Reviewed, UniProtKB/Swiss-Prot P29803 (ODPAT_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Testis. Expressed in postmeiotic spermatogenic cells.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	pyruvate dehydrogenase (acetyl-transferring) activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 27	27	Mitochondrion By similarity
	Chain	28 – 388	361	Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial		PRO_0000020447
Amino acid modifications
	Modified residue	230	1	Phosphoserine By similarity
	Modified residue	287	1	Phosphotyrosine Ref.5
	Modified residue	291	1	Phosphoserine Ref.4 Ref.6 Ref.7
	Modified residue	298	1	Phosphoserine Ref.4 Ref.7
	Modified residue	299	1	Phosphotyrosine Ref.5
Natural variations
	Natural variant	280	1	M → L: dbSNP rs2229137.		VAR_034358
	Natural variant	376	1	R → G: dbSNP rs17024795.		VAR_034359
Experimental info
	Sequence conflict	127	1	L → P in AAH66953. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P29803-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 075B6CFF6DC73CC5	FASTA	388	42,933
	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

References

	« Hide 'large scale' referencesShow '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: 2249846] [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. , 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: 14702039] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[4]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-298, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-287 AND TYR-299, MASS SPECTROMETRY. Tissue: Lung.
[6]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, MASS SPECTROMETRY. Tissue: Platelet.
[7]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-298, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00024087.
PIR	DEHUPT. A37104.
RefSeq	NP_005381.1.
UniGene	Hs.131361
3D structure databases
HSSP	HSSP built from PDB template 1NI4 based on UniProtKB P08559.
SMR	P29803. Positions 29-388.
ModBase	Search...
PTM databases
PhosphoSite	P29803.
Proteomic databases
PRIDE	P29803.
Genome annotation databases
Ensembl	ENSG00000163114. Homo sapiens. [Contig view]
GeneID	5161.
KEGG	hsa:5161.
Organism-specific databases
GeneCards	GC04P096974.
H-InvDB	HIX0031443.
HGNC	HGNC:8807. PDHA2.
MIM	179061. gene.
PharmGKB	PA33151.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	P29803.
OMA	P29803. LEYETYR.
Enzyme and pathway databases
BRENDA	1.2.4.1. 247.
Gene expression databases
ArrayExpress	P29803.
Bgee	P29803.
CleanEx	HS_PDHA2.
GermOnline	ENSG00000163114. Homo sapiens.
Family and domain databases
InterPro	IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view]
Pfam	PF00676. E1_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNet	Search...
Other Resources
DrugBank	DB00157. NADH.
NextBio	19966.
SOURCE	Search...

Entry information

Entry name

ODPAT_HUMAN

Accession

Primary (citable) accession number: P29803
Secondary accession number(s): B2R9Q3 , Q0VDI5, Q4VC02, Q6NXQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)