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UniProtKB/Swiss-Prot entry P29803


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

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Entry information
Entry name ODPAT_HUMAN
Primary accession number P29803
Secondary accession numbers Q0VDI5 Q4VC02 Q6NXQ1
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 80)
Name and origin of the protein
Protein name Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial [Precursor]
Synonyms EC 1.2.4.1
PDHE1-A type II
Gene name
Name: PDHA2
Synonyms: PDHAL
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=Testis;
DOI=10.1016/0888-7543(90)90275-Y; PubMed=2249846 [NCBI, ExPASy, EBI, Israel, Japan]
Dahl H.H.M., Brown R.M., Hutchison W.M., Maragos C., Brown G.K.;
"A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4.";
Genomics 8:225-232(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-298, 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).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-287 AND TYR-299, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, 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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-298, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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.
  • SUBCELLULAR LOCATION: Mitochondrion matrix.
  • TISSUE SPECIFICITY: Testis. Expressed in postmeiotic spermatogenic cells.
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
M86808; AAA60232.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030697; AAH30697.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066953; AAH66953.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC094760; AAH94760.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119656; AAI19657.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC119657; AAI19658.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC127637; AAI27638.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC127638; AAI27639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A37104; DEHUPT.
RefSeq NP_005381.1; -.
UniGene Hs.131361
3D structure databases
HSSP P08559; 1NI4. [HSSP ENTRY / PDB]
SMR P29803; 29-388.
ModBase P29803.
PTM databases
PhosphoSite P29803; -.
Organism-specific databases
H-InvDB HIX0031443; -.
HGNC HGNC:8807; PDHA2.
GenAtlas PDHA2.
MIM 179061; gene. [NCBI / EBI]
PharmGKB PA33151; -.
GeneCards P29803.
Gene expression databases
ArrayExpress P29803; -.
CleanEx HS_PDHA2; -.
GermOnline ENSG00000163114; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004739; Molecular function: pyruvate dehydrogenase (acetyl-transferring) activity (traceable author statement from ProtInc).
GO:0006096; Biological process: glycolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
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.
ProtoNet P29803.
Genome annotation databases
Ensembl ENSG00000163114; Homo sapiens. [Contig view]
GeneID 5161; -.
KEGG hsa:5161; -.
Phylogenomic databases
HOVERGEN P29803; -.
Other
DrugBank DB00157; NADH.
NextBio 19966; -.
SOURCE PDHA2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Glycolysis; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Pyruvate; Thiamine pyrophosphate; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    27  27     Mitochondrion (By similarity). 
CHAIN   28   388  361     Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial. PRO_0000020447
MOD_RES   230   230        Phosphoserine (By similarity). 
MOD_RES   287   287        Phosphotyrosine. 
MOD_RES   291   291        Phosphoserine. 
MOD_RES   298   298        Phosphoserine. 
MOD_RES   299   299        Phosphotyrosine. 
VARIANT   280   280  1     M -> L (in dbSNP:rs2229137 [NCBI]). VAR_034358 [3D]
VARIANT   376   376  1     R -> G (in dbSNP:rs17024795 [NCBI]). VAR_034359 [3D]
CONFLICT   127   127        L -> P (in Ref. 2; AAH66953). 
Sequence information
Length: 388 AA [This is the length of the unprocessed precursor] Molecular weight: 42933 Da [This is the MW of the unprocessed precursor] CRC64: 075B6CFF6DC73CC5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLAAFISRVL RRVAQKSARR VLVASRNSSN DATFEIKKCD LYLLEEGPPV TTVLTRAEGL 

        70         80         90        100        110        120 
KYYRMMLTVR RMELKADQLY KQKFIRGFCH LCDGQEACCV GLEAGINPSD HVITSYRAHG 

       130        140        150        160        170        180 
VCYTRGLSVR SILAELTGRR GGCAKGKGGS MHMYTKNFYG GNGIVGAQGP LGAGIALACK 

       190        200        210        220        230        240 
YKGNDEICLT LYGDGAANQG QIAEAFNMAA LWKLPCVFIC ENNLYGMGTS TERAAASPDY 

       250        260        270        280        290        300 
YKRGNFIPGL KVDGMDVLCV REATKFAANY CRSGKGPILM ELQTYRYHGH SMSDPGVSYR 

       310        320        330        340        350        360 
TREEIQEVRS KRDPIIILQD RMVNSKLATV EELKEIGAEV RKEIDDAAQF ATTDPEPHLE 

       370        380 
ELGHHIYSSD SSFEVRGANP WIKFKSVS 

P29803 in FASTA format

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