Pyruvate kinase PKLR

PKLR
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VGB, 2VGF, 2VGG, 2VGI, 4IMA, 4IP7
Identifiers
Aliases	PKLR, PK1, PKL, PKR, PKRL, RPK, pyruvate kinase, liver and RBC, pyruvate kinase L/R
External IDs	OMIM: 609712; MGI: 97604; HomoloGene: 37286; GeneCards: PKLR; OMA:PKLR - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q22 Start 155,289,293 bp End 155,301,438 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 F1|3 39.01 cM Start 89,043,449 bp End 89,054,091 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in liver right lobe of liver duodenum bone marrow bone marrow cells renal cortex cerebellum cerebellar cortex cerebellar hemisphere human kidney Top expressed in fetal liver hematopoietic progenitor cell jejunum yolk sac duodenum left lobe of liver ileum intestinal villus epithelium of small intestine Ileal epithelium lumbar subsegment of spinal cord More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding potassium ion binding metal ion binding kinase activity catalytic activity ATP binding magnesium ion binding pyruvate kinase activity Cellular component cytosol extracellular exosome cytoplasm Biological process response to ATP response to hypoxia phosphorylation response to nutrient canonical glycolysis response to metal ion pyruvate biosynthetic process response to heat response to glucose response to lithium ion ATP biosynthetic process metabolism response to cAMP glycolytic process cellular response to insulin stimulus cellular response to epinephrine stimulus carbohydrate metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5313 18770 Ensembl ENSG00000262785 ENSG00000143627 ENSMUSG00000041237 UniProt P30613 P53657 RefSeq (mRNA) NM_000298 NM_181871 NM_001099779 NM_013631 RefSeq (protein) NP_000289 NP_870986 n/a Location (UCSC) Chr 1: 155.29 – 155.3 Mb Chr 3: 89.04 – 89.05 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Pyruvate kinase PKLR is an enzyme that in humans is encoded by the PKLR gene.

The protein encoded by this gene is a pyruvate kinase that catalyzes the production of pyruvate and ATP from phosphoenolpyruvate. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Alternatively spliced transcript variants encoding distinct isoforms have been described.

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.

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Glycolysis and Gluconeogenesis edit

Further reading

• Beutler E, Baronciani L (1996). "Mutations in pyruvate kinase". Hum. Mutat. 7 (1): 1–6. doi:10.1002/(SICI)1098-1004(1996)7:1<1::AID-HUMU1>3.0.CO;2-H. PMID 8664896. S2CID 2481467.
• Baronciani L, Bianchi P, Zanella A (1999). "Hematologically important mutations: red cell pyruvate kinase (2nd update)". Blood Cells Mol. Dis. 24 (3): 273–9. doi:10.1006/bcmd.1998.0193. PMID 10087985.
• Zanella A, Fermo E, Bianchi P, et al. (2007). "Pyruvate kinase deficiency: the genotype-phenotype association". Blood Rev. 21 (4): 217–31. doi:10.1016/j.blre.2007.01.001. PMID 17360088.
• Kanno H, Fujii H, Miwa S (1992). "Structural analysis of human pyruvate kinase L-gene and identification of the promoter activity in erythroid cells". Biochem. Biophys. Res. Commun. 188 (2): 516–23. doi:10.1016/0006-291X(92)91086-6. PMID 1445295.
• Kanno H, Fujii H, Hirono A, et al. (1992). "Identical point mutations of the R-type pyruvate kinase (PK) cDNA found in unrelated PK variants associated with hereditary hemolytic anemia". Blood. 79 (5): 1347–50. doi:10.1182/blood.V79.5.1347.1347. PMID 1536957.
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Kanno H, Fujii H, Hirono A, Miwa S (1991). "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 (18): 8218–21. Bibcode:1991PNAS...88.8218K. doi:10.1073/pnas.88.18.8218. PMC 52478. PMID 1896471.
• Neubauer B, Lakomek M, Winkler H, et al. (1991). "Point mutations in the L-type pyruvate kinase gene of two children with hemolytic anemia caused by pyruvate kinase deficiency". Blood. 77 (9): 1871–5. doi:10.1182/blood.V77.9.1871.1871. PMID 2018831.
• Tani K, Fujii H, Nagata S, Miwa S (1988). "Human liver type pyruvate kinase: complete amino acid sequence and the expression in mammalian cells". Proc. Natl. Acad. Sci. U.S.A. 85 (6): 1792–5. Bibcode:1988PNAS...85.1792T. doi:10.1073/pnas.85.6.1792. PMC 279865. PMID 3126495.
• Satoh H, Tani K, Yoshida MC, et al. (1988). "The human liver-type pyruvate kinase (PKL) gene is on chromosome 1 at band q21". Cytogenet. Cell Genet. 47 (3): 132–3. doi:10.1159/000132530. PMID 3378452.
• Baronciani L, Beutler E (1995). "Molecular study of pyruvate kinase deficient patients with hereditary nonspherocytic hemolytic anemia". J. Clin. Invest. 95 (4): 1702–9. doi:10.1172/JCI117846. PMC 295683. PMID 7706479.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Kanno H, Ballas SK, Miwa S, et al. (1994). "Molecular abnormality of erythrocyte pyruvate kinase deficiency in the Amish". Blood. 83 (8): 2311–6. doi:10.1182/blood.V83.8.2311.2311. PMID 8161798.
• Lenzner C, Nürnberg P, Thiele BJ, et al. (1994). "Mutations in the pyruvate kinase L gene in patients with hereditary hemolytic anemia". Blood. 83 (10): 2817–22. doi:10.1182/blood.V83.10.2817.2817. PMID 8180378.
• Kanno H, Fujii H, Tsujino G, Miwa S (1993). "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 (1): 46–52. doi:10.1006/bbrc.1993.1379. PMID 8476433.
• Kanno H, Fujii H, Miwa S (1993). "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 (9): 2439–41. doi:10.1182/blood.V81.9.2439.bloodjournal8192439. PMID 8481523.
• Baronciani L, Beutler E (1993). "Analysis of pyruvate kinase-deficiency mutations that produce nonspherocytic hemolytic anemia". Proc. Natl. Acad. Sci. U.S.A. 90 (9): 4324–7. Bibcode:1993PNAS...90.4324B. doi:10.1073/pnas.90.9.4324. PMC 46499. PMID 8483951.
• Baronciani L, Bianchi P, Zanella A (1996). "Hematologically important mutations: red cell pyruvate kinase". Blood Cells Mol. Dis. 22 (1): 85–9. doi:10.1006/bcmd.1996.0012. PMID 8807089.