PFKFB2

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2 is an enzyme that in humans is encoded by the PFKFB2 gene.[5]

PFKFB2
Identifiers
Aliases	PFKFB2, PFK-2/FBPase-2, 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2
External IDs	OMIM: 171835 MGI: 107815 HomoloGene: 88554 GeneCards: PFKFB2
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q32.1 Start 207,034,366 bp[1] End 207,081,024 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 E4 Start 130,689,182 bp[2] End 130,729,253 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • kinase activity • GO:0001948 protein binding • catalytic activity • fructose-2,6-bisphosphate 2-phosphatase activity • hydrolase activity • ATP binding • protein kinase binding • 6-phosphofructo-2-kinase activity • kinase binding Cellular component • cytoplasm • cytosol • cell nucleus • nucleoplasm Biological process • lactate metabolic process • glycolytic process • phosphorylation • fructose metabolic process • response to glucose • positive regulation of glucokinase activity • fructose 2,6-bisphosphate metabolic process • pyruvate metabolic process • glucose catabolic process • metabolism • positive regulation of insulin secretion • dephosphorylation • carbohydrate phosphorylation • positive regulation of glycolytic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5208	18640
Ensembl	ENSG00000123836	ENSMUSG00000026409
UniProt	O60825	P70265
RefSeq (mRNA)	NM_001018053 NM_006212	NM_001162415 NM_001162416 NM_008825 NM_001368843
RefSeq (protein)	NP_001018063 NP_006203	NP_001155887 NP_001155888 NP_032851 NP_001355772
Location (UCSC)	Chr 1: 207.03 – 207.08 Mb	Chr 1: 130.69 – 130.73 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[5]

Interactions

PFKFB2 has been shown to interact with YWHAQ.[6]

References

1. GRCh38: Ensembl release 89: ENSG00000123836 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000026409 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: PFKFB2 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 2".
6. 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

• Rider MH, Vandamme J, Lebeau E, et al. (1992). "The two forms of bovine heart 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase result from alternative splicing". Biochem. J. 285 (2): 405–11. doi:10.1042/bj2850405. PMC 1132803. PMID 1322130.
• Hilliker CE, Darville MI, Aly MS, et al. (1991). "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". Genomics. 10 (4): 867–73. doi:10.1016/0888-7543(91)90174-D. PMID 1655632.
• Goldmuntz EA, Remmers EF, Zha H, et al. (1994). "Genetic map of seven polymorphic markers comprising a single linkage group on rat chromosome 5". Mamm. Genome. 4 (11): 670–5. doi:10.1007/BF00360905. PMID 7904197. S2CID 1892799.
• Hirata T, Kato M, Okamura N, et al. (1998). "Expression of human placental-type 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase in various cells and cell lines". Biochem. Biophys. Res. Commun. 242 (3): 680–4. doi:10.1006/bbrc.1997.8024. PMID 9464277.
• Heine-Suñer D, Díaz-Guillén MA, Lange AJ, Rodríguez de Córdoba S (1998). "Sequence and structure of the human 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase heart isoform gene (PFKFB2)". Eur. J. Biochem. 254 (1): 103–10. doi:10.1046/j.1432-1327.1998.2540103.x. PMID 9652401.
• Hirata T, Watanabe M, Miura S, et al. (2001). "Inhibition of tumor cell growth by a specific 6-phosphofructo-2-kinase inhibitor, N-bromoacetylethanolamine phosphate, and its analogues". Biosci. Biotechnol. Biochem. 64 (10): 2047–52. doi:10.1271/bbb.64.2047. PMID 11129574. S2CID 38413244.
• Kessler R, Eschrich K (2001). "Splice isoforms of ubiquitous 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase in human brain". Brain Res. Mol. Brain Res. 87 (2): 190–5. doi:10.1016/S0169-328X(01)00014-6. PMID 11245921.
• Soejima H, Kawamoto S, Akai J, et al. (2001). "Isolation of novel heart-specific genes using the BodyMap database". Genomics. 74 (1): 115–20. doi:10.1006/geno.2001.6527. PMID 11374908.
• Baltrusch S, Lenzen S, Okar DA, et al. (2001). "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". J. Biol. Chem. 276 (47): 43915–23. doi:10.1074/jbc.M105470200. PMID 11522786.
• Marsin AS, Bouzin C, Bertrand L, Hue L (2002). "The stimulation of glycolysis by hypoxia in activated monocytes is mediated by AMP-activated protein kinase and inducible 6-phosphofructo-2-kinase". J. Biol. Chem. 277 (34): 30778–83. doi:10.1074/jbc.M205213200. PMID 12065600.
• 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Pozuelo Rubio M, Peggie M, Wong BH, et al. (2003). "14-3-3s regulate fructose-2,6-bisphosphate levels by binding to PKB-phosphorylated cardiac fructose-2,6-bisphosphate kinase/phosphatase". EMBO J. 22 (14): 3514–23. doi:10.1093/emboj/cdg363. PMC 165633. PMID 12853467.
• 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.
• Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
• 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. PMC 528928. PMID 15489334.
• Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi:10.1038/nature04727. PMID 16710414.