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Fructosamine 3 kinase related protein

FN3KRP, FN3K-related protein, fructosamine-3-kinase-related protein
A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Proteins modified in this way are less active or functional. This gene encodes an enzyme which catalyzes the phosphorylation of psicosamines and ribulosamines compared to the neighboring gene which encodes a highly similar enzyme, fructosamine-3-kinase, which has different substrate specificity. The activity of both enzymes may result in deglycation of proteins to restore their function. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2012] (from NCBI)
Top mentioned proteins: FN3K, CAN, fibrillin-1, FACT, Protein-Tyrosine-Phosphatase
Papers on FN3KRP
Genetic Variations in MicroRNA-Binding Sites Affect MicroRNA-Mediated Regulation of Several Genes Associated With Cardio-metabolic Phenotypes.
Dehghan et al., Rotterdam, Netherlands. In Circ Cardiovasc Genet, Jun 2015
These cotransfection experiments showed that rs174545 (FADS1:miR-181a-2), rs1059611 (LPL:miR-136), rs13702 (LPL:miR-410), rs1046875 (FN3KRP:miR-34a), rs7956 (MKRN2:miR-154), rs3217992 (CDKN2B:miR-138-2-3p), and rs11735092 (HSD17B13:miR-375) decrease or abrogate miRNA-dependent regulation of the genes.
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes.
Henle et al., In Clin Chem Lab Med, 2014
BACKGROUND: An impact on glycation, and possibly on diabetic complications, is attributed to fructosamine-3-kinase (FN3K) and its related protein (FN3K-RP) because they degrade Amadori compounds in vivo.
Mapping eQTLs in the Norfolk Island genetic isolate identifies candidate genes for CVD risk traits.
Griffiths et al., Griffith, Australia. In Am J Hum Genet, 2014
In addition, we implicated several genes previously associated with CVD risk traits, including MTHFR and FN3KRP.
Enzymatic repair of Amadori products.
Veiga-da-Cunha et al., Brussels, Belgium. In Amino Acids, 2012
Mammals and birds also have an enzyme designated 'FN3K-related protein' (FN3KRP), which shares ≈ 65% sequence identity with FN3K.
The physiological substrates of fructosamine-3-kinase-related-protein (FN3KRP) are intermediates of nonenzymatic reactions between biological amines and ketose sugars (fructation products).
Loomes et al., United States. In Med Hypotheses, 2011
In contrast with FN3K, very little is known about the function of the fructosamine-3-kinase-related-protein (FN3KRP) even though it has a 65% amino-acid sequence identity with FN3K.
Purification and identification of activating enzymes of CS-0777, a selective sphingosine 1-phosphate receptor 1 modulator, in erythrocytes.
Nara et al., Tokyo, Japan. In J Biol Chem, 2011
We purified CS-0777 kinase activity from human RBCs by more than 10,000-fold using ammonium sulfate precipitation and successive chromatography steps, and we identified fructosamine 3-kinase (FN3K) and fructosamine 3-kinase-related protein (FN3K-RP) by mass spectrometry.
Mapping of the ATP-binding domain of human fructosamine 3-kinase-related protein by affinity labelling with 5'-[p-(fluorosulfonyl)benzoyl]adenosine.
Loomes et al., Auckland, New Zealand. In Biochem J, 2009
Studies provide evidence that Fn3KRP possesses an ATP-binding domain that is structurally related to that of both the aminoglycoside kinases and eukaryotic protein kinases.
Fructosamine-3-kinase-related-protein phosphorylates glucitolamines on the C-4 hydroxyl: novel substrate specificity of an enigmatic enzyme.
Loomes et al., United States. In Biochem Biophys Res Commun, 2007
FN3KRP phosphorylates meglumine to produce meglumine-4-phosphate.
Many fructosamine 3-kinase homologues in bacteria are ribulosamine/erythrulosamine 3-kinases potentially involved in protein deglycation.
Van Schaftingen et al., Brussels, Belgium. In Febs J, 2007
They also phosphorylated protein-bound ribulosamines or erythrulosamines, but not protein-bound fructosamines, therefore having properties similar to those of mammalian FN3K-related protein.
Identification of protein-ribulosamine-5-phosphatase as human low-molecular-mass protein tyrosine phosphatase-A.
Van Schaftingen et al., Brussels, Belgium. In Biochem J, 2007
Ribulosamines, which are substrates for the deglycating enzyme fructosamine-3-kinase-related protein, are presumably formed intracellularly through glycation of proteins with ribose 5-phosphate followed by dephosphorylation of resulting RN5Ps (ribulosamine 5-phosphates) by a putative RN5Pase (ribulosamine-5-phosphatase).
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).
Szwergold, United States. In Med Hypotheses, 2006
In this paper we propose a resolution of both these quandaries by proposing that fructosamine-6-phosphates are deglycated by phosphorylation to fructosamine-3,6-bisphosphates catalyzed by FN3KRP and/or possibly FN3K.
Plant ribulosamine/erythrulosamine 3-kinase, a putative protein-repair enzyme.
van Schaftingen et al., Brussels, Belgium. In Biochem J, 2005
The homologous mammalian enzyme, FN3K-RP (FN3K-related protein), does not phosphorylate fructosamines but ribulosamines, which are probably formed through a spontaneous reaction of amines with ribose 5-phosphate, an intermediate of the pentose-phosphate pathway and the Calvin cycle.
Some clues as to the regulation, expression, function, and distribution of fructosamine-3-kinase and fructosamine-3-kinase-related protein.
Szwergold et al., United States. In Ann N Y Acad Sci, 2005
Enzyme is a constitutive "housekeeping" gene and that ig plays an important role in cell metabolism, possibly as a deglycating enzyme.
Transglycation--a potential new mechanism for deglycation of Schiff's bases.
Beisswenger et al., United States. In Ann N Y Acad Sci, 2005
Over the past several years we and others have shown that in cells this nonenzymatic process can be reversed by an ATP-dependent reaction catalyzed by fructosamine-3-kinase (FN3K) and possibly by its isozyme, fructosamine-3-kinase-related protein (FN3KRP).
The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinase-related protein appears to be constitutive and unaffected by environmental signals.
Szwergold et al., United States. In Biochem Biophys Res Commun, 2004
These data suggest that FN3K and FN3KRP act as protein repair enzymes and are expressed constitutively in human cells independently of some of the variables altered in the diabetic state.
Enzymatic deglycation--a new paradigm or an epiphenomenon?
Beisswenger et al., United States. In Biochem Soc Trans, 2003
Following the discovery of FN3K (fructosamine 3-kinase), and more recently of FN3KRP (FN3K-related protein), research in our laboratory has been focused on testing the enzymatic deglycation hypothesis and investigating the roles of FN3K and FN3KRP.
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