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 PKLR (EC 2.7.1.40) (Pyruvate kinase 1) (Pyruvate kinase isozymes L/R) (R-type/L-type pyruvate kinase) (Red cell/liver pyruvate kinase)

 KPYR_HUMAN              Reviewed;         574 AA.
P30613; O75758; P11973;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
23-MAY-2018, entry version 214.
RecName: Full=Pyruvate kinase PKLR;
EC=2.7.1.40;
AltName: Full=Pyruvate kinase 1;
AltName: Full=Pyruvate kinase isozymes L/R;
AltName: Full=R-type/L-type pyruvate kinase;
AltName: Full=Red cell/liver pyruvate kinase;
Name=PKLR; Synonyms=PK1, PKL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PKRD MET-384.
PubMed=1896471; DOI=10.1073/pnas.88.18.8218;
Kanno H., Fujii H., Hirono A., Miwa S.;
"cDNA cloning of human R-type pyruvate kinase and identification of a
single amino acid substitution (Thr384-->Met) affecting enzymatic
stability in a pyruvate kinase variant (PK Tokyo) associated with
hereditary hemolytic anemia.";
Proc. Natl. Acad. Sci. U.S.A. 88:8218-8221(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3126495; DOI=10.1073/pnas.85.6.1792;
Tani K., Fujii H., Nagata S., Miwa S.;
"Human liver type pyruvate kinase: complete amino acid sequence and
the expression in mammalian cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:1792-1795(1988).
[3]
SEQUENCE REVISION TO 130 AND 232.
Kanno H.;
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1445295; DOI=10.1016/0006-291X(92)91086-6;
Kanno H., Fujii H., Miwa S.;
"Structural analysis of human pyruvate kinase L-gene and
identification of the promoter activity in erythroid cells.";
Biochem. Biophys. Res. Commun. 188:516-523(1992).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-506.
NIEHS SNPs program;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM R-TYPE).
TISSUE=Pancreas;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 470-574.
PubMed=3566732; DOI=10.1016/0006-291X(87)91372-6;
Tani K., Fujii H., Tsutsumi H., Sukegawa J., Toyoshima K.,
Yoshida M.C., Noguchi T., Tanaka T., Miwa S.;
"Human liver type pyruvate kinase: cDNA cloning and chromosomal
assignment.";
Biochem. Biophys. Res. Commun. 143:431-438(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 365-431, AND VARIANT PKRD PHE-368.
PubMed=8476433; DOI=10.1006/bbrc.1993.1379;
Kanno H., Fujii H., Tsujino G., Miwa S.;
"Molecular basis of impaired pyruvate kinase isozyme conversion in
erythroid cells: a single amino acid substitution near the active site
and decreased mRNA content of the R-type PK.";
Biochem. Biophys. Res. Commun. 192:46-52(1993).
[9]
REVIEW ON VARIANTS.
PubMed=8664896;
DOI=10.1002/(SICI)1098-1004(1996)7:1<1::AID-HUMU1>3.0.CO;2-H;
Beutler E., Baronciani L.;
"Mutations in pyruvate kinase.";
Hum. Mutat. 7:1-6(1996).
[10]
REVIEW ON VARIANTS.
PubMed=8807089; DOI=10.1006/bcmd.1996.0012;
Baronciani L., Bianchi P., Zanella A.;
"Hematologically important mutations: red cell pyruvate kinase.";
Blood Cells Mol. Dis. 22:85-89(1996).
[11]
REVIEW ON VARIANTS.
PubMed=9075576; DOI=10.1006/bcmd.1996.0107;
Baronciani L., Bianchi P., Zanella A.;
"Hematologically important mutations: red cell pyruvate kinase (1st
update).";
Blood Cells Mol. Dis. 22:259-264(1996).
[12]
REVIEW ON VARIANTS.
PubMed=10087985; DOI=10.1006/bcmd.1998.0193;
Baronciani L., Bianchi P., Zanella A.;
"Hematologically important mutations: red cell pyruvate kinase (2nd
update).";
Blood Cells Mol. Dis. 24:273-279(1998).
[13]
REVIEW ON VARIANTS.
PubMed=10772876; DOI=10.1006/bcmd.2000.0276;
Bianchi P., Zanella A.;
"Hematologically important mutations: red cell pyruvate kinase (third
update).";
Blood Cells Mol. Dis. 26:47-53(2000).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-19 AND SER-26,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-292, 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).
[16]
X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 47-574 IN COMPLEX WITH
SUBSTRATE ANALOG; FRUCTOSE 1,6-BISPHOSPHATE; POTASSIUM IONS AND
MANGANESE IONS, ALLOSTERIC ACTIVATION, ENZYME REGULATION,
CHARACTERIZATION OF VARIANTS PKRD SER-332; ASP-364; ASN-390; HIS-479;
TRP-486; LEU-504 AND TRP-532, CHARACTERIZATION OF VARIANT MET-384, AND
SUBUNIT.
PubMed=11960989; DOI=10.1074/jbc.M202107200;
Valentini G., Chiarelli L.R., Fortin R., Dolzan M., Galizzi A.,
Abraham D.J., Wang C., Bianchi P., Zanella A., Mattevi A.;
"Structure and function of human erythrocyte pyruvate kinase.
Molecular basis of nonspherocytic hemolytic anemia.";
J. Biol. Chem. 277:23807-23814(2002).
[17]
VARIANTS PKRD CYS-163 AND MET-384.
PubMed=2018831;
Neubauer B., Lakomek M., Winkler H., Parke M., Hofferbert S.,
Schroter W.;
"Point mutations in the L-type pyruvate kinase gene of two children
with hemolytic anemia caused by pyruvate kinase deficiency.";
Blood 77:1871-1875(1991).
[18]
VARIANT PKRD LYS-421.
PubMed=1536957;
Kanno H., Fujii H., Hirono A., Omine M., Miwa S.;
"Identical point mutations of the R-type pyruvate kinase (PK) cDNA
found in unrelated PK variants associated with hereditary hemolytic
anemia.";
Blood 79:1347-1350(1992).
[19]
VARIANT PKRD GLN-426.
PubMed=8481523;
Kanno H., Fujii H., Miwa S.;
"Low substrate affinity of pyruvate kinase variant (PK Sapporo) caused
by a single amino acid substitution (426 Arg-->Gln) associated with
hereditary hemolytic anemia.";
Blood 81:2439-2441(1993).
[20]
VARIANTS PKRD ASP-134; PRO-155; HIS-359; TRP-486; VAL-495 AND GLN-510.
PubMed=8483951; DOI=10.1073/pnas.90.9.4324;
Baronciani L., Beutler E.;
"Analysis of pyruvate kinase-deficiency mutations that produce
nonspherocytic hemolytic anemia.";
Proc. Natl. Acad. Sci. U.S.A. 90:4324-4327(1993).
[21]
VARIANT PKRD HIS-479.
PubMed=8161798;
Kanno H., Ballas S.K., Miwa S., Fujii H., Bowman H.S.;
"Molecular abnormality of erythrocyte pyruvate kinase deficiency in
the Amish.";
Blood 83:2311-2316(1994).
[22]
VARIANTS PKRD SER-332; SER-336; LYS-354 DEL; ASP-361; THR-392;
HIS-498; GLN-510 AND TRP-532.
PubMed=8180378;
Lenzner C., Nuernberg P., Thiele B.-J., Reis A., Brabec V.,
Sakalova A., Jacobasch G.;
"Mutations in the pyruvate kinase L gene in patients with hereditary
hemolytic anemia.";
Blood 83:2817-2822(1994).
[23]
VARIANTS PKRD GLU-331; ALA-341; LYS-393; SER-393; ASP-458; MET-460 AND
HIS-498.
PubMed=7706479; DOI=10.1172/JCI117846;
Baronciani L., Beutler E.;
"Molecular study of pyruvate kinase deficient patients with hereditary
nonspherocytic hemolytic anemia.";
J. Clin. Invest. 95:1702-1709(1995).
[24]
VARIANTS PKRD.
Baronciani L., Westwood B., Beutler E.;
"Study of the molecular defects in pyruvate kinase (PK) deficient
patients affected by hereditary nonspherocytic hemolytic anemia
(HNHA).";
J. Invest. Med. 43:341A-341A(1995).
[25]
VARIANT PKHYP GLU-37.
PubMed=9090535;
DOI=10.1002/(SICI)1098-1004(1997)9:3<282::AID-HUMU13>3.0.CO;2-Z;
Beutler E., Westwood B., van Zwieten R., Roos D.;
"G-to-T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase)
gene is the molecular basis of a case of hereditary increase of red
blood cell ATP.";
Hum. Mutat. 9:282-285(1997).
[26]
VARIANTS PKRD GLN-172; GLN-337; HIS-339; THR-357; ILE-408; THR-431;
TRP-486 AND GLN-532.
PubMed=9827908; DOI=10.1046/j.1365-2141.1998.01013.x;
Zarza R., Alvarez R., Pujades A., Nomdedeu B., Carrera A., Estella J.,
Remacha A., Sanchez J.M., Morey M., Cortes T., Perez Lungmus G.,
Bureo E., Vives Corrons J.L.;
"Molecular characterization of the PK-LR gene in pyruvate kinase
deficient Spanish patients.";
Br. J. Haematol. 103:377-382(1998).
[27]
VARIANT PKRD TYR-130.
PubMed=9886305; DOI=10.1046/j.1365-2141.1998.01094.x;
Cohen-Solal M., Prehu C., Wajcman H., Poyart C.,
Bardakdjian-Michau J., Kister J., Prome D., Valentin C., Bachir D.,
Galacteros F.;
"A new sickle cell disease phenotype associating Hb S trait, severe
pyruvate kinase deficiency (PK Conakry), and an alpha-2 globin gene
variant (Hb Conakry).";
Br. J. Haematol. 103:950-956(1998).
[28]
VARIANTS PKRD SER-332; PRO-337; TRP-486; CYS-498 AND GLN-510.
PubMed=9482576;
DOI=10.1002/(SICI)1098-1004(1998)11:2<127::AID-HUMU5>3.0.CO;2-G;
Pastore L., della Morte R., Frisso G., Alfinito F., Vitale D.,
Calise R.M., Ferraro F., Zagari A., Rotoli B., Salvatore F.;
"Novel mutations and structural implications in R-type pyruvate
kinase-deficient patients from Southern Italy.";
Hum. Mutat. 11:127-134(1998).
[29]
VARIANTS PKRD MET-335; LYS-348 DEL; GLY-387; ASP-394 AND VAL-394.
PubMed=11328279; DOI=10.1046/j.1365-2141.2001.02711.x;
Zanella A., Bianchi P., Fermo E., Iurlo A., Zappa M., Vercellati C.,
Boschetti C., Baronciani L., Cotton F.;
"Molecular characterization of the PK-LR gene in sixteen pyruvate
kinase-deficient patients.";
Br. J. Haematol. 113:43-48(2001).
[30]
VARIANTS PKRD TRP-40; 48-THR--THR-53 DEL; PRO-73; ASN-90; ARG-111;
THR-154; LEU-163; VAL-165; VAL-272; ASN-310; LEU-320; GLU-358 AND
PRO-374.
PubMed=19085939; DOI=10.1002/humu.20915;
van Wijk R., Huizinga E.G., van Wesel A.C.W., van Oirschot B.A.,
Hadders M.A., van Solinge W.W.;
"Fifteen novel mutations in PKLR associated with pyruvate kinase (PK)
deficiency: structural implications of amino acid substitutions in
PK.";
Hum. Mutat. 30:446-453(2009).
[31]
VARIANTS PKRD ALA-341 AND GLN-569.
PubMed=21794208;
Lyon G.J., Jiang T., Van Wijk R., Wang W., Bodily P.M., Xing J.,
Tian L., Robison R.J., Clement M., Lin Y., Zhang P., Liu Y., Moore B.,
Glessner J.T., Elia J., Reimherr F., van Solinge W.W., Yandell M.,
Hakonarson H., Wang J., Johnson W.E., Wei Z., Wang K.;
"Exome sequencing and unrelated findings in the context of complex
disease research: ethical and clinical implications.";
Discov. Med. 12:41-55(2011).
-!- FUNCTION: Plays a key role in glycolysis. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000305|PubMed:11960989};
-!- COFACTOR:
Name=K(+); Xref=ChEBI:CHEBI:29103;
Evidence={ECO:0000305|PubMed:11960989};
-!- ENZYME REGULATION: Allosterically activated by fructose 1,6-
bisphosphate. {ECO:0000269|PubMed:11960989}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 5/5.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11960989}.
-!- INTERACTION:
Q9UBL6-2:CPNE7; NbExp=4; IntAct=EBI-2117450, EBI-12012272;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=R-type; Synonyms=PKR;
IsoId=P30613-1; Sequence=Displayed;
Name=L-type; Synonyms=PKL;
IsoId=P30613-2; Sequence=VSP_002883;
-!- DISEASE: Pyruvate kinase hyperactivity (PKHYP) [MIM:102900]:
Autosomal dominant phenotype characterized by increase of red
blood cell ATP. {ECO:0000269|PubMed:9090535}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Pyruvate kinase deficiency of red cells (PKRD)
[MIM:266200]: A frequent cause of hereditary non-spherocytic
hemolytic anemia. Clinically, pyruvate kinase-deficient patients
suffer from a highly variable degree of chronic hemolysis, ranging
from severe neonatal jaundice and fatal anemia at birth, severe
transfusion-dependent chronic hemolysis, moderate hemolysis with
exacerbation during infection, to a fully compensated hemolysis
without apparent anemia. {ECO:0000269|PubMed:11328279,
ECO:0000269|PubMed:11960989, ECO:0000269|PubMed:1536957,
ECO:0000269|PubMed:1896471, ECO:0000269|PubMed:19085939,
ECO:0000269|PubMed:2018831, ECO:0000269|PubMed:21794208,
ECO:0000269|PubMed:7706479, ECO:0000269|PubMed:8161798,
ECO:0000269|PubMed:8180378, ECO:0000269|PubMed:8476433,
ECO:0000269|PubMed:8481523, ECO:0000269|PubMed:8483951,
ECO:0000269|PubMed:9482576, ECO:0000269|PubMed:9827908,
ECO:0000269|PubMed:9886305, ECO:0000269|Ref.24}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals:
L, R, M1 and M2. 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.
-!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA02515.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/pklr/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Pyruvate kinase entry;
URL="https://en.wikipedia.org/wiki/Pyruvate_kinase";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB015983; BAA31706.1; -; mRNA.
EMBL; M15465; AAA60104.1; -; mRNA.
EMBL; D13243; BAA02515.1; ALT_SEQ; Genomic_DNA.
EMBL; AY316591; AAP69527.1; -; Genomic_DNA.
EMBL; BC025737; AAH25737.1; -; mRNA.
EMBL; S60712; AAB26262.1; -; mRNA.
CCDS; CCDS1109.1; -. [P30613-1]
CCDS; CCDS44240.1; -. [P30613-2]
PIR; I52269; KIHUPR.
RefSeq; NP_000289.1; NM_000298.5. [P30613-1]
RefSeq; NP_870986.1; NM_181871.3. [P30613-2]
UniGene; Hs.95990; -.
PDB; 2VGB; X-ray; 2.73 A; A/B/C/D=47-574.
PDB; 2VGF; X-ray; 2.75 A; A/B/C/D=47-574.
PDB; 2VGG; X-ray; 2.74 A; A/B/C/D=47-574.
PDB; 2VGI; X-ray; 2.87 A; A/B/C/D=47-574.
PDB; 4IMA; X-ray; 1.95 A; A/B/C/D=34-574.
PDB; 4IP7; X-ray; 1.80 A; A/B/C/D=34-574.
PDBsum; 2VGB; -.
PDBsum; 2VGF; -.
PDBsum; 2VGG; -.
PDBsum; 2VGI; -.
PDBsum; 4IMA; -.
PDBsum; 4IP7; -.
ProteinModelPortal; P30613; -.
SMR; P30613; -.
BioGrid; 111330; 15.
IntAct; P30613; 7.
STRING; 9606.ENSP00000339933; -.
BindingDB; P30613; -.
ChEMBL; CHEMBL1075126; -.
DrugBank; DB02726; 2-Phosphoglycolic Acid.
DrugBank; DB00119; Pyruvic acid.
iPTMnet; P30613; -.
PhosphoSitePlus; P30613; -.
SwissPalm; P30613; -.
BioMuta; PKLR; -.
REPRODUCTION-2DPAGE; P30613; -.
SWISS-2DPAGE; P30613; -.
MaxQB; P30613; -.
PaxDb; P30613; -.
PeptideAtlas; P30613; -.
PRIDE; P30613; -.
DNASU; 5313; -.
Ensembl; ENST00000342741; ENSP00000339933; ENSG00000143627. [P30613-1]
Ensembl; ENST00000392414; ENSP00000376214; ENSG00000143627. [P30613-2]
Ensembl; ENST00000571194; ENSP00000461487; ENSG00000262785. [P30613-2]
Ensembl; ENST00000572740; ENSP00000459921; ENSG00000262785. [P30613-1]
GeneID; 5313; -.
KEGG; hsa:5313; -.
UCSC; uc001fka.5; human. [P30613-1]
CTD; 5313; -.
DisGeNET; 5313; -.
EuPathDB; HostDB:ENSG00000143627.17; -.
GeneCards; PKLR; -.
HGNC; HGNC:9020; PKLR.
HPA; CAB034376; -.
HPA; CAB034378; -.
HPA; HPA006653; -.
MalaCards; PKLR; -.
MIM; 102900; phenotype.
MIM; 266200; phenotype.
MIM; 609712; gene.
neXtProt; NX_P30613; -.
OpenTargets; ENSG00000143627; -.
Orphanet; 766; Hemolytic anemia due to red cell pyruvate kinase deficiency.
PharmGKB; PA33352; -.
eggNOG; KOG2323; Eukaryota.
eggNOG; COG0469; LUCA.
GeneTree; ENSGT00390000008859; -.
HOGENOM; HOG000021559; -.
HOVERGEN; HBG000941; -.
InParanoid; P30613; -.
KO; K12406; -.
OMA; ICVEAEK; -.
OrthoDB; EOG091G0597; -.
PhylomeDB; P30613; -.
TreeFam; TF300390; -.
BioCyc; MetaCyc:HS07088-MONOMER; -.
BRENDA; 2.7.1.40; 2681.
Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
Reactome; R-HSA-70171; Glycolysis.
SABIO-RK; P30613; -.
UniPathway; UPA00109; UER00188.
EvolutionaryTrace; P30613; -.
GeneWiki; PKLR; -.
GenomeRNAi; 5313; -.
PMAP-CutDB; P30613; -.
PRO; PR:P30613; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143627; -.
CleanEx; HS_PKLR; -.
ExpressionAtlas; P30613; baseline and differential.
Genevisible; P30613; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
GO; GO:0004743; F:pyruvate kinase activity; EXP:Reactome.
GO; GO:0061621; P:canonical glycolysis; TAS:Reactome.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
GO; GO:0033198; P:response to ATP; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; 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; Allosteric enzyme; Alternative splicing; ATP-binding;
Complete proteome; Disease mutation; Glycolysis;
Hereditary hemolytic anemia; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Potassium; Pyruvate;
Reference proteome; Transferase.
CHAIN 1 574 Pyruvate kinase PKLR.
/FTId=PRO_0000112094.
REGION 475 480 Allosteric activator binding.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
REGION 559 564 Allosteric activator binding.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
METAL 118 118 Potassium. {ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
METAL 120 120 Potassium. {ECO:0000244|PDB:2VGB,
ECO:0000269|PubMed:11960989}.
METAL 156 156 Potassium. {ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
METAL 157 157 Potassium; via carbonyl oxygen.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
METAL 315 315 Manganese. {ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
METAL 339 339 Manganese. {ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
BINDING 116 116 Substrate. {ECO:0000244|PDB:2VGB,
ECO:0000269|PubMed:11960989}.
BINDING 313 313 Substrate; via amide nitrogen.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
BINDING 338 338 Substrate; via amide nitrogen.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
BINDING 339 339 Substrate; via amide nitrogen.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
BINDING 371 371 Substrate. {ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
BINDING 525 525 Allosteric activator.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
BINDING 532 532 Allosteric activator.
{ECO:0000244|PDB:2VGF,
ECO:0000269|PubMed:11960989}.
SITE 313 313 Transition state stabilizer.
{ECO:0000250|UniProtKB:P00549}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 33 MSIQENISSLQLRSWVSKSQRDLAKSILIGAPG -> ME
(in isoform L-type). {ECO:0000305}.
/FTId=VSP_002883.
VARIANT 37 37 G -> E (in PKHYP; dbSNP:rs118204087).
{ECO:0000269|PubMed:9090535}.
/FTId=VAR_011435.
VARIANT 40 40 R -> W (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058467.
VARIANT 48 53 Missing (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058468.
VARIANT 73 73 L -> P (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058469.
VARIANT 80 80 S -> P (in PKRD).
/FTId=VAR_011436.
VARIANT 86 86 R -> P (in PKRD).
/FTId=VAR_011437.
VARIANT 90 90 I -> N (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_011438.
VARIANT 95 95 G -> R (in PKRD; dbSNP:rs750857114).
/FTId=VAR_011439.
VARIANT 107 107 M -> T (in PKRD).
/FTId=VAR_004028.
VARIANT 111 111 G -> R (in PKRD; dbSNP:rs918627824).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_011440.
VARIANT 115 115 A -> P (in PKRD; Val de Marne).
/FTId=VAR_011441.
VARIANT 120 120 S -> F (in PKRD; Beaujon).
/FTId=VAR_011442.
VARIANT 130 130 S -> Y (in PKRD; Conakry;
dbSNP:rs118204089).
{ECO:0000269|PubMed:9886305}.
/FTId=VAR_011443.
VARIANT 131 131 Missing (in PKRD).
/FTId=VAR_004029.
VARIANT 134 134 V -> D (in PKRD; dbSNP:rs574051756).
{ECO:0000269|PubMed:8483951}.
/FTId=VAR_004030.
VARIANT 153 153 I -> T (in PKRD).
/FTId=VAR_011474.
VARIANT 154 154 A -> T (in PKRD; dbSNP:rs780192373).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058470.
VARIANT 155 155 L -> P (in PKRD).
{ECO:0000269|PubMed:8483951}.
/FTId=VAR_004031.
VARIANT 159 159 G -> V (in PKRD).
/FTId=VAR_011444.
VARIANT 163 163 R -> C (in PKRD; Linz;
dbSNP:rs118204083).
{ECO:0000269|PubMed:2018831}.
/FTId=VAR_004033.
VARIANT 163 163 R -> L (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058471.
VARIANT 165 165 G -> V (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058472.
VARIANT 172 172 E -> Q (in PKRD; Sassari;
dbSNP:rs757359024).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004032.
VARIANT 219 219 I -> T (in PKRD; dbSNP:rs200572803).
/FTId=VAR_011475.
VARIANT 221 221 D -> DD (in PKRD).
/FTId=VAR_004034.
VARIANT 222 222 G -> A (in PKRD; Katsushika).
/FTId=VAR_011445.
VARIANT 263 263 G -> R (in PKRD).
/FTId=VAR_011447.
VARIANT 263 263 G -> W (in PKRD).
/FTId=VAR_011448.
VARIANT 272 272 L -> V (in PKRD; dbSNP:rs147659527).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058473.
VARIANT 275 275 G -> R (in PKRD; dbSNP:rs747549978).
/FTId=VAR_004035.
VARIANT 281 281 D -> N (in PKRD).
/FTId=VAR_004036.
VARIANT 287 287 F -> V (in PKRD).
/FTId=VAR_004037.
VARIANT 288 288 V -> L (in PKRD; Moriguchi).
/FTId=VAR_011449.
VARIANT 293 293 D -> N (in PKRD).
/FTId=VAR_011446.
VARIANT 295 295 A -> V (in PKRD; dbSNP:rs766353400).
/FTId=VAR_011450.
VARIANT 310 310 I -> N (in PKRD; Dordrecht).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_011451.
VARIANT 314 314 I -> T (in PKRD; Hong Kong;
dbSNP:rs981505482).
/FTId=VAR_004038.
VARIANT 315 315 E -> K (in PKRD).
/FTId=VAR_011452.
VARIANT 320 320 V -> L (in PKRD; dbSNP:rs549295725).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058474.
VARIANT 331 331 D -> E (in PKRD; Parma;
dbSNP:rs138476691).
{ECO:0000269|PubMed:7706479}.
/FTId=VAR_004039.
VARIANT 331 331 D -> N (in PKRD; dbSNP:rs773893686).
/FTId=VAR_011453.
VARIANT 332 332 G -> S (in PKRD; loss of catalytical
activity; dbSNP:rs773626254).
{ECO:0000269|PubMed:11960989,
ECO:0000269|PubMed:8180378,
ECO:0000269|PubMed:9482576}.
/FTId=VAR_004040.
VARIANT 335 335 V -> M (in PKRD).
{ECO:0000269|PubMed:11328279}.
/FTId=VAR_011476.
VARIANT 336 336 A -> S (in PKRD).
{ECO:0000269|PubMed:8180378}.
/FTId=VAR_004041.
VARIANT 337 337 R -> P (in PKRD).
{ECO:0000269|PubMed:9482576}.
/FTId=VAR_004042.
VARIANT 337 337 R -> Q (in PKRD).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004043.
VARIANT 339 339 D -> H (in PKRD).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004044.
VARIANT 341 341 G -> A (in PKRD).
{ECO:0000269|PubMed:21794208,
ECO:0000269|PubMed:7706479}.
/FTId=VAR_004045.
VARIANT 341 341 G -> D (in PKRD).
/FTId=VAR_011454.
VARIANT 342 342 I -> F (in PKRD).
/FTId=VAR_011455.
VARIANT 348 348 K -> N (in PKRD; Kamata).
/FTId=VAR_011456.
VARIANT 348 348 Missing (in PKRD; Brescia).
{ECO:0000269|PubMed:11328279}.
/FTId=VAR_011457.
VARIANT 352 352 A -> D (in PKRD).
/FTId=VAR_011477.
VARIANT 354 354 Missing (in PKRD).
{ECO:0000269|PubMed:8180378}.
/FTId=VAR_004046.
VARIANT 357 357 I -> T (in PKRD; dbSNP:rs779152555).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004047.
VARIANT 358 358 G -> E (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058475.
VARIANT 359 359 R -> C (in PKRD; Aomori;
dbSNP:rs138871700).
/FTId=VAR_004048.
VARIANT 359 359 R -> H (in PKRD).
{ECO:0000269|PubMed:8483951}.
/FTId=VAR_004049.
VARIANT 361 361 N -> D (in PKRD; dbSNP:rs765903674).
{ECO:0000269|PubMed:8180378}.
/FTId=VAR_004050.
VARIANT 364 364 G -> D (in PKRD; Tjaereborg; unstability
of the protein and decrease in catalytic
activity; dbSNP:rs981579065).
{ECO:0000269|PubMed:11960989}.
/FTId=VAR_011458.
VARIANT 368 368 V -> F (in PKRD; Osaka).
{ECO:0000269|PubMed:8476433}.
/FTId=VAR_004051.
VARIANT 374 374 L -> P (in PKRD).
{ECO:0000269|PubMed:19085939}.
/FTId=VAR_058476.
VARIANT 376 376 S -> I (in PKRD).
/FTId=VAR_011459.
VARIANT 384 384 T -> M (in PKRD; Tokyo/Beirut; most
common mutation in Japanese population;
no conformational change;
dbSNP:rs74315362).
{ECO:0000269|PubMed:11960989,
ECO:0000269|PubMed:1896471,
ECO:0000269|PubMed:2018831}.
/FTId=VAR_004052.
VARIANT 385 385 R -> W (in PKRD).
/FTId=VAR_011478.
VARIANT 387 387 E -> G (in PKRD).
{ECO:0000269|PubMed:11328279}.
/FTId=VAR_011460.
VARIANT 390 390 D -> N (in PKRD; Mantova; almost complete
inactivation; dbSNP:rs147034239).
{ECO:0000269|PubMed:11960989}.
/FTId=VAR_011461.
VARIANT 392 392 A -> T (in PKRD).
{ECO:0000269|PubMed:8180378}.
/FTId=VAR_004053.
VARIANT 393 393 N -> K (in PKRD).
{ECO:0000269|PubMed:7706479}.
/FTId=VAR_004054.
VARIANT 393 393 N -> S (in PKRD; Paris;
dbSNP:rs776594413).
{ECO:0000269|PubMed:7706479}.
/FTId=VAR_004055.
VARIANT 394 394 A -> D (in PKRD; dbSNP:rs1035640530).
{ECO:0000269|PubMed:11328279}.
/FTId=VAR_011462.
VARIANT 394 394 A -> V (in PKRD).
{ECO:0000269|PubMed:11328279}.
/FTId=VAR_011463.
VARIANT 401 401 C -> CS (in PKRD).
/FTId=VAR_004056.
VARIANT 408 408 T -> A (in PKRD; Hirosaki).
/FTId=VAR_011464.
VARIANT 408 408 T -> I (in PKRD).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004057.
VARIANT 421 421 Q -> K (in PKRD; Fukushima/Maebashi/
Sendai; dbSNP:rs118204084).
{ECO:0000269|PubMed:1536957}.
/FTId=VAR_004058.
VARIANT 426 426 R -> Q (in PKRD; Sapporo;
dbSNP:rs768002493).
{ECO:0000269|PubMed:8481523}.
/FTId=VAR_004059.
VARIANT 426 426 R -> W (in PKRD; Naniwa;
dbSNP:rs1023689443).
/FTId=VAR_004060.
VARIANT 427 427 E -> A (in PKRD).
/FTId=VAR_011465.
VARIANT 427 427 E -> D (in PKRD).
/FTId=VAR_011466.
VARIANT 431 431 A -> T (in PKRD; dbSNP:rs762591322).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004061.
VARIANT 458 458 G -> D (in PKRD; dbSNP:rs755522396).
{ECO:0000269|PubMed:7706479}.
/FTId=VAR_004062.
VARIANT 459 459 A -> V (in PKRD).
/FTId=VAR_004063.
VARIANT 460 460 V -> M (in PKRD; dbSNP:rs752034960).
{ECO:0000269|PubMed:7706479}.
/FTId=VAR_004064.
VARIANT 468 468 A -> G (in PKRD; dbSNP:rs750540943).
/FTId=VAR_011479.
VARIANT 468 468 A -> V (in PKRD; Hadano).
/FTId=VAR_004065.
VARIANT 477 477 T -> A (in PKRD; dbSNP:rs759466273).
/FTId=VAR_011467.
VARIANT 479 479 R -> H (in PKRD; Amish; no conformational
change; dbSNP:rs118204085).
{ECO:0000269|PubMed:11960989,
ECO:0000269|PubMed:8161798}.
/FTId=VAR_011480.
VARIANT 485 485 S -> F (in PKRD).
/FTId=VAR_011468.
VARIANT 486 486 R -> W (in PKRD; frequent mutation; no
conformational change;
dbSNP:rs116100695).
{ECO:0000269|PubMed:11960989,
ECO:0000269|PubMed:8483951,
ECO:0000269|PubMed:9482576,
ECO:0000269|PubMed:9827908}.
/FTId=VAR_004066.
VARIANT 488 488 R -> Q (in PKRD; dbSNP:rs369183199).
/FTId=VAR_011469.
VARIANT 490 490 R -> W (in PKRD; dbSNP:rs200133000).
/FTId=VAR_004067.
VARIANT 495 495 A -> T (in PKRD).
/FTId=VAR_011470.
VARIANT 495 495 A -> V (in PKRD; dbSNP:rs141560532).
{ECO:0000269|PubMed:8483951}.
/FTId=VAR_004068.
VARIANT 498 498 R -> C (in PKRD; dbSNP:rs551883218).
{ECO:0000269|PubMed:9482576}.
/FTId=VAR_004069.
VARIANT 498 498 R -> H (in PKRD; dbSNP:rs758327704).
{ECO:0000269|PubMed:7706479,
ECO:0000269|PubMed:8180378}.
/FTId=VAR_004070.
VARIANT 504 504 R -> L (in PKRD; instability of the
protein; dbSNP:rs185753709).
{ECO:0000269|PubMed:11960989}.
/FTId=VAR_011471.
VARIANT 506 506 V -> I (in dbSNP:rs8177988).
{ECO:0000269|Ref.5}.
/FTId=VAR_018848.
VARIANT 510 510 R -> Q (in PKRD; the most common mutation
in European population;
dbSNP:rs113403872).
{ECO:0000269|PubMed:8180378,
ECO:0000269|PubMed:8483951,
ECO:0000269|PubMed:9482576}.
/FTId=VAR_004071.
VARIANT 511 511 G -> R (in PKRD).
/FTId=VAR_011472.
VARIANT 531 531 R -> C (in PKRD).
/FTId=VAR_011473.
VARIANT 532 532 R -> Q (in PKRD; dbSNP:rs758278200).
{ECO:0000269|PubMed:9827908}.
/FTId=VAR_004072.
VARIANT 532 532 R -> W (in PKRD; Complete loss in the
responsiveness to fructose 1,6-
bisphosphate, FBP; dbSNP:rs201255024).
{ECO:0000269|PubMed:11960989,
ECO:0000269|PubMed:8180378}.
/FTId=VAR_004073.
VARIANT 552 552 V -> M (in PKRD; dbSNP:rs370316462).
/FTId=VAR_004074.
VARIANT 557 557 G -> A (in PKRD).
/FTId=VAR_011481.
VARIANT 559 559 R -> G (in PKRD).
/FTId=VAR_004075.
VARIANT 566 566 N -> K (in PKRD).
/FTId=VAR_004076.
VARIANT 569 569 R -> Q (in PKRD; dbSNP:rs61755431).
{ECO:0000269|PubMed:21794208}.
/FTId=VAR_011482.
CONFLICT 381 381 P -> A (in Ref. 3; BAA02515).
{ECO:0000305}.
CONFLICT 423 423 A -> R (in Ref. 2; AAA60104).
{ECO:0000305}.
TURN 49 51 {ECO:0000244|PDB:4IMA}.
HELIX 55 57 {ECO:0000244|PDB:4IMA}.
HELIX 61 64 {ECO:0000244|PDB:4IP7}.
HELIX 69 74 {ECO:0000244|PDB:4IP7}.
STRAND 88 93 {ECO:0000244|PDB:4IP7}.
TURN 96 98 {ECO:0000244|PDB:4IP7}.
HELIX 101 110 {ECO:0000244|PDB:4IP7}.
STRAND 112 118 {ECO:0000244|PDB:4IP7}.
HELIX 124 139 {ECO:0000244|PDB:4IP7}.
TURN 140 143 {ECO:0000244|PDB:2VGB}.
HELIX 145 147 {ECO:0000244|PDB:4IP7}.
STRAND 152 156 {ECO:0000244|PDB:4IP7}.
STRAND 162 164 {ECO:0000244|PDB:4IP7}.
STRAND 170 172 {ECO:0000244|PDB:2VGB}.
STRAND 175 177 {ECO:0000244|PDB:4IP7}.
STRAND 182 186 {ECO:0000244|PDB:4IP7}.
HELIX 189 191 {ECO:0000244|PDB:4IP7}.
STRAND 199 203 {ECO:0000244|PDB:4IP7}.
HELIX 207 210 {ECO:0000244|PDB:4IP7}.
STRAND 216 219 {ECO:0000244|PDB:4IP7}.
TURN 220 223 {ECO:0000244|PDB:4IP7}.
STRAND 224 232 {ECO:0000244|PDB:4IP7}.
STRAND 235 242 {ECO:0000244|PDB:4IP7}.
STRAND 244 246 {ECO:0000244|PDB:4IP7}.
STRAND 251 253 {ECO:0000244|PDB:4IP7}.
HELIX 266 277 {ECO:0000244|PDB:4IP7}.
STRAND 281 285 {ECO:0000244|PDB:4IP7}.
HELIX 291 301 {ECO:0000244|PDB:4IP7}.
HELIX 303 305 {ECO:0000244|PDB:4IP7}.
STRAND 309 314 {ECO:0000244|PDB:4IP7}.
HELIX 317 321 {ECO:0000244|PDB:4IP7}.
HELIX 323 329 {ECO:0000244|PDB:4IP7}.
STRAND 330 336 {ECO:0000244|PDB:4IP7}.
HELIX 337 343 {ECO:0000244|PDB:4IP7}.
HELIX 346 348 {ECO:0000244|PDB:4IP7}.
HELIX 349 363 {ECO:0000244|PDB:4IP7}.
STRAND 367 372 {ECO:0000244|PDB:4IP7}.
HELIX 375 378 {ECO:0000244|PDB:4IP7}.
HELIX 385 397 {ECO:0000244|PDB:4IP7}.
STRAND 400 405 {ECO:0000244|PDB:4IP7}.
HELIX 406 409 {ECO:0000244|PDB:4IP7}.
HELIX 414 430 {ECO:0000244|PDB:4IP7}.
HELIX 434 442 {ECO:0000244|PDB:4IP7}.
HELIX 451 466 {ECO:0000244|PDB:4IP7}.
STRAND 469 474 {ECO:0000244|PDB:4IP7}.
STRAND 476 478 {ECO:0000244|PDB:4IP7}.
HELIX 479 485 {ECO:0000244|PDB:4IP7}.
STRAND 490 498 {ECO:0000244|PDB:4IP7}.
HELIX 500 505 {ECO:0000244|PDB:4IP7}.
HELIX 506 508 {ECO:0000244|PDB:4IP7}.
STRAND 512 516 {ECO:0000244|PDB:4IP7}.
HELIX 525 542 {ECO:0000244|PDB:4IP7}.
STRAND 551 561 {ECO:0000244|PDB:4IP7}.
STRAND 565 572 {ECO:0000244|PDB:4IP7}.
SEQUENCE 574 AA; 61830 MW; 3B430896832032F5 CRC64;
MSIQENISSL QLRSWVSKSQ RDLAKSILIG APGGPAGYLR RASVAQLTQE LGTAFFQQQQ
LPAAMADTFL EHLCLLDIDS EPVAARSTSI IATIGPASRS VERLKEMIKA GMNIARLNFS
HGSHEYHAES IANVREAVES FAGSPLSYRP VAIALDTKGP EIRTGILQGG PESEVELVKG
SQVLVTVDPA FRTRGNANTV WVDYPNIVRV VPVGGRIYID DGLISLVVQK IGPEGLVTQV
ENGGVLGSRK GVNLPGAQVD LPGLSEQDVR DLRFGVEHGV DIVFASFVRK ASDVAAVRAA
LGPEGHGIKI ISKIENHEGV KRFDEILEVS DGIMVARGDL GIEIPAEKVF LAQKMMIGRC
NLAGKPVVCA TQMLESMITK PRPTRAETSD VANAVLDGAD CIMLSGETAK GNFPVEAVKM
QHAIAREAEA AVYHRQLFEE LRRAAPLSRD PTEVTAIGAV EAAFKCCAAA IIVLTTTGRS
AQLLSRYRPR AAVIAVTRSA QAARQVHLCR GVFPLLYREP PEAIWADDVD RRVQFGIESG
KLRGFLRVGD LVIVVTGWRP GSGYTNIMRV LSIS


Related products :

Catalog number Product name Quantity
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
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 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 kit 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
U0588r CLIA Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rat,Rattus norvegicus 96T
E0588r ELISA 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
E0588Rb ELISA Oryctolagus cuniculus,PKM2,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rabbit 96T
E0588r ELISA kit Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme,Rat,Rattus norvegicus 96T
E0588m ELISA Mouse,Mus musculus,Pk3,Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme 96T
U0588m CLIA Mouse,Mus musculus,Pk3,Pkm2,Pykm,Pyruvate kinase isozymes M1_M2,Pyruvate kinase muscle isozyme 96T
29-625 PKLR is a pyruvate kinase that catalyzes the production of phohsphoenolpyruvate from pyruvate and ATP. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chro 0.1 mg
SCH-7895-0104 NATIVE RABBIT PYRUVATE KINASE, Product Type Purified Protein, Specificity PYRUVATE KINASE, Target Species Rabbit, Host N_A, Format Purified, Isotypes , Applications E, Clone 50 KU
7895-0104 NATIVE RABBIT PYRUVATE KINASE, Product Type Purified Protein, Specificity PYRUVATE KINASE, Target Species Rabbit, Host N_A, Format Purified, Isotypes , Applications E, Clone 50 KU
SCH-7894-9988 GOAT ANTI PYRUVATE KINASE, Product Type Polyclonal Antibody, Specificity PYRUVATE KINASE, Target Species , Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, Clone 1 ml
7894-9988 GOAT ANTI PYRUVATE KINASE, Product Type Polyclonal Antibody, Specificity PYRUVATE KINASE, Target Species , Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, Clone 1 ml
EIAAB30391 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial,Homo sapiens,Human,PDK4,Pyruvate dehydrogenase kinase isoform 4
EIAAB30384 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial,Homo sapiens,Human,PDK2,Pyruvate dehydrogenase kinase isoform 2
EIAAB30379 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial,Homo sapiens,Human,PDK1,Pyruvate dehydrogenase kinase isoform 1
EIAAB30387 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial,Homo sapiens,Human,PDK3,Pyruvate dehydrogenase kinase isoform 3
EIAAB30389 [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 4, mitochondrial,Mouse,Mus musculus,Pdk4,Pyruvate dehydrogenase kinase isoform 4
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


 

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