Full text data of FN3KRP
FN3KRP
[Confidence: low (only semi-automatic identification from reviews)]
Ketosamine-3-kinase; 2.7.1.- (Fructosamine-3-kinase-related protein; FN3K-RP; FN3K-related protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ketosamine-3-kinase; 2.7.1.- (Fructosamine-3-kinase-related protein; FN3K-RP; FN3K-related protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9HA64
ID KT3K_HUMAN Reviewed; 309 AA.
AC Q9HA64; Q969F4; Q9H0U7;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2004, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Ketosamine-3-kinase;
DE EC=2.7.1.-;
DE AltName: Full=Fructosamine-3-kinase-related protein;
DE Short=FN3K-RP;
DE Short=FN3K-related protein;
GN Name=FN3KRP;
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], AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=14633848; DOI=10.2337/diabetes.52.12.2888;
RA Collard F., Delpierre G., Stroobant V., Matthijs G.,
RA Van Schaftingen E.;
RT "A mammalian protein homologous to fructosamine-3-kinase is a
RT ketosamine-3-kinase acting on psicosamines and ribulosamines but not
RT on fructosamines.";
RL Diabetes 52:2888-2895(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Placenta;
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15137908; DOI=10.1042/BJ20040307;
RA Collard F., Wiame E., Bergans N., Fortpied J., Vertommen D.,
RA Vanstapel F., Delpierre G., Van Schaftingen E.;
RT "Fructosamine 3-kinase-related protein and deglycation in human
RT erythrocytes.";
RL Biochem. J. 382:137-143(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
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: Phosphorylates psicosamines and ribulosamines, but not
CC fructosamines, on the third carbon of the sugar moiety. Protein-
CC bound psicosamine 3-phosphates and ribulosamine 3-phosphates are
CC unstable and decompose under physiological conditions. Thus
CC phosphorylation leads to deglycation.
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66566.1; Type=Erroneous termination; Positions=198; Note=Translated as Leu;
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; AY360465; AAQ72344.1; -; mRNA.
DR EMBL; AL136631; CAB66566.1; ALT_SEQ; mRNA.
DR EMBL; AK022233; BAB13992.1; -; mRNA.
DR EMBL; BC001458; AAH01458.2; -; mRNA.
DR EMBL; BC007611; AAH07611.1; -; mRNA.
DR EMBL; BC014408; AAH14408.1; -; mRNA.
DR RefSeq; NP_078895.2; NM_024619.3.
DR UniGene; Hs.31431; -.
DR ProteinModelPortal; Q9HA64; -.
DR SMR; Q9HA64; 38-287.
DR IntAct; Q9HA64; 1.
DR MINT; MINT-4715634; -.
DR STRING; 9606.ENSP00000269373; -.
DR PhosphoSite; Q9HA64; -.
DR DMDM; 47606765; -.
DR REPRODUCTION-2DPAGE; IPI00099986; -.
DR PaxDb; Q9HA64; -.
DR PeptideAtlas; Q9HA64; -.
DR PRIDE; Q9HA64; -.
DR DNASU; 79672; -.
DR Ensembl; ENST00000269373; ENSP00000269373; ENSG00000141560.
DR GeneID; 79672; -.
DR KEGG; hsa:79672; -.
DR UCSC; uc002kfu.3; human.
DR CTD; 79672; -.
DR GeneCards; GC17P080674; -.
DR H-InvDB; HIX0173719; -.
DR HGNC; HGNC:25700; FN3KRP.
DR MIM; 611683; gene.
DR neXtProt; NX_Q9HA64; -.
DR PharmGKB; PA164720079; -.
DR eggNOG; COG3001; -.
DR HOGENOM; HOG000023913; -.
DR HOVERGEN; HBG005740; -.
DR InParanoid; Q9HA64; -.
DR KO; K15523; -.
DR OMA; PFVDQFG; -.
DR OrthoDB; EOG7MH0ZF; -.
DR PhylomeDB; Q9HA64; -.
DR BioCyc; MetaCyc:ENSG00000141560-MONOMER; -.
DR ChiTaRS; FN3KRP; human.
DR GeneWiki; FN3KRP; -.
DR GenomeRNAi; 79672; -.
DR NextBio; 68903; -.
DR PRO; PR:Q9HA64; -.
DR ArrayExpress; Q9HA64; -.
DR Bgee; Q9HA64; -.
DR Genevestigator; Q9HA64; -.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 Complete proteome; Kinase; Phosphoprotein; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 309 Ketosamine-3-kinase.
FT /FTId=PRO_0000216339.
FT MOD_RES 20 20 Phosphoserine.
FT VARIANT 57 57 A -> V (in dbSNP:rs3748811).
FT /FTId=VAR_034057.
FT CONFLICT 129 129 G -> W (in Ref. 2; CAB66566).
FT CONFLICT 265 265 G -> C (in Ref. 4; AAH01458).
FT CONFLICT 278 278 Q -> R (in Ref. 3; BAB13992).
SQ SEQUENCE 309 AA; 34412 MW; EE6101C5BB2A7FF3 CRC64;
MEELLRRELG CSSVRATGHS GGGCISQGRS YDTDQGRVFV KVNPKAEARR MFEGEMASLT
AILKTNTVKV PKPIKVLDAP GGGSVLVMEH MDMRHLSSHA AKLGAQLADL HLDNKKLGEM
RLKEAGTVGR GGGQEERPFV ARFGFDVVTC CGYLPQVNDW QEDWVVFYAR QRIQPQMDMV
EKESGDREAL QLWSALQLKI PDLFRDLEII PALLHGDLWG GNVAEDSSGP VIFDPASFYG
HSEYELAIAG MFGGFSSSFY SAYHGKIPKA PGFEKRLQLY QLFHYLNHWN HFGSGYRGSS
LNIMRNLVK
//
ID KT3K_HUMAN Reviewed; 309 AA.
AC Q9HA64; Q969F4; Q9H0U7;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-MAY-2004, sequence version 2.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Ketosamine-3-kinase;
DE EC=2.7.1.-;
DE AltName: Full=Fructosamine-3-kinase-related protein;
DE Short=FN3K-RP;
DE Short=FN3K-related protein;
GN Name=FN3KRP;
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], AND FUNCTION.
RC TISSUE=Kidney;
RX PubMed=14633848; DOI=10.2337/diabetes.52.12.2888;
RA Collard F., Delpierre G., Stroobant V., Matthijs G.,
RA Van Schaftingen E.;
RT "A mammalian protein homologous to fructosamine-3-kinase is a
RT ketosamine-3-kinase acting on psicosamines and ribulosamines but not
RT on fructosamines.";
RL Diabetes 52:2888-2895(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and Placenta;
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 [5]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15137908; DOI=10.1042/BJ20040307;
RA Collard F., Wiame E., Bergans N., Fortpied J., Vertommen D.,
RA Vanstapel F., Delpierre G., Van Schaftingen E.;
RT "Fructosamine 3-kinase-related protein and deglycation in human
RT erythrocytes.";
RL Biochem. J. 382:137-143(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [7]
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: Phosphorylates psicosamines and ribulosamines, but not
CC fructosamines, on the third carbon of the sugar moiety. Protein-
CC bound psicosamine 3-phosphates and ribulosamine 3-phosphates are
CC unstable and decompose under physiological conditions. Thus
CC phosphorylation leads to deglycation.
CC -!- TISSUE SPECIFICITY: Expressed in erythrocytes.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66566.1; Type=Erroneous termination; Positions=198; Note=Translated as Leu;
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; AY360465; AAQ72344.1; -; mRNA.
DR EMBL; AL136631; CAB66566.1; ALT_SEQ; mRNA.
DR EMBL; AK022233; BAB13992.1; -; mRNA.
DR EMBL; BC001458; AAH01458.2; -; mRNA.
DR EMBL; BC007611; AAH07611.1; -; mRNA.
DR EMBL; BC014408; AAH14408.1; -; mRNA.
DR RefSeq; NP_078895.2; NM_024619.3.
DR UniGene; Hs.31431; -.
DR ProteinModelPortal; Q9HA64; -.
DR SMR; Q9HA64; 38-287.
DR IntAct; Q9HA64; 1.
DR MINT; MINT-4715634; -.
DR STRING; 9606.ENSP00000269373; -.
DR PhosphoSite; Q9HA64; -.
DR DMDM; 47606765; -.
DR REPRODUCTION-2DPAGE; IPI00099986; -.
DR PaxDb; Q9HA64; -.
DR PeptideAtlas; Q9HA64; -.
DR PRIDE; Q9HA64; -.
DR DNASU; 79672; -.
DR Ensembl; ENST00000269373; ENSP00000269373; ENSG00000141560.
DR GeneID; 79672; -.
DR KEGG; hsa:79672; -.
DR UCSC; uc002kfu.3; human.
DR CTD; 79672; -.
DR GeneCards; GC17P080674; -.
DR H-InvDB; HIX0173719; -.
DR HGNC; HGNC:25700; FN3KRP.
DR MIM; 611683; gene.
DR neXtProt; NX_Q9HA64; -.
DR PharmGKB; PA164720079; -.
DR eggNOG; COG3001; -.
DR HOGENOM; HOG000023913; -.
DR HOVERGEN; HBG005740; -.
DR InParanoid; Q9HA64; -.
DR KO; K15523; -.
DR OMA; PFVDQFG; -.
DR OrthoDB; EOG7MH0ZF; -.
DR PhylomeDB; Q9HA64; -.
DR BioCyc; MetaCyc:ENSG00000141560-MONOMER; -.
DR ChiTaRS; FN3KRP; human.
DR GeneWiki; FN3KRP; -.
DR GenomeRNAi; 79672; -.
DR NextBio; 68903; -.
DR PRO; PR:Q9HA64; -.
DR ArrayExpress; Q9HA64; -.
DR Bgee; Q9HA64; -.
DR Genevestigator; Q9HA64; -.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 Complete proteome; Kinase; Phosphoprotein; Polymorphism;
KW Reference proteome; Transferase.
FT CHAIN 1 309 Ketosamine-3-kinase.
FT /FTId=PRO_0000216339.
FT MOD_RES 20 20 Phosphoserine.
FT VARIANT 57 57 A -> V (in dbSNP:rs3748811).
FT /FTId=VAR_034057.
FT CONFLICT 129 129 G -> W (in Ref. 2; CAB66566).
FT CONFLICT 265 265 G -> C (in Ref. 4; AAH01458).
FT CONFLICT 278 278 Q -> R (in Ref. 3; BAB13992).
SQ SEQUENCE 309 AA; 34412 MW; EE6101C5BB2A7FF3 CRC64;
MEELLRRELG CSSVRATGHS GGGCISQGRS YDTDQGRVFV KVNPKAEARR MFEGEMASLT
AILKTNTVKV PKPIKVLDAP GGGSVLVMEH MDMRHLSSHA AKLGAQLADL HLDNKKLGEM
RLKEAGTVGR GGGQEERPFV ARFGFDVVTC CGYLPQVNDW QEDWVVFYAR QRIQPQMDMV
EKESGDREAL QLWSALQLKI PDLFRDLEII PALLHGDLWG GNVAEDSSGP VIFDPASFYG
HSEYELAIAG MFGGFSSSFY SAYHGKIPKA PGFEKRLQLY QLFHYLNHWN HFGSGYRGSS
LNIMRNLVK
//
MIM
611683
*RECORD*
*FIELD* NO
611683
*FIELD* TI
*611683 FRUCTOSAMINE 3-KINASE-RELATED PROTEIN
;;FN3K-RELATED PROTEIN; FN3KRP
*FIELD* TX
read more
DESCRIPTION
FN3KRP and FN3K (608425) protect proteins from nonenzymatic glycation by
phosphorylating the modified amino acid. This phosphorylation
destabilizes the sugar-amine linkage and leads to spontaneous
decomposition (Conner et al., 2004).
CLONING
By searching an EST database for homologs of FN3K, Collard et al. (2003)
identified FN3KRP. The deduced 309-amino acid protein has a calculated
molecular mass of 34.4 kD and shares 88% identity with mouse Fn3krp.
Like FN3K, FN3KRP has an HGDxxxxN motif that is also found in
aminoglycoside kinases. Northern blot analysis detected Fn3krp
expression in all mouse tissues examined except intestinal mucosa.
Highest expression was in bone marrow, brain, spleen, and kidney.
Using RT-PCR, Conner et al. (2004) detected FN3KRP expression in all
human tissues examined.
GENE FUNCTION
Collard et al. (2003) partially purified FN3KRP following expression in
human embryonic kidney cells and found that it phosphorylated
psicosamines and ribulosamines, but not fructosamines. Mass spectrometry
and NMR spectroscopy of a phosphorylated synthetic psicose substrate
identified C3 as the phosphorylated carbon. Collard et al. (2003)
concluded that FN3KRP is a ketosamine 3-kinase with a substrate
specificity distinct from that of FN3K.
Collard et al. (2004) found that human erythrocytes had higher
intracellular levels of active FN3KRP than FN3K.
Szwergold et al. (2007) found that human erythrocytes that contain both
FN3K and FN3KRP phosphorylated N-methylglucamine to 2 different
products, and FN3KRP specifically phosphorylated the C-4 hydroxyl.
FN3KRP also phosphorylated other glucitolamines at the C-4 position.
Szwergold et al. (2007) noted that all substrates used to characterize
FN3KRP to that time were nonphysiologic. This and the unique
stereospecificity displayed by FN3KRP suggested to them that the primary
role of FN3KRP may not be as a deglycating enzyme.
GENE STRUCTURE
Collard et al. (2003) determined that the FN3KRP gene contains 6 exons.
Conner et al. (2004) found that the promoter region of the FN3KRP gene
has a high GC content, but no TATA or CAAT boxes.
MAPPING
By genomic sequence analysis, Collard et al. (2003) mapped the FN3KR
gene 8.5 kb upstream of the FN3K gene on chromosome 17q25.
*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. Collard, F.; Wiame, E.; Bergans, N.; Fortpied, J.; Vertommen, D.;
Vanstapel, F.; Delpierre, G.; Van Schaftingen, E.: Fructosamine 3-kinase-related
protein and deglycation in human erythrocytes. Biochem. J. 382:
137-143, 2004.
3. 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.
4. Szwergold, B.; Manevich, Y.; Payne, L.; Loomes, K.: Fructosamine-3-kinase-related
protein phosphorylates glucitolamines on the C-4 hydroxyl: novel substrate
specificity of an enigmatic enzyme. Biochem. Biophys. Res. Commun. 361:
870-875, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 6/24/2008
*FIELD* CD
Patricia A. Hartz: 12/17/2007
*FIELD* ED
alopez: 06/25/2008
terry: 6/24/2008
mgross: 12/17/2007
*RECORD*
*FIELD* NO
611683
*FIELD* TI
*611683 FRUCTOSAMINE 3-KINASE-RELATED PROTEIN
;;FN3K-RELATED PROTEIN; FN3KRP
*FIELD* TX
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DESCRIPTION
FN3KRP and FN3K (608425) protect proteins from nonenzymatic glycation by
phosphorylating the modified amino acid. This phosphorylation
destabilizes the sugar-amine linkage and leads to spontaneous
decomposition (Conner et al., 2004).
CLONING
By searching an EST database for homologs of FN3K, Collard et al. (2003)
identified FN3KRP. The deduced 309-amino acid protein has a calculated
molecular mass of 34.4 kD and shares 88% identity with mouse Fn3krp.
Like FN3K, FN3KRP has an HGDxxxxN motif that is also found in
aminoglycoside kinases. Northern blot analysis detected Fn3krp
expression in all mouse tissues examined except intestinal mucosa.
Highest expression was in bone marrow, brain, spleen, and kidney.
Using RT-PCR, Conner et al. (2004) detected FN3KRP expression in all
human tissues examined.
GENE FUNCTION
Collard et al. (2003) partially purified FN3KRP following expression in
human embryonic kidney cells and found that it phosphorylated
psicosamines and ribulosamines, but not fructosamines. Mass spectrometry
and NMR spectroscopy of a phosphorylated synthetic psicose substrate
identified C3 as the phosphorylated carbon. Collard et al. (2003)
concluded that FN3KRP is a ketosamine 3-kinase with a substrate
specificity distinct from that of FN3K.
Collard et al. (2004) found that human erythrocytes had higher
intracellular levels of active FN3KRP than FN3K.
Szwergold et al. (2007) found that human erythrocytes that contain both
FN3K and FN3KRP phosphorylated N-methylglucamine to 2 different
products, and FN3KRP specifically phosphorylated the C-4 hydroxyl.
FN3KRP also phosphorylated other glucitolamines at the C-4 position.
Szwergold et al. (2007) noted that all substrates used to characterize
FN3KRP to that time were nonphysiologic. This and the unique
stereospecificity displayed by FN3KRP suggested to them that the primary
role of FN3KRP may not be as a deglycating enzyme.
GENE STRUCTURE
Collard et al. (2003) determined that the FN3KRP gene contains 6 exons.
Conner et al. (2004) found that the promoter region of the FN3KRP gene
has a high GC content, but no TATA or CAAT boxes.
MAPPING
By genomic sequence analysis, Collard et al. (2003) mapped the FN3KR
gene 8.5 kb upstream of the FN3K gene on chromosome 17q25.
*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. Collard, F.; Wiame, E.; Bergans, N.; Fortpied, J.; Vertommen, D.;
Vanstapel, F.; Delpierre, G.; Van Schaftingen, E.: Fructosamine 3-kinase-related
protein and deglycation in human erythrocytes. Biochem. J. 382:
137-143, 2004.
3. 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.
4. Szwergold, B.; Manevich, Y.; Payne, L.; Loomes, K.: Fructosamine-3-kinase-related
protein phosphorylates glucitolamines on the C-4 hydroxyl: novel substrate
specificity of an enigmatic enzyme. Biochem. Biophys. Res. Commun. 361:
870-875, 2007.
*FIELD* CN
Patricia A. Hartz - updated: 6/24/2008
*FIELD* CD
Patricia A. Hartz: 12/17/2007
*FIELD* ED
alopez: 06/25/2008
terry: 6/24/2008
mgross: 12/17/2007