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edit Phosphofructokinase, platelet Identifiers Symbols PFKP; FLJ40226; PFK-C; PFKF External IDs OMIM: 171840 MGI: 1891833 HomoloGene: 20579 GeneCards: PFKP Gene EC number 2.7.1.11 Gene Ontology Molecular function • nucleotide binding • magnesium ion binding • 6-phosphofructokinase activity • ATP binding • kinase activity • transferase activity Cellular component • cytoplasm • 6-phosphofructokinase complex Biological process • glycolysis Sources: Amigo / QuickGO RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 5214 56421 Ensembl ENSG00000067057 ENSMUSG00000021196 UniProt Q01813 Q8C605 RefSeq (mRNA) NM_002627 NM_019703 RefSeq (protein) NP_002618 NP_062677 Location (UCSC) Chr 10: 3.1 - 3.17 Mb Chr 13: 6.58 - 6.65 Mb PubMed search [1] [2] Phosphofructokinase, platelet, also known as PFKP is an enzyme which in humans is encoded by the PFKP gene.[1] Function The PFKP gene encodes the platelet isoform of phosphofructokinase (PFK) (ATP:D-fructose-6-phosphate-1-phosphotransferase, EC 2.7.1.11). PFK catalyzes the irreversible conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and is a key regulatory enzyme in glycolysis. The PFKP gene, which maps to chromosome 10p, is also expressed in fibroblasts. See also the muscle (PFKM) and liver (PFKL) isoforms of phosphofructokinase, which map to chromosomes 12q13 and 21q22, respectively. Full tetrameric phophofructokinase enzyme expressed in platelets can be composed of subunits P4, P3L, and P2L2.[2][1] References ^ a b "Entrez Gene: PFKP phosphofructokinase, platelet". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5214.  ^ Vora S (April 1981). "Isozymes of human phosphofructokinase in blood cells and cultured cell lines: molecular and genetic evidence for a trigenic system". Blood 57 (4): 724–32. PMID 6451249. http://www.bloodjournal.org/cgi/pmidlookup?view=long&pmid=6451249.  Further reading Meienhofer MC, Lagrange JL, Cottreau D, et al. (1979). "Phosphofructokinase in human blood cells.". Blood 54 (2): 389–400. PMID 156568.  Kahn A, Meienhofer MC, Cottreau D, et al. (1979). "Phosphofructokinase (PFK) isozymes in man. I. Studies of adult human tissues.". Hum. Genet. 48 (1): 93–108. PMID 156693.  Morrison N, Simpson C, Fothergill-Gilmore L, et al. (1992). "Regional chromosomal assignment of the human platelet phosphofructokinase gene to 10p15.". Hum. Genet. 89 (1): 105–6. doi:10.1007/BF00207053. PMID 1533608.  Simpson CJ, Fothergill-Gilmore LA (1991). "Isolation and sequence of a cDNA encoding human platelet phosphofructokinase.". Biochem. Biophys. Res. Commun. 180 (1): 197–203. doi:10.1016/S0006-291X(05)81276-8. PMID 1834056.  Nakajima H, Noguchi T, Yamasaki T, et al. (1987). "Cloning of human muscle phosphofructokinase cDNA.". FEBS Lett. 223 (1): 113–6. doi:10.1016/0014-5793(87)80519-7. PMID 2822475.  Eto K, Sakura H, Yasuda K, et al. (1994). "Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet.". Biochem. Biophys. Res. Commun. 198 (3): 990–8. doi:10.1006/bbrc.1994.1141. PMID 8117307.  Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.  Adam GC, Sorensen EJ, Cravatt BF (2003). "Trifunctional chemical probes for the consolidated detection and identification of enzyme activities from complex proteomes.". Mol. Cell Proteomics 1 (10): 828–35. PMID 12438565.  Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.  Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.  Navarro-Lérida I, Martínez Moreno M, Roncal F, et al. (2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8.". Proteomics 4 (2): 339–46. doi:10.1002/pmic.200300528. PMID 14760703.  Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.  Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.  Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.  Hannemann A, Jandrig B, Gaunitz F, et al. (2005). "Characterization of the human P-type 6-phosphofructo-1-kinase gene promoter in neural cell lines.". Gene 345 (2): 237–47. doi:10.1016/j.gene.2004.11.018. PMID 15716112.  Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization.". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.  Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.  Martínez-Costa OH, Sánchez-Martínez C, Sánchez V, Aragón JJ (2007). "Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: implications for ligand binding sites.". FEBS Lett. 581 (16): 3033–8. doi:10.1016/j.febslet.2007.05.059. PMID 17544406.  This article incorporates text from the United States National Library of Medicine, which is in the public domain. This article on a gene on chromosome 10 is a stub. You can help Wikipedia by expanding it. v • d • e v • d • e Transferases: phosphorus-containing groups (EC 2.7) 2.7.1-2.7.4: phosphotransferase/kinase (PO4) 2.7.1: OH acceptor Hexo- · Gluco- · Fructo- (Hepatic) · Galacto- · Phosphofructo- (1, Liver, Muscle, Platelet, 2) · Riboflavin · Shikimate · Thymidine (ADP-thymidine) · NAD+ · Glycerol · Pantothenate · Mevalonate · Pyruvate · Deoxycytidine · PFP · Diacylglycerol · Phosphoinositide 3 (Class I PI 3, Class II PI 3) · Sphingosine · Glucose-1,6-bisphosphate synthase 2.7.2: COOH acceptor Phosphoglycerate · Aspartate 2.7.3: N acceptor Creatine 2.7.4: PO4 acceptor Phosphomevalonate · Adenylate · Nucleoside-diphosphate 2.7.6: diphosphotransferase (P2O7) Ribose-phosphate diphosphokinase · Thiamine pyrophosphokinase 2.7.7: nucleotidyltransferase (PO4-nucleoside) Polymerase DNA polymerase DNA-directed DNA polymerase: DNA polymerase I · DNA polymerase II · DNA polymerase III holoenzyme RNA-directed DNA polymerase: Reverse transcriptase (Telomerase) DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase RNA nucleotidyltransferase RNA polymerase/DNA-directed RNA polymerase: RNA polymerase I · RNA polymerase II · RNA polymerase III · RNA polymerase IV · Primase · RNA-dependent RNA polymerase PNPase Phosphorolytic 3' to 5' exoribonuclease RNase PH · PNPase Uridylyltransferase Glucose-1-phosphate uridylyltransferase · Galactose-1-phosphate uridylyltransferase Guanylyltransferase mRNA capping enzyme Other Recombinase (Integrase) · Transposase 2.7.8: miscellaneous Phosphatidyltransferases CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase · CDP-diacylglycerol—serine O-phosphatidyltransferase · CDP-diacylglycerol—inositol 3-phosphatidyltransferase · CDP-diacylglycerol—choline O-phosphatidyltransferase Glycosyl-1-phosphotransferase N-acetylglucosamine-1-phosphate transferase 2.7.10-2.7.13: protein kinase (PO4; protein acceptor) 2.7.10: protein-tyrosine see tyrosine kinases 2.7.11: protein-serine/threonine see serine/threonine-specific protein kinases 2.7.12: protein-dual-specificity see serine/threonine-specific protein kinases 2.7.13: protein-histidine Protein-histidine pros-kinase · Protein-histidine tele-kinase · Histidine kinase B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6 v • d • e Metabolism: carbohydrate metabolism: glycolysis/gluconeogenesis enzymes Glycolysis Hexokinase (HK1, HK2, HK3, Glucokinase)→/Glucose 6-phosphatase← · Glucose isomerase · Phosphofructokinase 1 (Liver, Muscle, Platelet)→/Fructose 1,6-bisphosphatase← Aldolase (A, B)  · Triosephosphate isomerase Glyceraldehyde 3-phosphate dehydrogenase · Phosphoglycerate kinase · Phosphoglycerate mutase · Enolase · Pyruvate kinase (PKLR, PKM2) Gluconeogenesis only to oxaloacetate: Pyruvate carboxylase · Phosphoenolpyruvate carboxykinase from lactate (Cori cycle): Lactate dehydrogenase from alanine (Alanine cycle): Alanine transaminase from glycerol: Glycerol kinase · Glycerol dehydrogenase Regulatory Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase (PFKFB1, PFKFB2, PFKFB3, PFKFB4) · Bisphosphoglycerate mutase M: MET mt, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, h cgrp/y/i, f/h/s/l/o, au, n, h, epon m(A16, C10),i(c/g/r/p/y/i, f/h/s/o/e, a/u,n, h)