3011Phosphotyrosine By similarity
Modified residue3131N6-acetyllysine; alternate By similarity
Modified residue3131N6-succinyllysine; alternate By similarity
Modified residue3211N6-acetyllysine Ref.24
Modified residue3361N6-acetyllysine By similarity
Modified residue3851N6-succinyllysine By similarity

Natural variations

Alternative sequence191P → PRHGLATLPSLVSISRLKQS SHLGLPKCWDYSHSLKTRQ in isoform 4.
VSP_043363
Alternative sequence961G → GQFLLPLT in isoform 2.
VSP_042569
Alternative sequence170 – 20031Missing in isoform 3.
VSP_042570
Natural variant101R → P in PDHAD; affects mitochondrial import of precursor protein. Ref.42
VAR_010238
Natural variant721R → C in PDHAD. Ref.41 Ref.44
VAR_004949
Natural variant1131H → D in PDHAD. Ref.44
VAR_004950
Natural variant1361A → T Probable disease-associated mutation found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate. Ref.48
VAR_069381
Natural variant1621G → R in PDHAD. Ref.44
VAR_004951
Natural variant1671V → M in PDHAD. Ref.36
VAR_004952
Natural variant1991A → T in PDHAD. Ref.36
VAR_004953
Natural variant2051F → L in X-LS; PDHAD. Ref.39 Ref.41
VAR_004954
Natural variant2101M → V in PDHAD. Ref.45
VAR_004955
Natural variant2171P → L in PDHAD. Ref.43
VAR_004956
Natural variant2311T → A in PDHAD. Ref.36
VAR_004957
Natural variant2431Y → N in PDHAD. Ref.37
VAR_021053
Natural variant2581D → A in X-LS; PDHAD. Ref.35
VAR_004958
Natural variant2631R → G in PDHAD and X-LS. Ref.36 Ref.41 Ref.44 Ref.46
Corresponds to variant rs28936081 [ dbSNP | Ensembl ].
VAR_004959
Natural variant2631R → Q in PDHAD. Ref.40
VAR_004960
Natural variant2821M → L. Ref.10 Ref.14 Ref.37
Corresponds to variant rs2229137 [ dbSNP | Ensembl ].
VAR_021054
Natural variant2881R → H in PDHAD. Ref.44
VAR_021055
Natural variant2921H → L in PDHAD. Ref.36
VAR_004961
Natural variant3021R → C in PDHAD; loss of activity; common mutation. Ref.34 Ref.44 Ref.47
VAR_004962
Natural variant3021R → H in PDHAD. Ref.47
VAR_004963
Natural variant3051E → EDSYRTRE in PDHAD.
VAR_020908
Natural variant3071I → IPPHSYRTREEI in PDHAD.
VAR_020909
Natural variant3111Missing in PDHAD. Ref.41 Ref.45
VAR_004964
Natural variant3131Missing in PDHAD. Ref.32
VAR_004965
Natural variant3151D → N in PDHAD. Ref.37
Corresponds to variant rs28935187 [ dbSNP | Ensembl ].
VAR_021056
Natural variant3331E → D.
Corresponds to variant rs2228067 [ dbSNP | Ensembl ].
VAR_050436
Natural variant3781R → H in X-LS; PDHAD. Ref.32 Ref.37 Ref.41
VAR_004966

Experimental info

Mutagenesis2321S → A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300. Ref.16 Ref.30
Mutagenesis2931S → A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300. Ref.16 Ref.30
Mutagenesis2931S → E: Interferes with substrate binding. Ref.16 Ref.30
Mutagenesis3001S → A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293. Ref.16
Sequence conflict2781G → E in BAG35194. Ref.9
Sequence conflict3011Y → S in AAD23857. Ref.14
Sequence conflict3061E → D in AAD23857. Ref.14
Sequence conflict3491A → P in AAA60055. Ref.6
Sequence conflict3541T → A in AAA60055. Ref.6

Secondary structure

............................................................... 390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1992. Version 3.
Checksum: 4D685BBE44A92D4B

FASTA39043,296
        10         20         30         40         50         60 
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

        70         80         90        100        110        120 
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 

       130        140        150        160        170        180 
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

       190        200        210        220        230        240 
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 

       250        260        270        280        290        300 
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 

       310        320        330        340        350        360 
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 

« Hide

Isoform 2 [UniParc].

Checksum: 4BE156001F9994A5
Show »

FASTA39744,109
Isoform 3 [UniParc].

Checksum: 7E94F39FC1293065
Show »

FASTA35940,188
Isoform 4 [UniParc].

Checksum: 14FE765CFF2C7120
Show »

FASTA42847,580

References

« Hide 'large scale' references
[1]"Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit."
Koike K., Urata Y., Matsuo S., Koike M.
Gene 93:307-311(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Leukocyte.
[2]"Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit."
Ho L., Wexler I.D., Liu T.C., Thekkumkara T.J., Patel M.S.
Proc. Natl. Acad. Sci. U.S.A. 86:5330-5334(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Huh T.L., Chi Y.T., Casazza J.P., Veech R.L., Song B.J.
Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain and Liver.
[4]"The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA."
Dahl H.-H.M., Hunt S.M., Hutchison W.M., Brown G.K.
J. Biol. Chem. 262:7398-7403(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex."
Maragos C., Hutchinson W.M., Hayasaki K., Brown G.K., Dahl H.-H.M.
J. Biol. Chem. 264:12294-12298(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex."
de Meirleir L., MacKay N., Wah A.M.L.H., Robinson B.H.
J. Biol. Chem. 263:1991-1995(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]"Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase."
Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.
Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]Okajima K.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[9]"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. expand/collapse author list , 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] (ISOFORMS 1; 2; 3 AND 4).
Tissue: Thalamus.
[10]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-282.
Tissue: Dermoid cancer.
[11]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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: Muscle.
[14]"X chromosome evidence for ancient human histories."
Harris E.E., Hey J.
Proc. Natl. Acad. Sci. U.S.A. 96:3320-3324(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-336, VARIANT LEU-282.
[15]"Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein."
Ito M., Huq A.H., Naito E., Saijo T., Takeda E., Kuroda Y.
J. Inherit. Metab. Dis. 15:848-856(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PDHAD.
[16]"Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation."
Korotchkina L.G., Patel M.S.
J. Biol. Chem. 270:14297-14304(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-232; SER-293 AND SER-300.
[17]"Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase."
Korotchkina L.G., Patel M.S.
J. Biol. Chem. 276:37223-37229(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-232; SER-293 AND SER-300.
[18]"Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components."
Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.
J. Biol. Chem. 279:6921-6933(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[21]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase."
Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.
J. Biol. Chem. 278:21240-21246(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THIAMINE PYROPHOSPHATE, COFACTOR.
[29]"Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene."
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.
Hum. Mutat. 1:97-102(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[30]"Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex."
Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.
Biochemistry 46:6277-6287(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-390, ENZYME REGULATION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-293, PHOSPHORYLATION AT SER-293.
[31]"Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops."
Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J., Chuang D.T.
Structure 16:1849-1859(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-390 IN COMPLEX WITH PDHB, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, PHOSPHORYLATION AT SER-293 AND SER-300 BY PDK4.
[32]"Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency."
Hansen L.L., Brown G.K., Kirby D.M., Dahl H.-H.M.
J. Inherit. Metab. Dis. 14:140-151(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD LYS-313 DEL, VARIANT X-LS HIS-378.
[33]"Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit."
De Meirleir L., Lissens W., Vamos E., Liebaers I.
Hum. Genet. 88:649-652(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD ASP-SER-TYR-ARG-THR-ARG-GLU-305 INS.
[34]"X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation."
Dahl H.-H.M., Hansen L.L., Brown R.M., Danks D.M., Rogers J.G., Brown G.K.
J. Inherit. Metab. Dis. 15:835-847(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD CYS-302.
[35]"Molecular genetic characterization of an X-linked form of Leigh's syndrome."
Matthews P.M., Marchington D.R., Squier M., Land J., Brown R.M., Brown G.K.
Ann. Neurol. 33:652-655(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT X-LS ALA-258.
[36]"Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex."
Chun K., McKay N., Petrova-Benedict R., Robinson B.H.
Hum. Mol. Genet. 2:449-454(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDHAD MET-167; THR-199; ALA-231; GLY-263 AND LEU-292.
[37]"Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients."
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.
Brain 117:435-443(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDHAD ASN-243; ASN-315 AND HIS-378, VARIANT LEU-282.
[38]"Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit."
Hansen L.L., Horn N., Dahl H.-H.M., Kruse T.A.
Hum. Mol. Genet. 3:1021-1022(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD PRO-PRO-HIS-SER-TYR-ARG-THR-ARG-GLU-GLU-ILE-307 INS.
[39]"Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit."
Dahl H.-H.M., Brown G.K.
Hum. Mutat. 3:152-155(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT X-LS LEU-205.
[40]"Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia."
Awata H., Endo F., Tanoue A., Kitano A., Matsuda I.
J. Inherit. Metab. Dis. 17:189-195(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD GLN-263.
[41]"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."
Chun K., MacKay N., Petrova-Benedict R., Federico A., Fois A., Cole D.E.C., Robertson E., Robinson B.H.
Am. J. Hum. Genet. 56:558-569(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDHAD CYS-72; GLY-263 AND ARG-311 DEL, VARIANTS X-LS LEU-205 AND HIS-378.
[42]"An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein."
Takakubo F., Cartwright P., Hoogenraad N., Thorburn D.R., Collins F., Lithgow T., Dahl H.-H.M.
Am. J. Hum. Genet. 57:772-780(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD PRO-10.
[43]"Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit."
Hemalatha S.G., Kerr D.S., Wexler I.D., Lusk M.M., Kaung M., Du Y., Kolli M., Schelper R.L., Patel M.S.
Hum. Mol. Genet. 4:315-318(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PDHAD LEU-217.
[44]"Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency."
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.
Hum. Mutat. 7:46-51(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDHAD CYS-72; ASP-113; ARG-162; GLY-263; HIS-288 AND CYS-302.
[45]"Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS)."
Tripatara A., Kerr D.S., Lusk M.M., Kolli M., Tan J., Patel M.S.
Hum. Mutat. 8:180-182(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDHAD VAL-210 AND ARG-311 DEL.
[46]"Biochemical and molecular analysis of an X-linked case of Leigh syndrome associated with thiamin-responsive pyruvate dehydrogenase deficiency."
Naito E., Ito M., Yokota I., Saijo T., Matsuda J., Osaka H., Kimura S., Kuroda Y.
J. Inherit. Metab. Dis. 20:539-548(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT X-LS GLY-263.
[47]"Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity."
Otero L.J., Brown R.M., Brown G.K.
Hum. Mutat. 12:114-121(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PDHAD CYS-302 AND HIS-302.
[48]"Diagnostic exome sequencing in persons with severe intellectual disability."
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., Veltman J.A., Vissers L.E.
N. Engl. J. Med. 367:1921-1929(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT THR-136.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D90084 Genomic DNA. Translation: BAA14121.1.
M24848 mRNA. Translation: AAA36533.1.
X52709 mRNA. Translation: CAA36933.1.
X52710 mRNA. Translation: CAA36934.1.
M27257 expand/collapse EMBL AC list , M29155, M29156, M29157, M29158, M29159, M29160, M29161, M29162, M29163, M29164 Genomic DNA. Translation: AAA60051.1.
L13318 mRNA. Translation: AAA60227.1.
J03503 mRNA. Translation: AAA60055.1. Different initiation.
J03575 mRNA. Translation: AAA60050.1.
L48690 mRNA. Translation: AAB59581.1. Frameshift.
EF590117 mRNA. Translation: ABQ59099.1.
AK293250 mRNA. Translation: BAH11476.1.
AK296457 mRNA. Translation: BAH12361.1.
AK312263 mRNA. Translation: BAG35194.1.
AK296341 mRNA. Translation: BAH12323.1.
AK222740 mRNA. Translation: BAD96460.1.
AL732326 Genomic DNA. Translation: CAI41291.1.
CH471074 Genomic DNA. Translation: EAW98960.1.
BC002406 mRNA. Translation: AAH02406.1.
AF125053 Genomic DNA. Translation: AAD23841.1.
AF125054 Genomic DNA. Translation: AAD23842.1.
AF125055 Genomic DNA. Translation: AAD23843.1.
AF125056 Genomic DNA. Translation: AAD23844.1.
AF125057 Genomic DNA. Translation: AAD23845.1.
AF125058 Genomic DNA. Translation: AAD23846.1.
AF125059 Genomic DNA. Translation: AAD23847.1.
AF125060 Genomic DNA. Translation: AAD23848.1.
AF125061 Genomic DNA. Translation: AAD23849.1.
AF125062 Genomic DNA. Translation: AAD23850.1.
AF125063 Genomic DNA. Translation: AAD23851.1.
AF125064 Genomic DNA. Translation: AAD23852.1.
AF125065 Genomic DNA. Translation: AAD23853.1.
AF125066 Genomic DNA. Translation: AAD23854.1.
AF125067 Genomic DNA. Translation: AAD23855.1.
AF125068 Genomic DNA. Translation: AAD23856.1.
AF125069 Genomic DNA. Translation: AAD23857.1.
AF125070 Genomic DNA. Translation: AAD23858.1.
AF125071 Genomic DNA. Translation: AAD23859.1.
AF125072 Genomic DNA. Translation: AAD23860.1.
AF125073 Genomic DNA. Translation: AAD23861.1.
AF125074 Genomic DNA. Translation: AAD23862.1.
AF125075 Genomic DNA. Translation: AAD23863.1.
AF125076 Genomic DNA. Translation: AAD23864.1.
AF125078 Genomic DNA. Translation: AAD23866.1.
AF125079 Genomic DNA. Translation: AAD23867.1.
AF125080 Genomic DNA. Translation: AAD23868.1.
AF125081 Genomic DNA. Translation: AAD23869.1.
AF125082 Genomic DNA. Translation: AAD23870.1.
AF125083 Genomic DNA. Translation: AAD23871.1.
AF125084 Genomic DNA. Translation: AAD23872.1.
AF125085 Genomic DNA. Translation: AAD23873.1.
AF125086 Genomic DNA. Translation: AAD23874.1.
AF125087 Genomic DNA. Translation: AAD23875.1.
AF125088 Genomic DNA. Translation: AAD23876.1.
PIRDEHUPA. JQ0770.
RefSeqNP_000275.1. NM_000284.3.
NP_001166925.1. NM_001173454.1.
NP_001166926.1. NM_001173455.1.
NP_001166927.1. NM_001173456.1.
UniGeneHs.530331.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NI4X-ray1.95A/C30-390[»]
2OZLX-ray1.90A/C30-390[»]
3EXEX-ray1.98A/C/E/G30-390[»]
3EXFX-ray3.00A/C/E/G30-390[»]
3EXGX-ray3.011/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y30-390[»]
3EXHX-ray2.44A/C/E/G30-390[»]
3EXIX-ray2.20A30-390[»]
ProteinModelPortalP08559.
SMRP08559. Positions 29-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111186. 25 interactions.
DIPDIP-37652N.
IntActP08559. 9 interactions.
MINTMINT-3006251.
STRING9606.ENSP00000394382.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP08559.

Polymorphism databases

DMDM129063.

2D gel databases

REPRODUCTION-2DPAGEIPI00306301.
UCD-2DPAGEP08559.

Proteomic databases

PaxDbP08559.
PeptideAtlasP08559.
PRIDEP08559.

Protocols and materials databases

DNASU5160.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379806; ENSP00000369134; ENSG00000131828. [P08559-4]
ENST00000422285; ENSP00000394382; ENSG00000131828. [P08559-1]
ENST00000540249; ENSP00000440761; ENSG00000131828. [P08559-3]
ENST00000545074; ENSP00000438550; ENSG00000131828. [P08559-2]
GeneID5160.
KEGGhsa:5160.
UCSCuc004czg.4. human. [P08559-1]
uc004czh.4. human. [P08559-4]
uc011mjc.2. human. [P08559-2]
uc011mjd.2. human. [P08559-3]

Organism-specific databases

CTD5160.
GeneCardsGC0XP019271.
HGNCHGNC:8806. PDHA1.
HPAHPA047487.
HPA047864.
MIM300502. gene.
308930. phenotype.
312170. phenotype.
neXtProtNX_P08559.
Orphanet70474. Leigh syndrome with cardiomyopathy.
79243. Pyruvate dehydrogenase E1-alpha deficiency.
PharmGKBPA33150.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281336.
HOVERGENHBG001863.
InParanoidP08559.
KOK00161.
OMAEVKHYRE.
PhylomeDBP08559.
TreeFamTF300742.

Enzyme and pathway databases

BioCycMetaCyc:HS05573-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP08559.

Gene expression databases

ArrayExpressP08559.
BgeeP08559.
CleanExHS_PDHA1.
GenevestigatorP08559.

Family and domain databases

InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPDHA1. human.
EvolutionaryTraceP08559.
GeneWikiPyruvate_dehydrogenase_(lipoamide)_alpha_1.
GenomeRNAi5160.
NextBio19962.
PROP08559.
SOURCESearch...

Entry information

Entry nameODPA_HUMAN
AccessionPrimary (citable) accession number: P08559
Secondary accession number(s): A5YVE9 expand/collapse secondary AC list , B2R5P7, B7Z3T7, B7Z3X5, Q53H41, Q5JPT8, Q9NP12, Q9UBJ8, Q9UBU0, Q9UNG4, Q9UNG5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1992
Last modified: April 16, 2014
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM