ID   FBXW5_HUMAN             Reviewed;         566 AA.
AC   Q969U6; B2RDZ6; Q59ET5; Q5SPZ8; Q5SPZ9; Q5SQ00; Q5SQ02; Q5SQ03; Q5SQ04;
AC   Q8WY79; Q96GJ6; Q9BSU8; Q9H6A8; Q9HBQ6; Q9NSZ3;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   10-JUN-2026, entry version 196.
DE   RecName: Full=F-box/WD repeat-containing protein 5;
DE   AltName: Full=F-box and WD-40 domain-containing protein 5;
GN   Name=FBXW5; Synonyms=FBW5; ORFNames=PP3971;
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 [LARGE SCALE MRNA] (ISOFORM 1).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Cervix, Colon, Ovary, Placenta, and Skin;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-566 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-566 (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-566 (ISOFORM 1).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [8]
RP   FUNCTION, INTERACTION WITH TSC1 AND TSC2, AND IDENTIFICATION IN A DCX
RP   PROTEIN LIGASE COMPLEX.
RX   PubMed=18381890; DOI=10.1101/gad.1624008;
RA   Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J., Xiong Y.;
RT   "WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by
RT   DDB1-CUL4-ROC1 ligase.";
RL   Genes Dev. 22:866-871(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=19232515; DOI=10.1016/j.bbrc.2009.02.052;
RA   Minoda Y., Sakurai H., Kobayashi T., Yoshimura A., Takaesu G.;
RT   "An F-box protein, FBXW5, negatively regulates TAK1 MAP3K in the IL-1beta
RT   signaling pathway.";
RL   Biochem. Biophys. Res. Commun. 381:412-417(2009).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SASS6 AND CDC20,
RP   IDENTIFICATION IN A SCF PROTEIN LIGASE COMPLEX, DEVELOPMENTAL STAGE,
RP   UBIQUITINATION, PHOSPHORYLATION AT SER-151, AND MUTAGENESIS OF SER-151.
RX   PubMed=21725316; DOI=10.1038/ncb2282;
RA   Puklowski A., Homsi Y., Keller D., May M., Chauhan S., Kossatz U.,
RA   Grunwald V., Kubicka S., Pich A., Manns M.P., Hoffmann I., Gonczy P.,
RA   Malek N.P.;
RT   "The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6
RT   to control centrosome duplication.";
RL   Nat. Cell Biol. 13:1004-1009(2011).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
CC   -!- FUNCTION: Substrate recognition component of both SCF (SKP1-CUL1-F-box
CC       protein) and DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase
CC       complexes. Substrate recognition component of the SCF(FBXW5) E3
CC       ubiquitin-protein ligase complex which mediates the ubiquitination and
CC       subsequent proteasomal degradation of SASS6 during S phase, leading to
CC       prevent centriole reduplication. The SCF(FBXW5) complex also mediates
CC       ubiquitination and degradation of actin-regulator EPS8 during G2 phase,
CC       leading to the transient degradation of EPS8 and subsequent cell shape
CC       changes required to allow mitotic progression. Substrate-specific
CC       adapter of the DCX(FBXW5) E3 ubiquitin-protein ligase complex which
CC       mediates the polyubiquitination and subsequent degradation of TSC2. May
CC       also act as a negative regulator of MAP3K7/TAK1 signaling in the
CC       interleukin-1B (IL1B) signaling pathway. {ECO:0000269|PubMed:18381890,
CC       ECO:0000269|PubMed:19232515, ECO:0000269|PubMed:21725316}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC       complex SCF(FBXW5) composed of CUL1, SKP1, RBX1 and FBXW5. Component of
CC       the DCX(FBXW5) E3 ubiquitin ligase complex, at least composed of (CUL4A
CC       or CUL4B), DDB1, FBXW5 and RBX1. Interacts with CDC20, EPS8, TSC1, TSC2
CC       and SASS6. Interacts with TNFAIP8L1; TNFAIP8L1 competes with TSC2 to
CC       bind FBXW5 increasing TSC2 stability by preventing its ubiquitination.
CC       {ECO:0000250|UniProtKB:Q9QXW2, ECO:0000269|PubMed:18381890,
CC       ECO:0000269|PubMed:21725316}.
CC   -!- INTERACTION:
CC       Q969U6; Q6UY14-3: ADAMTSL4; NbExp=6; IntAct=EBI-741068, EBI-10173507;
CC       Q969U6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-741068, EBI-3867333;
CC       Q969U6; O95967: EFEMP2; NbExp=3; IntAct=EBI-741068, EBI-743414;
CC       Q969U6; P98095: FBLN2; NbExp=3; IntAct=EBI-741068, EBI-947973;
CC       Q969U6; Q15323: KRT31; NbExp=6; IntAct=EBI-741068, EBI-948001;
CC       Q969U6; O76011: KRT34; NbExp=5; IntAct=EBI-741068, EBI-1047093;
CC       Q969U6; O76014: KRT37; NbExp=3; IntAct=EBI-741068, EBI-1045716;
CC       Q969U6; Q6A162: KRT40; NbExp=3; IntAct=EBI-741068, EBI-10171697;
CC       Q969U6; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-741068, EBI-11749135;
CC       Q969U6; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-741068, EBI-10171774;
CC       Q969U6; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-741068, EBI-10172052;
CC       Q969U6; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-741068, EBI-11953334;
CC       Q969U6; Q9BYQ7: KRTAP4-1; NbExp=3; IntAct=EBI-741068, EBI-34579671;
CC       Q969U6; Q3LI67: KRTAP6-3; NbExp=3; IntAct=EBI-741068, EBI-22311199;
CC       Q969U6; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-741068, EBI-1043191;
CC       Q969U6; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-741068, EBI-10185730;
CC       Q969U6; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-741068, EBI-10172526;
CC       Q969U6; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-741068, EBI-11522433;
CC       Q969U6; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-741068, EBI-945833;
CC       Q969U6; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-741068, EBI-22310682;
CC       Q969U6; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-741068, EBI-742388;
CC       Q969U6; P63208: SKP1; NbExp=8; IntAct=EBI-741068, EBI-307486;
CC       Q969U6; P14373: TRIM27; NbExp=6; IntAct=EBI-741068, EBI-719493;
CC       Q969U6; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-741068, EBI-11957238;
CC       Q969U6-1; Q16531: DDB1; NbExp=3; IntAct=EBI-16031873, EBI-350322;
CC       Q969U6-1; Q12929: EPS8; NbExp=3; IntAct=EBI-16031873, EBI-375576;
CC       Q969U6-1; P63208-1: SKP1; NbExp=3; IntAct=EBI-16031873, EBI-307497;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21725316}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q969U6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q969U6-2; Sequence=VSP_009479, VSP_009480;
CC   -!- DEVELOPMENTAL STAGE: Degraded by the APC/C complex during G1 phase and
CC       reaccumulates at the G1/S phase transition.
CC       {ECO:0000269|PubMed:21725316}.
CC   -!- DOMAIN: The F-box domain mediates interaction with components of SCF
CC       (SKP1-CUL1-F-box protein) complexes, while WD repeats mediate
CC       interaction with components of DCX (DDB1-CUL4-X-box) complexes.
CC       {ECO:0000305}.
CC   -!- DOMAIN: The D-box (destruction box) mediate the interaction with APC
CC       proteins, and acts as a recognition signal for degradation via the
CC       ubiquitin-proteasome pathway. {ECO:0000250}.
CC   -!- PTM: Phosphorylated at Ser-151 by PLK4 during the G1/S transition,
CC       leading to inhibit its ability to ubiquitinate SASS6.
CC       {ECO:0000269|PubMed:21725316}.
CC   -!- PTM: Ubiquitinated and degraded by the APC/C complex during mitosis and
CC       G1 phase. {ECO:0000269|PubMed:21725316}.
CC   -!- SIMILARITY: Belongs to the FBXW5 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG17240.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAG23772.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAH00850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK026081; BAB15354.1; -; mRNA.
DR   EMBL; AK315738; BAG38093.1; -; mRNA.
DR   EMBL; CH471090; EAW88307.1; -; Genomic_DNA.
DR   EMBL; BC000850; AAH00850.1; ALT_INIT; mRNA.
DR   EMBL; BC004541; AAH04541.2; -; mRNA.
DR   EMBL; BC009429; AAH09429.1; -; mRNA.
DR   EMBL; BC014297; AAH14297.1; -; mRNA.
DR   EMBL; AL807752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014130; AAH14130.1; -; mRNA.
DR   EMBL; AB209726; BAD92963.1; -; mRNA.
DR   EMBL; AL137631; CAB70851.1; -; mRNA.
DR   EMBL; AF217998; AAG17240.1; ALT_FRAME; mRNA.
DR   EMBL; AF258569; AAG23772.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS7014.1; -. [Q969U6-1]
DR   PIR; T46483; T46483.
DR   RefSeq; NP_061871.1; NM_018998.4. [Q969U6-1]
DR   AlphaFoldDB; Q969U6; -.
DR   BioGRID; 119967; 192.
DR   ComplexPortal; CPX-7762; SCF E3 ubiquitin ligase complex, FBXW5 variant.
DR   DIP; DIP-37971N; -.
DR   FunCoup; Q969U6; 419.
DR   IntAct; Q969U6; 128.
DR   MINT; Q969U6; -.
DR   NDEx; MUSIC2-C5179-FBXW5; Osteosarcoma (U2OS) cell map - Mitochondrial ribosome (68 proteins).
DR   STRING; 9606.ENSP00000313034; -.
DR   BindingDB; Q969U6; -.
DR   GlyGen; Q969U6; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR   iPTMnet; Q969U6; -.
DR   PhosphoSitePlus; Q969U6; -.
DR   BioMuta; FBXW5; -.
DR   DMDM; 44887886; -.
DR   jPOST; Q969U6; -.
DR   MassIVE; Q969U6; -.
DR   PaxDb; 9606-ENSP00000313034; -.
DR   PeptideAtlas; Q969U6; -.
DR   ProteomicsDB; 75846; -. [Q969U6-1]
DR   ProteomicsDB; 75847; -. [Q969U6-2]
DR   Pumba; Q969U6; -.
DR   Antibodypedia; 32276; 157 antibodies from 23 providers.
DR   DNASU; 54461; -.
DR   Ensembl; ENST00000325285.8; ENSP00000313034.3; ENSG00000159069.15. [Q969U6-1]
DR   Ensembl; ENST00000940105.1; ENSP00000610164.1; ENSG00000159069.15. [Q969U6-1]
DR   GeneID; 54461; -.
DR   KEGG; hsa:54461; -.
DR   MANE-Select; ENST00000325285.8; ENSP00000313034.3; NM_018998.4; NP_061871.1.
DR   UCSC; uc004cjx.4; human. [Q969U6-1]
DR   AGR; HGNC:13613; -.
DR   ClinPGx; PA134928070; -.
DR   CTD; 54461; -.
DR   DisGeNET; 54461; -.
DR   GeneCards; FBXW5; -.
DR   HGNC; HGNC:13613; FBXW5.
DR   HPA; ENSG00000159069; Tissue enhanced (testis).
DR   MIM; 609072; gene.
DR   OpenTargets; ENSG00000159069; -.
DR   VEuPathDB; HostDB:ENSG00000159069; -.
DR   eggNOG; ENOG502QTGQ; Eukaryota.
DR   GeneTree; ENSGT00730000111276; -.
DR   HOGENOM; CLU_021121_0_0_1; -.
DR   InParanoid; Q969U6; -.
DR   OMA; NPRDSEM; -.
DR   OrthoDB; 192402at2759; -.
DR   PAN-GO; Q969U6; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; Q969U6; -.
DR   PathwayCommons; Q969U6; -.
DR   Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q969U6; -.
DR   SIGNOR; Q969U6; -.
DR   UniPathway; UPA00143; -.
DR   Agora; ENSG00000159069; -.
DR   BioGRID-ORCS; 54461; 19 hits in 1192 CRISPR screens.
DR   ChiTaRS; FBXW5; human.
DR   GeneWiki; FBXW5; -.
DR   GenomeRNAi; 54461; -.
DR   Pharos; Q969U6; Tbio.
DR   PRO; PR:Q969U6; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q969U6; protein.
DR   Bgee; ENSG00000159069; Expressed in right testis and 149 other cell types or tissues.
DR   ExpressionAtlas; Q969U6; baseline and differential.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0051298; P:centrosome duplication; NAS:ComplexPortal.
DR   GO; GO:0060271; P:cilium assembly; NAS:ComplexPortal.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IEA:Ensembl.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   CDD; cd22132; F-box_FBXW5; 1.
DR   FunFam; 1.20.1280.50:FF:000032; F-box/WD repeat-containing protein 5 isoform X1; 1.
DR   FunFam; 2.130.10.10:FF:000305; F-box/WD repeat-containing protein 5 isoform X1; 1.
DR   FunFam; 2.130.10.10:FF:000335; F-box/WD repeat-containing protein 5 isoform X1; 1.
DR   Gene3D; 1.20.1280.50; -; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR042508; FBXW5.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   PANTHER; PTHR20995; F-BOX/WD REPEAT-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR20995:SF17; F-BOX_WD REPEAT-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF12937; F-box-like; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF81383; F-box domain; 1.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway;
KW   WD repeat.
FT   CHAIN           1..566
FT                   /note="F-box/WD repeat-containing protein 5"
FT                   /id="PRO_0000050992"
FT   DOMAIN          3..49
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT   REPEAT          83..125
FT                   /note="WD 1"
FT   REPEAT          126..178
FT                   /note="WD 2"
FT   REPEAT          179..238
FT                   /note="WD 3"
FT   REPEAT          239..281
FT                   /note="WD 4"
FT   REPEAT          394..447
FT                   /note="WD 5"
FT   REPEAT          458..501
FT                   /note="WD 6"
FT   REPEAT          502..539
FT                   /note="WD 7"
FT   MOTIF           303..311
FT                   /note="D-box"
FT   MOD_RES         151
FT                   /note="Phosphoserine; by PLK4"
FT                   /evidence="ECO:0000269|PubMed:21725316"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         367..377
FT                   /note="IKQILPHQMTT -> TPLPPCCPPRS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_009479"
FT   VAR_SEQ         378..566
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_009480"
FT   VARIANT         340
FT                   /note="E -> K (in dbSNP:rs7850438)"
FT                   /id="VAR_053393"
FT   MUTAGEN         151
FT                   /note="S->A: Impairs phosphorylation by PLK4 and enhances
FT                   ubiquitination of SASS6."
FT                   /evidence="ECO:0000269|PubMed:21725316"
FT   CONFLICT        490
FT                   /note="D -> G (in Ref. 1; BAB15354)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        508
FT                   /note="R -> Q (in Ref. 5; BAD92963)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   566 AA;  63922 MW;  7D389AB6F50193B1 CRC64;
     MDEGGTPLLP DSLVYQIFLS LGPADVLAAG LVCRQWQAVS RDEFLWREQF YRYYQVARDV
     PRHPAAMSWY EEFQRLYDTV PCVEVQTLRE HTDQVLHLSF SHSGYQFASC SKDCTVKIWS
     NDLTISLLHS ADMRPYNWSY TQFSQFNKDD SLLLASGVFL GPHNSSSGEI AVISLDSFAL
     LSRVRNKPYD VFGCWLTETS LISGNLHRIG DITSCSVLWL NNAFQDVESE NVNVVKRLFK
     IQNLNASTVR TVMVADCSRF DSPDLLLEAG DPATSPCRIF DLGSDNEEVV AGPAPAHAKE
     GLRHFLDRVL EGRAQPQLSE RMLETKVAEL LAQGHTKPPE RSATGAKSKY LIFTTGCLTY
     SPHQIGIKQI LPHQMTTAGP VLGEGRGSDA FFDALDHVID IHGHIIGMGL SPDNRYLYVN
     SRAWPNGAVV ADPMQPPPIA EEIDLLVFDL KTMREVRRAL RAHRAYTPND ECFFIFLDVS
     RDFVASGAED RHGYIWDRHY NICLARLRHE DVVNSVVFSP QEQELLLTAS DDATIKAWRS
     PRTMRVLQAP RPRPRTFFSW LASQRR
//