NP_000289.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
63.8 kDa
NCBI Official Full Name
pyruvate kinase PKLR isoform 1
NCBI Official Synonym Full Names
pyruvate kinase, liver and RBC
NCBI Protein Information
pyruvate kinase PKLR
UniProt Protein Name
Pyruvate kinase PKLR
UniProt Synonym Protein Names
Pyruvate kinase 1; Pyruvate kinase isozymes L/R; R-type/L-type pyruvate kinase; Red cell/liver pyruvate kinase
UniProt Synonym Gene Names
UniProt Entry Name
KPYR_HUMAN
NCBI Summary for PKLR
The protein encoded by this gene is a pyruvate kinase that catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP, which is the rate-limiting step of glycolysis. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008]
UniProt Comments for PKLR
PKLR: one of three rate-limiting enzymes in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule ATP and a pyruvate molecule, which is a central metabolic intermediate that can be used as a building block or oxidized further. There are several mammalian isozymes of pyruvate kinase encoded by different genes. The L type predominates in liver, and the M type in muscle and brain. Two alternatively spliced human isoforms have been described: the R- and L-types.
Protein type: Kinase, other; EC 2.7.1.40; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Carbohydrate Metabolism - pyruvate; Nucleotide Metabolism - purine
Chromosomal Location of Human Ortholog: 1q21
Cellular Component: cytosol
Molecular Function: ATP binding; kinase activity; magnesium ion binding; potassium ion binding; pyruvate kinase activity
Biological Process: ATP biosynthetic process; carbohydrate metabolic process; cellular response to insulin stimulus; endocrine pancreas development; energy reserve metabolic process; glucose metabolic process; positive regulation of cellular metabolic process; pyruvate biosynthetic process; response to ATP; response to cAMP; response to glucose stimulus; response to heat; response to hypoxia; response to lithium ion; response to nutrient; response to other organism
Disease: Adenosine Triphosphate, Elevated, Of Erythrocytes; Pyruvate Kinase Deficiency Of Red Cells
Product References and Citations for PKLR recombinant protein
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.Kanno H., Fujii H., Hirono A., Miwa S.Proc. Natl. Acad. Sci. U.S.A. 88:8218-8221(1991)
Human liver type pyruvate kinase
complete amino acid sequence and the expression in mammalian cells.Tani K., Fujii H., Nagata S., Miwa S.Proc. Natl. Acad. Sci. U.S.A. 85:1792-1795(1988)
Kanno H.Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells.Kanno H., Fujii H., Miwa S.Biochem. Biophys. Res. Commun. 188:516-523(1992)
NIEHS SNPs program
Human liver type pyruvate kinase
cDNA cloning and chromosomal assignment.Tani K., Fujii H., Tsutsumi H., Sukegawa J., Toyoshima K., Yoshida M.C., Noguchi T., Tanaka T., Miwa S.Biochem. Biophys. Res. Commun. 143:431-438(1987)
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.Kanno H., Fujii H., Tsujino G., Miwa S.Biochem. Biophys. Res. Commun. 192:46-52(1993)
Mutations in pyruvate kinase.Beutler E., Baronciani L.3.0.CO;2-H>Hum. Mutat. 7:1-6(1996)
Hematologically important mutations
red cell pyruvate kinase.Baronciani L., Bianchi P., Zanella A.Blood Cells Mol. Dis. 22:85-89(1996)
Hematologically important mutations
red cell pyruvate kinase (1st update)
.Baronciani L., Bianchi P., Zanella A.Blood Cells Mol. Dis. 22:259-264(1996)
Hematologically important mutations
red cell pyruvate kinase (2nd update)
.Baronciani L., Bianchi P., Zanella A.Blood Cells Mol. Dis. 24:273-279(1998)
Hematologically important mutations
red cell pyruvate kinase (third update)
.Bianchi P., Zanella A.Blood Cells Mol. Dis. 26:47-53(2000)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.Valentini G., Chiarelli L.R., Fortin R., Dolzan M., Galizzi A., Abraham D.J., Wang C., Bianchi P., Zanella A., Mattevi A.J. Biol. Chem. 277:23807-23814(2002)
Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency.Neubauer B., Lakomek M., Winkler H., Parke M., Hofferbert S., Schroter W.Blood 77:1871-1875(1991)
Identical point mutations of the R-type pyruvate kinase (PK)
cDNA found in unrelated PK variants associated with hereditary hemolytic anemia.Kanno H., Fujii H., Hirono A., Omine M., Miwa S.Blood 79:1347-1350(1992)
Low substrate affinity of pyruvate kinase variant (PK Sapporo)
caused by a single amino acid substitution (426 Arg-->Gln)
associated with hereditary hemolytic anemia.Kanno H., Fujii H., Miwa S.Blood 81:2439-2441(1993)
Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia.Baronciani L., Beutler E.Proc. Natl. Acad. Sci. U.S.A. 90:4324-4327(1993)
Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish.Kanno H., Ballas S.K., Miwa S., Fujii H., Bowman H.S.Blood 83:2311-2316(1994)
Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia.Lenzner C., Nuernberg P., Thiele B.-J., Reis A., Brabec V., Sakalova A., Jacobasch G.Blood 83:2817-2822(1994)
Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia.Baronciani L., Beutler E.J. Clin. Invest. 95:1702-1709(1995)
Study of the molecular defects in pyruvate kinase (PK)
deficient patients affected by hereditary nonspherocytic hemolytic anemia (HNHA)
.Baronciani L., Westwood B., Beutler E.J. Invest. Med. 43:341A-341A(1995)
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.Beutler E., Westwood B., van Zwieten R., Roos D.3.0.CO;2-Z>Hum. Mutat. 9:282-285(1997)
Molecular characterization of the PK-LR gene in pyruvate kinase deficient Spanish patients.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.Br. J. Haematol. 103:377-382(1998)
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)
.Cohen-Solal M., Prehu C., Wajcman H., Poyart C., Bardakdjian-Michau J., Kister J., Prome D., Valentin C., Bachir D., Galacteros F.Br. J. Haematol. 103:950-956(1998)
Novel mutations and structural implications in R-type pyruvate kinase-deficient patients from Southern Italy.Pastore L., della Morte R., Frisso G., Alfinito F., Vitale D., Calise R.M., Ferraro F., Zagari A., Rotoli B., Salvatore F.3.0.CO;2-G>Hum. Mutat. 11:127-134(1998)
Molecular characterization of the PK-LR gene in sixteen pyruvate kinase-deficient patients.Zanella A., Bianchi P., Fermo E., Iurlo A., Zappa M., Vercellati C., Boschetti C., Baronciani L., Cotton F.Br. J. Haematol. 113:43-48(2001)
Fifteen novel mutations in PKLR associated with pyruvate kinase (PK)
deficiency
structural implications of amino acid substitutions in PK.van Wijk R., Huizinga E.G., van Wesel A.C.W., van Oirschot B.A., Hadders M.A., van Solinge W.W.Hum. Mutat. 30:446-453(2009)
Exome sequencing and unrelated findings in the context of complex disease research
ethical and clinical implications.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.Discov. Med. 12:41-55(2011)
Research Articles on PKLR
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