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PFKFB2

{{Short description|Protein-coding gene in the species Homo sapiens}}

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{{Confusing|date=December 2022}}

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6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2 gene.{{cite web | title = Entrez Gene: PFKFB2 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5208}}

The protein encoded by this gene is involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls glycolysis in eukaryotes. The encoded protein has a 6-phosphofructo-2-kinase activity that catalyzes the synthesis of fructose-2,6-bisphosphate, and a fructose-2,6-biphosphatase activity that catalyzes the degradation of fructose-2,6-bisphosphate. This protein regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle. This enzyme functions as a homodimer. Two transcript variants encoding two different isoforms have been found for this gene.{{cite web | title = Entrez Gene: PFKFB2 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5208}}

Interactions

PFKFB2 has been shown to interact with YWHAQ.{{cite journal |last=Pozuelo Rubio |first=Mercedes |author2=Peggie Mark |author3=Wong Barry H C |author4=Morrice Nick |author5=MacKintosh Carol |date=Jul 2003 |title=14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase |journal=EMBO J. |volume=22 |issue=14 |pages=3514–23 |location = England| issn = 0261-4189| pmid = 12853467 |doi = 10.1093/emboj/cdg363 |pmc=165633 }}

References

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Further reading

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  • {{cite journal |vauthors=Rider MH, Vandamme J, Lebeau E, etal |title=The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing. |journal=Biochem. J. |volume=285 |issue= 2|pages= 405–11 |year= 1992 |doi=10.1042/bj2850405 |pmid= 1322130 | pmc=1132803 }}
  • {{cite journal |vauthors=Hilliker CE, Darville MI, Aly MS, etal |title=Human and rat chromosomal localization of two genes for 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase by analysis of somatic cell hybrids and in situ hybridization. |journal=Genomics |volume=10 |issue= 4 |pages= 867–73 |year= 1991 |pmid= 1655632 |doi=10.1016/0888-7543(91)90174-D }}
  • {{cite journal |vauthors=Goldmuntz EA, Remmers EF, Zha H, etal |title=Genetic map of seven polymorphic markers comprising a single linkage group on rat chromosome 5. |journal=Mamm. Genome |volume=4 |issue= 11 |pages= 670–5 |year= 1994 |pmid= 7904197 |doi=10.1007/BF00360905 |s2cid=1892799 |url=https://zenodo.org/record/1232430 }}
  • {{cite journal |vauthors=Hirata T, Kato M, Okamura N, etal |title=Expression of human placental-type 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase in various cells and cell lines. |journal=Biochem. Biophys. Res. Commun. |volume=242 |issue= 3 |pages= 680–4 |year= 1998 |pmid= 9464277 |doi= 10.1006/bbrc.1997.8024 }}
  • {{cite journal |vauthors=Heine-Suñer D, Díaz-Guillén MA, Lange AJ, Rodríguez de Córdoba S |title=Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2). |journal=Eur. J. Biochem. |volume=254 |issue= 1 |pages= 103–10 |year= 1998 |pmid= 9652401 |doi=10.1046/j.1432-1327.1998.2540103.x |doi-access=free }}
  • {{cite journal |vauthors=Hirata T, Watanabe M, Miura S, etal |title=Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues. |journal=Biosci. Biotechnol. Biochem. |volume=64 |issue= 10 |pages= 2047–52 |year= 2001 |pmid= 11129574 |doi=10.1271/bbb.64.2047 |s2cid=38413244 |doi-access=free }}
  • {{cite journal |vauthors=Kessler R, Eschrich K |title=Splice isoforms of ubiquitous 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in human brain. |journal=Brain Res. Mol. Brain Res. |volume=87 |issue= 2 |pages= 190–5 |year= 2001 |pmid= 11245921 |doi=10.1016/S0169-328X(01)00014-6 }}
  • {{cite journal |vauthors=Soejima H, Kawamoto S, Akai J, etal |title=Isolation of novel heart-specific genes using the BodyMap database. |journal=Genomics |volume=74 |issue= 1 |pages= 115–20 |year= 2001 |pmid= 11374908 |doi= 10.1006/geno.2001.6527 }}
  • {{cite journal |vauthors=Baltrusch S, Lenzen S, Okar DA, etal |title=Characterization of glucokinase-binding protein epitopes by a phage-displayed peptide library. Identification of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase as a novel interaction partner. |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 43915–23 |year= 2001 |pmid= 11522786 |doi= 10.1074/jbc.M105470200 |doi-access= free }}
  • {{cite journal |vauthors=Marsin AS, Bouzin C, Bertrand L, Hue L |title=The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase. |journal=J. Biol. Chem. |volume=277 |issue= 34 |pages= 30778–83 |year= 2002 |pmid= 12065600 |doi= 10.1074/jbc.M205213200 |doi-access= free |hdl= 2078.1/12913 |hdl-access= free }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Pozuelo Rubio M, Peggie M, Wong BH, etal |title=14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase. |journal=EMBO J. |volume=22 |issue= 14 |pages= 3514–23 |year= 2003 |pmid= 12853467 |doi= 10.1093/emboj/cdg363 | pmc=165633 }}
  • {{cite journal |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |doi-access= free }}
  • {{cite journal |vauthors=Jin J, Smith FD, Stark C, etal |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051 |s2cid=2371325 |doi-access=free |bibcode=2004CBio...14.1436J }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 |bibcode=2006Natur.441..315G |doi-access=free }}

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{{Glycolysis enzymes}}

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