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P08559

- ODPA_HUMAN

UniProt

P08559 - ODPA_HUMAN

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
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 3 (01 May 1992)
      Previous versions | rss
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    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 pyrophosphate.2 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

    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

    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

    ArrayExpressiP08559.
    BgeeiP08559.
    CleanExiHS_PDHA1.
    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. 25 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 – 376
    Beta strandi42 – 454
    Beta strandi52 – 576
    Helixi58 – 8326
    Beta strandi85 – 873
    Helixi98 – 1069
    Beta strandi112 – 1154
    Helixi121 – 1266
    Helixi131 – 1388
    Turni145 – 1484
    Helixi151 – 1533
    Turni167 – 1693
    Helixi170 – 18415
    Beta strandi190 – 1956
    Helixi198 – 2003
    Helixi202 – 21312
    Beta strandi218 – 2247
    Beta strandi226 – 2283
    Helixi233 – 2364
    Helixi242 – 2443
    Turni245 – 2484
    Beta strandi251 – 2555
    Helixi259 – 27416
    Turni275 – 2773
    Beta strandi280 – 2856
    Beta strandi300 – 3023
    Helixi304 – 31411
    Helixi316 – 32611
    Helixi332 – 35524
    Helixi361 – 3633
    Beta strandi367 – 3715
    Beta strandi375 – 3784
    Beta strandi385 – 3884

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP    50
    PVTTVLTRED GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC 100
    CVGLEAGINP TDHLITAYRA HGFTFTRGLS VREILAELTG RKGGCAKGKG 150
    GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA CKYNGKDEVC LTLYGDGAAN 200
    QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST DYYKRGDFIP 250
    GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 300
    YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA 350
    QFATADPEPP LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 390
    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 AAB59581.1 differs from that shown. Reason: Frameshift at positions 106 and 175.
    The sequence AAA60055.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 25 interactions.
    DIPi DIP-37652N.
    IntActi P08559. 9 interactions.
    MINTi MINT-3006251.
    STRINGi 9606.ENSP00000394382.

    Chemistry

    DrugBanki DB00157. NADH.

    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.
    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

    ArrayExpressi P08559.
    Bgeei P08559.
    CleanExi HS_PDHA1.
    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

    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: October 1, 2014
    This is version 183 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