Human Gene PKLR (ENST00000392414.7) Description and Page Index
Description: Homo sapiens pyruvate kinase L/R (PKLR), transcript variant 2, mRNA. (from RefSeq NM_181871) RefSeq Summary (NM_181871): 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]. Gencode Transcript: ENST00000392414.7 Gencode Gene: ENSG00000143627.19 Transcript (Including UTRs) Position: hg38 chr1:155,289,839-155,301,001 Size: 11,163 Total Exon Count: 11 Strand: - Coding Region Position: hg38 chr1:155,290,572-155,300,887 Size: 10,316 Coding Exon Count: 11
ID:KPYR_HUMAN DESCRIPTION: RecName: Full=Pyruvate kinase isozymes R/L; EC=18.104.22.168; AltName: Full=Pyruvate kinase 1; AltName: Full=R-type/L-type pyruvate kinase; AltName: Full=Red cell/liver pyruvate kinase; FUNCTION: Plays a key role in glycolysis (By similarity). CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. COFACTOR: Magnesium. COFACTOR: Potassium. ENZYME REGULATION: Allosterically activated by fructose 1,6- bisphosphate. PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- glyceraldehyde 3-phosphate: step 5/5. SUBUNIT: Homotetramer. DISEASE: Defects in PKLR are the cause of pyruvate kinase hyperactivity (PKHYP) [MIM:102900]; also known as high red cell ATP syndrome. This autosomal dominant phenotype is characterized by increase of red blood cell ATP. DISEASE: Defects in PKLR are the cause of 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. 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. WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/PKLR"; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/pklr/"; WEB RESOURCE: Name=Wikipedia; Note=Pyruvate kinase entry; URL="http://en.wikipedia.org/wiki/Pyruvate_kinase"; WEB RESOURCE: Name=PKLR Mutation Database; URL="http://www.pklrmutationdatabase.com/";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P30613
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.