LOCUS       NM_022158               1393 bp    mRNA    linear   PRI 07-FEB-2025
DEFINITION  Homo sapiens fructosamine 3 kinase (FN3K), mRNA.
ACCESSION   NM_022158
VERSION     NM_022158.4
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (bases 1 to 1393)
  AUTHORS   Lokhandwala,J., Matlack,J.K., Smalley,T.B., Miner,R.E. 3rd,
            Tran,T.H. and Binning,J.M.
  TITLE     Structural basis for FN3K-mediated protein deglycation
  JOURNAL   Structure 32 (10), 1711-1724 (2024)
   PUBMED   39173621
  REMARK    GeneRIF: Structural basis for FN3K-mediated protein deglycation.
REFERENCE   2  (bases 1 to 1393)
  AUTHORS   Alderawi,A., Caramori,G., Baker,E.H., Hitchings,A.W., Rahman,I.,
            Rossios,C., Adcock,I., Cassolari,P., Papi,A., Ortega,V.E.,
            Curtis,J.L., Dunmore,S. and Kirkham,P.
  TITLE     FN3K expression in COPD: a potential comorbidity factor for
            cardiovascular disease
  JOURNAL   BMJ Open Respir Res 7 (1) (2020)
   PUBMED   33208304
  REMARK    GeneRIF: FN3K expression in COPD: a potential comorbidity factor
            for cardiovascular disease.
            Erratum:[BMJ Open Respir Res. 2021 Jan;8(1):e000714corr1. doi:
            10.1136/bmjresp-2020-000714corr1.. PMID: 33462091]
REFERENCE   3  (bases 1 to 1393)
  AUTHORS   Shrestha,S., Katiyar,S., Sanz-Rodriguez,C.E., Kemppinen,N.R.,
            Kim,H.W., Kadirvelraj,R., Panagos,C., Keyhaninejad,N., Colonna,M.,
            Chopra,P., Byrne,D.P., Boons,G.J., van der Knaap,E., Eyers,P.A.,
            Edison,A.S., Wood,Z.A. and Kannan,N.
  TITLE     A redox-active switch in fructosamine-3-kinases expands the
            regulatory repertoire of the protein kinase superfamily
  JOURNAL   Sci Signal 13 (639) (2020)
   PUBMED   32636308
  REMARK    GeneRIF: A redox-active switch in fructosamine-3-kinases expands
            the regulatory repertoire of the protein kinase superfamily.
            Publication Status: Online-Only
REFERENCE   4  (bases 1 to 1393)
  AUTHORS   Sanghvi,V.R., Leibold,J., Mina,M., Mohan,P., Berishaj,M., Li,Z.,
            Miele,M.M., Lailler,N., Zhao,C., de Stanchina,E., Viale,A.,
            Akkari,L., Lowe,S.W., Ciriello,G., Hendrickson,R.C. and Wendel,H.G.
  TITLE     The Oncogenic Action of NRF2 Depends on De-glycation by
            Fructosamine-3-Kinase
  JOURNAL   Cell 178 (4), 807-819 (2019)
   PUBMED   31398338
  REMARK    GeneRIF: FN3K is a targetable modulator of NRF2 activity in cancer.
REFERENCE   5  (bases 1 to 1393)
  AUTHORS   Delplanque,J., Delpierre,G., Opperdoes,F.R. and Van Schaftingen,E.
  TITLE     Tissue distribution and evolution of fructosamine 3-kinase and
            fructosamine 3-kinase-related protein
  JOURNAL   J Biol Chem 279 (45), 46606-46613 (2004)
   PUBMED   15331600
REFERENCE   6  (bases 1 to 1393)
  AUTHORS   Delpierrre,G., Vertommen,D., Communi,D., Rider,M.H. and Van
            Schaftingen,E.
  TITLE     Identification of fructosamine residues deglycated by
            fructosamine-3-kinase in human hemoglobin
  JOURNAL   J Biol Chem 279 (26), 27613-27620 (2004)
   PUBMED   15102834
  REMARK    GeneRIF: The aim of this work was to identify the fructosamine
            residues on hemoglobin that are removed as a result of the action
            of FN3K in intact erythrocytes.
REFERENCE   7  (bases 1 to 1393)
  AUTHORS   Delpierre,G. and Van Schaftingen,E.
  TITLE     Fructosamine 3-kinase, an enzyme involved in protein deglycation
  JOURNAL   Biochem Soc Trans 31 (Pt 6), 1354-1357 (2003)
   PUBMED   14641062
REFERENCE   8  (bases 1 to 1393)
  AUTHORS   Delpierre,G., Collard,F., Fortpied,J. and Van Schaftingen,E.
  TITLE     Fructosamine 3-kinase is involved in an intracellular deglycation
            pathway in human erythrocytes
  JOURNAL   Biochem J 365 (Pt 3), 801-808 (2002)
   PUBMED   11975663
  REMARK    GeneRIF: involved in the removal of fructosamine residues from
            hemoglobin in erythrocytes.
REFERENCE   9  (bases 1 to 1393)
  AUTHORS   Szwergold,B.S., Howell,S. and Beisswenger,P.J.
  TITLE     Human fructosamine-3-kinase: purification, sequencing, substrate
            specificity, and evidence of activity in vivo
  JOURNAL   Diabetes 50 (9), 2139-2147 (2001)
   PUBMED   11522682
REFERENCE   10 (bases 1 to 1393)
  AUTHORS   Delpierre,G., Rider,M.H., Collard,F., Stroobant,V., Vanstapel,F.,
            Santos,H. and Van Schaftingen,E.
  TITLE     Identification, cloning, and heterologous expression of a mammalian
            fructosamine-3-kinase
  JOURNAL   Diabetes 49 (10), 1627-1634 (2000)
   PUBMED   11016445
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC024361.21.
            
            On Nov 24, 2018 this sequence version replaced NM_022158.3.
            
            Summary: A high concentration of glucose can result in
            non-enzymatic oxidation of proteins by reaction of glucose and
            lysine residues (glycation). Proteins modified in this way,
            fructosamines, are less active or functional. This gene encodes an
            enzyme which catalyzes the phosphorylation of fructosamines which
            may result in deglycation. [provided by RefSeq, Feb 2012].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR3476690.679976.1,
                                           SRR3476690.256366.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1966682, SAMEA1968540
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000300784.8/ ENSP00000300784.7
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
            COMPLETENESS: full length.
PRIMARY     REFSEQ_SPAN         PRIMARY_IDENTIFIER PRIMARY_SPAN        COMP
            1-163               AC024361.21        86780-86942
            164-315             AC024361.21        89654-89805
            316-407             AC024361.21        91928-92019
            408-490             AC024361.21        92476-92558
            491-613             AC024361.21        100020-100142
            614-1393            AC024361.21        101582-102361
FEATURES             Location/Qualifiers
     source          1..1393
                     /organism="Homo sapiens"
                     /mol_type="mRNA"
                     /db_xref="taxon:9606"
                     /chromosome="17"
                     /map="17q25.3"
     gene            1..1393
                     /gene="FN3K"
                     /note="fructosamine 3 kinase"
                     /db_xref="GeneID:64122"
                     /db_xref="HGNC:HGNC:24822"
                     /db_xref="MIM:608425"
     exon            1..163
                     /gene="FN3K"
                     /inference="alignment:Splign:2.1.0"
     CDS             23..952
                     /gene="FN3K"
                     /EC_number="2.7.1.172"
                     /EC_number="2.7.1.171"
                     /note="protein-psicosamine 3-kinase FN3K;
                     protein-ribulosamine 3-kinase FN3K"
                     /codon_start=1
                     /product="fructosamine-3-kinase"
                     /protein_id="NP_071441.1"
                     /db_xref="CCDS:CCDS11818.1"
                     /db_xref="GeneID:64122"
                     /db_xref="HGNC:HGNC:24822"
                     /db_xref="MIM:608425"
                     /translation="MEQLLRAELRTATLRAFGGPGAGCISEGRAYDTDAGPVFVKVNR
                     RTQARQMFEGEVASLEALRSTGLVRVPRPMKVIDLPGGGAAFVMEHLKMKSLSSQASK
                     LGEQMADLHLYNQKLREKLKEEENTVGRRGEGAEPQYVDKFGFHTVTCCGFIPQVNEW
                     QDDWPTFFARHRLQAQLDLIEKDYADREARELWSRLQVKIPDLFCGLEIVPALLHGDL
                     WSGNVAEDDVGPIIYDPASFYGHSEFELAIALMFGGFPRSFFTAYHRKIPKAPGFDQR
                     LLLYQLFNYLNHWNHFGREYRSPSLGTMRRLLK"
     exon            164..315
                     /gene="FN3K"
                     /inference="alignment:Splign:2.1.0"
     exon            316..407
                     /gene="FN3K"
                     /inference="alignment:Splign:2.1.0"
     exon            408..490
                     /gene="FN3K"
                     /inference="alignment:Splign:2.1.0"
     exon            491..613
                     /gene="FN3K"
                     /inference="alignment:Splign:2.1.0"
     exon            614..1393
                     /gene="FN3K"
                     /inference="alignment:Splign:2.1.0"
     regulatory      1365..1370
                     /regulatory_class="polyA_signal_sequence"
                     /gene="FN3K"
                     /note="hexamer: AATAAA"
     polyA_site      1393
                     /gene="FN3K"
                     /note="major polyA site"
ORIGIN      
        1 agagtcccgc gccccgcact ccatggagca gctgctgcgc gccgagctgc gcaccgcgac
       61 cctgcgggcc ttcggcggcc ccggcgccgg ctgcatcagc gagggccgag cctacgacac
      121 ggacgcaggc ccagtgttcg tcaaagtcaa ccgcaggacg caggcccggc agatgtttga
      181 gggggaggtg gccagcctgg aggccctcag gagcacgggc ctggtgcggg tgccgaggcc
      241 catgaaggtc atcgacctgc cgggaggtgg ggccgccttt gtgatggagc atttgaagat
      301 gaagagcttg agcagtcaag catcaaaact tggagagcag atggcagatt tgcatcttta
      361 caaccagaag ctcagggaga agttgaagga ggaggagaac acagtgggcc gaagaggtga
      421 gggtgctgag cctcagtatg tggacaagtt cggcttccac acggtgacgt gctgcggctt
      481 catcccgcag gtgaatgagt ggcaggatga ctggccgacc tttttcgccc ggcaccggct
      541 ccaggcgcag ctggacctca ttgagaagga ctatgctgac cgagaggcac gagaactctg
      601 gtcccggcta caggtgaaga tcccggatct gttttgtggc ctagagattg tccccgcgtt
      661 gctccacggg gatctctggt cgggaaacgt ggctgaggac gacgtggggc ccattattta
      721 cgacccggct tccttctatg gccattccga gtttgaactg gcaatcgcct tgatgtttgg
      781 ggggttcccc agatccttct tcaccgccta ccaccggaag atccccaagg ctccgggctt
      841 cgaccagcgg ctgctgctct accagctgtt taactacctg aaccactgga accacttcgg
      901 gcgggagtac aggagccctt ccttgggcac catgcgaagg ctgctcaagt agcggcccct
      961 gccctccctt cccctgtccc cgtccccgtc tccgtctccc cgtccctgtc cccccgtccc
     1021 ccgtccctgt gcccccgtcc ctgtccccct gttcccgtct ccccgtccct ccgtctccat
     1081 ccccccgtcc ccccatcctc ctgtccccgt ccccccgtcc ccgtccctcc atccctgtcc
     1141 cccgtccccc tgtccccctg tccacatacc aatccccctg tccccgaccc cccatccccg
     1201 tcccccatct ccgtccccgt cccccctgcc ccgtccccgt ctccgttccc ccgtccccat
     1261 cctccatccc cgtctcccat cgccgtcccc ccgtccccgt cccccgtccc cgtcccccct
     1321 gtccctgtcc cccttccccc gacccctccc agatcctggg gaccaataaa gcccgcagcg
     1381 ggtctcggct ggc
//
