FN3K

Fructosamine 3 kinase, also known as FN3K, is a human gene.cite web | title = Entrez Gene: FN3K fructosamine 3 kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64122| accessdate = ]

PBB_Summary
section_title =
summary_text = FN3K catalyzes phosphorylation of fructosamines formed by glycation, the nonenzymatic reaction of glucose with primary amines followed by Amadori rearrangement. Phosphorylation of fructosamines may initiate metabolism of the modified amine and result in deglycation of glycated proteins (Delpierre et al., 2000). [supplied by OMIM] cite web | title = Entrez Gene: FN3K fructosamine 3 kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=64122| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Delpierre G, Rider MH, Collard F, "et al." |title=Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase. |journal=Diabetes |volume=49 |issue= 10 |pages= 1627–34 |year= 2000 |pmid= 11016445 |doi=
*cite journal | author=Szwergold BS, Howell S, Beisswenger PJ |title=Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo. |journal=Diabetes |volume=50 |issue= 9 |pages= 2139–47 |year= 2001 |pmid= 11522682 |doi=
*cite journal | author=Delpierre G, Collard F, Fortpied J, Van Schaftingen E |title=Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. |journal=Biochem. J. |volume=365 |issue= Pt 3 |pages= 801–8 |year= 2002 |pmid= 11975663 |doi= 10.1042/BJ20020325
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=Delpierre G, Van Schaftingen E |title=Fructosamine 3-kinase, an enzyme involved in protein deglycation. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 6 |pages= 1354–7 |year= 2004 |pmid= 14641062 |doi= 10.1042/
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |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 | author=Delpierrre G, Vertommen D, Communi D, "et al." |title=Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin. |journal=J. Biol. Chem. |volume=279 |issue= 26 |pages= 27613–20 |year= 2004 |pmid= 15102834 |doi= 10.1074/jbc.M402091200
*cite journal | author=Delplanque J, Delpierre G, Opperdoes FR, Van Schaftingen E |title=Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein. |journal=J. Biol. Chem. |volume=279 |issue= 45 |pages= 46606–13 |year= 2004 |pmid= 15331600 |doi= 10.1074/jbc.M407678200
*cite journal | author=Conner JR, Beisswenger PJ, Szwergold BS |title=The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinase-related protein appears to be constitutive and unaffected by environmental signals. |journal=Biochem. Biophys. Res. Commun. |volume=323 |issue= 3 |pages= 932–6 |year= 2004 |pmid= 15381090 |doi= 10.1016/j.bbrc.2004.08.181
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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
*cite journal | author=Conner JR, Beisswenger PJ, Szwergold BS |title=Some clues as to the regulation, expression, function, and distribution of fructosamine-3-kinase and fructosamine-3-kinase-related protein. |journal=Ann. N. Y. Acad. Sci. |volume=1043 |issue= |pages= 824–36 |year= 2005 |pmid= 16037310 |doi= 10.1196/annals.1333.095
*cite journal | author=Delpierre G, Veiga-da-Cunha M, Vertommen D, "et al." |title=Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites. |journal=Diabetes Metab. |volume=32 |issue= 1 |pages= 31–9 |year= 2006 |pmid= 16523184 |doi=
*cite journal | author=Szwergold BS |title=Fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by fructosamine-3-kinase (FN3K) and/or fructosamine-3-kinase-related-protein (FN3KRP). |journal=Med. Hypotheses |volume=68 |issue= 1 |pages= 37–45 |year= 2007 |pmid= 16920277 |doi= 10.1016/j.mehy.2006.06.030

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