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Protein

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

Gene

PDHA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Enzyme regulationi

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

GO - Molecular functioni

GO - Biological processi

  • glucose metabolic process Source: UniProtKB-KW
  • pyruvate metabolic process Source: UniProtKB
  • 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

Enzyme and pathway databases

BioCyciZFISH:HS08790-MONOMER.
SIGNORiP29803.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:8807. PDHA2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: GO_Central
  • nucleus Source: UniProtKB
  • pyruvate dehydrogenase complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi230S → A: Slightly reduces enzyme activity. 1 Publication1
Mutagenesisi291S → A: Strongly reduces enzyme activity. 1 Publication1
Mutagenesisi291S → E: Abolishes enzyme activity. 1 Publication1
Mutagenesisi298S → A: Slightly reduces enzyme activity. 1 Publication1

Organism-specific databases

DisGeNETi5161.
OpenTargetsiENSG00000163114.
PharmGKBiPA33151.

Polymorphism and mutation databases

BioMutaiPDHA2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 27MitochondrionBy similarityAdd BLAST27
ChainiPRO_000002044728 – 388Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrialAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei291Phosphoserine; by PDK1, PDK2, PDK3 and PDK41 Publication1
Modified residuei298Phosphoserine; by PDK31 Publication1

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP29803.
MaxQBiP29803.
PaxDbiP29803.
PeptideAtlasiP29803.
PRIDEiP29803.

PTM databases

iPTMnetiP29803.
PhosphoSitePlusiP29803.

Expressioni

Tissue specificityi

Testis. Expressed in postmeiotic spermatogenic cells.1 Publication

Gene expression databases

BgeeiENSG00000163114.
CleanExiHS_PDHA2.
GenevisibleiP29803. HS.

Organism-specific databases

HPAiHPA047487.
HPA047864.
HPA063053.

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. 10 interactors.
IntActiP29803. 2 interactors.
STRINGi9606.ENSP00000295266.

Structurei

3D structure databases

ProteinModelPortaliP29803.
SMRiP29803.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0225. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP29803.
KOiK00161.
OMAiNDEICLT.
OrthoDBiEOG091G0966.
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

        10         20         30         40         50
MLAAFISRVL RRVAQKSARR VLVASRNSSN DATFEIKKCD LYLLEEGPPV
60 70 80 90 100
TTVLTRAEGL KYYRMMLTVR RMELKADQLY KQKFIRGFCH LCDGQEACCV
110 120 130 140 150
GLEAGINPSD HVITSYRAHG VCYTRGLSVR SILAELTGRR GGCAKGKGGS
160 170 180 190 200
MHMYTKNFYG GNGIVGAQGP LGAGIALACK YKGNDEICLT LYGDGAANQG
210 220 230 240 250
QIAEAFNMAA LWKLPCVFIC ENNLYGMGTS TERAAASPDY YKRGNFIPGL
260 270 280 290 300
KVDGMDVLCV REATKFAANY CRSGKGPILM ELQTYRYHGH SMSDPGVSYR
310 320 330 340 350
TREEIQEVRS KRDPIIILQD RMVNSKLATV EELKEIGAEV RKEIDDAAQF
360 370 380
ATTDPEPHLE ELGHHIYSSD SSFEVRGANP WIKFKSVS
Length:388
Mass (Da):42,933
Last modified:April 1, 1993 - v1
Checksum:i075B6CFF6DC73CC5
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti127L → P in AAH66953 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034359376R → G.Corresponds to variant rs17024795dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP29803.
SMRiP29803.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111187. 10 interactors.
IntActiP29803. 2 interactors.
STRINGi9606.ENSP00000295266.

PTM databases

iPTMnetiP29803.
PhosphoSitePlusiP29803.

Polymorphism and mutation databases

BioMutaiPDHA2.

Proteomic databases

EPDiP29803.
MaxQBiP29803.
PaxDbiP29803.
PeptideAtlasiP29803.
PRIDEiP29803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295266; ENSP00000295266; ENSG00000163114.
GeneIDi5161.
KEGGihsa:5161.
UCSCiuc003htr.5. human.

Organism-specific databases

CTDi5161.
DisGeNETi5161.
GeneCardsiPDHA2.
HGNCiHGNC:8807. PDHA2.
HPAiHPA047487.
HPA047864.
HPA063053.
MIMi179061. gene.
neXtProtiNX_P29803.
OpenTargetsiENSG00000163114.
PharmGKBiPA33151.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0225. Eukaryota.
COG1071. LUCA.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP29803.
KOiK00161.
OMAiNDEICLT.
OrthoDBiEOG091G0966.
PhylomeDBiP29803.
TreeFamiTF300742.

Enzyme and pathway databases

BioCyciZFISH:HS08790-MONOMER.
SIGNORiP29803.

Miscellaneous databases

ChiTaRSiPDHA2. human.
GeneWikiiPyruvate_dehydrogenase_(lipoamide)_alpha_2.
GenomeRNAii5161.
PROiP29803.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000163114.
CleanExiHS_PDHA2.
GenevisibleiP29803. HS.

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.
ProtoNetiSearch...

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: November 30, 2016
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.