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P29803

- ODPAT_HUMAN

UniProt

P29803 - ODPAT_HUMAN

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Protein

Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial

Gene
PDHA2, PDHAL
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.1 Publication

Cofactori

Thiamine pyrophosphate.

Enzyme regulationi

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

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB

GO - Biological processi

  1. glucose metabolic process Source: UniProtKB-KW
  2. glycolytic process Source: InterPro
  3. pyruvate metabolic process Source: UniProtKB
  4. tricarboxylic acid cycle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Names & Taxonomyi

Protein namesi
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 namesi
Name:PDHA2
Synonyms:PDHAL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:8807. PDHA2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
  2. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi230 – 2301S → A: Slightly reduces enzyme activity. 1 Publication
Mutagenesisi291 – 2911S → A: Strongly reduces enzyme activity. 1 Publication
Mutagenesisi291 – 2911S → E: Abolishes enzyme activity. 1 Publication
Mutagenesisi298 – 2981S → A: Slightly reduces enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA33151.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2727Mitochondrion By similarityAdd
BLAST
Chaini28 – 388361Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrialPRO_0000020447Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911Phosphoserine; by PDK1, PDK2, PDK3 and PDK41 Publication
Modified residuei298 – 2981Phosphoserine; by PDK31 Publication

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29803.
PaxDbiP29803.
PRIDEiP29803.

PTM databases

PhosphoSiteiP29803.

Expressioni

Tissue specificityi

Testis. Expressed in postmeiotic spermatogenic cells.1 Publication

Gene expression databases

BgeeiP29803.
CleanExiHS_PDHA2.
GenevestigatoriP29803.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi111187. 8 interactions.
IntActiP29803. 1 interaction.
STRINGi9606.ENSP00000295266.

Structurei

3D structure databases

ProteinModelPortaliP29803.
SMRiP29803. Positions 29-388.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP29803.
KOiK00161.
OMAiIANGPIV.
OrthoDBiEOG73JKVQ.
PhylomeDBiP29803.
TreeFamiTF300742.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29803-1 [UniParc]FASTAAdd to Basket

« Hide

MLAAFISRVL RRVAQKSARR VLVASRNSSN DATFEIKKCD LYLLEEGPPV    50
TTVLTRAEGL KYYRMMLTVR RMELKADQLY KQKFIRGFCH LCDGQEACCV 100
GLEAGINPSD HVITSYRAHG VCYTRGLSVR SILAELTGRR GGCAKGKGGS 150
MHMYTKNFYG GNGIVGAQGP LGAGIALACK YKGNDEICLT LYGDGAANQG 200
QIAEAFNMAA LWKLPCVFIC ENNLYGMGTS TERAAASPDY YKRGNFIPGL 250
KVDGMDVLCV REATKFAANY CRSGKGPILM ELQTYRYHGH SMSDPGVSYR 300
TREEIQEVRS KRDPIIILQD RMVNSKLATV EELKEIGAEV RKEIDDAAQF 350
ATTDPEPHLE ELGHHIYSSD SSFEVRGANP WIKFKSVS 388
Length:388
Mass (Da):42,933
Last modified:April 1, 1993 - v1
Checksum:i075B6CFF6DC73CC5
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti280 – 2801M → L.
Corresponds to variant rs2229137 [ dbSNP | Ensembl ].
VAR_034358
Natural varianti376 – 3761R → G.
Corresponds to variant rs17024795 [ dbSNP | Ensembl ].
VAR_034359

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271L → P in AAH66953. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3644.1.
PIRiA37104. DEHUPT.
RefSeqiNP_005381.1. NM_005390.4.
UniGeneiHs.131361.

Genome annotation databases

EnsembliENST00000295266; ENSP00000295266; ENSG00000163114.
GeneIDi5161.
KEGGihsa:5161.
UCSCiuc003htr.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3644.1.
PIRi A37104. DEHUPT.
RefSeqi NP_005381.1. NM_005390.4.
UniGenei Hs.131361.

3D structure databases

ProteinModelPortali P29803.
SMRi P29803. Positions 29-388.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111187. 8 interactions.
IntActi P29803. 1 interaction.
STRINGi 9606.ENSP00000295266.

Chemistry

DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei P29803.

Proteomic databases

MaxQBi P29803.
PaxDbi P29803.
PRIDEi P29803.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295266 ; ENSP00000295266 ; ENSG00000163114 .
GeneIDi 5161.
KEGGi hsa:5161.
UCSCi uc003htr.4. human.

Organism-specific databases

CTDi 5161.
GeneCardsi GC04P096761.
HGNCi HGNC:8807. PDHA2.
MIMi 179061. gene.
neXtProti NX_P29803.
PharmGKBi PA33151.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1071.
HOGENOMi HOG000281336.
HOVERGENi HBG001863.
InParanoidi P29803.
KOi K00161.
OMAi IANGPIV.
OrthoDBi EOG73JKVQ.
PhylomeDBi P29803.
TreeFami TF300742.

Miscellaneous databases

ChiTaRSi PDHA2. human.
GeneWikii Pyruvate_dehydrogenase_(lipoamide)_alpha_2.
GenomeRNAii 5161.
NextBioi 19966.
PROi P29803.
SOURCEi Search...

Gene expression databases

Bgeei P29803.
CleanExi HS_PDHA2.
Genevestigatori P29803.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiODPAT_HUMAN
AccessioniPrimary (citable) accession number: P29803
Secondary accession number(s): B2R9Q3
, Q0VDI5, Q4VC02, Q6NXQ1
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3

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