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P08559

- ODPA_HUMAN

UniProt

P08559 - ODPA_HUMAN

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Protein

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Gene

PDHA1

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.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

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

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  2. cellular metabolic process Source: Reactome
  3. glucose metabolic process Source: UniProtKB-KW
  4. glycolytic process Source: InterPro
  5. pyruvate metabolic process Source: Reactome
  6. regulation of acetyl-CoA biosynthetic process from pyruvate Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. tricarboxylic acid cycle Source: UniProtKB
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.
ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
SABIO-RKP08559.

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
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:8806. PDHA1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
  2. mitochondrion Source: UniProt
  3. nucleus Source: UniProt
  4. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:312170]: An 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.14 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101R → P in PDHAD; affects mitochondrial import of precursor protein. 1 Publication
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 X-LS; PDHAD. 2 Publications
VAR_004954
Natural varianti210 – 2101M → V in PDHAD. 1 Publication
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
VAR_021053
Natural varianti258 – 2581D → A in X-LS; PDHAD. 1 Publication
VAR_004958
Natural varianti263 – 2631R → G in PDHAD and X-LS. 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
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
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 X-LS; PDHAD. 3 Publications
VAR_004966
Leigh syndrome, X-linked (X-LS) [MIM:308930]: A X-linked form of Leigh syndrome, an early-onset progressive neurodegenerative disorder characterized by the presence of focal, bilateral lesions in one or more areas of the central nervous system including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved and include psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, dysphagia, and lactic acidosis.
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti205 – 2051F → L in X-LS; PDHAD. 2 Publications
VAR_004954
Natural varianti258 – 2581D → A in X-LS; PDHAD. 1 Publication
VAR_004958
Natural varianti263 – 2631R → G in PDHAD and X-LS. 4 Publications
Corresponds to variant rs28936081 [ dbSNP | Ensembl ].
VAR_004959
Natural varianti378 – 3781R → H in X-LS; PDHAD. 3 Publications
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

MIMi308930. phenotype.
312170. phenotype.
Orphaneti70474. Leigh syndrome with cardiomyopathy.
79243. Pyruvate dehydrogenase E1-alpha deficiency.
PharmGKBiPA33150.

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 residuei232 – 2321Phosphoserine; by PDK13 Publications
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-acetyllysine1 Publication
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.5 Publications
Acetylation alters the phosphorylation pattern. Deacetylated by SIRT3 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP08559.
PaxDbiP08559.
PeptideAtlasiP08559.
PRIDEiP08559.

2D gel databases

REPRODUCTION-2DPAGEIPI00306301.
UCD-2DPAGEP08559.

PTM databases

PhosphoSiteiP08559.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP08559.
CleanExiHS_PDHA1.
ExpressionAtlasiP08559. baseline and differential.
GenevestigatoriP08559.

Organism-specific databases

HPAiHPA047487.
HPA047864.

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. 28 interactions.
DIPiDIP-37652N.
IntActiP08559. 9 interactions.
MINTiMINT-3006251.
STRINGi9606.ENSP00000394382.

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

eggNOGiCOG1071.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
HOVERGENiHBG001863.
InParanoidiP08559.
KOiK00161.
OMAiRGPNQWI.
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. Align

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 AAA60055.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB59581.1 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
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
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 X-LS; PDHAD. 2 Publications
VAR_004954
Natural varianti210 – 2101M → V in PDHAD. 1 Publication
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
VAR_021053
Natural varianti258 – 2581D → A in X-LS; PDHAD. 1 Publication
VAR_004958
Natural varianti263 – 2631R → G in PDHAD and X-LS. 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
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
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 X-LS; PDHAD. 3 Publications
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.4. human. [P08559-1]
uc004czh.4. human. [P08559-4]
uc011mjc.2. human. [P08559-2]
uc011mjd.2. human. [P08559-3]

Polymorphism databases

DMDMi129063.

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 .
CCDSi CCDS14192.1. [P08559-1 ]
CCDS55380.1. [P08559-4 ]
CCDS55381.1. [P08559-2 ]
CCDS55382.1. [P08559-3 ]
PIRi JQ0770. DEHUPA.
RefSeqi NP_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 ]
UniGenei Hs.530331.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NI4 X-ray 1.95 A/C 30-390 [» ]
2OZL X-ray 1.90 A/C 30-390 [» ]
3EXE X-ray 1.98 A/C/E/G 30-390 [» ]
3EXF X-ray 3.00 A/C/E/G 30-390 [» ]
3EXG X-ray 3.01 1/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y 30-390 [» ]
3EXH X-ray 2.44 A/C/E/G 30-390 [» ]
3EXI X-ray 2.20 A 30-390 [» ]
ProteinModelPortali P08559.
SMRi P08559. Positions 29-390.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111186. 28 interactions.
DIPi DIP-37652N.
IntActi P08559. 9 interactions.
MINTi MINT-3006251.
STRINGi 9606.ENSP00000394382.

PTM databases

PhosphoSitei P08559.

Polymorphism databases

DMDMi 129063.

2D gel databases

REPRODUCTION-2DPAGE IPI00306301.
UCD-2DPAGE P08559.

Proteomic databases

MaxQBi P08559.
PaxDbi P08559.
PeptideAtlasi P08559.
PRIDEi P08559.

Protocols and materials databases

DNASUi 5160.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379806 ; ENSP00000369134 ; ENSG00000131828 . [P08559-4 ]
ENST00000422285 ; ENSP00000394382 ; ENSG00000131828 . [P08559-1 ]
ENST00000540249 ; ENSP00000440761 ; ENSG00000131828 . [P08559-3 ]
ENST00000545074 ; ENSP00000438550 ; ENSG00000131828 . [P08559-2 ]
GeneIDi 5160.
KEGGi hsa:5160.
UCSCi uc004czg.4. human. [P08559-1 ]
uc004czh.4. human. [P08559-4 ]
uc011mjc.2. human. [P08559-2 ]
uc011mjd.2. human. [P08559-3 ]

Organism-specific databases

CTDi 5160.
GeneCardsi GC0XP019271.
HGNCi HGNC:8806. PDHA1.
HPAi HPA047487.
HPA047864.
MIMi 300502. gene.
308930. phenotype.
312170. phenotype.
neXtProti NX_P08559.
Orphaneti 70474. Leigh syndrome with cardiomyopathy.
79243. Pyruvate dehydrogenase E1-alpha deficiency.
PharmGKBi PA33150.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1071.
GeneTreei ENSGT00530000063174.
HOGENOMi HOG000281336.
HOVERGENi HBG001863.
InParanoidi P08559.
KOi K00161.
OMAi RGPNQWI.
PhylomeDBi P08559.
TreeFami TF300742.

Enzyme and pathway databases

BioCyci MetaCyc:HS05573-MONOMER.
Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.
REACT_2071. Pyruvate metabolism.
SABIO-RK P08559.

Miscellaneous databases

ChiTaRSi PDHA1. human.
EvolutionaryTracei P08559.
GeneWikii Pyruvate_dehydrogenase_(lipoamide)_alpha_1.
GenomeRNAii 5160.
NextBioi 19962.
PROi P08559.
SOURCEi Search...

Gene expression databases

Bgeei P08559.
CleanExi HS_PDHA1.
ExpressionAtlasi P08559. baseline and differential.
Genevestigatori P08559.

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. "Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit."
    Koike K., Urata Y., Matsuo S., Koike M.
    Gene 93:307-311(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Leukocyte.
  2. "Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit."
    Ho L., Wexler I.D., Liu T.C., Thekkumkara T.J., Patel M.S.
    Proc. Natl. Acad. Sci. U.S.A. 86:5330-5334(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Huh T.L., Chi Y.T., Casazza J.P., Veech R.L., Song B.J.
    Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain and Liver.
  4. "The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA."
    Dahl H.-H.M., Hunt S.M., Hutchison W.M., Brown G.K.
    J. Biol. Chem. 262:7398-7403(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex."
    Maragos C., Hutchinson W.M., Hayasaki K., Brown G.K., Dahl H.-H.M.
    J. Biol. Chem. 264:12294-12298(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  6. "Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex."
    de Meirleir L., MacKay N., Wah A.M.L.H., Robinson B.H.
    J. Biol. Chem. 263:1991-1995(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase."
    Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.
    Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  8. Okajima K.
    Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
  9. "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] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Thalamus.
  10. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-282.
    Tissue: Dermoid cancer.
  11. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. "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] (ISOFORM 1).
    Tissue: Muscle.
  14. "Experimental determination of organelle targeting-peptide cleavage sites using transient expression of green fluorescent protein translational fusions."
    Candat A., Poupart P., Andrieu J.P., Chevrollier A., Reynier P., Rogniaux H., Avelange-Macherel M.H., Macherel D.
    Anal. Biochem. 434:44-51(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 31-37, TRANSIT PEPTIDE.
  15. "X chromosome evidence for ancient human histories."
    Harris E.E., Hey J.
    Proc. Natl. Acad. Sci. U.S.A. 96:3320-3324(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-336, VARIANT LEU-282.
  16. "Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein."
    Ito M., Huq A.H., Naito E., Saijo T., Takeda E., Kuroda Y.
    J. Inherit. Metab. Dis. 15:848-856(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PDHAD.
  17. "Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation."
    Korotchkina L.G., Patel M.S.
    J. Biol. Chem. 270:14297-14304(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-232; SER-293 AND SER-300.
  18. "Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase."
    Korotchkina L.G., Patel M.S.
    J. Biol. Chem. 276:37223-37229(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-232; SER-293 AND SER-300.
  19. "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.
  20. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  22. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. "Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase."
    Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.
    J. Biol. Chem. 278:21240-21246(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THIAMINE PYROPHOSPHATE, COFACTOR.
  30. Cited for: REVIEW ON VARIANTS.
  31. "Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex."
    Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.
    Biochemistry 46:6277-6287(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-390, ENZYME REGULATION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-293, PHOSPHORYLATION AT SER-293.
  32. "Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops."
    Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J., Chuang D.T.
    Structure 16:1849-1859(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-390 IN COMPLEX WITH PDHB, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, PHOSPHORYLATION AT SER-293 AND SER-300 BY PDK4.
  33. "Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency."
    Hansen L.L., Brown G.K., Kirby D.M., Dahl H.-H.M.
    J. Inherit. Metab. Dis. 14:140-151(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD LYS-313 DEL, VARIANT X-LS HIS-378.
  34. "Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit."
    De Meirleir L., Lissens W., Vamos E., Liebaers I.
    Hum. Genet. 88:649-652(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD ASP-SER-TYR-ARG-THR-ARG-GLU-305 INS.
  35. "X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation."
    Dahl H.-H.M., Hansen L.L., Brown R.M., Danks D.M., Rogers J.G., Brown G.K.
    J. Inherit. Metab. Dis. 15:835-847(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD CYS-302.
  36. "Molecular genetic characterization of an X-linked form of Leigh's syndrome."
    Matthews P.M., Marchington D.R., Squier M., Land J., Brown R.M., Brown G.K.
    Ann. Neurol. 33:652-655(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT X-LS ALA-258.
  37. "Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex."
    Chun K., McKay N., Petrova-Benedict R., Robinson B.H.
    Hum. Mol. Genet. 2:449-454(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHAD MET-167; THR-199; ALA-231; GLY-263 AND LEU-292.
  38. "Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients."
    Matthews P.M., Brown R.M., Otero L.J., Marchington D.R., LeGris M., Howes R., Meadows L.S., Shevell M., Scriver C.R., Brown G.K.
    Brain 117:435-443(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHAD ASN-243; ASN-315 AND HIS-378, VARIANT LEU-282.
  39. "Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit."
    Hansen L.L., Horn N., Dahl H.-H.M., Kruse T.A.
    Hum. Mol. Genet. 3:1021-1022(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD PRO-PRO-HIS-SER-TYR-ARG-THR-ARG-GLU-GLU-ILE-307 INS.
  40. "Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit."
    Dahl H.-H.M., Brown G.K.
    Hum. Mutat. 3:152-155(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT X-LS LEU-205.
  41. "Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia."
    Awata H., Endo F., Tanoue A., Kitano A., Matsuda I.
    J. Inherit. Metab. Dis. 17:189-195(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD GLN-263.
  42. "Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex."
    Chun K., MacKay N., Petrova-Benedict R., Federico A., Fois A., Cole D.E.C., Robertson E., Robinson B.H.
    Am. J. Hum. Genet. 56:558-569(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHAD CYS-72; GLY-263 AND ARG-311 DEL, VARIANTS X-LS LEU-205 AND HIS-378.
  43. "An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein."
    Takakubo F., Cartwright P., Hoogenraad N., Thorburn D.R., Collins F., Lithgow T., Dahl H.-H.M.
    Am. J. Hum. Genet. 57:772-780(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD PRO-10.
  44. "Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit."
    Hemalatha S.G., Kerr D.S., Wexler I.D., Lusk M.M., Kaung M., Du Y., Kolli M., Schelper R.L., Patel M.S.
    Hum. Mol. Genet. 4:315-318(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PDHAD LEU-217.
  45. "Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency."
    Lissens W., de Meirleir L., Seneca S., Benelli C., Marsac C., Poll-The B.T., Briones P., Ruitenbeek W., van Diggelen O., Chaigne D., Ramaekers V., Liebaers I.
    Hum. Mutat. 7:46-51(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHAD CYS-72; ASP-113; ARG-162; GLY-263; HIS-288 AND CYS-302.
  46. "Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS)."
    Tripatara A., Kerr D.S., Lusk M.M., Kolli M., Tan J., Patel M.S.
    Hum. Mutat. 8:180-182(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHAD VAL-210 AND ARG-311 DEL.
  47. "Biochemical and molecular analysis of an X-linked case of Leigh syndrome associated with thiamin-responsive pyruvate dehydrogenase deficiency."
    Naito E., Ito M., Yokota I., Saijo T., Matsuda J., Osaka H., Kimura S., Kuroda Y.
    J. Inherit. Metab. Dis. 20:539-548(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT X-LS GLY-263.
  48. "Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity."
    Otero L.J., Brown R.M., Brown G.K.
    Hum. Mutat. 12:114-121(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDHAD CYS-302 AND HIS-302.
  49. Cited for: VARIANT THR-136.

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 26, 2014
This is version 185 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

External Data

Dasty 3