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Information on EC 2.7.1.171 - protein-fructosamine 3-kinase
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2.7.1.171 protein-fructosamine 3-kinaseIUBMB Comments
Non-enzymic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as [protein]-N6-D-fructosyl-L-lysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from non-enzymically glycated proteins. The phosphorylation destablilizes the [protein]-N6-D-fructosyl-L-lysine adduct and leads to its spontaneous decomposition. cf. EC 2.7.1.172, protein-ribulosamine 3-kinase.
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Word Map
- 2.7.1.171
-
deglycation
- erythrocyte
- fructoselysine
-
protein-bound
-
non-enzymatic
-
fn3k-related
- fn3krp
-
amadori
- 5-phosphate
- dmf
- haemoglobin
-
maillard
-
glycemia
-
protein-repairing
-
3-kinase-related
- 3-deoxyglucosone
- analysis
- medicine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
FL3P, FN3K, fructosamine 3 kinase, fructosamine 3-kinase, fructosamine-3-kinase, fructose-3-kinase, ketosamine 3-kinase 1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FN3K
fructosamine 3-kinase
fructosamine-3-kinase
fructose-3-kinase
ketosamine 3-kinase 1
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
phosphorylation destablilizes the fructoselysine adduct and leads to its spontaneous decomposition
-
ATP + [protein]-N6-D-fructosyl-L-lysine = ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
ATP:[protein]-N6-D-fructosyl-L-lysine 3-phosphotransferase
Non-enzymic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as [protein]-N6-D-fructosyl-L-lysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from non-enzymically glycated proteins. The phosphorylation destablilizes the [protein]-N6-D-fructosyl-L-lysine adduct and leads to its spontaneous decomposition. cf. EC 2.7.1.172, protein-ribulosamine 3-kinase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
ATP + 1-deoxy-1-morpholin-4-yl-D-psicose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-psicose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-ribulose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-ribulose
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
ATP + N2-(1-deoxy-D-fructosyl)-glycylglycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycylglycine
-
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-L-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-L-valine
-
-
-
-
?
ATP + N5-D-fructosyl-L-ornithine
ADP + N5-(O3-phosphono-D-fructosyl)-L-ornithine
-
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-L-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-fructosyl-L-lysine
ADP + N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + N6-D-psicosyl-L-lysine
ADP + N6-(O3-phosphono-D-psicosyl)-L-lysine
-
-
-
?
ATP + Nalpha-hippuryl-Nepsilon-(1-deoxy-D-fructosyl)lysine
ADP + Nalpha-hippuryl-Nepsilon-(1-deoxy-3-phospho-D-fructosyl)lysine
-
-
Nalpha-hippuryl-Nepsilon-(3-phosphofructosyl)lysine like other 3-phosphofructosylamines, is not stable. Terminating the enzyme reaction with trichloracetic acid stabilises the analyte
-
?
ATP + [hemoglobin]-N6-D-fructosyl-L-lysine
ADP + [hemoglobin]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
mass-spectrometric identification of the fructosamine residues that are removed from hemoglobin in intact erythrocytes as a result of the action of fructosamine-3-kinase: Lys16, Lys61 and Lys139 in the alpha-chain of hemoglobin, Val1, Lys17, Lys59, Lys66, Lys132, and Lys144 in the beta-chain of hemoglobin. Some (e.g. Lys139 in the alph-chain of hemoglobin) are readily phosphorylated to a maximal extent by fructosamine-3-kinase in vitro whereas others (e.g. Val1 in the beta-chain of hemoglobin) are slowly and only very partially phosphorylated
-
-
?
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
glycated bovine serum albumin + ATP
?
-
derived from dialyzed glycated bovine serum albumin
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + 1-deoxy-1-morpholin-4-yl-D-fructose
ADP + 1-deoxy-1-morpholin-4-yl-3-O-phosphono-D-fructose
-
-
-
-
?
ATP + D-fructose
ADP + O3-phosphono-D-fructose
-
Vmax is 35% of the value for N6-D-fructosyl-L-lysine
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
-
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-glycine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-glycine
-
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
-
-
-
-
?
ATP + N2-(1-deoxy-D-fructosyl)-valine
ADP + N2-(1-deoxy-O3-phosphono-D-fructosyl)-valine
-
-
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
-
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + N6-(1-deoxy-D-fructosyl)-lysine
ADP + N6-(1-deoxy-O3-phosphono-D-fructosyl)-lysine
-
displays about 10times less affinity than for 1-deoxy-1-morpholin-4-yl-D-fructose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Spontaneous conversion of fructosamine 3-phosphates into 3-deoxyglucosone
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as protein-bound fructoselysines. The fructosamine most frequently encountered in nature is fructoselysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins and protecting cells from the deleterious effects of nonenzymatic glycation
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
protein repair mechanism. Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates. The latter are unstable and spontaneously decompose into inorganic phosphate and 3-deoxyglucosone, with concomitant regeneration of the unglycated amine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
repairing glucose-mediated non-enzymatic modification of proteins. The function of fructosamine-3-kinase is seen in catalysing the ATP-dependent phosphorylation of the protein-bound fructosamine (Amadori compound) fructoselysine, which is the first stable intermediate resulting from the Maillard reaction between glucose and lysine, on its 3-hydroxy group to 3-phosphofructosyllysine. The phosphorylation destabilises the fructose-amine linkage leading to a spontaneous decomposition of 3-phosphofructosyllysine to the unmodified lysine residue as well as to 3-deoxyglucosulose and inorganic phosphate
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
[histone]-N6-D-fructosyl-L-lysine, [hemoglobin]-N6-D-fructosyl-L-lysine. Similar experiments with other glycated proteins, including bovine serum albumin, and lysozyme indicate that fructoselysine residues on glycated proteins are readily phosphorylated by fructosamine 3-kinase, apparently irrespective of the protein. Phosphorylation destablilizes the fructoselysine adduct and leads to its spontaneous decomposition
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone. This pathway appears to dominate 3-deoxyglucosone production in vivo, making it possible to modulate 3-deoxyglucosone levels by stimulating or inhibiting the reaction
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
additional information
?
-
FN3K-RP does not phosphorylate fructoselysine, 1-deoxy-1-morpholin-4-yl-D-fructose, or lysozyme glycated with glucose
-
-
-
additional information
?
-
-
the kinase is specific for 1-deoxy-1-amino fructose adducts and does not catalyze phosphorylation of other monosaccharides and polyols, such as glucose, galactose, mannose, glucosamine, galactosamine, or myo-inositol
-
-
-
additional information
?
-
development of a PLC-based assay with substrate N-alpha-hippuryl-N-epsilon-psicosyllysine for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes, method evaluation, overview
-
-
-
additional information
?
-
-
development of a simple colorimetric method for assaying FN3K activity in human body fluids
-
-
-
additional information
?
-
-
the fructosamines bound to Lys139alpha, located near the C-terminus of the alpha subunits, and Lys16alpha, located on a loop of the alpha subunits, are good substrates. The N-terminal glycated valine is a poor substrate, consistent with free fructosevaline being a much poorer substrate than free fructoselysine
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + [protein]-N5-D-ribulosyl-L-lysine
ADP + [protein]-N5-(O3-phosphono-D-fructosyl)-L-lysine
Q9HA64
proteins glycated with allose, ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
ATP + [protein]-N6-D-psicosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-psicosyl)-L-lysine
Q9HA64
ketosamine-3-kinase 2 plays a role in freeing proteins from ribulosamines or psicosamines, which might arise in a several step process, from the reaction of amines with glucose and/or glycolytic intermediates. This role is shared by fructosamine-3-kinase (ketosamine-3-kinase 1), which has, in addition, the unique capacity to phosphorylate fructosamines
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
Q9H479
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(3-O-phospho-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
-
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
Q9H479
fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes. Spontaneous conversion of fructosamine 3-phosphates into 3-deoxyglucosone
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructosamine-3-kinase phosphorylates fructosamine residues, leading to their destabilization and their shedding from protein
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
nonenzymatic glycation is an important factor in the pathogenesis of diabetic complications. Key early intermediates in this process are fructosamines, such as protein-bound fructoselysines. The fructosamine most frequently encountered in nature is fructoselysine. Fructosamine-3-kinase is part of an ATP-dependent system for removing carbohydrates from nonenzymatically glycated proteins and protecting cells from the deleterious effects of nonenzymatic glycation
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
Q9H479
protein repair mechanism. Fructosamine 3-kinase phosphorylates with high affinity both low-molecular-mass and protein-bound fructosamines on the third carbon of their deoxyfructose moiety, leading to the formation of fructosamine 3-phosphates. The latter are unstable and spontaneously decompose into inorganic phosphate and 3-deoxyglucosone, with concomitant regeneration of the unglycated amine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
repairing glucose-mediated non-enzymatic modification of proteins. The function of fructosamine-3-kinase is seen in catalysing the ATP-dependent phosphorylation of the protein-bound fructosamine (Amadori compound) fructoselysine, which is the first stable intermediate resulting from the Maillard reaction between glucose and lysine, on its 3-hydroxy group to 3-phosphofructosyllysine. The phosphorylation destabilises the fructose-amine linkage leading to a spontaneous decomposition of 3-phosphofructosyllysine to the unmodified lysine residue as well as to 3-deoxyglucosulose and inorganic phosphate
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
fructoselysine 3-phosphate spontaneously decomposes to lysine, phosphate and 3-deoxyglucosone. This pathway appears to dominate 3-deoxyglucosone production in vivo, making it possible to modulate 3-deoxyglucosone levels by stimulating or inhibiting the reaction
-
-
?
ATP + [protein]-N6-D-fructosyl-L-lysine
ADP + [protein]-N6-(O3-phosphono-D-fructosyl)-L-lysine
-
specific role of fructosamine 3-kinase to repair protein damage caused by glucose
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-deoxy-1-morpholinofructose
-
substrate and competitive inhibitor of fructosamine 3-kinase, doubles the rate of accumulation of glycated haemoglobin, but markedly decreases the amount of haemoglobin containing alkali-labile phosphate
3-O-methylsorbitol-lysine
-
inhibitors based on sorbitol show competitive inhibition of the fructoseamine-3-kinase reaction but also prevent the formation of 3-deoxyglucosone, because there is no spontaneous decomposition of the product to 3-deoxyglucosone. For compounds blocked at C3, also there is no product formed. The Ki values of these compounds are approx. 0.5 mM. Although high for an in vivo drug, their apparent low toxicity make it possible to use them, at least in animals, to lower 3-deoxyglucosone levels
additional information
-
neither transferrin saturation nor ferritin are confounders for the FN3K activity
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
FN3K activity is significantly correlated with HbA1c values, although the correlation between FN3K and HbA1c is weak
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Autoimmune Diseases
Enzymatic kinetics regarding reversible metabolism of CS-0777, a sphingosine 1-phosphate receptor modulator, via phosphorylation and dephosphorylation in humans.
Colorectal Neoplasms
Gene expression of fructosamine 3 kinase in patients with colorectal cancer.
Colorectal Neoplasms
Reduced fructosamine-3-kinase activity and its mRNA in human distal colorectal carcinoma.
Diabetes Complications
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes.
Diabetes Mellitus
A Polymorphism within the Fructosamine-3-kinase Gene is Associated with HbA1c Levels and the Onset of Type 2 Diabetes Mellitus.
Diabetes Mellitus, Type 2
A Polymorphism within the Fructosamine-3-kinase Gene is Associated with HbA1c Levels and the Onset of Type 2 Diabetes Mellitus.
Diabetic Nephropathies
Genetic variability in enzymes of metabolic pathways conferring protection against non-enzymatic glycation versus diabetes-related morbidity and mortality.
Neoplasms
Identification of a gene-expression signature for predicting lymph node metastasis in patients with early stage cervical carcinoma.
protein-fructosamine 3-kinase deficiency
Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
1-deoxy-1-morpholin-4-yl-D-fructose
-
pH 7.8, 30°C, erythrocyte enzyme; pH 7.8, 30°C, recombinant enzyme
0.1
1-deoxy-1-morpholin-4-yl-D-fructose
-
37°C, pH not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
3-O-methylsorbitol-lysine
-
inhibitors based on sorbitol show competitive inhibition of the fructoseamine-3-kinase reaction but also prevent the formation of 3-deoxyglucosone, because there is no spontaneous decomposition of the product to 3-deoxyglucosone. For compounds blocked at C3, also there is no product formed. The Ki values of these compounds are approx. 0.5 mM. Although high for an in vivo drug, their apparent low toxicity make it possible to use them, at least in animals, to lower 3-deoxyglucosone levels
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.69
1-deoxy-1-morpholin-4-yl-D-psicose
Homo sapiens
Q9HA64
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.0036
1-deoxy-1-morpholin-4-yl-D-ribulose
Homo sapiens
Q9HA64
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
0.72
N6-D-psicosyl-L-lysine
Homo sapiens
Q9HA64
pH 7.8, 30°C, phosphorylation of lysozyme glycated with allose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.8
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the mean level of FN3K gene expression is significantly lower in cancer than in the corresponding normal colorectal mucosa. No difference between cancer versus normal mucosa is detected in mRNA FN3K levels stratifying for age, sex, tumour stage and histological grading
-
-
brenda
Sprague–Dawley or Fisher 344. Rats carrying the Tsc2 gene (Eker rats) in a Fisher 344 background
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
highest levels of expression in bone marrow, brain, spleen and kidney
brenda
-
fructosamine-3-kinase is a functionally active enzyme in human colon tissue, without significant differences between normal mucosa and cancer. The mean level of fructosamine-3-kinase mRNA is significantly lower in cancer than in the corresponding normal colorectal mucosa. The colorectal tumors located on the left side show lower levels of both enzymatic activity and mRNA fructosamine-3-kinase than tumors located in the right side of colon
brenda
-
cultured fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state show no changes in fructosamine-3-kinase expression relative to untreated cells. FN3K acts as protein repair enzyme and is expressed constitutively in human cells independently of some of the variables altered in the diabetic state
brenda
-
highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons
brenda
highest levels of expression in bone marrow, brain, spleen and kidney
brenda
additional information
highest levels of expression in bone marrow, brain, spleen and kidney
brenda
-
the human erythrocyte FN3K activity, which is stable with time in a single individual, is highly variable from person to person. This variability, which is linked to single nucleotide polymorphisms that are present in the FN3K gene, affects the glycation level of at least one specific site in haemoglobin
brenda
-
the mean erythrocyte FN3K activity does not differ between normoglycaemic subjects and type 1 diabetic patients, but there is a wide interindividual variability in both groups (from about 1 to 4 mU/g haemoglobin). This variability is stable with time and associated with two single nucleotide polymorphisms in the promoter region and exon 6 of the FN3K gene. There is no significant correlation between FN3K activity and the levels of HbA1c, total glycated haemoglobin and haemoglobin fructoselysine residues, either in the normoglycaemic or diabetic group. The glycation level of Lys144 (in beta-chain of hemoglobin) is about twice as high in normoglycaemic subjects with the lowest FN3K activities as compared to those with the highest FN3K activities
brenda
-
highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons
brenda
-
the enzyme is present in all tissues, with the highest level of expression in the kidney
brenda
highest levels of expression in bone marrow, brain, spleen and kidney
brenda
additional information
-
FN3K is more active in tissues containing proteins with long (half-)lives, such as erythrocytes, lens and brain
brenda
additional information
-
enzyme FN3K activity is neither age- nor sex-dependent. The various FN3K SNP rs1056534 genotypes show no significant differences in serum FN3K activity. In diabetics, enzyme activity values are comparable to those of the controls. FN3K activity in erythrocytes is significantly higher
brenda
additional information
no expression is observed in the intestinal mucosa
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the FN3K gene may have arisen by an event of duplication of an ancestral gene, FN3K-related protein (FN3K-RP). The gene encoding FN3K-RP is located next to the one encoding FN3K, and share a 65% sequence homology with FN3K and an identical genome organization. Both FN3K and FN3K-RP phosphorylate psicosamines and ribulosamines, but only the former act on fructosamines
malfunction
metabolism
physiological function
additional information
-
no correlations of enzyme activity with age, sex, body weight, blood cholesterol, or plasma glucose in an oral glucose tolerance test are observed. Subjects whose parents or siblings had a stroke show lower FN3K activity
malfunction
-
mice deficient in FN3K accumulate protein-bound fructosamines and free fructoselysine, indicating that the deglycation mechanism initiated by FN3K is operative in vivo
malfunction
-
Fn3k-/- mice look healthy and have normal blood glucose and serum fructosamine levels. Their level of haemoglobin-bound fructosamines is approx. 2.5-fold higher than that of control (Fn3k+/+) or Fn3k+/- mice. Other intracellular proteins are also significantly more glycated in Fn3k-/- mice in erythrocytes and in brain, kidney, liver and skeletal muscle, indicating that FN3K removes fructosamines from intracellular proteins in vivo
malfunction
-
significant relationship of FN3K (rs1056534) and (rs3848403) polymorphisms with with endothelial dysfunction and concentration of soluble receptor for advanced glycation end-products (sRAGE) in patients with diabetes, clinical parameters, overview
metabolism
-
despite its ability to reduce the glycation of intracellular islet proteins, fructosamine-3-kinase is neither required for the maintenance of beta-cell survival and function under control conditions nor involved in protection against beta-cell glucotoxicity
metabolism
-
starvation and diabetes do not change the level of expression of FN3K in different tissues, and no regulation of FN3K expression is observed in human fibroblasts treated with condition mimicking the diabetic state
physiological function
-
FN3K serves as a protein repair enzyme and also in the metabolism of endogenously produced free fructose-epsilon-lysine. Repairing lysine residues may be important to restore enzymatic activity, protein–protein interaction or recognition sites for phosphorylation (which often comprise basic residues) or ubiquitinylation
physiological function
-
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
physiological function
-
the physiological function of fructosamine-3-kinase may be to initiate a process leading to the deglycation of fructoselysine and of glycated proteins
physiological function
-
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. Individual differences in FN3K-RP activity might contribute to an individual risk for diabetic complications
physiological function
-
fructosamine 3-kinase (FN3K) is involved in protein deglycation FN3K phosphorylates fructosamines on the third carbon of their sugar moiety, making them unstable and causing them to detach from proteins, suggesting a protective role of this enzyme. FN3K is able to break down the second intermediate of the non-enzymatic glycation cascade by phosphorylating fructoselysine to a fructoselysine-3-phosphate. The variability in FN3K activity is associated with some polymorphisms in the FN3K gene, FN3K involvement in diabetes, overview. FN3K might act in concert with other molecular mechanisms and may impact on gene expression and activity of other enzymes involved in deglycation process
physiological function
-
fructosamine 3 kinase is a deglycating enzyme, which may play a key role in reducing diabetes-induced organ damage by removing bound glucose from glycated proteins
physiological function
-
advanced glycation end-products are key players in pathogenesis of long-term vascular diabetes complications, several enzymes such as fructosamine 3-kinase (FN3K) and glyoxalase I (GLO I) are crucial in preventing glycation processes
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
35032
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 35000, SDS-PAGE; x * 35032, calculated from sequence; x * 35171, calculated from sequence
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
diabetic subjects with the CC variant of SNP rs1056534 (G900C), which is associated with a higher FN3K activity, have lower HbA1c levels compared with other genotypes
additional information
-
the G900C (rs1056534) single nucleotide polymorphism of the FN3K gene is associated with the enzyme activity, with the level of HbA and the onset of the disease, but not with either of the diabetic microvascular complications
additional information
-
analysis of the FN3K gene on a Caucasian cohort of diabetic patients, molecular characterization of the FN3K gene by analyzing its promoter and of polymorphisms, c-385A/G (rs3859206) and the c-232A/T (rs2256339), associated with FN3K enzymatic activity in erythrocytes, as well as two variants c-421C/T and c-429delATCGGAG
additional information
-
while GG and CG genotypes of rs1056534 with mutated G allele are associated with significant decrease of sRAGE, in rs3848403 polymorphism TT genotype with mutated T allele is related with significant sRAGE increase
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
partial
recombinant enzyme, partially purified by chromatography on Blue Sepharose
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
genotyping of FN3K SNP rs1056534 and the ferroportin SNP rs1156350. FN3K activity depends on the ferroportin Q248H genotypes, with the highest value for the wild-type genotype
-
human FN3K-RP is transfected in human embryonic kidney cells and expressed
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
highest levels of FN3K expression are found in tissues known to be susceptible to glycation and diabetic complications such as kidney and neurons. Cultured fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state show no changes in fructosamine-3-kinase expression relative to untreated cells. FN3K acts as protein repair enzyme and is expressed constitutively in human cells independently of some of the variables altered in the diabetic state
-
mildly glycated casein in a standard diet stimulates 3-deoxyglucosone levels 10–20fold in the plasma and approximately 3fold in the kidney compared with a control diet containing identical constituents
-
no regulation of the expression of fructose-3-kinase is observed in human fibroblasts treated with conditions mimicking the hormonal and biochemical profile of the diabetic state
-
rats are starved for 2 days or rendered diabetic with streptozotocin and analyzed 5 days later. No detectable change in the activity of fructosamine 3-kinase is observed in liver, heart, kidney, and brain
-
the down-regulation of FN3K gene expression in cancer tissue compared with normal mucosa is a characteristic only of the left-sided tumours of the colon
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
convenient assay for the determination of FN3K activity in erythrocytes, which can be performed in routine laboratories
medicine
-
inhibition of fructoseamine-3-kinase is a promising new therapeutic target for diabetic complications, as well as other 3-deoxyglucosone-dependent pathologies
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pascal, S.M.; Veiga-da-Cunha, M.; Gilon, P.; van Schaftingen, E.; Jonas, J.C.
Effects of fructosamine-3-kinase deficiency on function and survival of mouse pancreatic islets after prolonged culture in high glucose or ribose concentrations
Am. J. Physiol. Endocrinol. Metab.
298
E586-596
2009
Mus musculus, Mus musculus (Q9ER35)
brenda
van Schaftingen, E.; Collard, F.; Wiame, E.; Veiga-da-Cunha, M.
Enzymatic repair of Amadori products
Amino Acids
42
1143-1150
2012
Homo sapiens, Mus musculus
brenda
Krause, R.; Oehme, A.; Wolf, K.; Henle, T.
A convenient HPLC assay for the determination of fructosamine-3-kinase activity in erythrocytes
Anal. Bioanal. Chem.
386
2019-2025
2006
Homo sapiens
brenda
Conner, J.R.; Beisswenger, P.J.; Szwergold, B.S.
The expression of the genes for fructosamine-3-kinase and fructosamine-3-kinase-related protein appears to be constitutive and unaffected by environmental signals
Biochem. Biophys. Res. Commun.
323
932-936
2004
Homo sapiens
brenda
Delpierre, G.; Collard, F.; Fortpied, J.; van Schaftingen, E.
Fructosamine 3-kinase is involved in an intracellular deglycation pathway in human erythrocytes
Biochem. J.
365
801-808
2002
Homo sapiens, Homo sapiens (Q9H479)
brenda
Veiga da-Cunha, M.; Jacquemin, P.; Delpierre, G.; Godfraind, C.; Theate, I.; Vertommen, D.; Clotman, F.; Lemaigre, F.; Devuyst, O.; van Schaftingen, E.
Increased protein glycation in fructosamine 3-kinase-deficient mice
Biochem. J.
399
257-264
2006
Mus musculus (Q9ER35)
brenda
Brown, T.R.; Su, B.; Brown, K.A.; Schwartz, M.A.; Tobia, A.M.; Kappler, F.
Modulation of in vivo 3-deoxyglucosone levels
Biochem. Soc. Trans.
31
1433-1437
2003
Rattus norvegicus
brenda
Delpierre, G.; Veiga-da-Cunha, M.; Vertommen, D.; Buysschaert, M.;, Van Schaftingen E.
Variability in erythrocyte fructosamine 3-kinase activity in humans correlates with polymorphisms in the FN3K gene and impacts on haemoglobin glycation at specific sites
Diabetes Metab.
32
31-39
2005
Homo sapiens, Homo sapiens (Q9H479)
brenda
Delpierre, G.; Rider, M.H.; Collard, F.; Stroobant, V.; Vanstapel, F.; Santos, H.; van Schaftingen, E.
Identification, cloning, and heterologous expression of a mammalian fructosamine-3-kinase
Diabetes
49
1627-1634
2000
Homo sapiens, Homo sapiens (Q9H479), Mus musculus, Mus musculus (Q9ER35)
brenda
Szwergold, B.S.; Howell, S.; Beisswenger, P.J.
Human fructosamine-3-kinase: purification, sequencing, substrate specificity, and evidence of activity in vivo
Diabetes
50
2139-2147
2001
Homo sapiens
brenda
Collard, F.; Delpierre, G.; Stroobant, V.; Matthijs, G.; van Schaftingen, E.
A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-kinase acting on psicosamines and ribulosamines but not on fructosamines
Diabetes
52
2888-2895
2004
Homo sapiens, Homo sapiens (Q9HA64), Mus musculus, Mus musculus (Q8K274)
brenda
Mohas, M.; Kisfali, P.; Baricza, E.; Merei, A.; Maasz, A.; Cseh, J.; Mikolas, E.; Szijarto, I.A.; Melegh, B.; Wittmann, I.
A polymorphism within the fructosamine-3-kinase gene is associated with HbA1c levels and the onset of type 2 diabetes mellitus
Exp. Clin. Endocrinol. Diabetes
118
209-212
2009
Homo sapiens, Homo sapiens (Q9H479)
brenda
Notarnicola, M.; Caruso, M.G.; Tutino, V.; Guerra, V.; Frisullo, S.; Altomare, D.F.; Misciagna, G.
Reduced fructosamine-3-kinase activity and its mRNA in human distal colorectal carcinoma
Genes Nutr.
5
257-262
2010
Homo sapiens
brenda
Delpierrre, G.; Vertommen. D.; Communi, D.; Rider, M.H.; van Schaftingen, E.
Identification of fructosamine residues deglycated by fructosamine-3-kinase in human hemoglobin
J. Biol. Chem.
279
27613-27620
2004
Homo sapiens
brenda
Delplanque, J.; Delpierre, G.; Opperdoes, F.R.; van Schaftingen, E.
Tissue distribution and evolution of fructosamine 3-kinase and fructosamine 3-kinase-related protein
J. Biol. Chem.
279
46606-46613
2004
Gallus gallus, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Caruso, M.G.; Notarnicola, M.; Altomare, D.F.; Misciagna, G.
Gene expression of fructosamine 3 kinase in patients with colorectal cancer
Oncology
73
72-75
2008
Homo sapiens
brenda
Hellwig, A.; Scherber, A.; Koehler, C.; Hanefeld, M.; Henle, T.
A new HPLC-based assay for the measurement of fructosamine-3-kinase (FN3K) and FN3K-related protein activity in human erythrocytes
Clin. Chem. Lab. Med.
52
93-101
2014
Homo sapiens (Q9H479)
-
brenda
Avemaria, F.; Carrera, P.; Lapolla, A.; Sartore, G.; Chilelli, N.C.; Paleari, R.; Ambrosi, A.; Ferrari, M.; Mosca, A.
Possible role of fructosamine 3-kinase genotyping for the management of diabetic patients
Clin. Chem. Lab. Med.
53
1315-1320
2015
Homo sapiens, Homo sapiens (Q9H479)
brenda
Cikomola, J.C.; Kishabongo, A.S.; Vandepoele, K.; Mulder, M.; Katchunga, P.B.; Laukens, B.; Schie, L.V.; Grootaert, H.; Callewaert, N.; Speeckaert, M.M.; Delanghe, J.R.
A simple colorimetric assay for measuring fructosamine 3 kinase activity
Clin. Chem. Lab. Med.
55
154-159
2017
Homo sapiens, Homo sapiens (Q9H479)
brenda
Skrha, J.; Muravska, A.; Flekac, M.; Horova, E.; Novak, J.; Novotny, A.; Prazny, M.; Skrha, J.; Kvasnicka, J.; Landova, L.; Jachymova, M.; Zima, T.; Kalousova, M.
Fructosamine 3-kinase and glyoxalase I polymorphisms and their association with soluble RAGE and adhesion molecules in diabetes
Physiol. Res.
63 Suppl 2
S283-S291
2014
Homo sapiens, Homo sapiens (Q9H479)
brenda
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