Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Pyruvate kinase PKM (EC 2.7.1.40) (Cytosolic thyroid hormone-binding protein) (CTHBP) (Opa-interacting protein 3) (OIP-3) (Pyruvate kinase 2/3) (Pyruvate kinase muscle isozyme) (Thyroid hormone-binding protein 1) (THBP1) (Tumor M2-PK) (p58)

 KPYM_HUMAN              Reviewed;         531 AA.
P14618; A6NFK3; B2R5N8; B3KRY0; B4DFX8; B4DUU6; P14786; Q53GK4;
Q96E76; Q9BWB5; Q9UCV6; Q9UPF2;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
20-JUN-2018, entry version 237.
RecName: Full=Pyruvate kinase PKM;
EC=2.7.1.40;
AltName: Full=Cytosolic thyroid hormone-binding protein;
Short=CTHBP;
AltName: Full=Opa-interacting protein 3;
Short=OIP-3;
AltName: Full=Pyruvate kinase 2/3;
AltName: Full=Pyruvate kinase muscle isozyme;
AltName: Full=Thyroid hormone-binding protein 1;
Short=THBP1;
AltName: Full=Tumor M2-PK;
AltName: Full=p58;
Name=PKM; Synonyms=OIP3, PK2, PK3, PKM2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
TISSUE=Liver;
PubMed=2854097; DOI=10.1016/0378-1119(88)90515-X;
Tani K., Yoshida M.C., Satoh H., Mitamura K., Noguchi T., Tanaka T.,
Fujii H., Miwa S.;
"Human M2-type pyruvate kinase: cDNA cloning, chromosomal assignment
and expression in hepatoma.";
Gene 73:509-516(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2), PROTEIN SEQUENCE OF 70-98,
SUBUNIT, AND ENZYME REGULATION.
PubMed=2813362; DOI=10.1073/pnas.86.20.7861;
Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.;
"Cytosolic thyroid hormone-binding protein is a monomer of pyruvate
kinase.";
Proc. Natl. Acad. Sci. U.S.A. 86:7861-7865(1989).
[3]
ERRATUM.
Kato H., Fukuda T., Parkison C., McPhie P., Cheng S.-Y.;
Proc. Natl. Acad. Sci. U.S.A. 87:1625-1625(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=2040271; DOI=10.1111/j.1432-1033.1991.tb15991.x;
Takenaka M., Noguchi T., Sadahiro S., Hirai H., Yamada K., Matsuda T.,
Imai E., Tanaka T.;
"Isolation and characterization of the human pyruvate kinase M gene.";
Eur. J. Biochem. 198:101-106(1991).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS M1 AND 3).
TISSUE=Astrocyte, and Fetal brain;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2).
TISSUE=Kidney;
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.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[9]
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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2), AND VARIANT
VAL-204.
TISSUE=Kidney, Lung carcinoma, Ovary, Retina, and Rhabdomyosarcoma;
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).
[11]
PROTEIN SEQUENCE OF 2-43; 57-73; 93-115; 126-135; 167-186; 231-246;
271-311; 401-422; 448-455 AND 490-498, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUL-2005) to UniProtKB.
[12]
PROTEIN SEQUENCE OF 2-18, CATALYTIC ACTIVITY, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND INTERACTION WITH THYROID
HORMONE.
PubMed=1854723; DOI=10.1021/bi00243a010;
Ashizawa K., McPhie P., Lin K.-H., Cheng S.-Y.;
"An in vitro novel mechanism of regulating the activity of pyruvate
kinase M2 by thyroid hormone and fructose 1, 6-bisphosphate.";
Biochemistry 30:7105-7111(1991).
[13]
PROTEIN SEQUENCE OF 2-32.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[14]
PROTEIN SEQUENCE OF 74-89, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[15]
PROTEIN SEQUENCE OF 174-186; 295-305 AND 401-422 (ISOFORMS M2/3),
INTERACTION WITH TRIM35 (ISOFORM M2), SUBCELLULAR LOCATION, AND MASS
SPECTROMETRY.
PubMed=25263439; DOI=10.1038/onc.2014.325;
Chen Z., Wang Z., Guo W., Zhang Z., Zhao F., Zhao Y., Jia D., Ding J.,
Wang H., Yao M., He X.;
"TRIM35 Interacts with pyruvate kinase isoform M2 to suppress the
Warburg effect and tumorigenicity in hepatocellular carcinoma.";
Oncogene 34:3946-3956(2015).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 368-531 (ISOFORM M2).
PubMed=9466265; DOI=10.1046/j.1365-2958.1998.00670.x;
Williams J.M., Chen G.-C., Zhu L., Rest R.F.;
"Using the yeast two-hybrid system to identify human epithelial cell
proteins that bind gonococcal Opa proteins: intracellular gonococci
bind pyruvate kinase via their Opa proteins and require host pyruvate
for growth.";
Mol. Microbiol. 27:171-186(1998).
[17]
INTERACTION WITH HERC1.
PubMed=12650930; DOI=10.1016/S0014-5793(03)00205-9;
Garcia-Gonzalo F.R., Cruz C., Munoz P., Mazurek S., Eigenbrodt E.,
Ventura F., Bartrons R., Rosa J.L.;
"Interaction between HERC1 and M2-type pyruvate kinase.";
FEBS Lett. 539:78-84(2003).
[18]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[22]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17308100; DOI=10.1158/0008-5472.CAN-06-2870;
Stetak A., Veress R., Ovadi J., Csermely P., Keri G., Ullrich A.;
"Nuclear translocation of the tumor marker pyruvate kinase M2 induces
programmed cell death.";
Cancer Res. 67:1602-1608(2007).
[23]
INTERACTION WITH PML, ENZYME REGULATION, SUBUNIT, AND SUBCELLULAR
LOCATION.
PubMed=18298799; DOI=10.1111/j.1365-2443.2008.01165.x;
Shimada N., Shinagawa T., Ishii S.;
"Modulation of M2-type pyruvate kinase activity by the cytoplasmic PML
tumor suppressor protein.";
Genes Cells 13:245-254(2008).
[24]
INTERACTION WITH POU5F1, IDENTIFICATION BY MASS SPECTROMETRY,
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18191611; DOI=10.1016/j.biocel.2007.11.009;
Lee J., Kim H.K., Han Y.-M., Kim J.;
"Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with
Oct-4 in regulating transcription.";
Int. J. Biochem. Cell Biol. 40:1043-1054(2008).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND 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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND 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).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; TYR-175 AND THR-195,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62; LYS-89; LYS-166; LYS-266
AND LYS-433, 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).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, 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).
[32]
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).
[33]
INTERACTION WITH EGLN3 AND HIF1A, SUBCELLULAR LOCATION, INDUCTION,
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, HYDROXYLATION AT
PRO-403 AND PRO-408, AND MUTAGENESIS OF PRO-403 AND PRO-408.
PubMed=21620138; DOI=10.1016/j.cell.2011.03.054;
Luo W., Hu H., Chang R., Zhong J., Knabel M., O'Meally R., Cole R.N.,
Pandey A., Semenza G.L.;
"Pyruvate kinase M2 is a PHD3-stimulated coactivator for hypoxia-
inducible factor 1.";
Cell 145:732-744(2011).
[34]
INTERACTION WITH EGLN3.
PubMed=21483450; DOI=10.1038/cr.2011.66;
Chen N., Rinner O., Czernik D., Nytko K.J., Zheng D., Stiehl D.P.,
Zamboni N., Gstaiger M., Frei C.;
"The oxygen sensor PHD3 limits glycolysis under hypoxia via direct
binding to pyruvate kinase.";
Cell Res. 21:983-986(2011).
[35]
ACETYLATION AT LYS-305.
PubMed=21700219; DOI=10.1016/j.molcel.2011.04.025;
Lv L., Li D., Zhao D., Lin R., Chu Y., Zhang H., Zha Z., Liu Y.,
Li Z., Xu Y., Wang G., Huang Y., Xiong Y., Guan K.L., Lei Q.Y.;
"Acetylation targets the M2 isoform of pyruvate kinase for degradation
through chaperone-mediated autophagy and promotes tumor growth.";
Mol. Cell 42:719-730(2011).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, 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).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; THR-41; TYR-105 AND
SER-127, 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).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND 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).
[39]
METHYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-166, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[41]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115; LYS-266 AND LYS-270,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[43]
X-RAY CRYSTALLOGRAPHY (2.82 ANGSTROMS) OF ISOFORM M2 IN COMPLEX WITH
OXALATE AND FBP, CATALYTIC ACTIVITY, SUBUNIT, ENZYME MECHANISM, ENZYME
REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15996096; DOI=10.1021/bi0474923;
Dombrauckas J.D., Santarsiero B.D., Mesecar A.D.;
"Structural basis for tumor pyruvate kinase M2 allosteric regulation
and catalysis.";
Biochemistry 44:9417-9429(2005).
[44]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
Structural genomics consortium (SGC);
"Structure of human muscle pyruvate kinase (PKM2).";
Submitted (MAY-2005) to the PDB data bank.
[45]
X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 14-531 ALONE AND IN COMPLEX
WITH FBP, AND ENZYME REGULATION.
PubMed=18337815; DOI=10.1038/nature06667;
Christofk H.R., Vander Heiden M.G., Wu N., Asara J.M., Cantley L.C.;
"Pyruvate kinase M2 is a phosphotyrosine-binding protein.";
Nature 452:181-186(2008).
[46]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 2-531, ENZYME REGULATION BY
SERINE, MAGNESIUM-BINDING SITES, SUBUNIT, AND MUTAGENESIS OF SER-437
AND HIS-464.
PubMed=23064226; DOI=10.1038/nature11540;
Chaneton B., Hillmann P., Zheng L., Martin A.C., Maddocks O.D.,
Chokkathukalam A., Coyle J.E., Jankevics A., Holding F.P.,
Vousden K.H., Frezza C., O'Reilly M., Gottlieb E.;
"Serine is a natural ligand and allosteric activator of pyruvate
kinase M2.";
Nature 491:458-462(2012).
[47]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH ATP;
FRUCTOSE-1-6-DIPHOSPHATE; MAGNESIUM IONS AND POTASSIUM IONS.
PubMed=23530218; DOI=10.1073/pnas.1217157110;
Morgan H.P., O'Reilly F.J., Wear M.A., O'Neill J.R.,
Fothergill-Gilmore L.A., Hupp T., Walkinshaw M.D.;
"M2 pyruvate kinase provides a mechanism for nutrient sensing and
regulation of cell proliferation.";
Proc. Natl. Acad. Sci. U.S.A. 110:5881-5886(2013).
-!- FUNCTION: Glycolytic enzyme that catalyzes the transfer of a
phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating
ATP. Stimulates POU5F1-mediated transcriptional activation. Plays
a general role in caspase independent cell death of tumor cells.
The ratio between the highly active tetrameric form and nearly
inactive dimeric form determines whether glucose carbons are
channeled to biosynthetic processes or used for glycolytic ATP
production. The transition between the 2 forms contributes to the
control of glycolysis and is important for tumor cell
proliferation and survival. {ECO:0000269|PubMed:17308100,
ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:21620138}.
-!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
{ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:23530218};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000305|PubMed:23530218};
-!- ENZYME REGULATION: Isoform M2 is allosterically activated by D-
fructose 1,6-bisphosphate (FBP). Inhibited by oxalate and 3,3',5-
triiodo-L-thyronine (T3). The activity of the tetrameric form is
inhibited by PML. Selective binding to tyrosine-phosphorylated
peptides releases the allosteric activator FBP, leading to
inhibition of PKM enzymatic activity, this diverts glucose
metabolites from energy production to anabolic processes when
cells are stimulated by certain growth factors. Glycolytic flux
are highly dependent on de novo biosynthesis of serine and
glycine, and serine is a natural ligand and allosteric activator
of isoform M2. {ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:18298799, ECO:0000269|PubMed:18337815,
ECO:0000269|PubMed:1854723, ECO:0000269|PubMed:23064226,
ECO:0000269|PubMed:2813362}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.7 mM for phosphoenolpyruvate (at 32 degrees Celsius, pH
8.0) {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723};
KM=0.17 mM for phosphoenolpyruvate (in the presence of 2 mM D-
fructose 1,6-bisphosphate (FBP), at 32 degrees Celsius, pH 8.0)
{ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723};
KM=0.34 mM for ADP (at 32 degrees Celsius, pH 8.0)
{ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723};
KM=0.24 mM for ADP (in the presence of 2 mM FBP, at 32 degrees
Celsius, pH 8.0) {ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:1854723};
KM=0.13 mM for phosphoenolpyruvate (in the presence of 2 mM FBP,
at 25 degrees Celsius) {ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:1854723};
KM=0.63 mM for ADP (in the presence of 2 mM FBP, at 25 degrees
Celsius) {ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:1854723};
pH dependence:
Optimum pH for T3 binding is 6.0-6.5. Increase in pH causes T3
binding to drop, does not bind T3 above pH 9.0 or below pH 5.0.
{ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723};
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 5/5.
-!- SUBUNIT: Monomer and homotetramer. Exists as a monomer in the
absence of D-fructose 1,6-bisphosphate (FBP), and reversibly
associates to form a homotetramer in the presence of FBP. The
monomeric form binds T3. Tetramer formation induces pyruvate
kinase activity. The tetrameric form has high affinity for the
substrate and is associated within the glycolytic enzyme complex.
Exists in a nearly inactive dimeric form in tumor cells and the
dimeric form has less affinity for the substrate. Binding to
certain oncoproteins such as HPV-16 E7 oncoprotein can trigger
dimerization. FBP stimulates the formation of tetramers from
dimers. Interacts with HERC1, POU5F1 and PML. Interacts (isoform
M2) with EGLN3; the interaction hydroxylates PKM under hypoxia and
enhances binding to HIF1A. Interacts (isoform M2) with HIF1A; the
interaction is enhanced by binding of EGLN3, promoting enhanced
transcription activity under hypoxia. Interacts (isoform M2, but
not isoform M1) with TRIM35; this interaction prevents FGFR1-
dependent tyrosine phosphorylation (PubMed:25263439).
{ECO:0000269|PubMed:12650930, ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:18298799,
ECO:0000269|PubMed:18337815, ECO:0000269|PubMed:1854723,
ECO:0000269|PubMed:21483450, ECO:0000269|PubMed:21620138,
ECO:0000269|PubMed:23064226, ECO:0000269|PubMed:25263439,
ECO:0000269|PubMed:2813362}.
-!- INTERACTION:
Q9WMX2:- (xeno); NbExp=4; IntAct=EBI-353408, EBI-710918;
P10398:ARAF; NbExp=2; IntAct=EBI-353408, EBI-365961;
P49407:ARRB1; NbExp=3; IntAct=EBI-353408, EBI-743313;
P32121:ARRB2; NbExp=4; IntAct=EBI-353408, EBI-714559;
P35222:CTNNB1; NbExp=4; IntAct=EBI-353408, EBI-491549;
P53355:DAPK1; NbExp=3; IntAct=EBI-353408, EBI-358616;
Q9H6Z9:EGLN3; NbExp=2; IntAct=EBI-4304679, EBI-1175354;
Q16665:HIF1A; NbExp=7; IntAct=EBI-4304679, EBI-447269;
P68431:HIST1H3D; NbExp=3; IntAct=EBI-4304679, EBI-79722;
P42858:HTT; NbExp=3; IntAct=EBI-353408, EBI-466029;
P27361:MAPK3; NbExp=3; IntAct=EBI-4304679, EBI-73995;
P04049:RAF1; NbExp=3; IntAct=EBI-353408, EBI-365996;
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-353408, EBI-717399;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25263439}.
Nucleus. Note=Translocates to the nucleus in response to different
apoptotic stimuli. Nuclear translocation is sufficient to induce
cell death that is caspase independent, isoform-specific and
independent of its enzymatic activity.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=M2; Synonyms=M2-PK, PKM2;
IsoId=P14618-1; Sequence=Displayed;
Name=M1; Synonyms=M1-PK, PKM1;
IsoId=P14618-2, P14786-1;
Sequence=VSP_011101;
Name=3;
IsoId=P14618-3; Sequence=VSP_043370;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Specifically expressed in proliferating cells,
such as embryonic stem cells, embryonic carcinoma cells, as well
as cancer cells. {ECO:0000269|PubMed:18191611}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- PTM: Under hypoxia, hydroxylated by EGLN3.
{ECO:0000269|PubMed:21620138}.
-!- PTM: Acetylation at Lys-305 is stimulated by high glucose
concentration, it decreases enzyme activity and promotes its
lysosomal-dependent degradation via chaperone-mediated autophagy.
{ECO:0000269|PubMed:21700219, ECO:0000269|Ref.11}.
-!- PTM: FGFR1-dependent tyrosine phosphorylation is reduced by
interaction with TRIM35. {ECO:0000269|PubMed:25263439}.
-!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals
(L, R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L
and R isozymes are generated from the PKLR by differential
splicing of RNA; the M1 and M2 forms are produced from the PKM
gene by differential splicing. L type is major isozyme in the
liver, R is found in red cells, M1 is the main form in muscle,
heart and brain, and M2 is found in early fetal tissues as well as
in most cancer cells.
-!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAG57589.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pkm2/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Pyruvate kinase entry;
URL="https://en.wikipedia.org/wiki/Pyruvate_kinase";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PKM2ID41728ch15q22.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M23725; AAA36449.1; -; mRNA.
EMBL; M26252; AAA36672.1; -; mRNA.
EMBL; X56494; CAA39849.1; -; Genomic_DNA.
EMBL; AK092369; BAG52542.1; -; mRNA.
EMBL; AK222927; BAD96647.1; -; mRNA.
EMBL; AK294315; BAG57589.1; ALT_INIT; mRNA.
EMBL; AK300800; BAG62458.1; -; mRNA.
EMBL; AK312253; BAG35185.1; -; mRNA.
EMBL; AY352517; AAQ15274.1; -; Genomic_DNA.
EMBL; AC020779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77884.1; -; Genomic_DNA.
EMBL; CH471082; EAW77888.1; -; Genomic_DNA.
EMBL; BC000481; AAH00481.3; -; mRNA.
EMBL; BC007640; AAH07640.1; -; mRNA.
EMBL; BC007952; AAH07952.3; -; mRNA.
EMBL; BC012811; AAH12811.3; -; mRNA.
EMBL; BC035198; AAH35198.1; -; mRNA.
EMBL; AF025439; AAC39559.1; -; mRNA.
CCDS; CCDS32284.1; -. [P14618-1]
CCDS; CCDS32285.1; -. [P14618-2]
CCDS; CCDS55972.1; -. [P14618-3]
PIR; S30038; S30038.
PIR; S64635; S64635.
RefSeq; NP_001193725.1; NM_001206796.2.
RefSeq; NP_001193726.1; NM_001206797.2.
RefSeq; NP_001193727.1; NM_001206798.2. [P14618-3]
RefSeq; NP_001193728.1; NM_001206799.1.
RefSeq; NP_001303247.1; NM_001316318.1.
RefSeq; NP_002645.3; NM_002654.5. [P14618-1]
RefSeq; NP_872270.1; NM_182470.3. [P14618-2]
RefSeq; NP_872271.1; NM_182471.3. [P14618-2]
RefSeq; XP_005254502.1; XM_005254445.4. [P14618-1]
RefSeq; XP_016877802.1; XM_017022313.1. [P14618-2]
UniGene; Hs.534770; -.
UniGene; Hs.704299; -.
PDB; 1T5A; X-ray; 2.80 A; A/B/C/D=1-531.
PDB; 1ZJH; X-ray; 2.20 A; A=3-531.
PDB; 3BJF; X-ray; 2.03 A; A/B/C/D=14-531.
PDB; 3BJT; X-ray; 2.50 A; A/B/C/D=2-531.
PDB; 3G2G; X-ray; 2.00 A; A/B/C/D=1-531.
PDB; 3GQY; X-ray; 1.85 A; A/B/C/D=1-531.
PDB; 3GR4; X-ray; 1.60 A; A/B/C/D=1-531.
PDB; 3H6O; X-ray; 2.00 A; A/B/C/D=1-531.
PDB; 3ME3; X-ray; 1.95 A; A/B/C/D=1-531.
PDB; 3SRD; X-ray; 2.90 A; A/B/C/D=1-531.
PDB; 3SRF; X-ray; 2.84 A; A/B/C/D/E/F/G/H=1-531.
PDB; 3SRH; X-ray; 2.60 A; A/B/C/D=1-531.
PDB; 3U2Z; X-ray; 2.10 A; A/B/C/D=1-531.
PDB; 4B2D; X-ray; 2.30 A; A/B/C/D=2-531.
PDB; 4FXF; X-ray; 2.55 A; A/B/C/D=1-531.
PDB; 4FXJ; X-ray; 2.90 A; A/B/C/D=1-531.
PDB; 4G1N; X-ray; 2.30 A; A/B/C/D=14-531.
PDB; 4JPG; X-ray; 2.33 A; A/B/C/D=1-531.
PDB; 4QG6; X-ray; 3.21 A; A/B/C/D=1-531.
PDB; 4QG8; X-ray; 2.30 A; A/B/C/D=1-531.
PDB; 4QG9; X-ray; 2.38 A; A/B/C/D=1-531.
PDB; 4QGC; X-ray; 2.30 A; A/B/C/D=1-531.
PDB; 4RPP; X-ray; 2.58 A; A/B/C/D=1-531.
PDB; 4WJ8; X-ray; 2.87 A; A/B/C/D=1-531.
PDB; 4YJ5; X-ray; 2.41 A; A/B/C/D=14-531.
PDB; 5X0I; X-ray; 2.64 A; A/B/C/D=1-531.
PDB; 5X1V; X-ray; 2.10 A; A/B/C/D=1-531.
PDB; 5X1W; X-ray; 3.00 A; A/B/C/D=1-531.
PDB; 6B6U; X-ray; 1.35 A; A/B=7-531.
PDBsum; 1T5A; -.
PDBsum; 1ZJH; -.
PDBsum; 3BJF; -.
PDBsum; 3BJT; -.
PDBsum; 3G2G; -.
PDBsum; 3GQY; -.
PDBsum; 3GR4; -.
PDBsum; 3H6O; -.
PDBsum; 3ME3; -.
PDBsum; 3SRD; -.
PDBsum; 3SRF; -.
PDBsum; 3SRH; -.
PDBsum; 3U2Z; -.
PDBsum; 4B2D; -.
PDBsum; 4FXF; -.
PDBsum; 4FXJ; -.
PDBsum; 4G1N; -.
PDBsum; 4JPG; -.
PDBsum; 4QG6; -.
PDBsum; 4QG8; -.
PDBsum; 4QG9; -.
PDBsum; 4QGC; -.
PDBsum; 4RPP; -.
PDBsum; 4WJ8; -.
PDBsum; 4YJ5; -.
PDBsum; 5X0I; -.
PDBsum; 5X1V; -.
PDBsum; 5X1W; -.
PDBsum; 6B6U; -.
ProteinModelPortal; P14618; -.
SMR; P14618; -.
BioGrid; 111332; 197.
ComplexPortal; CPX-3057; PKM2 protein kinase complex (dimer). [P14618-1]
ComplexPortal; CPX-3058; PKM2 pyruvate kinase complex (tetramer). [P14618-1]
ComplexPortal; CPX-3093; PKM1 pyruvate kinase complex. [P14618-2]
DIP; DIP-31273N; -.
IntAct; P14618; 246.
MINT; P14618; -.
STRING; 9606.ENSP00000320171; -.
BindingDB; P14618; -.
ChEMBL; CHEMBL1075189; -.
DrugBank; DB02726; 2-Phosphoglycolic Acid.
DrugBank; DB01733; L-Phospholactate.
DrugBank; DB00119; Pyruvic acid.
MoonDB; P14618; Curated.
MoonProt; P14618; -.
iPTMnet; P14618; -.
PhosphoSitePlus; P14618; -.
SwissPalm; P14618; -.
BioMuta; PKM; -.
DMDM; 20178296; -.
DOSAC-COBS-2DPAGE; P14618; -.
OGP; P14618; -.
REPRODUCTION-2DPAGE; IPI00220644; -.
REPRODUCTION-2DPAGE; IPI00479186; -.
UCD-2DPAGE; P14618; -.
EPD; P14618; -.
PaxDb; P14618; -.
PeptideAtlas; P14618; -.
PRIDE; P14618; -.
ProteomicsDB; 53063; -.
ProteomicsDB; 53064; -. [P14618-2]
ProteomicsDB; 53065; -. [P14618-3]
TopDownProteomics; P14618-1; -. [P14618-1]
TopDownProteomics; P14618-2; -. [P14618-2]
DNASU; 5315; -.
Ensembl; ENST00000319622; ENSP00000320171; ENSG00000067225. [P14618-2]
Ensembl; ENST00000335181; ENSP00000334983; ENSG00000067225. [P14618-1]
Ensembl; ENST00000449901; ENSP00000403365; ENSG00000067225. [P14618-3]
Ensembl; ENST00000565154; ENSP00000455901; ENSG00000067225. [P14618-2]
Ensembl; ENST00000565184; ENSP00000455736; ENSG00000067225. [P14618-2]
Ensembl; ENST00000568459; ENSP00000456970; ENSG00000067225. [P14618-2]
GeneID; 5315; -.
KEGG; hsa:5315; -.
UCSC; uc002atw.2; human. [P14618-1]
CTD; 5315; -.
DisGeNET; 5315; -.
EuPathDB; HostDB:ENSG00000067225.17; -.
GeneCards; PKM; -.
HGNC; HGNC:9021; PKM.
HPA; CAB019421; -.
HPA; HPA029501; -.
MIM; 179050; gene.
neXtProt; NX_P14618; -.
OpenTargets; ENSG00000067225; -.
PharmGKB; PA33353; -.
eggNOG; KOG2323; Eukaryota.
eggNOG; COG0469; LUCA.
GeneTree; ENSGT00390000008859; -.
HOGENOM; HOG000021559; -.
HOVERGEN; HBG000941; -.
InParanoid; P14618; -.
KO; K00873; -.
OMA; KHEAIEQ; -.
PhylomeDB; P14618; -.
TreeFam; TF300390; -.
BioCyc; MetaCyc:HS00906-MONOMER; -.
BRENDA; 2.7.1.40; 2681.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-70171; Glycolysis.
SABIO-RK; P14618; -.
SIGNOR; P14618; -.
UniPathway; UPA00109; UER00188.
ChiTaRS; PKM; human.
EvolutionaryTrace; P14618; -.
GeneWiki; PKM2; -.
GenomeRNAi; 5315; -.
PRO; PR:P14618; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000067225; -.
CleanEx; HS_PKM2; -.
ExpressionAtlas; P14618; baseline and differential.
Genevisible; P14618; HS.
GO; GO:0005929; C:cilium; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
GO; GO:1902912; C:pyruvate kinase complex; IEA:Ensembl.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0031982; C:vesicle; HDA:UniProtKB.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
GO; GO:0004743; F:pyruvate kinase activity; IDA:CACAO.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0070324; F:thyroid hormone binding; IEA:Ensembl.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
GO; GO:0001889; P:liver development; IEA:Ensembl.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0012501; P:programmed cell death; IDA:UniProtKB.
GO; GO:0051289; P:protein homotetramerization; IEA:Ensembl.
GO; GO:0009629; P:response to gravity; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0014870; P:response to muscle inactivity; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IEA:Ensembl.
CDD; cd00288; Pyruvate_Kinase; 1.
Gene3D; 2.40.33.10; -; 1.
Gene3D; 3.40.1380.20; -; 2.
InterPro; IPR001697; Pyr_Knase.
InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
InterPro; IPR018209; Pyrv_Knase_AS.
InterPro; IPR015793; Pyrv_Knase_brl.
InterPro; IPR015795; Pyrv_Knase_C.
InterPro; IPR036918; Pyrv_Knase_C_sf.
InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
PANTHER; PTHR11817; PTHR11817; 1.
Pfam; PF00224; PK; 1.
Pfam; PF02887; PK_C; 1.
PRINTS; PR01050; PYRUVTKNASE.
SUPFAM; SSF50800; SSF50800; 1.
SUPFAM; SSF51621; SSF51621; 2.
SUPFAM; SSF52935; SSF52935; 1.
TIGRFAMs; TIGR01064; pyruv_kin; 1.
PROSITE; PS00110; PYRUVATE_KINASE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing;
Glycolysis; Hydroxylation; Isopeptide bond; Kinase; Magnesium;
Metal-binding; Methylation; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Potassium; Pyruvate; Reference proteome;
Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:1854723,
ECO:0000269|Ref.11}.
CHAIN 2 531 Pyruvate kinase PKM.
/FTId=PRO_0000112088.
NP_BIND 75 78 ATP. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
REGION 307 531 Interaction with POU5F1.
{ECO:0000269|PubMed:18191611}.
REGION 389 433 Intersubunit contact.
REGION 432 437 D-fructose 1,6-bisphosphate binding; part
of allosteric site.
{ECO:0000244|PDB:1T5A,
ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:23530218}.
REGION 516 521 D-fructose 1,6-bisphosphate binding; part
of allosteric site.
{ECO:0000244|PDB:1T5A,
ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:23530218}.
METAL 75 75 Potassium. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
METAL 77 77 Potassium. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
METAL 113 113 Potassium. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
METAL 114 114 Potassium; via carbonyl oxygen.
{ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
METAL 272 272 Magnesium. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
METAL 296 296 Magnesium. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
BINDING 70 70 Serine.
BINDING 73 73 Substrate.
{ECO:0000250|UniProtKB:P30613}.
BINDING 106 106 Serine.
BINDING 120 120 ATP. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
BINDING 207 207 ATP. {ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:23530218}.
BINDING 270 270 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P30613}.
BINDING 295 295 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P30613}.
BINDING 296 296 Substrate; via amide nitrogen.
{ECO:0000250|UniProtKB:P30613}.
BINDING 328 328 Substrate.
{ECO:0000250|UniProtKB:P30613}.
BINDING 464 464 Serine.
BINDING 482 482 D-fructose 1,6-bisphosphate; part of
allosteric site. {ECO:0000244|PDB:1T5A,
ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:23530218}.
BINDING 489 489 D-fructose 1,6-bisphosphate; part of
allosteric site. {ECO:0000244|PDB:1T5A,
ECO:0000244|PDB:4FXF,
ECO:0000269|PubMed:15996096,
ECO:0000269|PubMed:23530218}.
SITE 270 270 Transition state stabilizer.
{ECO:0000250|UniProtKB:P00549}.
SITE 433 433 Crucial for phosphotyrosine binding.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.11}.
MOD_RES 3 3 N6,N6,N6-trimethyllysine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 41 41 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 62 62 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 66 66 N6-succinyllysine.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 89 89 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:P11980}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:P11980}.
MOD_RES 105 105 Phosphotyrosine.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:23186163}.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 148 148 Phosphotyrosine.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 166 166 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 166 166 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 175 175 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 195 195 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 266 266 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 270 270 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 305 305 N6-acetyllysine.
{ECO:0000269|PubMed:21700219}.
MOD_RES 322 322 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 322 322 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 403 403 4-hydroxyproline.
{ECO:0000269|PubMed:21620138}.
MOD_RES 408 408 4-hydroxyproline.
{ECO:0000269|PubMed:21620138}.
MOD_RES 433 433 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 475 475 N6-acetyllysine.
{ECO:0000250|UniProtKB:P52480}.
MOD_RES 498 498 N6-succinyllysine.
{ECO:0000250|UniProtKB:P52480}.
CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 266 266 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 270 270 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 82 MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPIT
ARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHE
-> MSPEAQPQRTKGPQQPCRSPIVKPGLPSFRPSSCTQPW
LTHSWSTCAAWTLIHHPSQPGTLASSVPL (in isoform
3). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_043370.
VAR_SEQ 389 433 IYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAII
VLTK -> MFHRKLFEELVRASSHSTDLMEAMAMGSVEASY
KCLAAALIVLTE (in isoform M1).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_011101.
VARIANT 204 204 G -> V (in dbSNP:rs17853396).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_033067.
MUTAGEN 403 403 P->A: Significant reduction in
hydroxylation and in PKM-mediated
transcriptional activity of HIF1A; when
associated with A-408.
{ECO:0000269|PubMed:21620138}.
MUTAGEN 408 408 P->A: Significant reduction in
hydroxylation and in PKM-mediated
transcriptional activity of HIF1A; when
associated with A-403.
{ECO:0000269|PubMed:21620138}.
MUTAGEN 437 437 S->Y: Unable to bind FBP but still
activated by serine.
{ECO:0000269|PubMed:23064226}.
MUTAGEN 464 464 H->A: Abolishes serine binding and
allosteric activation.
{ECO:0000269|PubMed:23064226}.
CONFLICT 7 7 E -> Q (in Ref. 10; AAH12811).
{ECO:0000305}.
CONFLICT 54 54 A -> T (in Ref. 5; BAG52542).
{ECO:0000305}.
CONFLICT 103 103 I -> Y (in Ref. 2; AAA36672).
{ECO:0000305}.
CONFLICT 132 132 V -> L (in Ref. 2; AAA36672).
{ECO:0000305}.
CONFLICT 187 187 Q -> R (in Ref. 6; BAD96647).
{ECO:0000305}.
CONFLICT 252 252 H -> R (in Ref. 6; BAD96647).
{ECO:0000305}.
CONFLICT 339 339 R -> P (in Ref. 4; CAA39849).
{ECO:0000305}.
CONFLICT 349 349 A -> V (in Ref. 5; BAG52542).
{ECO:0000305}.
CONFLICT 379 379 H -> N (in Ref. 1; AAA36449).
{ECO:0000305}.
CONFLICT 507 507 D -> H (in Ref. 10; AAH12811).
{ECO:0000305}.
HELIX 9 11 {ECO:0000244|PDB:6B6U}.
HELIX 15 17 {ECO:0000244|PDB:4WJ8}.
HELIX 18 21 {ECO:0000244|PDB:6B6U}.
HELIX 26 31 {ECO:0000244|PDB:6B6U}.
STRAND 35 37 {ECO:0000244|PDB:4QGC}.
STRAND 45 50 {ECO:0000244|PDB:6B6U}.
TURN 53 55 {ECO:0000244|PDB:6B6U}.
HELIX 58 67 {ECO:0000244|PDB:6B6U}.
STRAND 71 75 {ECO:0000244|PDB:6B6U}.
HELIX 76 78 {ECO:0000244|PDB:4QG6}.
HELIX 81 96 {ECO:0000244|PDB:6B6U}.
TURN 97 100 {ECO:0000244|PDB:6B6U}.
TURN 102 104 {ECO:0000244|PDB:6B6U}.
STRAND 109 113 {ECO:0000244|PDB:6B6U}.
STRAND 119 121 {ECO:0000244|PDB:6B6U}.
TURN 125 127 {ECO:0000244|PDB:6B6U}.
STRAND 128 130 {ECO:0000244|PDB:4WJ8}.
STRAND 132 134 {ECO:0000244|PDB:6B6U}.
STRAND 139 143 {ECO:0000244|PDB:6B6U}.
HELIX 146 148 {ECO:0000244|PDB:6B6U}.
STRAND 154 160 {ECO:0000244|PDB:6B6U}.
HELIX 164 167 {ECO:0000244|PDB:6B6U}.
STRAND 173 176 {ECO:0000244|PDB:6B6U}.
TURN 177 180 {ECO:0000244|PDB:6B6U}.
STRAND 181 188 {ECO:0000244|PDB:6B6U}.
STRAND 190 199 {ECO:0000244|PDB:6B6U}.
STRAND 201 203 {ECO:0000244|PDB:6B6U}.
STRAND 204 206 {ECO:0000244|PDB:4B2D}.
STRAND 208 210 {ECO:0000244|PDB:6B6U}.
STRAND 212 214 {ECO:0000244|PDB:5X1V}.
HELIX 223 234 {ECO:0000244|PDB:6B6U}.
STRAND 238 242 {ECO:0000244|PDB:6B6U}.
HELIX 248 257 {ECO:0000244|PDB:6B6U}.
TURN 258 264 {ECO:0000244|PDB:6B6U}.
STRAND 265 271 {ECO:0000244|PDB:6B6U}.
HELIX 274 278 {ECO:0000244|PDB:6B6U}.
HELIX 280 286 {ECO:0000244|PDB:6B6U}.
STRAND 287 293 {ECO:0000244|PDB:6B6U}.
HELIX 294 300 {ECO:0000244|PDB:6B6U}.
HELIX 303 305 {ECO:0000244|PDB:6B6U}.
HELIX 306 320 {ECO:0000244|PDB:6B6U}.
STRAND 324 329 {ECO:0000244|PDB:6B6U}.
HELIX 332 335 {ECO:0000244|PDB:6B6U}.
STRAND 337 339 {ECO:0000244|PDB:3BJT}.
HELIX 342 354 {ECO:0000244|PDB:6B6U}.
STRAND 357 362 {ECO:0000244|PDB:6B6U}.
HELIX 363 366 {ECO:0000244|PDB:6B6U}.
STRAND 367 369 {ECO:0000244|PDB:1ZJH}.
HELIX 371 388 {ECO:0000244|PDB:6B6U}.
HELIX 391 400 {ECO:0000244|PDB:6B6U}.
TURN 402 404 {ECO:0000244|PDB:3SRF}.
HELIX 408 423 {ECO:0000244|PDB:6B6U}.
STRAND 428 431 {ECO:0000244|PDB:6B6U}.
STRAND 433 435 {ECO:0000244|PDB:6B6U}.
HELIX 436 442 {ECO:0000244|PDB:6B6U}.
STRAND 450 455 {ECO:0000244|PDB:6B6U}.
HELIX 457 462 {ECO:0000244|PDB:6B6U}.
HELIX 463 465 {ECO:0000244|PDB:6B6U}.
STRAND 469 473 {ECO:0000244|PDB:6B6U}.
HELIX 482 499 {ECO:0000244|PDB:6B6U}.
STRAND 508 512 {ECO:0000244|PDB:6B6U}.
TURN 517 519 {ECO:0000244|PDB:3G2G}.
STRAND 525 529 {ECO:0000244|PDB:6B6U}.
SEQUENCE 531 AA; 57937 MW; AA94D7818ED6BBAD CRC64;
MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET
LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR
TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL
ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV
FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM
LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS
FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE
AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P


Related products :

Catalog number Product name Quantity
U0588h CLIA CTHBP,Cytosolic thyroid hormone-binding protein,Homo sapiens,Human,OIP3,OIP-3,Opa-interacting protein 3,p58,PK2,PK3,PKM,PKM2,Pyruvate kinase 2_3,Pyruvate kinase isozymes M1_M2,Pyruvate kinase mus 96T
E0588h ELISA CTHBP,Cytosolic thyroid hormone-binding protein,Homo sapiens,Human,OIP3,OIP-3,Opa-interacting protein 3,p58,PK2,PK3,PKM,PKM2,Pyruvate kinase 2_3,Pyruvate kinase isozymes M1_M2,Pyruvate kinase mu 96T
E0588h ELISA kit CTHBP,Cytosolic thyroid hormone-binding protein,Homo sapiens,Human,OIP3,OIP-3,Opa-interacting protein 3,p58,PK2,PK3,PKM,PKM2,Pyruvate kinase 2_3,Pyruvate kinase isozymes M1_M2,Pyruvate kina 96T
E0588Rb ELISA Oryctolagus cuniculus,PKM2,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rabbit 96T
U0588r CLIA Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rat,Rattus norvegicus 96T
E0588r ELISA kit Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rat,Rattus norvegicus 96T
U0588Rb CLIA Oryctolagus cuniculus,PKM2,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rabbit 96T
E0588m ELISA kit Mouse,Mus musculus,Pk3,Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme 96T
E0588m ELISA Mouse,Mus musculus,Pk3,Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme 96T
E0588Rb ELISA kit Oryctolagus cuniculus,PKM2,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rabbit 96T
U0588m CLIA Mouse,Mus musculus,Pk3,Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme 96T
E0588r ELISA Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rat,Rattus norvegicus 96T
EIAAB30379 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial,Homo sapiens,Human,PDK1,Pyruvate dehydrogenase kinase isoform 1
EIAAB30384 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial,Homo sapiens,Human,PDK2,Pyruvate dehydrogenase kinase isoform 2
EIAAB30391 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial,Homo sapiens,Human,PDK4,Pyruvate dehydrogenase kinase isoform 4
EIAAB30387 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial,Homo sapiens,Human,PDK3,Pyruvate dehydrogenase kinase isoform 3
EIAAB30380 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial,Mouse,Mus musculus,Pdk1,Pyruvate dehydrogenase kinase isoform 1
EIAAB30389 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial,Mouse,Mus musculus,Pdk4,Pyruvate dehydrogenase kinase isoform 4
EIAAB30381 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial,Pdh,PDK p48,Pdk1,Pyruvate dehydrogenase kinase isoform 1,Rat,Rattus norvegicus
EIAAB30385 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial,Mouse,Mus musculus,Pdk2,Pyruvate dehydrogenase kinase isoform 2
EIAAB30388 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial,Mouse,Mus musculus,Pdk3,Pyruvate dehydrogenase kinase isoform 3
EIAAB30390 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial,Pdk4,Pyruvate dehydrogenase kinase isoform 4,Rat,Rattus norvegicus
EIAAB30386 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial,PDK P45,Pdk2,Pyruvate dehydrogenase kinase isoform 2,Rat,Rattus norvegicus
18-003-43425 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4. mitochondrial - EC 2.7.11.2; Pyruvate dehydrogenase kinase isoform 4 Polyclonal 0.05 mg Aff Pur
18-003-43213 Thyroid receptor-interacting protein 13 - Thyroid hormone receptor interactor 13; Trip-13; Human papillomavirus type 16 E1 protein-binding protein; HPV16 E1 protein-binding protein; 16E1-BP Polyclonal 0.1 mg Protein A


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur