KT3K_MOUSE
ID KT3K_MOUSE Reviewed; 309 AA.
AC Q8K274; B1ATT5;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ketosamine-3-kinase {ECO:0000303|PubMed:14633848};
DE EC=2.7.1.172 {ECO:0000250|UniProtKB:Q9HA64};
DE AltName: Full=Fructosamine-3-kinase-related protein {ECO:0000250|UniProtKB:Q9HA64};
DE Short=FN3K-RP {ECO:0000250|UniProtKB:Q9HA64};
DE Short=FN3K-related protein {ECO:0000250|UniProtKB:Q9HA64};
DE AltName: Full=Protein-psicosamine 3-kinase FN3KRP {ECO:0000305};
DE EC=2.7.1.- {ECO:0000250|UniProtKB:Q9HA64};
GN Name=Fn3krp {ECO:0000312|MGI:MGI:2679256};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=NMRI;
RX PubMed=14633848; DOI=10.2337/diabetes.52.12.2888;
RA Collard F., Delpierre G., Stroobant V., Matthijs G., Van Schaftingen E.;
RT "A mammalian protein homologous to fructosamine-3-kinase is a ketosamine-3-
RT kinase acting on psicosamines and ribulosamines but not on fructosamines.";
RL Diabetes 52:2888-2895(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ketosamine-3-kinase involved in protein deglycation by
CC mediating phosphorylation of ribuloselysine and psicoselysine on
CC glycated proteins, to generate ribuloselysine-3 phosphate and
CC psicoselysine-3 phosphate, respectively (PubMed:14633848).
CC Ribuloselysine-3 phosphate and psicoselysine-3 phosphate adducts are
CC unstable and decompose under physiological conditions
CC (PubMed:14633848). Not able to phosphorylate fructoselysine
CC (PubMed:14633848). {ECO:0000269|PubMed:14633848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-D-ribulosyl-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-ribulosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:48432,
CC Rhea:RHEA-COMP:12103, Rhea:RHEA-COMP:12104, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:90418, ChEBI:CHEBI:90420,
CC ChEBI:CHEBI:456216; EC=2.7.1.172;
CC Evidence={ECO:0000250|UniProtKB:Q9HA64};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000250|UniProtKB:Q9HA64};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(6)-(D-psicosyl)-L-lysyl-[protein] = ADP + H(+) + N(6)-
CC (3-O-phospho-D-psicosyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:61392,
CC Rhea:RHEA-COMP:15796, Rhea:RHEA-COMP:15797, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:144621, ChEBI:CHEBI:144622,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9HA64};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61393;
CC Evidence={ECO:0000250|UniProtKB:Q9HA64};
CC -!- DOMAIN: The ATP-binding domain is structurally related to
CC aminoglycoside phosphotransferase family.
CC {ECO:0000250|UniProtKB:Q9HA64}.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
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DR EMBL; AY360466; AAQ72345.1; -; mRNA.
DR EMBL; AL663088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466558; EDL34839.1; -; Genomic_DNA.
DR EMBL; BC032265; AAH32265.1; -; mRNA.
DR CCDS; CCDS25775.1; -.
DR RefSeq; NP_852085.2; NM_181420.3.
DR AlphaFoldDB; Q8K274; -.
DR SMR; Q8K274; -.
DR BioGRID; 231941; 1.
DR STRING; 10090.ENSMUSP00000038061; -.
DR iPTMnet; Q8K274; -.
DR PhosphoSitePlus; Q8K274; -.
DR SwissPalm; Q8K274; -.
DR EPD; Q8K274; -.
DR MaxQB; Q8K274; -.
DR PaxDb; Q8K274; -.
DR PeptideAtlas; Q8K274; -.
DR PRIDE; Q8K274; -.
DR ProteomicsDB; 289991; -.
DR Antibodypedia; 33041; 106 antibodies from 24 providers.
DR DNASU; 238024; -.
DR Ensembl; ENSMUST00000038096; ENSMUSP00000038061; ENSMUSG00000039253.
DR GeneID; 238024; -.
DR KEGG; mmu:238024; -.
DR UCSC; uc007mvv.2; mouse.
DR CTD; 79672; -.
DR MGI; MGI:2679256; Fn3krp.
DR VEuPathDB; HostDB:ENSMUSG00000039253; -.
DR eggNOG; KOG3021; Eukaryota.
DR GeneTree; ENSGT00390000005730; -.
DR HOGENOM; CLU_036517_0_1_1; -.
DR InParanoid; Q8K274; -.
DR OMA; GSFYSAY; -.
DR OrthoDB; 943202at2759; -.
DR PhylomeDB; Q8K274; -.
DR TreeFam; TF313452; -.
DR BRENDA; 2.7.1.171; 3474.
DR BRENDA; 2.7.1.172; 3474.
DR Reactome; R-MMU-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR BioGRID-ORCS; 238024; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Fn3krp; mouse.
DR PRO; PR:Q8K274; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8K274; protein.
DR Bgee; ENSMUSG00000039253; Expressed in lens of camera-type eye and 60 other tissues.
DR Genevisible; Q8K274; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0102193; F:protein-ribulosamine 3-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR016477; Fructo-/Ketosamine-3-kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR12149; PTHR12149; 1.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Ketosamine-3-kinase"
FT /id="PRO_0000216340"
FT ACT_SITE 217
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P9WI99"
FT BINDING 89..91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HA64"
FT CONFLICT 120
FT /note="R -> K (in Ref. 4; AAH32265)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34468 MW; 95BA25D1206E1B6E CRC64;
METLLKRELG CSSVKATGHS GGGCISQGQS YDTDKGRVFV KVNSKAEARR MFEGEMASLT
AILKTGTVKV PKPIKVVDAP GGGSMLVMEH LDMRYLSSHA TKLGTQLADL HLENKRLGER
LLKEAGTVGK GGEQAERQYV DQFGFDVVTC CGYLPQVNDW QKNWVEFYAR QRIQPQMDMV
EKKSGDREAL ELWSALQLKI PDLFRDLEIV PALLHGDLWG GNVAEDSSGP IIFDPASFYG
HSEYELAIAG MFGGFSSSFY SAYHSKIPKT PGFEKRLQLY QLFHYLNHWN HFGSGYRGSS
LNIMRNLSK
