ODPB_HUMAN
ID ODPB_HUMAN Reviewed; 359 AA.
AC P11177; B2R7L0; B4DDD7; Q6FH45; Q9BQ27; Q9UFK3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 239.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta, mitochondrial;
DE Short=PDHE1-B;
DE EC=1.2.4.1;
DE Flags: Precursor;
GN Name=PDHB; Synonyms=PHE1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2323578; DOI=10.1016/0378-1119(90)90294-2;
RA Ho L., Patel M.S.;
RT "Cloning and cDNA sequence of the beta-subunit component of human pyruvate
RT dehydrogenase complex.";
RL Gene 86:297-302(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1702713; DOI=10.1111/j.1432-1033.1990.tb15656.x;
RA Chun K., MacKay N., Willard H.F., Robinson B.H.;
RT "Isolation, characterization and chromosomal localization of cDNA clones
RT for the E1 beta subunit of the pyruvate dehydrogenase complex.";
RL Eur. J. Biochem. 194:587-592(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT VAL-31.
RX PubMed=2376596; DOI=10.1016/s0021-9258(19)38301-2;
RA Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J.;
RT "Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta
RT subunit and its regulation in tricarboxylic acid cycle-deficient
RT fibroblast.";
RL J. Biol. Chem. 265:13320-13326(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=2377599; DOI=10.1073/pnas.87.15.5594;
RA Koike K., Urata Y., Koike M.;
RT "Molecular cloning and characterization of human pyruvate dehydrogenase
RT beta subunit gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-31.
RX PubMed=3422424; DOI=10.1073/pnas.85.1.41;
RA Koike K., Ohta S., Urata Y., Kagawa Y., Koike M.;
RT "Cloning and sequencing of cDNAs encoding alpha and beta subunits of human
RT pyruvate dehydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain cortex;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
RX PubMed=2829898; DOI=10.1016/0006-291x(88)90714-0;
RA Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E.,
RA Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S.;
RT "Identification of a cDNA clone for the beta-subunit of the pyruvate
RT dehydrogenase component of human pyruvate dehydrogenase complex.";
RL Biochem. Biophys. Res. Commun. 150:904-908(1988).
RN [13]
RP PROTEIN SEQUENCE OF 31-43.
RC TISSUE=Heart;
RX PubMed=7895732; DOI=10.1002/elps.11501501209;
RA Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J.;
RT "The human myocardial two-dimensional gel protein database: update 1994.";
RL Electrophoresis 15:1459-1465(1994).
RN [14]
RP PROTEIN SEQUENCE OF 31-55.
RX PubMed=2295468; DOI=10.1002/hep.1840110105;
RA Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y.,
RA Namihisa T.;
RT "Isolation of tryptic fragment of antigen from mitochondrial inner membrane
RT proteins reacting with antimitochondrial antibody in sera of patients with
RT primary biliary cirrhosis.";
RL Hepatology 11:16-23(1990).
RN [15]
RP SUBUNIT.
RX PubMed=14638692; DOI=10.1074/jbc.m308172200;
RA Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
RT "Organization of the cores of the mammalian pyruvate dehydrogenase complex
RT formed by E2 and E2 plus the E3-binding protein and their capacities to
RT bind the E1 and E3 components.";
RL J. Biol. Chem. 279:6921-6933(2004).
RN [16]
RP INTERACTION WITH DLAT, AND MUTAGENESIS OF GLU-259; GLU-262; GLU-264;
RP ASP-319 AND ILE-359.
RX PubMed=20160912; DOI=10.1016/j.molcatb.2009.05.001;
RA Patel M.S., Korotchkina L.G., Sidhu S.;
RT "Interaction of E1 and E3 components with the core proteins of the human
RT pyruvate dehydrogenase complex.";
RL J. Mol. Catal., B Enzym. 61:2-6(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 32-359 IN COMPLEX WITH THIAMINE
RP PYROPHOSPHATE, AND COFACTOR.
RX PubMed=12651851; DOI=10.1074/jbc.m300339200;
RA Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S.;
RT "Structural basis for flip-flop action of thiamin pyrophosphate-dependent
RT enzymes revealed by human pyruvate dehydrogenase.";
RL J. Biol. Chem. 278:21240-21246(2003).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 32-359, SUBUNIT, AND FUNCTION.
RX PubMed=17474719; DOI=10.1021/bi700083z;
RA Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P.,
RA Sidhu S., Brauer J., Patel M.S., Tittmann K.;
RT "Phosphorylation of serine 264 impedes active site accessibility in the E1
RT component of the human pyruvate dehydrogenase multienzyme complex.";
RL Biochemistry 46:6277-6287(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 31-359, CATALYTIC ACTIVITY,
RP SUBUNIT, COFACTOR, AND FUNCTION.
RX PubMed=19081061; DOI=10.1016/j.str.2008.10.010;
RA Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J., Chuang D.T.;
RT "Structural basis for inactivation of the human pyruvate dehydrogenase
RT complex by phosphorylation: role of disordered phosphorylation loops.";
RL Structure 16:1849-1859(2008).
RN [23]
RP VARIANTS PDHBD CYS-132 AND SER-344.
RX PubMed=15138885; DOI=10.1007/s00439-004-1124-8;
RA Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H.,
RA Brown G.K.;
RT "Mutations in the gene for the E1beta subunit: a novel cause of pyruvate
RT dehydrogenase deficiency.";
RL Hum. Genet. 115:123-127(2004).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the
CC glycolytic pathway to the tricarboxylic cycle.
CC {ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000269|PubMed:19081061};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:19081061};
CC -!- SUBUNIT: Heterotetramer of two PDHA1 and two PDHB subunits
CC (PubMed:12651851, PubMed:17474719, PubMed:19081061). The heterotetramer
CC interacts with DLAT, and is part of the multimeric pyruvate
CC dehydrogenase complex that contains multiple copies of pyruvate
CC dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and
CC lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). These subunits are
CC bound to an inner core composed of about 48 DLAT and 12 PDHX molecules
CC (PubMed:14638692). Interacts with DLAT (PubMed:20160912).
CC {ECO:0000269|PubMed:12651851, ECO:0000269|PubMed:14638692,
CC ECO:0000269|PubMed:17474719, ECO:0000269|PubMed:19081061,
CC ECO:0000269|PubMed:20160912}.
CC -!- INTERACTION:
CC P11177; P10515: DLAT; NbExp=7; IntAct=EBI-1035872, EBI-2959723;
CC P11177; P08559: PDHA1; NbExp=4; IntAct=EBI-1035872, EBI-715747;
CC P11177-1; P08559-1: PDHA1; NbExp=4; IntAct=EBI-25766519, EBI-25766512;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P11177-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11177-2; Sequence=VSP_012675;
CC Name=3;
CC IsoId=P11177-3; Sequence=VSP_043364;
CC -!- DISEASE: Pyruvate dehydrogenase E1-beta deficiency (PDHBD)
CC [MIM:614111]: An enzymatic defect causing primary lactic acidosis in
CC children. It is associated with a broad clinical spectrum ranging from
CC fatal lactic acidosis in the newborn to chronic neurologic dysfunction
CC with structural abnormalities in the central nervous system without
CC systemic acidosis. {ECO:0000269|PubMed:15138885}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
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DR EMBL; M34479; AAA36428.1; -; mRNA.
DR EMBL; M19123; AAA60052.1; ALT_SEQ; mRNA.
DR EMBL; M54788; AAA60053.1; -; mRNA.
DR EMBL; M34055; AAA60233.1; -; mRNA.
DR EMBL; M34056; AAA60054.1; -; mRNA.
DR EMBL; D90086; BAA14123.1; -; Genomic_DNA.
DR EMBL; J03576; AAA88097.1; -; mRNA.
DR EMBL; AL117618; CAB56017.1; -; mRNA.
DR EMBL; CR541911; CAG46709.1; -; mRNA.
DR EMBL; AK293153; BAG56698.1; -; mRNA.
DR EMBL; AK313022; BAG35857.1; -; mRNA.
DR EMBL; AC135507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65371.1; -; Genomic_DNA.
DR EMBL; BC000439; AAH00439.1; -; mRNA.
DR EMBL; BC001924; AAH01924.1; -; mRNA.
DR EMBL; X57778; CAA40924.1; -; mRNA.
DR CCDS; CCDS2890.1; -. [P11177-1]
DR CCDS; CCDS54602.1; -. [P11177-3]
DR CCDS; CCDS82795.1; -. [P11177-2]
DR PIR; JU0145; DEHUPB.
DR RefSeq; NP_000916.2; NM_000925.3. [P11177-1]
DR RefSeq; NP_001166939.1; NM_001173468.1. [P11177-3]
DR RefSeq; NP_001302465.1; NM_001315536.1. [P11177-2]
DR PDB; 1NI4; X-ray; 1.95 A; B/D=31-359.
DR PDB; 2OZL; X-ray; 1.90 A; B/D=32-359.
DR PDB; 3EXE; X-ray; 1.98 A; B/D/F/H=31-359.
DR PDB; 3EXF; X-ray; 3.00 A; B/D/F/H=31-359.
DR PDB; 3EXG; X-ray; 3.01 A; 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z=31-359.
DR PDB; 3EXH; X-ray; 2.44 A; B/D/F/H=31-359.
DR PDB; 3EXI; X-ray; 2.20 A; B=31-359.
DR PDB; 6CER; X-ray; 2.69 A; B/D/F/H=31-359.
DR PDB; 6CFO; X-ray; 2.70 A; B/D=31-359.
DR PDBsum; 1NI4; -.
DR PDBsum; 2OZL; -.
DR PDBsum; 3EXE; -.
DR PDBsum; 3EXF; -.
DR PDBsum; 3EXG; -.
DR PDBsum; 3EXH; -.
DR PDBsum; 3EXI; -.
DR PDBsum; 6CER; -.
DR PDBsum; 6CFO; -.
DR AlphaFoldDB; P11177; -.
DR SMR; P11177; -.
DR BioGRID; 111188; 263.
DR ComplexPortal; CPX-376; Pyruvate dehydrogenase E1 heterotetramer.
DR ComplexPortal; CPX-6233; Mitochondrial pyruvate dehydrogenase complex, somatic variant.
DR ComplexPortal; CPX-6242; Mitochondrial pyruvate dehydrogenase complex, testis-specific variant.
DR DIP; DIP-37651N; -.
DR IntAct; P11177; 59.
DR MINT; P11177; -.
DR STRING; 9606.ENSP00000307241; -.
DR ChEMBL; CHEMBL4882; -.
DR DrugBank; DB00157; NADH.
DR DrugBank; DB00119; Pyruvic acid.
DR GlyGen; P11177; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P11177; -.
DR MetOSite; P11177; -.
DR PhosphoSitePlus; P11177; -.
DR SwissPalm; P11177; -.
DR BioMuta; PDHB; -.
DR DMDM; 134044259; -.
DR REPRODUCTION-2DPAGE; IPI00549885; -.
DR SWISS-2DPAGE; P11177; -.
DR UCD-2DPAGE; P11177; -.
DR EPD; P11177; -.
DR jPOST; P11177; -.
DR MassIVE; P11177; -.
DR MaxQB; P11177; -.
DR PaxDb; P11177; -.
DR PeptideAtlas; P11177; -.
DR PRIDE; P11177; -.
DR ProteomicsDB; 52715; -. [P11177-1]
DR ProteomicsDB; 52716; -. [P11177-2]
DR ProteomicsDB; 52717; -. [P11177-3]
DR TopDownProteomics; P11177-1; -. [P11177-1]
DR Antibodypedia; 31652; 240 antibodies from 34 providers.
DR DNASU; 5162; -.
DR Ensembl; ENST00000302746.11; ENSP00000307241.6; ENSG00000168291.13. [P11177-1]
DR Ensembl; ENST00000383714.8; ENSP00000373220.4; ENSG00000168291.13. [P11177-2]
DR Ensembl; ENST00000485460.5; ENSP00000417267.1; ENSG00000168291.13. [P11177-3]
DR GeneID; 5162; -.
DR KEGG; hsa:5162; -.
DR MANE-Select; ENST00000302746.11; ENSP00000307241.6; NM_000925.4; NP_000916.2.
DR UCSC; uc003dkf.4; human. [P11177-1]
DR CTD; 5162; -.
DR DisGeNET; 5162; -.
DR GeneCards; PDHB; -.
DR GeneReviews; PDHB; -.
DR HGNC; HGNC:8808; PDHB.
DR HPA; ENSG00000168291; Tissue enhanced (skeletal muscle, tongue).
DR MalaCards; PDHB; -.
DR MIM; 179060; gene.
DR MIM; 614111; phenotype.
DR neXtProt; NX_P11177; -.
DR OpenTargets; ENSG00000168291; -.
DR Orphanet; 255138; Pyruvate dehydrogenase E1-beta deficiency.
DR PharmGKB; PA33152; -.
DR VEuPathDB; HostDB:ENSG00000168291; -.
DR eggNOG; KOG0524; Eukaryota.
DR GeneTree; ENSGT00940000155146; -.
DR HOGENOM; CLU_012907_1_1_1; -.
DR InParanoid; P11177; -.
DR OMA; SRMRHHC; -.
DR OrthoDB; 875272at2759; -.
DR PhylomeDB; P11177; -.
DR TreeFam; TF105674; -.
DR BioCyc; MetaCyc:HS09727-MON; -.
DR BRENDA; 1.2.1.104; 2681.
DR BRENDA; 1.2.4.1; 2681.
DR PathwayCommons; P11177; -.
DR Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
DR Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
DR Reactome; R-HSA-70268; Pyruvate metabolism.
DR SABIO-RK; P11177; -.
DR SignaLink; P11177; -.
DR SIGNOR; P11177; -.
DR BioGRID-ORCS; 5162; 40 hits in 1084 CRISPR screens.
DR ChiTaRS; PDHB; human.
DR EvolutionaryTrace; P11177; -.
DR GeneWiki; Pyruvate_dehydrogenase_(lipoamide)_beta; -.
DR GenomeRNAi; 5162; -.
DR Pharos; P11177; Tbio.
DR PRO; PR:P11177; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P11177; protein.
DR Bgee; ENSG00000168291; Expressed in endothelial cell and 210 other tissues.
DR ExpressionAtlas; P11177; baseline and differential.
DR Genevisible; P11177; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; IPI:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IDA:GO_Central.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
DR GO; GO:0006099; P:tricarboxylic acid cycle; TAS:ProtInc.
DR Gene3D; 3.40.50.920; -; 1.
DR InterPro; IPR027110; PDHB.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR033248; Transketolase_C.
DR PANTHER; PTHR11624; PTHR11624; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; SSF52518; 1.
DR SUPFAM; SSF52922; SSF52922; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism;
KW Direct protein sequencing; Disease variant; Glucose metabolism;
KW Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate;
KW Reference proteome; Thiamine pyrophosphate; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..30
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:2295468,
FT ECO:0000269|PubMed:7895732"
FT CHAIN 31..359
FT /note="Pyruvate dehydrogenase E1 component subunit beta,
FT mitochondrial"
FT /id="PRO_0000020457"
FT BINDING 89
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000269|PubMed:12651851"
FT SITE 319
FT /note="Important for interaction with DLAT"
FT /evidence="ECO:0000269|PubMed:20160912"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9D051"
FT MOD_RES 354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D051"
FT VAR_SEQ 16..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11230166"
FT /id="VSP_012675"
FT VAR_SEQ 135..152
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043364"
FT VARIANT 31
FT /note="L -> V"
FT /evidence="ECO:0000269|PubMed:2376596,
FT ECO:0000269|PubMed:3422424"
FT /id="VAR_004967"
FT VARIANT 132
FT /note="Y -> C (in PDHBD; dbSNP:rs28935769)"
FT /evidence="ECO:0000269|PubMed:15138885"
FT /id="VAR_030954"
FT VARIANT 344
FT /note="P -> S (in PDHBD; dbSNP:rs28933391)"
FT /evidence="ECO:0000269|PubMed:15138885"
FT /id="VAR_021058"
FT MUTAGEN 259
FT /note="E->A,Q: Does not affect interaction with DLAT."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 262
FT /note="E->A,Q: Does not affect interaction with DLAT."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 264
FT /note="E->A,Q: Does not affect interaction with DLAT."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 319
FT /note="D->A: Inhibits interaction with DLAT. Does not
FT affect pyruvate decarboxylase activity. Loss of multienzyme
FT pyruvate dehydrogenase complex activity."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 319
FT /note="D->N: Reduces interaction with DLAT. Reduces
FT multienzyme pyruvate dehydrogenase complex activity. Does
FT not affect pyruvate decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 359
FT /note="I->A: Reduces pyruvate decarboxylase and multienzyme
FT pyruvate dehydrogenase complex activity. Does not affect
FT interaction with DLAT."
FT /evidence="ECO:0000269|PubMed:20160912"
FT MUTAGEN 359
FT /note="Missing: Reduces pyruvate decarboxylase and
FT multienzyme pyruvate dehydrogenase complex activity. Does
FT not affect interaction with DLAT."
FT /evidence="ECO:0000269|PubMed:20160912"
FT CONFLICT 9..13
FT /note="RRPLR -> AETPS (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="M -> G (in Ref. 13; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="Q -> G (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 213..221
FT /note="PPEAQSKDF -> LRKLSQKIL (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="P -> L (in Ref. 4; AAA88097/BAA14123)"
FT /evidence="ECO:0000305"
FT CONFLICT 310..312
FT /note="MEG -> NGS (in Ref. 5)"
FT /evidence="ECO:0000305"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2OZL"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:3EXI"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:2OZL"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 89..101
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 113..119
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 120..124
FT /evidence="ECO:0007829|PDB:2OZL"
FT TURN 125..129
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2OZL"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3EXI"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 180..192
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:2OZL"
FT TURN 203..207
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 245..257
FT /evidence="ECO:0007829|PDB:2OZL"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 276..286
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2OZL"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3EXE"
FT HELIX 336..340
FT /evidence="ECO:0007829|PDB:2OZL"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:2OZL"
SQ SEQUENCE 359 AA; 39233 MW; AB459B1259FBDBD3 CRC64;
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI
DQVINSAAKT YYMSGGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV
SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI
