KT3K_HUMAN
ID KT3K_HUMAN Reviewed; 309 AA.
AC Q9HA64; Q969F4; Q9H0U7;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Ketosamine-3-kinase {ECO:0000303|PubMed:14633848};
DE EC=2.7.1.172 {ECO:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908};
DE AltName: Full=Fructosamine-3-kinase-related protein {ECO:0000303|PubMed:15137908};
DE Short=FN3K-RP {ECO:0000303|PubMed:15137908};
DE Short=FN3K-related protein {ECO:0000303|PubMed:15137908};
DE AltName: Full=Protein-psicosamine 3-kinase FN3KRP {ECO:0000305};
DE EC=2.7.1.- {ECO:0000269|PubMed:14633848};
GN Name=FN3KRP {ECO:0000303|PubMed:15137908, ECO:0000312|HGNC:HGNC:25700};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., 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 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., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=15137908; DOI=10.1042/bj20040307;
RA Collard F., Wiame E., Bergans N., Fortpied J., Vertommen D., Vanstapel F.,
RA 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 TISSUE SPECIFICITY.
RX PubMed=15331600; DOI=10.1074/jbc.m407678200;
RA Delplanque J., Delpierre G., Opperdoes F.R., Van Schaftingen E.;
RT "Tissue distribution and evolution of fructosamine 3-kinase and
RT fructosamine 3-kinase-related protein.";
RL J. Biol. Chem. 279:46606-46613(2004).
RN [7]
RP DOMAIN.
RX PubMed=18637789; DOI=10.1042/bj20080389;
RA Payne L.S., Brown P.M., Middleditch M., Baker E., Cooper G.J., Loomes K.M.;
RT "Mapping of the ATP-binding domain of human fructosamine 3-kinase-related
RT protein by affinity labelling with 5'-[p-
RT (fluorosulfonyl)benzoyl]adenosine.";
RL Biochem. J. 416:281-288(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [9]
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., Buerckstuemmer T.,
RA 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: 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 PubMed:15137908). Ribuloselysine-3 phosphate and psicoselysine-3
CC phosphate adducts are unstable and decompose under physiological
CC conditions (PubMed:14633848, PubMed:15137908). Not able to
CC phosphorylate fructoselysine (PubMed:14633848).
CC {ECO:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908}.
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:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48433;
CC Evidence={ECO:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908};
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:0000269|PubMed:14633848,
CC ECO:0000269|PubMed:15137908};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61393;
CC Evidence={ECO:0000269|PubMed:14633848, ECO:0000269|PubMed:15137908};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=160 uM for deoxymorpholinopsicose {ECO:0000269|PubMed:14633848};
CC KM=270 uM for psicoselysine {ECO:0000269|PubMed:14633848};
CC KM=3.5 uM for deoxymorpholinoribulose {ECO:0000269|PubMed:14633848};
CC -!- TISSUE SPECIFICITY: Widely expressed; except in skeletal muscle where
CC it is expressed at very low level (PubMed:15331600). Expressed in
CC erythrocytes (PubMed:15137908). {ECO:0000269|PubMed:15137908,
CC ECO:0000269|PubMed:15331600}.
CC -!- DOMAIN: The ATP-binding domain is structurally related to
CC aminoglycoside phosphotransferase family.
CC {ECO:0000305|PubMed:18637789}.
CC -!- SIMILARITY: Belongs to the fructosamine kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB66566.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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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 CCDS; CCDS11817.1; -.
DR RefSeq; NP_078895.2; NM_024619.3.
DR AlphaFoldDB; Q9HA64; -.
DR SMR; Q9HA64; -.
DR BioGRID; 122797; 39.
DR IntAct; Q9HA64; 18.
DR STRING; 9606.ENSP00000269373; -.
DR ChEMBL; CHEMBL4295947; -.
DR GlyGen; Q9HA64; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9HA64; -.
DR PhosphoSitePlus; Q9HA64; -.
DR BioMuta; FN3KRP; -.
DR DMDM; 47606765; -.
DR REPRODUCTION-2DPAGE; IPI00099986; -.
DR EPD; Q9HA64; -.
DR jPOST; Q9HA64; -.
DR MassIVE; Q9HA64; -.
DR MaxQB; Q9HA64; -.
DR PaxDb; Q9HA64; -.
DR PeptideAtlas; Q9HA64; -.
DR PRIDE; Q9HA64; -.
DR ProteomicsDB; 81378; -.
DR Antibodypedia; 33041; 106 antibodies from 24 providers.
DR DNASU; 79672; -.
DR Ensembl; ENST00000269373.11; ENSP00000269373.6; ENSG00000141560.15.
DR GeneID; 79672; -.
DR KEGG; hsa:79672; -.
DR MANE-Select; ENST00000269373.11; ENSP00000269373.6; NM_024619.4; NP_078895.2.
DR UCSC; uc002kfu.4; human.
DR CTD; 79672; -.
DR DisGeNET; 79672; -.
DR GeneCards; FN3KRP; -.
DR HGNC; HGNC:25700; FN3KRP.
DR HPA; ENSG00000141560; Low tissue specificity.
DR MIM; 611683; gene.
DR neXtProt; NX_Q9HA64; -.
DR OpenTargets; ENSG00000141560; -.
DR PharmGKB; PA164720079; -.
DR VEuPathDB; HostDB:ENSG00000141560; -.
DR eggNOG; KOG3021; Eukaryota.
DR GeneTree; ENSGT00390000005730; -.
DR HOGENOM; CLU_036517_0_1_1; -.
DR InParanoid; Q9HA64; -.
DR OMA; GSFYSAY; -.
DR OrthoDB; 943202at2759; -.
DR PhylomeDB; Q9HA64; -.
DR TreeFam; TF313452; -.
DR BioCyc; MetaCyc:ENSG00000141560-MON; -.
DR BRENDA; 2.7.1.171; 2681.
DR BRENDA; 2.7.1.172; 2681.
DR PathwayCommons; Q9HA64; -.
DR Reactome; R-HSA-163841; Gamma carboxylation, hypusine formation and arylsulfatase activation.
DR SignaLink; Q9HA64; -.
DR BioGRID-ORCS; 79672; 3 hits in 1074 CRISPR screens.
DR ChiTaRS; FN3KRP; human.
DR GeneWiki; FN3KRP; -.
DR GenomeRNAi; 79672; -.
DR Pharos; Q9HA64; Tbio.
DR PRO; PR:Q9HA64; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9HA64; protein.
DR Bgee; ENSG00000141560; Expressed in C1 segment of cervical spinal cord and 170 other tissues.
DR ExpressionAtlas; Q9HA64; baseline and differential.
DR Genevisible; Q9HA64; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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 GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
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_0000216339"
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:0000305|PubMed:18637789"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT VARIANT 57
FT /note="A -> V (in dbSNP:rs3748811)"
FT /id="VAR_034057"
FT CONFLICT 129
FT /note="G -> W (in Ref. 2; CAB66566)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="G -> C (in Ref. 4; AAH01458)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Q -> R (in Ref. 3; BAB13992)"
FT /evidence="ECO:0000305"
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
