FBX2_HUMAN
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 03-AUG-2022, entry version 179.
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; P63208: SKP1; NbExp=11; 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; 432.
DR IntAct; Q9UK22; 33.
DR MINT; Q9UK22; -.
DR STRING; 9606.ENSP00000346240; -.
DR GlyGen; Q9UK22; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UK22; -.
DR PhosphoSitePlus; Q9UK22; -.
DR BioMuta; FBXO2; -.
DR DMDM; 51338836; -.
DR EPD; Q9UK22; -.
DR jPOST; Q9UK22; -.
DR MassIVE; Q9UK22; -.
DR MaxQB; Q9UK22; -.
DR PaxDb; Q9UK22; -.
DR PeptideAtlas; Q9UK22; -.
DR PRIDE; Q9UK22; -.
DR ProteomicsDB; 84707; -.
DR Antibodypedia; 28127; 204 antibodies from 30 providers.
DR DNASU; 26232; -.
DR Ensembl; ENST00000354287.5; ENSP00000346240.4; ENSG00000116661.11.
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 CTD; 26232; -.
DR DisGeNET; 26232; -.
DR GeneCards; FBXO2; -.
DR HGNC; HGNC:13581; FBXO2.
DR HPA; ENSG00000116661; Group enriched (brain, choroid plexus, pancreas, pituitary gland).
DR MIM; 607112; gene.
DR neXtProt; NX_Q9UK22; -.
DR OpenTargets; ENSG00000116661; -.
DR PharmGKB; PA31895; -.
DR VEuPathDB; HostDB:ENSG00000116661; -.
DR eggNOG; ENOG502QS9C; Eukaryota.
DR GeneTree; ENSGT00940000160929; -.
DR HOGENOM; CLU_068548_0_0_1; -.
DR InParanoid; Q9UK22; -.
DR OMA; YEWCRKA; -.
DR OrthoDB; 922544at2759; -.
DR PhylomeDB; Q9UK22; -.
DR TreeFam; TF320527; -.
DR PathwayCommons; Q9UK22; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UK22; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26232; 19 hits in 1109 CRISPR screens.
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 170 other tissues.
DR ExpressionAtlas; Q9UK22; baseline and differential.
DR Genevisible; Q9UK22; HS.
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:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0004842; F:ubiquitin-protein transferase activity; TAS:ProtInc.
DR GO; GO:0006516; P:glycoprotein catabolic process; ISS:UniProtKB.
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:0031396; P:regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
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; PTHR12125; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF04300; FBA; 1.
DR SMART; SM01198; FBA; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF81383; SSF81383; 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 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 17..36
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
