PFKFB2: Difference between revisions

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*{{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 }}
*{{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 }}
*{{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 }}
*{{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 }}
*{{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 }}
*{{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 }}
*{{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=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 }}
*{{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 }}
*{{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 }}
*{{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 }}
*{{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=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 }}
*{{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 }}
}}
}}
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Latest revision as of 19:41, 25 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2 gene.[1]

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.[1]

Interactions

PFKFB2 has been shown to interact with YWHAQ.[2]

References

  1. 1.0 1.1 "Entrez Gene: PFKFB2 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2".
  2. Pozuelo Rubio, Mercedes; Peggie Mark; Wong Barry H C; Morrice Nick; MacKintosh Carol (Jul 2003). "14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase". EMBO J. England. 22 (14): 3514–23. doi:10.1093/emboj/cdg363. ISSN 0261-4189. PMC 165633. PMID 12853467.

Further reading