Full text data of FN3K
FN3K
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Fructosamine-3-kinase; 2.7.1.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Fructosamine-3-kinase; 2.7.1.-
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H479
ID FN3K_HUMAN Reviewed; 309 AA.
AC Q9H479;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Fructosamine-3-kinase;
DE EC=2.7.1.-;
GN Name=FN3K;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT
RP MET-1, AND CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=11016445; DOI=10.2337/diabetes.49.10.1627;
RA Delpierre G., Rider M.H., Collard F., Stroobant V., Vanstapel F.,
RA Santos H., Van Schaftingen E.;
RT "Identification, cloning, and heterologous expression of a mammalian
RT fructosamine-3-kinase.";
RL Diabetes 49:1627-1634(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May initiate a process leading to the deglycation of
CC fructoselysine and of glycated proteins. May play a role in the
CC phosphorylation of 1-deoxy-1-morpholinofructose (DMF),
CC fructoselysine, fructoseglycine, fructose and glycated lysozyme.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ404615; CAC16393.1; -; mRNA.
DR EMBL; BC042680; AAH42680.1; -; mRNA.
DR RefSeq; NP_071441.1; NM_022158.3.
DR UniGene; Hs.151135; -.
DR ProteinModelPortal; Q9H479; -.
DR SMR; Q9H479; 38-309.
DR STRING; 9606.ENSP00000300784; -.
DR DMDM; 13959371; -.
DR PaxDb; Q9H479; -.
DR PRIDE; Q9H479; -.
DR DNASU; 64122; -.
DR Ensembl; ENST00000300784; ENSP00000300784; ENSG00000167363.
DR GeneID; 64122; -.
DR KEGG; hsa:64122; -.
DR UCSC; uc010wvs.1; human.
DR CTD; 64122; -.
DR GeneCards; GC17P080693; -.
DR HGNC; HGNC:24822; FN3K.
DR MIM; 608425; gene.
DR neXtProt; NX_Q9H479; -.
DR PharmGKB; PA134870460; -.
DR eggNOG; COG3001; -.
DR HOGENOM; HOG000023913; -.
DR HOVERGEN; HBG005740; -.
DR InParanoid; Q9H479; -.
DR KO; K15522; -.
DR OMA; YIPQVNE; -.
DR OrthoDB; EOG7MH0ZF; -.
DR PhylomeDB; Q9H479; -.
DR BioCyc; MetaCyc:ENSG00000167363-MONOMER; -.
DR GeneWiki; FN3K; -.
DR GeneWiki; Fructosamine-3-kinase; -.
DR GenomeRNAi; 64122; -.
DR NextBio; 66000; -.
DR PRO; PR:Q9H479; -.
DR Bgee; Q9H479; -.
DR CleanEx; HS_FN3K; -.
DR Genevestigator; Q9H479; -.
DR GO; GO:0030387; F:fructosamine-3-kinase activity; NAS:UniProtKB.
DR GO; GO:0030393; P:fructoselysine metabolic process; NAS:UniProtKB.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing; Kinase;
KW Reference proteome; Transferase.
FT CHAIN 1 309 Fructosamine-3-kinase.
FT /FTId=PRO_0000216337.
FT MOD_RES 1 1 N-acetylmethionine.
SQ SEQUENCE 309 AA; 35171 MW; BA886A86655DE28F CRC64;
MEQLLRAELR TATLRAFGGP GAGCISEGRA YDTDAGPVFV KVNRRTQARQ MFEGEVASLE
ALRSTGLVRV PRPMKVIDLP GGGAAFVMEH LKMKSLSSQA SKLGEQMADL HLYNQKLREK
LKEEENTVGR RGEGAEPQYV DKFGFHTVTC CGFIPQVNEW QDDWPTFFAR HRLQAQLDLI
EKDYADREAR ELWSRLQVKI PDLFCGLEIV PALLHGDLWS GNVAEDDVGP IIYDPASFYG
HSEFELAIAL MFGGFPRSFF TAYHRKIPKA PGFDQRLLLY QLFNYLNHWN HFGREYRSPS
LGTMRRLLK
//
ID FN3K_HUMAN Reviewed; 309 AA.
AC Q9H479;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Fructosamine-3-kinase;
DE EC=2.7.1.-;
GN Name=FN3K;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT
RP MET-1, AND CHARACTERIZATION.
RC TISSUE=Kidney;
RX PubMed=11016445; DOI=10.2337/diabetes.49.10.1627;
RA Delpierre G., Rider M.H., Collard F., Stroobant V., Vanstapel F.,
RA Santos H., Van Schaftingen E.;
RT "Identification, cloning, and heterologous expression of a mammalian
RT fructosamine-3-kinase.";
RL Diabetes 49:1627-1634(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May initiate a process leading to the deglycation of
CC fructoselysine and of glycated proteins. May play a role in the
CC phosphorylation of 1-deoxy-1-morpholinofructose (DMF),
CC fructoselysine, fructoseglycine, fructose and glycated lysozyme.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AJ404615; CAC16393.1; -; mRNA.
DR EMBL; BC042680; AAH42680.1; -; mRNA.
DR RefSeq; NP_071441.1; NM_022158.3.
DR UniGene; Hs.151135; -.
DR ProteinModelPortal; Q9H479; -.
DR SMR; Q9H479; 38-309.
DR STRING; 9606.ENSP00000300784; -.
DR DMDM; 13959371; -.
DR PaxDb; Q9H479; -.
DR PRIDE; Q9H479; -.
DR DNASU; 64122; -.
DR Ensembl; ENST00000300784; ENSP00000300784; ENSG00000167363.
DR GeneID; 64122; -.
DR KEGG; hsa:64122; -.
DR UCSC; uc010wvs.1; human.
DR CTD; 64122; -.
DR GeneCards; GC17P080693; -.
DR HGNC; HGNC:24822; FN3K.
DR MIM; 608425; gene.
DR neXtProt; NX_Q9H479; -.
DR PharmGKB; PA134870460; -.
DR eggNOG; COG3001; -.
DR HOGENOM; HOG000023913; -.
DR HOVERGEN; HBG005740; -.
DR InParanoid; Q9H479; -.
DR KO; K15522; -.
DR OMA; YIPQVNE; -.
DR OrthoDB; EOG7MH0ZF; -.
DR PhylomeDB; Q9H479; -.
DR BioCyc; MetaCyc:ENSG00000167363-MONOMER; -.
DR GeneWiki; FN3K; -.
DR GeneWiki; Fructosamine-3-kinase; -.
DR GenomeRNAi; 64122; -.
DR NextBio; 66000; -.
DR PRO; PR:Q9H479; -.
DR Bgee; Q9H479; -.
DR CleanEx; HS_FN3K; -.
DR Genevestigator; Q9H479; -.
DR GO; GO:0030387; F:fructosamine-3-kinase activity; NAS:UniProtKB.
DR GO; GO:0030393; P:fructoselysine metabolic process; NAS:UniProtKB.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom.
DR Pfam; PF03881; Fructosamin_kin; 1.
DR PIRSF; PIRSF006221; Ketosamine-3-kinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing; Kinase;
KW Reference proteome; Transferase.
FT CHAIN 1 309 Fructosamine-3-kinase.
FT /FTId=PRO_0000216337.
FT MOD_RES 1 1 N-acetylmethionine.
SQ SEQUENCE 309 AA; 35171 MW; BA886A86655DE28F CRC64;
MEQLLRAELR TATLRAFGGP GAGCISEGRA YDTDAGPVFV KVNRRTQARQ MFEGEVASLE
ALRSTGLVRV PRPMKVIDLP GGGAAFVMEH LKMKSLSSQA SKLGEQMADL HLYNQKLREK
LKEEENTVGR RGEGAEPQYV DKFGFHTVTC CGFIPQVNEW QDDWPTFFAR HRLQAQLDLI
EKDYADREAR ELWSRLQVKI PDLFCGLEIV PALLHGDLWS GNVAEDDVGP IIYDPASFYG
HSEFELAIAL MFGGFPRSFF TAYHRKIPKA PGFDQRLLLY QLFNYLNHWN HFGREYRSPS
LGTMRRLLK
//
MIM
608425
*RECORD*
*FIELD* NO
608425
*FIELD* TI
*608425 FRUCTOSAMINE 3-KINASE
;;FN3K
*FIELD* TX
DESCRIPTION
FN3K catalyzes phosphorylation of fructosamines formed by glycation, the
read morenonenzymatic 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).
CLONING
Delpierre et al. (2000) purified FN3K from erythrocyte extracts. By
partial sequencing of tryptic peptides, followed by examination of an
EST database and PCR amplification, they cloned FN3K from a kidney cDNA
library. They cloned mouse Fn3k from a brain cDNA library. Both
predicted proteins contain 309 amino acids and have calculated molecular
masses of 35 kD. Human and mouse FN3K share 86% amino acid identity.
Purified FN3K showed an apparent molecular mass of 35 kD by SDS-PAGE.
Using RT-PCR, Conner et al. (2004) detected variable FN3K expression in
all human tissues examined, with highest levels in brain, kidney, spinal
cord, and heart.
GENE FUNCTION
Delpierre et al. (2000) demonstrated that purified FN3K catalyzed
ATP-dependent phosphorylation of a synthetic fructosamine,
1-deoxy-1-morpholinofructose (DMF). Recombinant mouse and human FN3K,
expressed in E. coli, catalyzed phosphorylation of DMF, fructoselysine,
fructoseglycine, and fructose in order of decreasing affinity. They also
phosphorylated glycated lysozyme, but not unmodified lysozyme. In
addition to ATP, FN3K was able to utilize GTP, CTP, and UTP as phosphate
donors. Nuclear magnetic resonance analysis showed that the phosphate
was bound to the third carbon of the 1-deoxyfructose moiety.
GENE STRUCTURE
Collard et al. (2003) determined that the FN3K gene contains 6 exons.
Conner et al. (2004) found that the promoter region of the FN3K gene has
a high GC content, but no TATA or CAAT boxes. It also has 2 putative
NFKB (see 164011)-binding sites.
MAPPING
By genomic sequence analysis and FISH, Collard et al. (2003) mapped the
FN3K gene to chromosome 17q25. They identified 2 FN3K pseudogene
fragments on chromosome 22.
*FIELD* RF
1. 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, 2003.
2. 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.
3. 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.
*FIELD* CN
Patricia A. Hartz - updated: 12/17/2007
*FIELD* CD
Patricia A. Hartz: 1/23/2004
*FIELD* ED
mgross: 12/17/2007
terry: 12/17/2007
mgross: 1/23/2004
*RECORD*
*FIELD* NO
608425
*FIELD* TI
*608425 FRUCTOSAMINE 3-KINASE
;;FN3K
*FIELD* TX
DESCRIPTION
FN3K catalyzes phosphorylation of fructosamines formed by glycation, the
read morenonenzymatic 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).
CLONING
Delpierre et al. (2000) purified FN3K from erythrocyte extracts. By
partial sequencing of tryptic peptides, followed by examination of an
EST database and PCR amplification, they cloned FN3K from a kidney cDNA
library. They cloned mouse Fn3k from a brain cDNA library. Both
predicted proteins contain 309 amino acids and have calculated molecular
masses of 35 kD. Human and mouse FN3K share 86% amino acid identity.
Purified FN3K showed an apparent molecular mass of 35 kD by SDS-PAGE.
Using RT-PCR, Conner et al. (2004) detected variable FN3K expression in
all human tissues examined, with highest levels in brain, kidney, spinal
cord, and heart.
GENE FUNCTION
Delpierre et al. (2000) demonstrated that purified FN3K catalyzed
ATP-dependent phosphorylation of a synthetic fructosamine,
1-deoxy-1-morpholinofructose (DMF). Recombinant mouse and human FN3K,
expressed in E. coli, catalyzed phosphorylation of DMF, fructoselysine,
fructoseglycine, and fructose in order of decreasing affinity. They also
phosphorylated glycated lysozyme, but not unmodified lysozyme. In
addition to ATP, FN3K was able to utilize GTP, CTP, and UTP as phosphate
donors. Nuclear magnetic resonance analysis showed that the phosphate
was bound to the third carbon of the 1-deoxyfructose moiety.
GENE STRUCTURE
Collard et al. (2003) determined that the FN3K gene contains 6 exons.
Conner et al. (2004) found that the promoter region of the FN3K gene has
a high GC content, but no TATA or CAAT boxes. It also has 2 putative
NFKB (see 164011)-binding sites.
MAPPING
By genomic sequence analysis and FISH, Collard et al. (2003) mapped the
FN3K gene to chromosome 17q25. They identified 2 FN3K pseudogene
fragments on chromosome 22.
*FIELD* RF
1. 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, 2003.
2. 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.
3. 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.
*FIELD* CN
Patricia A. Hartz - updated: 12/17/2007
*FIELD* CD
Patricia A. Hartz: 1/23/2004
*FIELD* ED
mgross: 12/17/2007
terry: 12/17/2007
mgross: 1/23/2004