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Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

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.2 Publications

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.3 Publications

Cofactori

thiamine diphosphate2 Publications

Enzyme regulationi

Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation.3 Publications

GO - Molecular functioni

GO - Biological processi

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

BioCyciMetaCyc:HS05573-MONOMER.
ZFISH:HS05573-MONOMER.
BRENDAi1.2.4.1. 2681.
ReactomeiR-HSA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-HSA-389661. Glyoxylate metabolism and glycine degradation.
R-HSA-5362517. Signaling by Retinoic Acid.
R-HSA-70268. Pyruvate metabolism.
SABIO-RKP08559.
SIGNORiP08559.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC:1.2.4.1)
Alternative name(s):
PDHE1-A type I
Gene namesi
Name:PDHA1
Synonyms:PHE1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:8806. PDHA1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: UniProtKB
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate dehydrogenase E1-alpha deficiency (PDHAD)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis.
See also OMIM:312170
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01023810R → P in PDHAD; affects mitochondrial import of precursor protein. 1 PublicationCorresponds to variant rs137853257dbSNPEnsembl.1
Natural variantiVAR_00494972R → C in PDHAD. 2 Publications1
Natural variantiVAR_004950113H → D in PDHAD. 1 Publication1
Natural variantiVAR_004951162G → R in PDHAD. 1 Publication1
Natural variantiVAR_004952167V → M in PDHAD. 1 Publication1
Natural variantiVAR_004953199A → T in PDHAD. 1 Publication1
Natural variantiVAR_004954205F → L in PDHAD. 2 PublicationsCorresponds to variant rs137853254dbSNPEnsembl.1
Natural variantiVAR_004955210M → V in PDHAD. 1 PublicationCorresponds to variant rs794727843dbSNPEnsembl.1
Natural variantiVAR_004956217P → L in PDHAD. 1 Publication1
Natural variantiVAR_004957231T → A in PDHAD. 1 Publication1
Natural variantiVAR_021053243Y → N in PDHAD. 1 PublicationCorresponds to variant rs137853255dbSNPEnsembl.1
Natural variantiVAR_004958258D → A in PDHAD. 1 PublicationCorresponds to variant rs137853253dbSNPEnsembl.1
Natural variantiVAR_004959263R → G in PDHAD. 4 PublicationsCorresponds to variant rs28936081dbSNPEnsembl.1
Natural variantiVAR_004960263R → Q in PDHAD. 1 Publication1
Natural variantiVAR_021055288R → H in PDHAD. 1 PublicationCorresponds to variant rs137853258dbSNPEnsembl.1
Natural variantiVAR_004961292H → L in PDHAD. 1 Publication1
Natural variantiVAR_004962302R → C in PDHAD; loss of activity; common mutation. 3 PublicationsCorresponds to variant rs137853252dbSNPEnsembl.1
Natural variantiVAR_004963302R → H in PDHAD. 1 Publication1
Natural variantiVAR_020908305E → EDSYRTRE in PDHAD. 1 Publication1
Natural variantiVAR_020909307I → IPPHSYRTREEI in PDHAD. 1 Publication1
Natural variantiVAR_004964311Missing in PDHAD. 2 Publications1
Natural variantiVAR_004965313Missing in PDHAD. 1 Publication1
Natural variantiVAR_021056315D → N in PDHAD. 1 PublicationCorresponds to variant rs28935187dbSNPEnsembl.1
Natural variantiVAR_004966378R → H in PDHAD. 3 PublicationsCorresponds to variant rs137853250dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi232S → A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300. 1 Publication1
Mutagenesisi293S → A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300. 2 Publications1
Mutagenesisi293S → E: Interferes with substrate binding. 2 Publications1
Mutagenesisi300S → A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293. 1 Publication1

Keywords - Diseasei

Disease mutation, Leigh syndrome

Organism-specific databases

DisGeNETi5160.
MalaCardsiPDHA1.
MIMi312170. phenotype.
OpenTargetsiENSG00000131828.
Orphaneti70474. Leigh syndrome with cardiomyopathy.
79243. Pyruvate dehydrogenase E1-alpha deficiency.
PharmGKBiPA33150.

Polymorphism and mutation databases

BioMutaiPDHA1.
DMDMi129063.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 30Mitochondrion1 PublicationAdd BLAST30
ChainiPRO_000002044031 – 390Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialAdd BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei63N6-acetyllysine; alternateBy similarity1
Modified residuei63N6-succinyllysine; alternateBy similarity1
Modified residuei231PhosphothreonineBy similarity1
Modified residuei232Phosphoserine; by PDK1Combined sources1 Publication1
Modified residuei244N6-acetyllysine; alternateBy similarity1
Modified residuei244N6-succinyllysine; alternateBy similarity1
Modified residuei277N6-succinyllysineBy similarity1
Modified residuei293Phosphoserine; by PDK1, PDK2, PDK3 and PDK43 Publications1
Modified residuei295PhosphoserineBy similarity1
Modified residuei300Phosphoserine; by PDK1, PDK2, PDK3 and PDK42 Publications1
Modified residuei301PhosphotyrosineBy similarity1
Modified residuei313N6-acetyllysine; alternateBy similarity1
Modified residuei313N6-succinyllysine; alternateBy similarity1
Modified residuei321N6-acetyllysineCombined sources1
Modified residuei336N6-acetyllysineBy similarity1
Modified residuei385N6-succinyllysineBy similarity1

Post-translational modificationi

Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.3 Publications
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP08559.
MaxQBiP08559.
PeptideAtlasiP08559.
PRIDEiP08559.
TopDownProteomicsiP08559-3. [P08559-3]
P08559-4. [P08559-4]

2D gel databases

REPRODUCTION-2DPAGEIPI00306301.
UCD-2DPAGEP08559.

PTM databases

iPTMnetiP08559.
PhosphoSitePlusiP08559.
SwissPalmiP08559.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000131828.
CleanExiHS_PDHA1.
ExpressionAtlasiP08559. baseline and differential.
GenevisibleiP08559. HS.

Organism-specific databases

HPAiHPA047487.
HPA047864.
HPA063053.

Interactioni

Subunit structurei

Heterotetramer of two PDHA1 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.3 Publications

Protein-protein interaction databases

BioGridi111186. 52 interactors.
DIPiDIP-37652N.
IntActiP08559. 15 interactors.
MINTiMINT-3006251.

Structurei

Secondary structure

1390
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Beta strandi42 – 45Combined sources4
Beta strandi52 – 57Combined sources6
Helixi58 – 83Combined sources26
Beta strandi85 – 87Combined sources3
Helixi98 – 106Combined sources9
Beta strandi112 – 115Combined sources4
Helixi121 – 126Combined sources6
Helixi131 – 138Combined sources8
Turni145 – 148Combined sources4
Helixi151 – 153Combined sources3
Turni167 – 169Combined sources3
Helixi170 – 184Combined sources15
Beta strandi190 – 195Combined sources6
Helixi198 – 200Combined sources3
Helixi202 – 213Combined sources12
Beta strandi218 – 224Combined sources7
Beta strandi226 – 228Combined sources3
Helixi233 – 236Combined sources4
Helixi242 – 244Combined sources3
Turni245 – 248Combined sources4
Beta strandi251 – 255Combined sources5
Helixi259 – 274Combined sources16
Turni275 – 277Combined sources3
Beta strandi280 – 285Combined sources6
Beta strandi300 – 302Combined sources3
Helixi304 – 314Combined sources11
Helixi316 – 326Combined sources11
Helixi332 – 355Combined sources24
Helixi361 – 363Combined sources3
Beta strandi367 – 371Combined sources5
Beta strandi375 – 378Combined sources4
Beta strandi385 – 388Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NI4X-ray1.95A/C30-390[»]
2OZLX-ray1.90A/C30-390[»]
3EXEX-ray1.98A/C/E/G30-390[»]
3EXFX-ray3.00A/C/E/G30-390[»]
3EXGX-ray3.011/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y30-390[»]
3EXHX-ray2.44A/C/E/G30-390[»]
3EXIX-ray2.20A30-390[»]
ProteinModelPortaliP08559.
SMRiP08559.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08559.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP08559.
KOiK00161.
OMAiWMYQKML.
OrthoDBiEOG091G0966.
PhylomeDBiP08559.
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.

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P08559-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP
60 70 80 90 100
PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC
110 120 130 140 150
CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG
160 170 180 190 200
GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN
210 220 230 240 250
QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP
260 270 280 290 300
GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
310 320 330 340 350
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA
360 370 380 390
QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
Length:390
Mass (Da):43,296
Last modified:May 1, 1992 - v3
Checksum:i4D685BBE44A92D4B
GO
Isoform 2 (identifier: P08559-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-96: G → GQFLLPLT

Note: No experimental confirmation available.
Show »
Length:397
Mass (Da):44,109
Checksum:i4BE156001F9994A5
GO
Isoform 3 (identifier: P08559-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-200: Missing.

Note: No experimental confirmation available.
Show »
Length:359
Mass (Da):40,188
Checksum:i7E94F39FC1293065
GO
Isoform 4 (identifier: P08559-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: P → PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLKTRQ

Show »
Length:428
Mass (Da):47,580
Checksum:i14FE765CFF2C7120
GO

Sequence cautioni

The sequence AAA60055 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB59581 differs from that shown. Reason: Frameshift at positions 106 and 175.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti278G → E in BAG35194 (PubMed:14702039).Curated1
Sequence conflicti301Y → S in AAD23857 (PubMed:10077682).Curated1
Sequence conflicti306E → D in AAD23857 (PubMed:10077682).Curated1
Sequence conflicti349A → P in AAA60055 (PubMed:2828359).Curated1
Sequence conflicti354T → A in AAA60055 (PubMed:2828359).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01023810R → P in PDHAD; affects mitochondrial import of precursor protein. 1 PublicationCorresponds to variant rs137853257dbSNPEnsembl.1
Natural variantiVAR_00494972R → C in PDHAD. 2 Publications1
Natural variantiVAR_004950113H → D in PDHAD. 1 Publication1
Natural variantiVAR_069381136A → T Probable disease-associated mutation found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate. 1 PublicationCorresponds to variant rs138727886dbSNPEnsembl.1
Natural variantiVAR_004951162G → R in PDHAD. 1 Publication1
Natural variantiVAR_004952167V → M in PDHAD. 1 Publication1
Natural variantiVAR_004953199A → T in PDHAD. 1 Publication1
Natural variantiVAR_004954205F → L in PDHAD. 2 PublicationsCorresponds to variant rs137853254dbSNPEnsembl.1
Natural variantiVAR_004955210M → V in PDHAD. 1 PublicationCorresponds to variant rs794727843dbSNPEnsembl.1
Natural variantiVAR_004956217P → L in PDHAD. 1 Publication1
Natural variantiVAR_004957231T → A in PDHAD. 1 Publication1
Natural variantiVAR_021053243Y → N in PDHAD. 1 PublicationCorresponds to variant rs137853255dbSNPEnsembl.1
Natural variantiVAR_004958258D → A in PDHAD. 1 PublicationCorresponds to variant rs137853253dbSNPEnsembl.1
Natural variantiVAR_004959263R → G in PDHAD. 4 PublicationsCorresponds to variant rs28936081dbSNPEnsembl.1
Natural variantiVAR_004960263R → Q in PDHAD. 1 Publication1
Natural variantiVAR_021054282M → L.3 PublicationsCorresponds to variant rs2229137dbSNPEnsembl.1
Natural variantiVAR_021055288R → H in PDHAD. 1 PublicationCorresponds to variant rs137853258dbSNPEnsembl.1
Natural variantiVAR_004961292H → L in PDHAD. 1 Publication1
Natural variantiVAR_004962302R → C in PDHAD; loss of activity; common mutation. 3 PublicationsCorresponds to variant rs137853252dbSNPEnsembl.1
Natural variantiVAR_004963302R → H in PDHAD. 1 Publication1
Natural variantiVAR_020908305E → EDSYRTRE in PDHAD. 1 Publication1
Natural variantiVAR_020909307I → IPPHSYRTREEI in PDHAD. 1 Publication1
Natural variantiVAR_004964311Missing in PDHAD. 2 Publications1
Natural variantiVAR_004965313Missing in PDHAD. 1 Publication1
Natural variantiVAR_021056315D → N in PDHAD. 1 PublicationCorresponds to variant rs28935187dbSNPEnsembl.1
Natural variantiVAR_050436333E → D.Corresponds to variant rs2228067dbSNPEnsembl.1
Natural variantiVAR_004966378R → H in PDHAD. 3 PublicationsCorresponds to variant rs137853250dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04336319P → PRHGLATLPSLVSISRLKQS SHLGLPKCWDYSHSLKTRQ in isoform 4. 2 Publications1
Alternative sequenceiVSP_04256996G → GQFLLPLT in isoform 2. 1 Publication1
Alternative sequenceiVSP_042570170 – 200Missing in isoform 3. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90084 Genomic DNA. Translation: BAA14121.1.
M24848 mRNA. Translation: AAA36533.1.
X52709 mRNA. Translation: CAA36933.1.
X52710 mRNA. Translation: CAA36934.1.
M27257
, M29155, M29156, M29157, M29158, M29159, M29160, M29161, M29162, M29163, M29164 Genomic DNA. Translation: AAA60051.1.
L13318 mRNA. Translation: AAA60227.1.
J03503 mRNA. Translation: AAA60055.1. Different initiation.
J03575 mRNA. Translation: AAA60050.1.
L48690 mRNA. Translation: AAB59581.1. Frameshift.
EF590117 mRNA. Translation: ABQ59099.1.
AK293250 mRNA. Translation: BAH11476.1.
AK296457 mRNA. Translation: BAH12361.1.
AK312263 mRNA. Translation: BAG35194.1.
AK296341 mRNA. Translation: BAH12323.1.
AK222740 mRNA. Translation: BAD96460.1.
AL732326 Genomic DNA. Translation: CAI41291.1.
CH471074 Genomic DNA. Translation: EAW98960.1.
BC002406 mRNA. Translation: AAH02406.1.
AF125053 Genomic DNA. Translation: AAD23841.1.
AF125054 Genomic DNA. Translation: AAD23842.1.
AF125055 Genomic DNA. Translation: AAD23843.1.
AF125056 Genomic DNA. Translation: AAD23844.1.
AF125057 Genomic DNA. Translation: AAD23845.1.
AF125058 Genomic DNA. Translation: AAD23846.1.
AF125059 Genomic DNA. Translation: AAD23847.1.
AF125060 Genomic DNA. Translation: AAD23848.1.
AF125061 Genomic DNA. Translation: AAD23849.1.
AF125062 Genomic DNA. Translation: AAD23850.1.
AF125063 Genomic DNA. Translation: AAD23851.1.
AF125064 Genomic DNA. Translation: AAD23852.1.
AF125065 Genomic DNA. Translation: AAD23853.1.
AF125066 Genomic DNA. Translation: AAD23854.1.
AF125067 Genomic DNA. Translation: AAD23855.1.
AF125068 Genomic DNA. Translation: AAD23856.1.
AF125069 Genomic DNA. Translation: AAD23857.1.
AF125070 Genomic DNA. Translation: AAD23858.1.
AF125071 Genomic DNA. Translation: AAD23859.1.
AF125072 Genomic DNA. Translation: AAD23860.1.
AF125073 Genomic DNA. Translation: AAD23861.1.
AF125074 Genomic DNA. Translation: AAD23862.1.
AF125075 Genomic DNA. Translation: AAD23863.1.
AF125076 Genomic DNA. Translation: AAD23864.1.
AF125078 Genomic DNA. Translation: AAD23866.1.
AF125079 Genomic DNA. Translation: AAD23867.1.
AF125080 Genomic DNA. Translation: AAD23868.1.
AF125081 Genomic DNA. Translation: AAD23869.1.
AF125082 Genomic DNA. Translation: AAD23870.1.
AF125083 Genomic DNA. Translation: AAD23871.1.
AF125084 Genomic DNA. Translation: AAD23872.1.
AF125085 Genomic DNA. Translation: AAD23873.1.
AF125086 Genomic DNA. Translation: AAD23874.1.
AF125087 Genomic DNA. Translation: AAD23875.1.
AF125088 Genomic DNA. Translation: AAD23876.1.
CCDSiCCDS14192.1. [P08559-1]
CCDS55380.1. [P08559-4]
CCDS55381.1. [P08559-2]
CCDS55382.1. [P08559-3]
PIRiJQ0770. DEHUPA.
RefSeqiNP_000275.1. NM_000284.3. [P08559-1]
NP_001166925.1. NM_001173454.1. [P08559-4]
NP_001166926.1. NM_001173455.1. [P08559-2]
NP_001166927.1. NM_001173456.1. [P08559-3]
UniGeneiHs.530331.

Genome annotation databases

EnsembliENST00000379806; ENSP00000369134; ENSG00000131828. [P08559-4]
ENST00000422285; ENSP00000394382; ENSG00000131828. [P08559-1]
ENST00000540249; ENSP00000440761; ENSG00000131828. [P08559-3]
ENST00000545074; ENSP00000438550; ENSG00000131828. [P08559-2]
GeneIDi5160.
KEGGihsa:5160.
UCSCiuc004czg.5. human. [P08559-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90084 Genomic DNA. Translation: BAA14121.1.
M24848 mRNA. Translation: AAA36533.1.
X52709 mRNA. Translation: CAA36933.1.
X52710 mRNA. Translation: CAA36934.1.
M27257
, M29155, M29156, M29157, M29158, M29159, M29160, M29161, M29162, M29163, M29164 Genomic DNA. Translation: AAA60051.1.
L13318 mRNA. Translation: AAA60227.1.
J03503 mRNA. Translation: AAA60055.1. Different initiation.
J03575 mRNA. Translation: AAA60050.1.
L48690 mRNA. Translation: AAB59581.1. Frameshift.
EF590117 mRNA. Translation: ABQ59099.1.
AK293250 mRNA. Translation: BAH11476.1.
AK296457 mRNA. Translation: BAH12361.1.
AK312263 mRNA. Translation: BAG35194.1.
AK296341 mRNA. Translation: BAH12323.1.
AK222740 mRNA. Translation: BAD96460.1.
AL732326 Genomic DNA. Translation: CAI41291.1.
CH471074 Genomic DNA. Translation: EAW98960.1.
BC002406 mRNA. Translation: AAH02406.1.
AF125053 Genomic DNA. Translation: AAD23841.1.
AF125054 Genomic DNA. Translation: AAD23842.1.
AF125055 Genomic DNA. Translation: AAD23843.1.
AF125056 Genomic DNA. Translation: AAD23844.1.
AF125057 Genomic DNA. Translation: AAD23845.1.
AF125058 Genomic DNA. Translation: AAD23846.1.
AF125059 Genomic DNA. Translation: AAD23847.1.
AF125060 Genomic DNA. Translation: AAD23848.1.
AF125061 Genomic DNA. Translation: AAD23849.1.
AF125062 Genomic DNA. Translation: AAD23850.1.
AF125063 Genomic DNA. Translation: AAD23851.1.
AF125064 Genomic DNA. Translation: AAD23852.1.
AF125065 Genomic DNA. Translation: AAD23853.1.
AF125066 Genomic DNA. Translation: AAD23854.1.
AF125067 Genomic DNA. Translation: AAD23855.1.
AF125068 Genomic DNA. Translation: AAD23856.1.
AF125069 Genomic DNA. Translation: AAD23857.1.
AF125070 Genomic DNA. Translation: AAD23858.1.
AF125071 Genomic DNA. Translation: AAD23859.1.
AF125072 Genomic DNA. Translation: AAD23860.1.
AF125073 Genomic DNA. Translation: AAD23861.1.
AF125074 Genomic DNA. Translation: AAD23862.1.
AF125075 Genomic DNA. Translation: AAD23863.1.
AF125076 Genomic DNA. Translation: AAD23864.1.
AF125078 Genomic DNA. Translation: AAD23866.1.
AF125079 Genomic DNA. Translation: AAD23867.1.
AF125080 Genomic DNA. Translation: AAD23868.1.
AF125081 Genomic DNA. Translation: AAD23869.1.
AF125082 Genomic DNA. Translation: AAD23870.1.
AF125083 Genomic DNA. Translation: AAD23871.1.
AF125084 Genomic DNA. Translation: AAD23872.1.
AF125085 Genomic DNA. Translation: AAD23873.1.
AF125086 Genomic DNA. Translation: AAD23874.1.
AF125087 Genomic DNA. Translation: AAD23875.1.
AF125088 Genomic DNA. Translation: AAD23876.1.
CCDSiCCDS14192.1. [P08559-1]
CCDS55380.1. [P08559-4]
CCDS55381.1. [P08559-2]
CCDS55382.1. [P08559-3]
PIRiJQ0770. DEHUPA.
RefSeqiNP_000275.1. NM_000284.3. [P08559-1]
NP_001166925.1. NM_001173454.1. [P08559-4]
NP_001166926.1. NM_001173455.1. [P08559-2]
NP_001166927.1. NM_001173456.1. [P08559-3]
UniGeneiHs.530331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NI4X-ray1.95A/C30-390[»]
2OZLX-ray1.90A/C30-390[»]
3EXEX-ray1.98A/C/E/G30-390[»]
3EXFX-ray3.00A/C/E/G30-390[»]
3EXGX-ray3.011/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y30-390[»]
3EXHX-ray2.44A/C/E/G30-390[»]
3EXIX-ray2.20A30-390[»]
ProteinModelPortaliP08559.
SMRiP08559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111186. 52 interactors.
DIPiDIP-37652N.
IntActiP08559. 15 interactors.
MINTiMINT-3006251.

PTM databases

iPTMnetiP08559.
PhosphoSitePlusiP08559.
SwissPalmiP08559.

Polymorphism and mutation databases

BioMutaiPDHA1.
DMDMi129063.

2D gel databases

REPRODUCTION-2DPAGEIPI00306301.
UCD-2DPAGEP08559.

Proteomic databases

EPDiP08559.
MaxQBiP08559.
PeptideAtlasiP08559.
PRIDEiP08559.
TopDownProteomicsiP08559-3. [P08559-3]
P08559-4. [P08559-4]

Protocols and materials databases

DNASUi5160.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379806; ENSP00000369134; ENSG00000131828. [P08559-4]
ENST00000422285; ENSP00000394382; ENSG00000131828. [P08559-1]
ENST00000540249; ENSP00000440761; ENSG00000131828. [P08559-3]
ENST00000545074; ENSP00000438550; ENSG00000131828. [P08559-2]
GeneIDi5160.
KEGGihsa:5160.
UCSCiuc004czg.5. human. [P08559-1]

Organism-specific databases

CTDi5160.
DisGeNETi5160.
GeneCardsiPDHA1.
HGNCiHGNC:8806. PDHA1.
HPAiHPA047487.
HPA047864.
HPA063053.
MalaCardsiPDHA1.
MIMi300502. gene.
312170. phenotype.
neXtProtiNX_P08559.
OpenTargetsiENSG00000131828.
Orphaneti70474. Leigh syndrome with cardiomyopathy.
79243. Pyruvate dehydrogenase E1-alpha deficiency.
PharmGKBiPA33150.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP08559.
KOiK00161.
OMAiWMYQKML.
OrthoDBiEOG091G0966.
PhylomeDBiP08559.
TreeFamiTF300742.

Enzyme and pathway databases

BioCyciMetaCyc:HS05573-MONOMER.
ZFISH:HS05573-MONOMER.
BRENDAi1.2.4.1. 2681.
ReactomeiR-HSA-204174. Regulation of pyruvate dehydrogenase (PDH) complex.
R-HSA-389661. Glyoxylate metabolism and glycine degradation.
R-HSA-5362517. Signaling by Retinoic Acid.
R-HSA-70268. Pyruvate metabolism.
SABIO-RKP08559.
SIGNORiP08559.

Miscellaneous databases

ChiTaRSiPDHA1. human.
EvolutionaryTraceiP08559.
GeneWikiiPyruvate_dehydrogenase_(lipoamide)_alpha_1.
GenomeRNAii5160.
PROiP08559.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131828.
CleanExiHS_PDHA1.
ExpressionAtlasiP08559. baseline and differential.
GenevisibleiP08559. 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 nameiODPA_HUMAN
AccessioniPrimary (citable) accession number: P08559
Secondary accession number(s): A5YVE9
, B2R5P7, B7Z3T7, B7Z3X5, Q53H41, Q5JPT8, Q9NP12, Q9UBJ8, Q9UBU0, Q9UNG4, Q9UNG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 206 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.