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P29803 (ODPAT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial

EC=1.2.4.1
Alternative name(s):
PDHE1-A type II
Gene names
Name:PDHA2
Synonyms:PDHAL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 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.5

Catalytic activity

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.5

Cofactor

Thiamine pyrophosphate.

Enzyme regulation

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA2; it is reactivated by dephosphorylation.

Subunit structure

Heterotetramer of two PDHA2 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.4

Subcellular location

Mitochondrion matrix.

Tissue specificity

Testis. Expressed in postmeiotic spermatogenic cells. Ref.7

Post-translational modification

Phosphorylation at Ser-205, Ser-266 and Ser-273 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Phosphorylation at Ser-266 interferes with access to active site, and thereby inactivates the enzyme. Dephosphorylation at all three sites, i.e. at Ser-205, Ser-266 and Ser-273, is required for reactivation.

Sequence caution

The sequence AAH94760.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion By similarity
Chain28 – 388361Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
PRO_0000020447

Amino acid modifications

Modified residue2911Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.5
Modified residue2981Phosphoserine; by PDK3 Ref.5

Natural variations

Natural variant2801M → L.
Corresponds to variant rs2229137 [ dbSNP | Ensembl ].
VAR_034358
Natural variant3761R → G.
Corresponds to variant rs17024795 [ dbSNP | Ensembl ].
VAR_034359

Experimental info

Mutagenesis2301S → A: Slightly reduces enzyme activity. Ref.5
Mutagenesis2911S → A: Strongly reduces enzyme activity. Ref.5
Mutagenesis2911S → E: Abolishes enzyme activity. Ref.5
Mutagenesis2981S → A: Slightly reduces enzyme activity. Ref.5
Sequence conflict1271L → P in AAH66953. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P29803 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 075B6CFF6DC73CC5

FASTA38842,933
        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 

« Hide

References

« Hide 'large scale' references
[1]"A testis-specific form of the human pyruvate dehydrogenase E1 alpha subunit is coded for by an intronless gene on chromosome 4."
Dahl H.-H.M., Brown R.M., Hutchison W.M., Maragos C., Brown G.K.
Genomics 8:225-232(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Testis.
[2]"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].
Tissue: Testis.
[3]"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].
Tissue: Testis.
[4]"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.
[5]"Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase."
Korotchkina L.G., Sidhu S., Patel M.S.
J. Biol. Chem. 281:9688-9696(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, PHOSPHORYLATION AT SER-291 AND SER-298, MUTAGENESIS OF SER-230; SER-291 AND SER-298.
[6]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Pyruvate dehydrogenase complex: mRNA and protein expression patterns of E1alpha subunit genes in human spermatogenesis."
Pinheiro A., Silva M.J., Graca I., Silva J., Sa R., Sousa M., Barros A., Tavares de Almeida I., Rivera I.
Gene 506:173-178(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86808 Genomic DNA. Translation: AAA60232.1.
AK313872 mRNA. Translation: BAG36600.1.
BC030697 mRNA. Translation: AAH30697.3.
BC066953 mRNA. Translation: AAH66953.2.
BC094760 mRNA. Translation: AAH94760.1. Different initiation.
BC119656 mRNA. Translation: AAI19657.1.
BC119657 mRNA. Translation: AAI19658.1.
BC127637 mRNA. Translation: AAI27638.1.
BC127638 mRNA. Translation: AAI27639.1.
CCDSCCDS3644.1.
PIRDEHUPT. A37104.
RefSeqNP_005381.1. NM_005390.4.
UniGeneHs.131361.

3D structure databases

ProteinModelPortalP29803.
SMRP29803. Positions 29-388.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111187. 8 interactions.
IntActP29803. 1 interaction.
STRING9606.ENSP00000295266.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP29803.

Proteomic databases

MaxQBP29803.
PaxDbP29803.
PRIDEP29803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295266; ENSP00000295266; ENSG00000163114.
GeneID5161.
KEGGhsa:5161.
UCSCuc003htr.4. human.

Organism-specific databases

CTD5161.
GeneCardsGC04P096761.
HGNCHGNC:8807. PDHA2.
MIM179061. gene.
neXtProtNX_P29803.
PharmGKBPA33151.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1071.
HOGENOMHOG000281336.
HOVERGENHBG001863.
InParanoidP29803.
KOK00161.
OMAIANGPIV.
OrthoDBEOG73JKVQ.
PhylomeDBP29803.
TreeFamTF300742.

Gene expression databases

BgeeP29803.
CleanExHS_PDHA2.
GenevestigatorP29803.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPDHA2. human.
GeneWikiPyruvate_dehydrogenase_(lipoamide)_alpha_2.
GenomeRNAi5161.
NextBio19966.
PROP29803.
SOURCESearch...

Entry information

Entry nameODPAT_HUMAN
AccessionPrimary (citable) accession number: P29803
Secondary accession number(s): B2R9Q3 expand/collapse secondary AC list , Q0VDI5, Q4VC02, Q6NXQ1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: July 9, 2014
This is version 133 of the entry and version 1 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

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 4

Human chromosome 4: entries, gene names and cross-references to MIM