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Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial (EC 1.2.4.1) (PDHE1-A type I)

 ODPA_HUMAN              Reviewed;         390 AA.
P08559; A5YVE9; B2R5P7; B7Z3T7; B7Z3X5; Q53H41; Q5JPT8; Q9NP12;
Q9UBJ8; Q9UBU0; Q9UNG4; Q9UNG5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 3.
25-OCT-2017, entry version 216.
RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial;
EC=1.2.4.1;
AltName: Full=PDHE1-A type I;
Flags: Precursor;
Name=PDHA1; Synonyms=PHE1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Leukocyte;
PubMed=2227443; DOI=10.1016/0378-1119(90)90241-I;
Koike K., Urata Y., Matsuo S., Koike M.;
"Characterization and nucleotide sequence of the gene encoding the
human pyruvate dehydrogenase alpha-subunit.";
Gene 93:307-311(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2748588; DOI=10.1073/pnas.86.14.5330;
Ho L., Wexler I.D., Liu T.C., Thekkumkara T.J., Patel M.S.;
"Characterization of cDNAs encoding human pyruvate dehydrogenase alpha
subunit.";
Proc. Natl. Acad. Sci. U.S.A. 86:5330-5334(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain, and Liver;
Huh T.L., Chi Y.T., Casazza J.P., Veech R.L., Song B.J.;
Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3034892;
Dahl H.-H.M., Hunt S.M., Hutchison W.M., Brown G.K.;
"The human pyruvate dehydrogenase complex. Isolation of cDNA clones
for the E1 alpha subunit, sequence analysis, and characterization of
the mRNA.";
J. Biol. Chem. 262:7398-7403(1987).
[5]
SEQUENCE REVISION.
PubMed=2745444;
Maragos C., Hutchinson W.M., Hayasaki K., Brown G.K., Dahl H.-H.M.;
"Structural organization of the gene for the E1 alpha subunit of the
human pyruvate dehydrogenase complex.";
J. Biol. Chem. 264:12294-12298(1989).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2828359;
de Meirleir L., MacKay N., Wah A.M.L.H., Robinson B.H.;
"Isolation of a full-length complementary DNA coding for human E1
alpha subunit of the pyruvate dehydrogenase complex.";
J. Biol. Chem. 263:1991-1995(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3422424; DOI=10.1073/pnas.85.1.41;
Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.;
"Cloning and sequencing of cDNAs encoding alpha and beta subunits of
human pyruvate dehydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Okajima K.;
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-282.
TISSUE=Dermoid cancer;
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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
PROTEIN SEQUENCE OF 31-37, AND TRANSIT PEPTIDE.
PubMed=23146587; DOI=10.1016/j.ab.2012.10.040;
Candat A., Poupart P., Andrieu J.P., Chevrollier A., Reynier P.,
Rogniaux H., Avelange-Macherel M.H., Macherel D.;
"Experimental determination of organelle targeting-peptide cleavage
sites using transient expression of green fluorescent protein
translational fusions.";
Anal. Biochem. 434:44-51(2013).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-336, AND VARIANT LEU-282.
PubMed=10077682; DOI=10.1073/pnas.96.6.3320;
Harris E.E., Hey J.;
"X chromosome evidence for ancient human histories.";
Proc. Natl. Acad. Sci. U.S.A. 96:3320-3324(1999).
[16]
INVOLVEMENT IN PDHAD.
PubMed=1338114; DOI=10.1007/BF01800220;
Ito M., Huq A.H., Naito E., Saijo T., Takeda E., Kuroda Y.;
"Mutation of E1 alpha gene in a female patient with pyruvate
dehydrogenase deficiency due to rapid degradation of E1 protein.";
J. Inherit. Metab. Dis. 15:848-856(1992).
[17]
CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF
SER-232; SER-293 AND SER-300.
PubMed=7782287; DOI=10.1074/jbc.270.24.14297;
Korotchkina L.G., Patel M.S.;
"Mutagenesis studies of the phosphorylation sites of recombinant human
pyruvate dehydrogenase. Site-specific regulation.";
J. Biol. Chem. 270:14297-14304(1995).
[18]
PHOSPHORYLATION AT SER-232; SER-293 AND SER-300.
PubMed=11486000; DOI=10.1074/jbc.M103069200;
Korotchkina L.G., Patel M.S.;
"Site specificity of four pyruvate dehydrogenase kinase isoenzymes
toward the three phosphorylation sites of human pyruvate
dehydrogenase.";
J. Biol. Chem. 276:37223-37229(2001).
[19]
SUBUNIT.
PubMed=14638692; DOI=10.1074/jbc.M308172200;
Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
"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.";
J. Biol. Chem. 279:6921-6933(2004).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THIAMINE
PYROPHOSPHATE, AND COFACTOR.
PubMed=12651851; DOI=10.1074/jbc.M300339200;
Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.;
"Structural basis for flip-flop action of thiamin pyrophosphate-
dependent enzymes revealed by human pyruvate dehydrogenase.";
J. Biol. Chem. 278:21240-21246(2003).
[33]
REVIEW ON VARIANTS.
PubMed=1301207; DOI=10.1002/humu.1380010203;
Dahl H.-H.M., Brown G.K., Brown R.M., Hansen L.L., Kerr D.S.,
Wexler I.D., Patel M.S., de Meirleir L., Lissens W., Chun K.,
McKay N., Robinson B.H.;
"Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha
gene.";
Hum. Mutat. 1:97-102(1992).
[34]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-390, ENZYME REGULATION,
CATALYTIC ACTIVITY, MUTAGENESIS OF SER-293, AND PHOSPHORYLATION AT
SER-293.
PubMed=17474719; DOI=10.1021/bi700083z;
Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M.,
Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K.;
"Phosphorylation of serine 264 impedes active site accessibility in
the E1 component of the human pyruvate dehydrogenase multienzyme
complex.";
Biochemistry 46:6277-6287(2007).
[35]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-390 IN COMPLEX WITH PDHB,
SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
AND PHOSPHORYLATION AT SER-293 AND SER-300 BY PDK4.
PubMed=19081061; DOI=10.1016/j.str.2008.10.010;
Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J.,
Chuang D.T.;
"Structural basis for inactivation of the human pyruvate dehydrogenase
complex by phosphorylation: role of disordered phosphorylation
loops.";
Structure 16:1849-1859(2008).
[36]
VARIANTS PDHAD LYS-313 DEL AND HIS-378.
PubMed=1909401; DOI=10.1007/BF01800586;
Hansen L.L., Brown G.K., Kirby D.M., Dahl H.-H.M.;
"Characterization of the mutations in three patients with pyruvate
dehydrogenase E1 alpha deficiency.";
J. Inherit. Metab. Dis. 14:140-151(1991).
[37]
VARIANT PDHAD ASP-SER-TYR-ARG-THR-ARG-GLU-305 INS.
PubMed=1551669; DOI=10.1007/BF02265291;
De Meirleir L., Lissens W., Vamos E., Liebaers I.;
"Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair
insertion mutation in the E1 alpha subunit.";
Hum. Genet. 88:649-652(1992).
[38]
VARIANT PDHAD CYS-302.
PubMed=1293379; DOI=10.1007/BF01800219;
Dahl H.-H.M., Hansen L.L., Brown R.M., Danks D.M., Rogers J.G.,
Brown G.K.;
"X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in
heterozygous females: variable manifestation of the same mutation.";
J. Inherit. Metab. Dis. 15:835-847(1992).
[39]
VARIANT PDHAD ALA-258.
PubMed=8498846; DOI=10.1002/ana.410330616;
Matthews P.M., Marchington D.R., Squier M., Land J., Brown R.M.,
Brown G.K.;
"Molecular genetic characterization of an X-linked form of Leigh's
syndrome.";
Ann. Neurol. 33:652-655(1993).
[40]
VARIANTS PDHAD MET-167; THR-199; ALA-231; GLY-263 AND LEU-292.
PubMed=8504306; DOI=10.1093/hmg/2.4.449;
Chun K., McKay N., Petrova-Benedict R., Robinson B.H.;
"Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase
leading to deficiency of the pyruvate dehydrogenase complex.";
Hum. Mol. Genet. 2:449-454(1993).
[41]
VARIANTS PDHAD ASN-243; ASN-315 AND HIS-378, AND VARIANT LEU-282.
PubMed=8032855; DOI=10.1093/brain/117.3.435;
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.;
"Pyruvate dehydrogenase deficiency. Clinical presentation and
molecular genetic characterization of five new patients.";
Brain 117:435-443(1994).
[42]
VARIANT PDHAD PRO-PRO-HIS-SER-TYR-ARG-THR-ARG-GLU-GLU-ILE-307 INS.
PubMed=7545958; DOI=10.1093/hmg/3.6.1021;
Hansen L.L., Horn N., Dahl H.-H.M., Kruse T.A.;
"Pyruvate dehydrogenase deficiency caused by a 33 base pair
duplication in the PDH E1 alpha subunit.";
Hum. Mol. Genet. 3:1021-1022(1994).
[43]
VARIANT PDHAD LEU-205.
PubMed=8199595; DOI=10.1002/humu.1380030210;
Dahl H.-H.M., Brown G.K.;
"Pyruvate dehydrogenase deficiency in a male caused by a point
mutation (F205L) in the E1 alpha subunit.";
Hum. Mutat. 3:152-155(1994).
[44]
VARIANT PDHAD GLN-263.
PubMed=7967473; DOI=10.1007/BF00711616;
Awata H., Endo F., Tanoue A., Kitano A., Matsuda I.;
"Characterization of a point mutation in the pyruvate dehydrogenase E1
alpha gene from two boys with primary lactic acidaemia.";
J. Inherit. Metab. Dis. 17:189-195(1994).
[45]
VARIANTS PDHAD CYS-72; LEU-205; GLY-263; ARG-311 DEL AND HIS-378.
PubMed=7887409;
Chun K., MacKay N., Petrova-Benedict R., Federico A., Fois A.,
Cole D.E.C., Robertson E., Robinson B.H.;
"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.";
Am. J. Hum. Genet. 56:558-569(1995).
[46]
VARIANT PDHAD PRO-10.
PubMed=7573035;
Takakubo F., Cartwright P., Hoogenraad N., Thorburn D.R., Collins F.,
Lithgow T., Dahl H.-H.M.;
"An amino acid substitution in the pyruvate dehydrogenase E1 alpha
gene, affecting mitochondrial import of the precursor protein.";
Am. J. Hum. Genet. 57:772-780(1995).
[47]
VARIANT PDHAD LEU-217.
PubMed=7757088; DOI=10.1093/hmg/4.2.315;
Hemalatha S.G., Kerr D.S., Wexler I.D., Lusk M.M., Kaung M., Du Y.,
Kolli M., Schelper R.L., Patel M.S.;
"Pyruvate dehydrogenase complex deficiency due to a point mutation
(P188L) within the thiamine pyrophosphate binding loop of the E1 alpha
subunit.";
Hum. Mol. Genet. 4:315-318(1995).
[48]
VARIANTS PDHAD CYS-72; ASP-113; ARG-162; GLY-263; HIS-288 AND CYS-302.
PubMed=8664900;
DOI=10.1002/(SICI)1098-1004(1996)7:1<46::AID-HUMU6>3.3.CO;2-2;
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.;
"Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in
eight patients with a pyruvate dehydrogenase complex deficiency.";
Hum. Mutat. 7:46-51(1996).
[49]
VARIANTS PDHAD VAL-210 AND ARG-311 DEL.
PubMed=8844217;
DOI=10.1002/(SICI)1098-1004(1996)8:2<180::AID-HUMU11>3.3.CO;2-O;
Tripatara A., Kerr D.S., Lusk M.M., Kolli M., Tan J., Patel M.S.;
"Three new mutations of the pyruvate dehydrogenase alpha subunit: a
point mutation (M181V), 3 bp deletion (-R282), and 16 bp
insertion/frameshift (K358SVS-->TVDQS).";
Hum. Mutat. 8:180-182(1996).
[50]
VARIANT PDHAD GLY-263.
PubMed=9266390; DOI=10.1023/A:1005305614374;
Naito E., Ito M., Yokota I., Saijo T., Matsuda J., Osaka H.,
Kimura S., Kuroda Y.;
"Biochemical and molecular analysis of an X-linked case of Leigh
syndrome associated with thiamin-responsive pyruvate dehydrogenase
deficiency.";
J. Inherit. Metab. Dis. 20:539-548(1997).
[51]
VARIANTS PDHAD CYS-302 AND HIS-302.
PubMed=9671272;
DOI=10.1002/(SICI)1098-1004(1998)12:2<114::AID-HUMU6>3.0.CO;2-#;
Otero L.J., Brown R.M., Brown G.K.;
"Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit
gene: identification of further patients and in vitro demonstration of
pathogenicity.";
Hum. Mutat. 12:114-121(1998).
[52]
VARIANT THR-136.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
[53]
VARIANT PDHAD CYS-302.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
-!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
conversion of pyruvate to acetyl-CoA and CO(2), and thereby links
the glycolytic pathway to the tricarboxylic cycle.
{ECO:0000269|PubMed:19081061, ECO:0000269|PubMed:7782287}.
-!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
{ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061,
ECO:0000269|PubMed:7782287}.
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Evidence={ECO:0000269|PubMed:12651851,
ECO:0000269|PubMed:19081061};
-!- ENZYME REGULATION: Pyruvate dehydrogenase activity is inhibited by
phosphorylation of PDHA1; it is reactivated by dephosphorylation.
{ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061,
ECO:0000269|PubMed:7782287}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:12651851,
ECO:0000269|PubMed:14638692, ECO:0000269|PubMed:19081061}.
-!- INTERACTION:
P11177:PDHB; NbExp=3; IntAct=EBI-715747, EBI-1035872;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=P08559-1; Sequence=Displayed;
Name=2;
IsoId=P08559-2; Sequence=VSP_042569;
Note=No experimental confirmation available.;
Name=3;
IsoId=P08559-3; Sequence=VSP_042570;
Note=No experimental confirmation available.;
Name=4;
IsoId=P08559-4; Sequence=VSP_043363;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- PTM: 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. {ECO:0000269|PubMed:11486000,
ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}.
-!- PTM: Acetylation alters the phosphorylation pattern. Deacetylated
by SIRT3 (By similarity). {ECO:0000250}.
-!- DISEASE: 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.
{ECO:0000269|PubMed:1293379, ECO:0000269|PubMed:1338114,
ECO:0000269|PubMed:1551669, ECO:0000269|PubMed:1909401,
ECO:0000269|PubMed:27864847, ECO:0000269|PubMed:7545958,
ECO:0000269|PubMed:7573035, ECO:0000269|PubMed:7757088,
ECO:0000269|PubMed:7887409, ECO:0000269|PubMed:7967473,
ECO:0000269|PubMed:8032855, ECO:0000269|PubMed:8199595,
ECO:0000269|PubMed:8498846, ECO:0000269|PubMed:8504306,
ECO:0000269|PubMed:8664900, ECO:0000269|PubMed:8844217,
ECO:0000269|PubMed:9266390, ECO:0000269|PubMed:9671272}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SEQUENCE CAUTION:
Sequence=AAA60055.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAB59581.1; Type=Frameshift; Positions=106, 175; Evidence={ECO:0000305};
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EMBL; D90084; BAA14121.1; -; Genomic_DNA.
EMBL; M24848; AAA36533.1; -; mRNA.
EMBL; X52709; CAA36933.1; -; mRNA.
EMBL; X52710; CAA36934.1; -; mRNA.
EMBL; M27257; AAA60051.1; -; Genomic_DNA.
EMBL; M29155; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29156; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29157; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29158; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29159; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29160; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29161; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29162; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29163; AAA60051.1; JOINED; Genomic_DNA.
EMBL; M29164; AAA60051.1; JOINED; Genomic_DNA.
EMBL; L13318; AAA60227.1; -; mRNA.
EMBL; J03503; AAA60055.1; ALT_INIT; mRNA.
EMBL; J03575; AAA60050.1; -; mRNA.
EMBL; L48690; AAB59581.1; ALT_FRAME; mRNA.
EMBL; EF590117; ABQ59099.1; -; mRNA.
EMBL; AK293250; BAH11476.1; -; mRNA.
EMBL; AK296457; BAH12361.1; -; mRNA.
EMBL; AK312263; BAG35194.1; -; mRNA.
EMBL; AK296341; BAH12323.1; -; mRNA.
EMBL; AK222740; BAD96460.1; -; mRNA.
EMBL; AL732326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471074; EAW98960.1; -; Genomic_DNA.
EMBL; BC002406; AAH02406.1; -; mRNA.
EMBL; AF125053; AAD23841.1; -; Genomic_DNA.
EMBL; AF125054; AAD23842.1; -; Genomic_DNA.
EMBL; AF125055; AAD23843.1; -; Genomic_DNA.
EMBL; AF125056; AAD23844.1; -; Genomic_DNA.
EMBL; AF125057; AAD23845.1; -; Genomic_DNA.
EMBL; AF125058; AAD23846.1; -; Genomic_DNA.
EMBL; AF125059; AAD23847.1; -; Genomic_DNA.
EMBL; AF125060; AAD23848.1; -; Genomic_DNA.
EMBL; AF125061; AAD23849.1; -; Genomic_DNA.
EMBL; AF125062; AAD23850.1; -; Genomic_DNA.
EMBL; AF125063; AAD23851.1; -; Genomic_DNA.
EMBL; AF125064; AAD23852.1; -; Genomic_DNA.
EMBL; AF125065; AAD23853.1; -; Genomic_DNA.
EMBL; AF125066; AAD23854.1; -; Genomic_DNA.
EMBL; AF125067; AAD23855.1; -; Genomic_DNA.
EMBL; AF125068; AAD23856.1; -; Genomic_DNA.
EMBL; AF125069; AAD23857.1; -; Genomic_DNA.
EMBL; AF125070; AAD23858.1; -; Genomic_DNA.
EMBL; AF125071; AAD23859.1; -; Genomic_DNA.
EMBL; AF125072; AAD23860.1; -; Genomic_DNA.
EMBL; AF125073; AAD23861.1; -; Genomic_DNA.
EMBL; AF125074; AAD23862.1; -; Genomic_DNA.
EMBL; AF125075; AAD23863.1; -; Genomic_DNA.
EMBL; AF125076; AAD23864.1; -; Genomic_DNA.
EMBL; AF125078; AAD23866.1; -; Genomic_DNA.
EMBL; AF125079; AAD23867.1; -; Genomic_DNA.
EMBL; AF125080; AAD23868.1; -; Genomic_DNA.
EMBL; AF125081; AAD23869.1; -; Genomic_DNA.
EMBL; AF125082; AAD23870.1; -; Genomic_DNA.
EMBL; AF125083; AAD23871.1; -; Genomic_DNA.
EMBL; AF125084; AAD23872.1; -; Genomic_DNA.
EMBL; AF125085; AAD23873.1; -; Genomic_DNA.
EMBL; AF125086; AAD23874.1; -; Genomic_DNA.
EMBL; AF125087; AAD23875.1; -; Genomic_DNA.
EMBL; AF125088; AAD23876.1; -; Genomic_DNA.
CCDS; CCDS14192.1; -. [P08559-1]
CCDS; CCDS55380.1; -. [P08559-4]
CCDS; CCDS55381.1; -. [P08559-2]
CCDS; CCDS55382.1; -. [P08559-3]
PIR; JQ0770; DEHUPA.
RefSeq; NP_000275.1; NM_000284.3. [P08559-1]
RefSeq; NP_001166925.1; NM_001173454.1. [P08559-4]
RefSeq; NP_001166926.1; NM_001173455.1. [P08559-2]
RefSeq; NP_001166927.1; NM_001173456.1. [P08559-3]
UniGene; Hs.530331; -.
PDB; 1NI4; X-ray; 1.95 A; A/C=30-390.
PDB; 2OZL; X-ray; 1.90 A; A/C=30-390.
PDB; 3EXE; X-ray; 1.98 A; A/C/E/G=30-390.
PDB; 3EXF; X-ray; 3.00 A; A/C/E/G=30-390.
PDB; 3EXG; X-ray; 3.01 A; 1/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y=30-390.
PDB; 3EXH; X-ray; 2.44 A; A/C/E/G=30-390.
PDB; 3EXI; X-ray; 2.20 A; A=30-390.
PDBsum; 1NI4; -.
PDBsum; 2OZL; -.
PDBsum; 3EXE; -.
PDBsum; 3EXF; -.
PDBsum; 3EXG; -.
PDBsum; 3EXH; -.
PDBsum; 3EXI; -.
ProteinModelPortal; P08559; -.
SMR; P08559; -.
BioGrid; 111186; 55.
CORUM; P08559; -.
DIP; DIP-37652N; -.
IntAct; P08559; 21.
MINT; MINT-3006251; -.
DrugBank; DB00157; NADH.
iPTMnet; P08559; -.
PhosphoSitePlus; P08559; -.
SwissPalm; P08559; -.
BioMuta; PDHA1; -.
DMDM; 129063; -.
REPRODUCTION-2DPAGE; IPI00306301; -.
UCD-2DPAGE; P08559; -.
EPD; P08559; -.
MaxQB; P08559; -.
PeptideAtlas; P08559; -.
PRIDE; P08559; -.
TopDownProteomics; P08559-3; -. [P08559-3]
TopDownProteomics; P08559-4; -. [P08559-4]
DNASU; 5160; -.
Ensembl; ENST00000379806; ENSP00000369134; ENSG00000131828. [P08559-4]
Ensembl; ENST00000422285; ENSP00000394382; ENSG00000131828. [P08559-1]
Ensembl; ENST00000540249; ENSP00000440761; ENSG00000131828. [P08559-3]
Ensembl; ENST00000545074; ENSP00000438550; ENSG00000131828. [P08559-2]
GeneID; 5160; -.
KEGG; hsa:5160; -.
UCSC; uc004czg.5; human. [P08559-1]
CTD; 5160; -.
DisGeNET; 5160; -.
EuPathDB; HostDB:ENSG00000131828.13; -.
GeneCards; PDHA1; -.
HGNC; HGNC:8806; PDHA1.
HPA; HPA047487; -.
HPA; HPA047864; -.
HPA; HPA063053; -.
MalaCards; PDHA1; -.
MIM; 300502; gene.
MIM; 312170; phenotype.
neXtProt; NX_P08559; -.
OpenTargets; ENSG00000131828; -.
Orphanet; 70474; Leigh syndrome with cardiomyopathy.
Orphanet; 79243; Pyruvate dehydrogenase E1-alpha deficiency.
PharmGKB; PA33150; -.
GeneTree; ENSGT00530000063174; -.
HOGENOM; HOG000281336; -.
HOVERGEN; HBG001863; -.
InParanoid; P08559; -.
KO; K00161; -.
OMA; RRFEDKC; -.
OrthoDB; EOG091G0966; -.
PhylomeDB; P08559; -.
TreeFam; TF300742; -.
BioCyc; MetaCyc:HS05573-MONOMER; -.
BRENDA; 1.2.4.1; 2681.
Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-70268; Pyruvate metabolism.
SABIO-RK; P08559; -.
SIGNOR; P08559; -.
ChiTaRS; PDHA1; human.
EvolutionaryTrace; P08559; -.
GeneWiki; Pyruvate_dehydrogenase_(lipoamide)_alpha_1; -.
GenomeRNAi; 5160; -.
PRO; PR:P08559; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000131828; -.
CleanEx; HS_PDHA1; -.
ExpressionAtlas; P08559; baseline and differential.
Genevisible; P08559; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
GO; GO:0034604; F:pyruvate dehydrogenase (NAD+) activity; IEA:Ensembl.
GO; GO:0004738; F:pyruvate dehydrogenase activity; IDA:UniProtKB.
GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IEA:Ensembl.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
GO; GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.
InterPro; IPR001017; DH_E1.
InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
InterPro; IPR029061; THDP-binding.
Pfam; PF00676; E1_dh; 1.
SUPFAM; SSF52518; SSF52518; 1.
TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Carbohydrate metabolism; Complete proteome; Direct protein sequencing;
Disease mutation; Glucose metabolism; Leigh syndrome; Mitochondrion;
Oxidoreductase; Phosphoprotein; Polymorphism;
Primary mitochondrial disease; Pyruvate; Reference proteome;
Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle.
TRANSIT 1 30 Mitochondrion.
{ECO:0000269|PubMed:23146587}.
CHAIN 31 390 Pyruvate dehydrogenase E1 component
subunit alpha, somatic form,
mitochondrial.
/FTId=PRO_0000020440.
MOD_RES 63 63 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 63 63 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 231 231 Phosphothreonine.
{ECO:0000250|UniProtKB:P26284}.
MOD_RES 232 232 Phosphoserine; by PDK1.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11486000}.
MOD_RES 244 244 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 244 244 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 277 277 N6-succinyllysine.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 293 293 Phosphoserine; by PDK1, PDK2, PDK3 and
PDK4. {ECO:0000269|PubMed:11486000,
ECO:0000269|PubMed:17474719,
ECO:0000269|PubMed:19081061}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 300 300 Phosphoserine; by PDK1, PDK2, PDK3 and
PDK4. {ECO:0000269|PubMed:11486000,
ECO:0000269|PubMed:19081061}.
MOD_RES 301 301 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 313 313 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 313 313 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 321 321 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 336 336 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35486}.
MOD_RES 385 385 N6-succinyllysine.
{ECO:0000250|UniProtKB:P35486}.
VAR_SEQ 19 19 P -> PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLK
TRQ (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.8}.
/FTId=VSP_043363.
VAR_SEQ 96 96 G -> GQFLLPLT (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042569.
VAR_SEQ 170 200 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042570.
VARIANT 10 10 R -> P (in PDHAD; affects mitochondrial
import of precursor protein;
dbSNP:rs137853257).
{ECO:0000269|PubMed:7573035}.
/FTId=VAR_010238.
VARIANT 72 72 R -> C (in PDHAD; dbSNP:rs863224148).
{ECO:0000269|PubMed:7887409,
ECO:0000269|PubMed:8664900}.
/FTId=VAR_004949.
VARIANT 113 113 H -> D (in PDHAD).
{ECO:0000269|PubMed:8664900}.
/FTId=VAR_004950.
VARIANT 136 136 A -> T (probable disease-associated
mutation found in a patient with moderate
developmental delay, mild dysmorphism and
mildly elevated serum lactate;
dbSNP:rs138727886).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_069381.
VARIANT 162 162 G -> R (in PDHAD; dbSNP:rs866868610).
{ECO:0000269|PubMed:8664900}.
/FTId=VAR_004951.
VARIANT 167 167 V -> M (in PDHAD).
{ECO:0000269|PubMed:8504306}.
/FTId=VAR_004952.
VARIANT 199 199 A -> T (in PDHAD).
{ECO:0000269|PubMed:8504306}.
/FTId=VAR_004953.
VARIANT 205 205 F -> L (in PDHAD; dbSNP:rs137853254).
{ECO:0000269|PubMed:7887409,
ECO:0000269|PubMed:8199595}.
/FTId=VAR_004954.
VARIANT 210 210 M -> V (in PDHAD; dbSNP:rs794727843).
{ECO:0000269|PubMed:8844217}.
/FTId=VAR_004955.
VARIANT 217 217 P -> L (in PDHAD).
{ECO:0000269|PubMed:7757088}.
/FTId=VAR_004956.
VARIANT 231 231 T -> A (in PDHAD).
{ECO:0000269|PubMed:8504306}.
/FTId=VAR_004957.
VARIANT 243 243 Y -> N (in PDHAD; dbSNP:rs137853255).
{ECO:0000269|PubMed:8032855}.
/FTId=VAR_021053.
VARIANT 258 258 D -> A (in PDHAD; dbSNP:rs137853253).
{ECO:0000269|PubMed:8498846}.
/FTId=VAR_004958.
VARIANT 263 263 R -> G (in PDHAD; dbSNP:rs137853259).
{ECO:0000269|PubMed:7887409,
ECO:0000269|PubMed:8504306,
ECO:0000269|PubMed:8664900,
ECO:0000269|PubMed:9266390}.
/FTId=VAR_004959.
VARIANT 263 263 R -> Q (in PDHAD).
{ECO:0000269|PubMed:7967473}.
/FTId=VAR_004960.
VARIANT 282 282 M -> L (in dbSNP:rs2229137).
{ECO:0000269|PubMed:10077682,
ECO:0000269|PubMed:8032855,
ECO:0000269|Ref.10}.
/FTId=VAR_021054.
VARIANT 288 288 R -> H (in PDHAD; dbSNP:rs137853258).
{ECO:0000269|PubMed:8664900}.
/FTId=VAR_021055.
VARIANT 292 292 H -> L (in PDHAD).
{ECO:0000269|PubMed:8504306}.
/FTId=VAR_004961.
VARIANT 302 302 R -> C (in PDHAD; loss of activity;
common mutation; dbSNP:rs137853252).
{ECO:0000269|PubMed:1293379,
ECO:0000269|PubMed:27864847,
ECO:0000269|PubMed:8664900,
ECO:0000269|PubMed:9671272}.
/FTId=VAR_004962.
VARIANT 302 302 R -> H (in PDHAD).
{ECO:0000269|PubMed:9671272}.
/FTId=VAR_004963.
VARIANT 305 305 E -> EDSYRTRE (in PDHAD).
{ECO:0000269|PubMed:1551669}.
/FTId=VAR_020908.
VARIANT 307 307 I -> IPPHSYRTREEI (in PDHAD).
{ECO:0000269|PubMed:7545958}.
/FTId=VAR_020909.
VARIANT 311 311 Missing (in PDHAD).
{ECO:0000269|PubMed:7887409,
ECO:0000269|PubMed:8844217}.
/FTId=VAR_004964.
VARIANT 313 313 Missing (in PDHAD).
{ECO:0000269|PubMed:1909401}.
/FTId=VAR_004965.
VARIANT 315 315 D -> N (in PDHAD; dbSNP:rs137853256).
{ECO:0000269|PubMed:8032855}.
/FTId=VAR_021056.
VARIANT 333 333 E -> D (in dbSNP:rs2228067).
/FTId=VAR_050436.
VARIANT 378 378 R -> H (in PDHAD; dbSNP:rs137853250).
{ECO:0000269|PubMed:1909401,
ECO:0000269|PubMed:7887409,
ECO:0000269|PubMed:8032855}.
/FTId=VAR_004966.
MUTAGEN 232 232 S->A: Abolishes inactivation by
phosphorylation; when associated with A-
293 and A-300.
{ECO:0000269|PubMed:7782287}.
MUTAGEN 293 293 S->A: Reduces enzyme activity. Abolishes
inactivation by phosphorylation; when
associated with A-232 and A-300.
{ECO:0000269|PubMed:17474719,
ECO:0000269|PubMed:7782287}.
MUTAGEN 293 293 S->E: Interferes with substrate binding.
{ECO:0000269|PubMed:17474719,
ECO:0000269|PubMed:7782287}.
MUTAGEN 300 300 S->A: Abolishes inactivation by
phosphorylation; when associated with A-
232 and A-293.
{ECO:0000269|PubMed:7782287}.
CONFLICT 278 278 G -> E (in Ref. 9; BAG35194).
{ECO:0000305}.
CONFLICT 301 301 Y -> S (in Ref. 15; AAD23857).
{ECO:0000305}.
CONFLICT 306 306 E -> D (in Ref. 15; AAD23857).
{ECO:0000305}.
CONFLICT 349 349 A -> P (in Ref. 6; AAA60055).
{ECO:0000305}.
CONFLICT 354 354 T -> A (in Ref. 6; AAA60055).
{ECO:0000305}.
STRAND 32 37 {ECO:0000244|PDB:2OZL}.
STRAND 42 45 {ECO:0000244|PDB:2OZL}.
STRAND 52 57 {ECO:0000244|PDB:2OZL}.
HELIX 58 83 {ECO:0000244|PDB:2OZL}.
STRAND 85 87 {ECO:0000244|PDB:3EXF}.
HELIX 98 106 {ECO:0000244|PDB:2OZL}.
STRAND 112 115 {ECO:0000244|PDB:2OZL}.
HELIX 121 126 {ECO:0000244|PDB:2OZL}.
HELIX 131 138 {ECO:0000244|PDB:2OZL}.
TURN 145 148 {ECO:0000244|PDB:2OZL}.
HELIX 151 153 {ECO:0000244|PDB:3EXE}.
TURN 167 169 {ECO:0000244|PDB:2OZL}.
HELIX 170 184 {ECO:0000244|PDB:2OZL}.
STRAND 190 195 {ECO:0000244|PDB:2OZL}.
HELIX 198 200 {ECO:0000244|PDB:2OZL}.
HELIX 202 213 {ECO:0000244|PDB:2OZL}.
STRAND 218 224 {ECO:0000244|PDB:2OZL}.
STRAND 226 228 {ECO:0000244|PDB:2OZL}.
HELIX 233 236 {ECO:0000244|PDB:2OZL}.
HELIX 242 244 {ECO:0000244|PDB:2OZL}.
TURN 245 248 {ECO:0000244|PDB:2OZL}.
STRAND 251 255 {ECO:0000244|PDB:2OZL}.
HELIX 259 274 {ECO:0000244|PDB:2OZL}.
TURN 275 277 {ECO:0000244|PDB:3EXG}.
STRAND 280 285 {ECO:0000244|PDB:2OZL}.
STRAND 300 302 {ECO:0000244|PDB:2OZL}.
HELIX 304 314 {ECO:0000244|PDB:2OZL}.
HELIX 316 326 {ECO:0000244|PDB:2OZL}.
HELIX 332 355 {ECO:0000244|PDB:2OZL}.
HELIX 361 363 {ECO:0000244|PDB:2OZL}.
STRAND 367 371 {ECO:0000244|PDB:2OZL}.
STRAND 375 378 {ECO:0000244|PDB:2OZL}.
STRAND 385 388 {ECO:0000244|PDB:2OZL}.
SEQUENCE 390 AA; 43296 MW; 4D685BBE44A92D4B CRC64;
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS


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