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Reviewed, UniProtKB/Swiss-Prot P35486 (ODPA_MOUSE)

Last modified February 9, 2010. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Pdha-1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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. 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 structure

Tetramer of 2 alpha and 2 beta subunits.

Subcellular location

Mitochondrion matrix.

Tissue specificity

In all tissues, but in very low amount in testis.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionpyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion By similarity
Chain30 – 390361Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
PRO_0000020442

Amino acid modifications

Modified residue771N6-acetyllysine By similarity
Modified residue831N6-acetyllysine By similarity
Modified residue2311Phosphothreonine By similarity
Modified residue2321Phosphoserine Ref.6 Ref.7
Modified residue2891Phosphotyrosine Ref.7
Modified residue2931Phosphoserine Ref.6 Ref.7 Ref.4 Ref.8
Modified residue2951Phosphoserine By similarity
Modified residue3001Phosphoserine Ref.6 Ref.7 Ref.8
Modified residue3011Phosphotyrosine Ref.5
Modified residue3211N6-acetyllysine By similarity
Modified residue3361N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P35486-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 40898944CE8E0A03

FASTA39043,232
        10         20         30         40         50         60 
MRKMLAAVSR VLAGSAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 

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

       130        140        150        160        170        180 
HGFTFTRGLP VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 

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

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

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

       370        380        390 
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterisation of the mouse pyruvate dehydrogenase E1 alpha genes."
Fitzgerald G.F., Hutchison W.M., Dahl H.-H.M.
Biochim. Biophys. Acta 1131:83-90(1992) [PubMed: 1581363] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[3]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 46-58; 120-127; 133-141; 159-182; 216-244; 246-263; 268-274; 278-321; 324-343 AND 379-385, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[4]"Proteomic analysis of in vivo phosphorylated synaptic proteins."
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.
J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, MASS SPECTROMETRY.
Tissue: Brain.
[5]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, MASS SPECTROMETRY.
Tissue: Brain.
[6]"Mitochondrial phosphoproteome revealed by an improved IMAC method and MS/MS/MS."
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.
Mol. Cell. Proteomics 6:669-676(2007) [PubMed: 17208939] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293 AND SER-300, MASS SPECTROMETRY.
Tissue: Liver.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; TYR-289; SER-293 AND SER-300, MASS SPECTROMETRY.
Tissue: Liver.
[8]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M76727 mRNA. Translation: AAA53046.1.
BC007142 mRNA. Translation: AAH07142.1.
IPIIPI00337893.
PIRS23506.
RefSeqNP_032836.1.
UniGeneMm.34775

3D structure databases

SMRP35486. Positions 29-390.
ModBaseSearch...

Protein-protein interaction databases

STRINGP35486.

PTM databases

PhosphoSiteP35486.

2-D gel databases

REPRODUCTION-2DPAGEP35486.

Proteomic databases

PRIDEP35486.

Genome annotation databases

EnsemblENSMUST00000033662; ENSMUSP00000033662; ENSMUSG00000031299; Mus musculus. [Genome view]
GeneID18597.
KEGGmmu:18597.
UCSCuc009utc.1. mouse.

Organism-specific databases

CTD18597.
MGIMGI:97532. Pdha1.

Phylogenomic databases

eggNOGroNOG13286.
HOGENOMHBG753263.
HOVERGENP35486.
InParanoidP35486.
OMAIVENNRY.
OrthoDBEOG91VNNQ.
PhylomeDBP35486.

Enzyme and pathway databases

BRENDA1.2.4.1. 244.

Gene expression databases

ArrayExpressP35486.
BgeeP35486.
CleanExMM_PDHA1.
GenevestigatorP35486.
GermOnlineENSMUSG00000031299. Mus musculus.

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 Resources

NextBio294490.
SOURCESearch...

Entry information

Entry nameODPA_MOUSE
AccessionPrimary (citable) accession number: P35486
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents