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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.
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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101R → P in PDHAD; affects mitochondrial import of precursor protein. 1 Publication
Corresponds to variant rs137853257 [ dbSNP | Ensembl ].
VAR_010238
Natural varianti72 – 721R → C in PDHAD. 2 Publications
VAR_004949
Natural varianti113 – 1131H → D in PDHAD. 1 Publication
VAR_004950
Natural varianti162 – 1621G → R in PDHAD. 1 Publication
VAR_004951
Natural varianti167 – 1671V → M in PDHAD. 1 Publication
VAR_004952
Natural varianti199 – 1991A → T in PDHAD. 1 Publication
VAR_004953
Natural varianti205 – 2051F → L in PDHAD. 2 Publications
Corresponds to variant rs137853254 [ dbSNP | Ensembl ].
VAR_004954
Natural varianti210 – 2101M → V in PDHAD. 1 Publication
Corresponds to variant rs794727843 [ dbSNP | Ensembl ].
VAR_004955
Natural varianti217 – 2171P → L in PDHAD. 1 Publication
VAR_004956
Natural varianti231 – 2311T → A in PDHAD. 1 Publication
VAR_004957
Natural varianti243 – 2431Y → N in PDHAD. 1 Publication
Corresponds to variant rs137853255 [ dbSNP | Ensembl ].
VAR_021053
Natural varianti258 – 2581D → A in PDHAD. 1 Publication
Corresponds to variant rs137853253 [ dbSNP | Ensembl ].
VAR_004958
Natural varianti263 – 2631R → G in PDHAD. 4 Publications
Corresponds to variant rs28936081 [ dbSNP | Ensembl ].
VAR_004959
Natural varianti263 – 2631R → Q in PDHAD. 1 Publication
VAR_004960
Natural varianti288 – 2881R → H in PDHAD. 1 Publication
Corresponds to variant rs137853258 [ dbSNP | Ensembl ].
VAR_021055
Natural varianti292 – 2921H → L in PDHAD. 1 Publication
VAR_004961
Natural varianti302 – 3021R → C in PDHAD; loss of activity; common mutation. 3 Publications
Corresponds to variant rs137853252 [ dbSNP | Ensembl ].
VAR_004962
Natural varianti302 – 3021R → H in PDHAD. 1 Publication
VAR_004963
Natural varianti305 – 3051E → EDSYRTRE in PDHAD. 1 Publication
VAR_020908
Natural varianti307 – 3071I → IPPHSYRTREEI in PDHAD. 1 Publication
VAR_020909
Natural varianti311 – 3111Missing in PDHAD. 2 Publications
VAR_004964
Natural varianti313 – 3131Missing in PDHAD. 1 Publication
VAR_004965
Natural varianti315 – 3151D → N in PDHAD. 1 Publication
Corresponds to variant rs28935187 [ dbSNP | Ensembl ].
VAR_021056
Natural varianti378 – 3781R → H in PDHAD. 3 Publications
Corresponds to variant rs137853250 [ dbSNP | Ensembl ].
VAR_004966

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2321S → A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300. 1 Publication
Mutagenesisi293 – 2931S → A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300. 2 Publications
Mutagenesisi293 – 2931S → E: Interferes with substrate binding. 2 Publications
Mutagenesisi300 – 3001S → A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293. 1 Publication

Keywords - Diseasei

Disease mutation, Leigh syndrome

Organism-specific databases

MalaCardsiPDHA1.
MIMi312170. phenotype.
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)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030Mitochondrion1 PublicationAdd
BLAST
Chaini31 – 390360Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrialPRO_0000020440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei63 – 631N6-acetyllysine; alternateBy similarity
Modified residuei63 – 631N6-succinyllysine; alternateBy similarity
Modified residuei231 – 2311PhosphothreonineBy similarity
Modified residuei232 – 2321Phosphoserine; by PDK1Combined sources1 Publication
Modified residuei244 – 2441N6-acetyllysine; alternateBy similarity
Modified residuei244 – 2441N6-succinyllysine; alternateBy similarity
Modified residuei277 – 2771N6-succinyllysineBy similarity
Modified residuei293 – 2931Phosphoserine; by PDK1, PDK2, PDK3 and PDK43 Publications
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei300 – 3001Phosphoserine; by PDK1, PDK2, PDK3 and PDK42 Publications
Modified residuei301 – 3011PhosphotyrosineBy similarity
Modified residuei313 – 3131N6-acetyllysine; alternateBy similarity
Modified residuei313 – 3131N6-succinyllysine; alternateBy similarity
Modified residuei321 – 3211N6-acetyllysineCombined sources
Modified residuei336 – 3361N6-acetyllysineBy similarity
Modified residuei385 – 3851N6-succinyllysineBy similarity

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.
PhosphoSiteiP08559.
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. 51 interactions.
DIPiDIP-37652N.
IntActiP08559. 15 interactions.
MINTiMINT-3006251.

Structurei

Secondary structure

1
390
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 376Combined sources
Beta strandi42 – 454Combined sources
Beta strandi52 – 576Combined sources
Helixi58 – 8326Combined sources
Beta strandi85 – 873Combined sources
Helixi98 – 1069Combined sources
Beta strandi112 – 1154Combined sources
Helixi121 – 1266Combined sources
Helixi131 – 1388Combined sources
Turni145 – 1484Combined sources
Helixi151 – 1533Combined sources
Turni167 – 1693Combined sources
Helixi170 – 18415Combined sources
Beta strandi190 – 1956Combined sources
Helixi198 – 2003Combined sources
Helixi202 – 21312Combined sources
Beta strandi218 – 2247Combined sources
Beta strandi226 – 2283Combined sources
Helixi233 – 2364Combined sources
Helixi242 – 2443Combined sources
Turni245 – 2484Combined sources
Beta strandi251 – 2555Combined sources
Helixi259 – 27416Combined sources
Turni275 – 2773Combined sources
Beta strandi280 – 2856Combined sources
Beta strandi300 – 3023Combined sources
Helixi304 – 31411Combined sources
Helixi316 – 32611Combined sources
Helixi332 – 35524Combined sources
Helixi361 – 3633Combined sources
Beta strandi367 – 3715Combined sources
Beta strandi375 – 3784Combined sources
Beta strandi385 – 3884Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 29-390.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti278 – 2781G → E in BAG35194 (PubMed:14702039).Curated
Sequence conflicti301 – 3011Y → S in AAD23857 (PubMed:10077682).Curated
Sequence conflicti306 – 3061E → D in AAD23857 (PubMed:10077682).Curated
Sequence conflicti349 – 3491A → P in AAA60055 (PubMed:2828359).Curated
Sequence conflicti354 – 3541T → A in AAA60055 (PubMed:2828359).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101R → P in PDHAD; affects mitochondrial import of precursor protein. 1 Publication
Corresponds to variant rs137853257 [ dbSNP | Ensembl ].
VAR_010238
Natural varianti72 – 721R → C in PDHAD. 2 Publications
VAR_004949
Natural varianti113 – 1131H → D in PDHAD. 1 Publication
VAR_004950
Natural varianti136 – 1361A → T Probable disease-associated mutation found in a patient with moderate developmental delay, mild dysmorphism and mildly elevated serum lactate. 1 Publication
Corresponds to variant rs138727886 [ dbSNP | Ensembl ].
VAR_069381
Natural varianti162 – 1621G → R in PDHAD. 1 Publication
VAR_004951
Natural varianti167 – 1671V → M in PDHAD. 1 Publication
VAR_004952
Natural varianti199 – 1991A → T in PDHAD. 1 Publication
VAR_004953
Natural varianti205 – 2051F → L in PDHAD. 2 Publications
Corresponds to variant rs137853254 [ dbSNP | Ensembl ].
VAR_004954
Natural varianti210 – 2101M → V in PDHAD. 1 Publication
Corresponds to variant rs794727843 [ dbSNP | Ensembl ].
VAR_004955
Natural varianti217 – 2171P → L in PDHAD. 1 Publication
VAR_004956
Natural varianti231 – 2311T → A in PDHAD. 1 Publication
VAR_004957
Natural varianti243 – 2431Y → N in PDHAD. 1 Publication
Corresponds to variant rs137853255 [ dbSNP | Ensembl ].
VAR_021053
Natural varianti258 – 2581D → A in PDHAD. 1 Publication
Corresponds to variant rs137853253 [ dbSNP | Ensembl ].
VAR_004958
Natural varianti263 – 2631R → G in PDHAD. 4 Publications
Corresponds to variant rs28936081 [ dbSNP | Ensembl ].
VAR_004959
Natural varianti263 – 2631R → Q in PDHAD. 1 Publication
VAR_004960
Natural varianti282 – 2821M → L.3 Publications
Corresponds to variant rs2229137 [ dbSNP | Ensembl ].
VAR_021054
Natural varianti288 – 2881R → H in PDHAD. 1 Publication
Corresponds to variant rs137853258 [ dbSNP | Ensembl ].
VAR_021055
Natural varianti292 – 2921H → L in PDHAD. 1 Publication
VAR_004961
Natural varianti302 – 3021R → C in PDHAD; loss of activity; common mutation. 3 Publications
Corresponds to variant rs137853252 [ dbSNP | Ensembl ].
VAR_004962
Natural varianti302 – 3021R → H in PDHAD. 1 Publication
VAR_004963
Natural varianti305 – 3051E → EDSYRTRE in PDHAD. 1 Publication
VAR_020908
Natural varianti307 – 3071I → IPPHSYRTREEI in PDHAD. 1 Publication
VAR_020909
Natural varianti311 – 3111Missing in PDHAD. 2 Publications
VAR_004964
Natural varianti313 – 3131Missing in PDHAD. 1 Publication
VAR_004965
Natural varianti315 – 3151D → N in PDHAD. 1 Publication
Corresponds to variant rs28935187 [ dbSNP | Ensembl ].
VAR_021056
Natural varianti333 – 3331E → D.
Corresponds to variant rs2228067 [ dbSNP | Ensembl ].
VAR_050436
Natural varianti378 – 3781R → H in PDHAD. 3 Publications
Corresponds to variant rs137853250 [ dbSNP | Ensembl ].
VAR_004966

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei19 – 191P → PRHGLATLPSLVSISRLKQS SHLGLPKCWDYSHSLKTRQ in isoform 4. 2 PublicationsVSP_043363
Alternative sequencei96 – 961G → GQFLLPLT in isoform 2. 1 PublicationVSP_042569
Alternative sequencei170 – 20031Missing in isoform 3. 1 PublicationVSP_042570Add
BLAST

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
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. Positions 29-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111186. 51 interactions.
DIPiDIP-37652N.
IntActiP08559. 15 interactions.
MINTiMINT-3006251.

PTM databases

iPTMnetiP08559.
PhosphoSiteiP08559.
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.
GeneCardsiPDHA1.
HGNCiHGNC:8806. PDHA1.
HPAiHPA047487.
HPA047864.
HPA063053.
MalaCardsiPDHA1.
MIMi300502. gene.
312170. phenotype.
neXtProtiNX_P08559.
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.
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: September 7, 2016
This is version 204 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.