LOCUS       NP_789818                297 aa            linear   ROD 02-MAY-2024
DEFINITION  F-box only protein 2 [Mus musculus].
ACCESSION   NP_789818
VERSION     NP_789818.1
DBSOURCE    REFSEQ: accession NM_176848.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 297)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 297)
  AUTHORS   Chen,N., Cao,R., Zhang,Z., Zhou,S. and Hu,S.
  TITLE     Sleeve Gastrectomy Improves Hepatic Glucose Metabolism by
            Downregulating FBXO2 and Activating the PI3K-AKT Pathway
  JOURNAL   Int J Mol Sci 24 (6), 5544 (2023)
   PUBMED   36982617
  REMARK    GeneRIF: Sleeve Gastrectomy Improves Hepatic Glucose Metabolism by
            Downregulating FBXO2 and Activating the PI3K-AKT Pathway.
            Publication Status: Online-Only
REFERENCE   3  (residues 1 to 297)
  AUTHORS   McGovern,M.M., Hartman,B., Thawani,A., Maunsell,H., Zhang,H.,
            Yousaf,R., Heller,S., Stone,J. and Groves,A.K.
  TITLE     Fbxo2CreERT2: A new model for targeting cells in the neonatal and
            mature inner ear
  JOURNAL   Hear Res 428, 108686 (2023)
   PUBMED   36587458
REFERENCE   4  (residues 1 to 297)
  AUTHORS   Yoshida,Y., Asahina,M., Murakami,A., Kawawaki,J., Yoshida,M.,
            Fujinawa,R., Iwai,K., Tozawa,R., Matsuda,N., Tanaka,K. and
            Suzuki,T.
  TITLE     Loss of peptide:N-glycanase causes proteasome dysfunction mediated
            by a sugar-recognizing ubiquitin ligase
  JOURNAL   Proc Natl Acad Sci U S A 118 (27) (2021)
   PUBMED   34215698
REFERENCE   5  (residues 1 to 297)
  AUTHORS   Hartman,B.H., Bscke,R., Ellwanger,D.C., Keymeulen,S.,
            Scheibinger,M. and Heller,S.
  TITLE     Fbxo2VHC mouse and embryonic stem cell reporter lines delineate in
            vitro-generated inner ear sensory epithelia cells and enable otic
            lineage selection and Cre-recombination
  JOURNAL   Dev Biol 443 (1), 64-77 (2018)
   PUBMED   30179592
REFERENCE   6  (residues 1 to 297)
  AUTHORS   Kato,A., Rouach,N., Nicoll,R.A. and Bredt,D.S.
  TITLE     Activity-dependent NMDA receptor degradation mediated by
            retrotranslocation and ubiquitination
  JOURNAL   Proc Natl Acad Sci U S A 102 (15), 5600-5605 (2005)
   PUBMED   15809437
  REMARK    GeneRIF: When expressed in hippocampal neurons, the Fbx2
            dominant-negative mutant augmented NR1 subunit levels and NMDA
            receptor-mediated currents in an activity-dependent fashion
REFERENCE   7  (residues 1 to 297)
  AUTHORS   Yoshida,Y., Adachi,E., Fukiya,K., Iwai,K. and Tanaka,K.
  TITLE     Glycoprotein-specific ubiquitin ligases recognize N-glycans in
            unfolded substrates
  JOURNAL   EMBO Rep 6 (3), 239-244 (2005)
   PUBMED   15723043
REFERENCE   8  (residues 1 to 297)
  AUTHORS   Yoshida,Y., Tokunaga,F., Chiba,T., Iwai,K., Tanaka,K. and Tai,T.
  TITLE     Fbs2 is a new member of the E3 ubiquitin ligase family that
            recognizes sugar chains
  JOURNAL   J Biol Chem 278 (44), 43877-43884 (2003)
   PUBMED   12939278
REFERENCE   9  (residues 1 to 297)
  AUTHORS   Yoshida,Y., Chiba,T., Tokunaga,F., Kawasaki,H., Iwai,K., Suzuki,T.,
            Ito,Y., Matsuoka,K., Yoshida,M., Tanaka,K. and Tai,T.
  TITLE     E3 ubiquitin ligase that recognizes sugar chains
  JOURNAL   Nature 418 (6896), 438-442 (2002)
   PUBMED   12140560
REFERENCE   10 (residues 1 to 297)
  AUTHORS   Yehiely,F., Bamborough,P., Da Costa,M., Perry,B.J., Thinakaran,G.,
            Cohen,F.E., Carlson,G.A. and Prusiner,S.B.
  TITLE     Identification of candidate proteins binding to prion protein
  JOURNAL   Neurobiol Dis 3 (4), 339-355 (1997)
   PUBMED   9173930
  REMARK    Erratum:[Neurobiol Dis 2002 Jun;10(1):67-8]
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AL606929.13.
            
            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 :: BC046586.1, SRR9219381.28560.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..297
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="4"
                     /map="4 78.68 cM"
     Protein         1..297
                     /product="F-box only protein 2"
                     /note="prion protein ligand 4"
                     /calculated_mol_wt=33545
     Region          1..47
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q80UW2.1)"
     Region          61..123
                     /region_name="F-box_FBXO2"
                     /note="F-box domain found in F-box only protein 2 (FBXO2)
                     and similar proteins; cd22167"
                     /db_xref="CDD:438938"
     Site            order(61..62,65..67,70,72..74,76..80,82,113,115,119,123)
                     /site_type="other"
                     /note="Skp1 binding site [polypeptide binding]"
                     /db_xref="CDD:438938"
     Site            106
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q80UW2.1)"
     Region          118..295
                     /region_name="FBA"
                     /note="F-box associated region; pfam04300"
                     /db_xref="CDD:461255"
     Site            159
                     /site_type="other"
                     /note="Important for carbohydrate binding; propagated from
                     UniProtKB/Swiss-Prot (Q80UW2.1)"
     Site            177
                     /site_type="other"
                     /note="Important for carbohydrate binding; propagated from
                     UniProtKB/Swiss-Prot (Q80UW2.1)"
     CDS             1..297
                     /gene="Fbxo2"
                     /gene_synonym="FBG1; Fbs1; Fbs2; FBX2; NFB42; Prpl4"
                     /coded_by="NM_176848.2:69..962"
                     /db_xref="CCDS:CCDS18935.1"
                     /db_xref="GeneID:230904"
                     /db_xref="MGI:MGI:2446216"
ORIGIN      
        1 mdgdgdpesv shpeeaspee qpeeagaeas aeeeqlreae eeeeaeavey laelpeplll
       61 rvlaelpate lvqacrlvcl rwkelvdgap lwllkcqqeg lvpegsadee rdhwqqfyfl
      121 skrrrnllrn pcgeedlegw sdvehggdgw rveelpgdng veftqddsvk kyfassfewc
      181 rkaqvidlqa egyweelldt tqpaivvkdw ysgrtdagsl yeltvrllse nedvlaefat
      241 gqvavpedgs wmeishtfid ygpgvrfvrf ehggqdsvyw kgwfgarvtn ssvwvep
//
