ID   FBX2_HUMAN              Reviewed;         296 AA.
AC   Q9UK22; B2R7K7; Q5TGY0; Q6FGJ7; Q8TB29; Q9UKC6;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   10-JUN-2026, entry version 197.
DE   RecName: Full=F-box only protein 2;
GN   Name=FBXO2; Synonyms=FBX2;
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].
RX   PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA   Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT   "A family of mammalian F-box proteins.";
RL   Curr. Biol. 9:1180-1182(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-118.
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
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 GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Pancreas;
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 40-296.
RX   PubMed=10531035; DOI=10.1016/s0960-9822(00)80020-2;
RA   Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
RA   Pagano M.;
RT   "Identification of a family of human F-box proteins.";
RL   Curr. Biol. 9:1177-1179(1999).
RN   [8]
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: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC       protein) E3 ubiquitin-protein ligase complex that mediates the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. Involved in the endoplasmic reticulum-associated degradation
CC       pathway (ERAD) for misfolded lumenal proteins by recognizing and
CC       binding sugar chains on unfolded glycoproteins that are
CC       retrotranslocated into the cytosol and promoting their ubiquitination
CC       and subsequent degradation. Prevents formation of cytosolic aggregates
CC       of unfolded glycoproteins that have been retrotranslocated into the
CC       cytosol. Able to recognize and bind denatured glycoproteins,
CC       preferentially those of the high-mannose type (By similarity).
CC       {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the SCF(FBXO2) complex consisting of CUL1, RBX1,
CC       SKP1 and FBXO2. Predominantly detected as heterodimer with SKP1; the
CC       heterodimer with SKP1 is not part of the SCF(FBXO2) complex (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9UK22; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-4287196, EBI-10240813;
CC       Q9UK22; O15212: PFDN6; NbExp=3; IntAct=EBI-4287196, EBI-356973;
CC       Q9UK22; Q9HAT2: SIAE; NbExp=2; IntAct=EBI-4287196, EBI-2908303;
CC       Q9UK22; P63208: SKP1; NbExp=15; IntAct=EBI-4287196, EBI-307486;
CC       Q9UK22; Q6UX27-3: VSTM1; NbExp=3; IntAct=EBI-4287196, EBI-12190699;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
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DR   EMBL; AF187318; AAF01822.1; -; mRNA.
DR   EMBL; CR542110; CAG46907.1; -; mRNA.
DR   EMBL; AK313019; BAG35854.1; -; mRNA.
DR   EMBL; AL031731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71689.1; -; Genomic_DNA.
DR   EMBL; BC025233; AAH25233.1; -; mRNA.
DR   EMBL; BC096747; AAH96747.1; -; mRNA.
DR   EMBL; AF174594; AAF04515.1; -; mRNA.
DR   CCDS; CCDS130.1; -.
DR   RefSeq; NP_036300.2; NM_012168.5.
DR   AlphaFoldDB; Q9UK22; -.
DR   SMR; Q9UK22; -.
DR   BioGRID; 117623; 441.
DR   ComplexPortal; CPX-7847; SCF E3 ubiquitin ligase complex, FBXO2 variant.
DR   FunCoup; Q9UK22; 792.
DR   IntAct; Q9UK22; 440.
DR   MINT; Q9UK22; -.
DR   NDEx; MUSIC2-C5212-FBXO2; Osteosarcoma (U2OS) cell map - C5212 (29 proteins).
DR   STRING; 9606.ENSP00000346240; -.
DR   GlyGen; Q9UK22; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9UK22; -.
DR   PhosphoSitePlus; Q9UK22; -.
DR   SwissPalm; Q9UK22; -.
DR   BioMuta; FBXO2; -.
DR   DMDM; 51338836; -.
DR   jPOST; Q9UK22; -.
DR   MassIVE; Q9UK22; -.
DR   PaxDb; 9606-ENSP00000346240; -.
DR   PeptideAtlas; Q9UK22; -.
DR   ProteomicsDB; 84707; -.
DR   Pumba; Q9UK22; -.
DR   Antibodypedia; 28127; 204 antibodies from 29 providers.
DR   DNASU; 26232; -.
DR   Ensembl; ENST00000354287.5; ENSP00000346240.4; ENSG00000116661.12.
DR   GeneID; 26232; -.
DR   KEGG; hsa:26232; -.
DR   MANE-Select; ENST00000354287.5; ENSP00000346240.4; NM_012168.6; NP_036300.2.
DR   UCSC; uc001asj.4; human.
DR   AGR; HGNC:13581; -.
DR   ClinPGx; PA31895; -.
DR   CTD; 26232; -.
DR   DisGeNET; 26232; -.
DR   GeneCards; FBXO2; -.
DR   HGNC; HGNC:13581; FBXO2.
DR   HPA; ENSG00000116661; Tissue enhanced (brain, pituitary gland).
DR   MIM; 607112; gene.
DR   OpenTargets; ENSG00000116661; -.
DR   VEuPathDB; HostDB:ENSG00000116661; -.
DR   eggNOG; ENOG502QS9C; Eukaryota.
DR   GeneTree; ENSGT00940000160929; -.
DR   HOGENOM; CLU_068548_0_0_1; -.
DR   InParanoid; Q9UK22; -.
DR   OMA; CLYELCV; -.
DR   OrthoDB; 1107553at2759; -.
DR   PAN-GO; Q9UK22; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9UK22; -.
DR   PathwayCommons; Q9UK22; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q9UK22; -.
DR   SIGNOR; Q9UK22; -.
DR   UniPathway; UPA00143; -.
DR   Agora; ENSG00000116661; -.
DR   BioGRID-ORCS; 26232; 19 hits in 1185 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; FBXO2; human.
DR   GeneWiki; FBXO2; -.
DR   GenomeRNAi; 26232; -.
DR   Pharos; Q9UK22; Tbio.
DR   PRO; PR:Q9UK22; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UK22; protein.
DR   Bgee; ENSG00000116661; Expressed in amygdala and 172 other cell types or tissues.
DR   ExpressionAtlas; Q9UK22; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR   GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:Ensembl.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0031249; F:denatured protein binding; IEA:Ensembl.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc.
DR   GO; GO:0036503; P:ERAD pathway; IBA:GO_Central.
DR   GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0099576; P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission; IEA:Ensembl.
DR   GO; GO:1904415; P:regulation of xenophagy; NAS:ComplexPortal.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   FunFam; 2.60.120.260:FF:000012; F-box only protein 2; 1.
DR   FunFam; 1.20.1280.50:FF:000002; F-box only protein 44; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR039752; F-box_only.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   PANTHER; PTHR12125:SF11; F-BOX ONLY PROTEIN 2; 1.
DR   PANTHER; PTHR12125; F-BOX ONLY PROTEIN 6-LIKE PROTEIN; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SMART; SM01198; FBA; 1.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Lectin; Membrane; Microsome;
KW   Proteomics identification; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..296
FT                   /note="F-box only protein 2"
FT                   /id="PRO_0000119875"
FT   DOMAIN          44..91
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   DOMAIN          113..296
FT                   /note="FBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00482"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..40
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         210..212
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         278..279
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   SITE            173
FT                   /note="Important for carbohydrate binding"
FT                   /evidence="ECO:0000250"
FT   VARIANT         118
FT                   /note="K -> T (in dbSNP:rs9614)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_049036"
FT   CONFLICT        45
FT                   /note="Missing (in Ref. 1; AAF01822)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="R -> C (in Ref. 2; CAG46907)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        163
FT                   /note="E -> D (in Ref. 2; CAG46907)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        275
FT                   /note="D -> G (in Ref. 7; AAF04515)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  33328 MW;  5226F19E27D884AF CRC64;
     MDGDGDPESV GQPEEASPEE QPEEASAEEE RPEDQQEEEA AAAAAYLDEL PEPLLLRVLA
     ALPAAELVQA CRLVCLRWKE LVDGAPLWLL KCQQEGLVPE GGVEEERDHW QQFYFLSKRR
     RNLLRNPCGE EDLEGWCDVE HGGDGWRVEE LPGDSGVEFT HDESVKKYFA SSFEWCRKAQ
     VIDLQAEGYW EELLDTTQPA IVVKDWYSGR SDAGCLYELT VKLLSEHENV LAEFSSGQVA
     VPQDSDGGGW MEISHTFTDY GPGVRFVRFE HGGQDSVYWK GWFGARVTNS SVWVEP
//