FBXW5_HUMAN
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 03-AUG-2022, entry version 178.
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; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-741068, EBI-11957260;
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=4; 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_018998.3. [Q969U6-1]
DR AlphaFoldDB; Q969U6; -.
DR BioGRID; 119967; 160.
DR DIP; DIP-37971N; -.
DR IntAct; Q969U6; 48.
DR MINT; Q969U6; -.
DR STRING; 9606.ENSP00000313034; -.
DR iPTMnet; Q969U6; -.
DR PhosphoSitePlus; Q969U6; -.
DR BioMuta; FBXW5; -.
DR DMDM; 44887886; -.
DR EPD; Q969U6; -.
DR jPOST; Q969U6; -.
DR MassIVE; Q969U6; -.
DR MaxQB; Q969U6; -.
DR PaxDb; Q969U6; -.
DR PeptideAtlas; Q969U6; -.
DR PRIDE; Q969U6; -.
DR ProteomicsDB; 75846; -. [Q969U6-1]
DR ProteomicsDB; 75847; -. [Q969U6-2]
DR Antibodypedia; 32276; 163 antibodies from 23 providers.
DR DNASU; 54461; -.
DR Ensembl; ENST00000325285.8; ENSP00000313034.3; ENSG00000159069.14. [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 CTD; 54461; -.
DR DisGeNET; 54461; -.
DR GeneCards; FBXW5; -.
DR HGNC; HGNC:13613; FBXW5.
DR HPA; ENSG00000159069; Tissue enhanced (testis).
DR MIM; 609072; gene.
DR neXtProt; NX_Q969U6; -.
DR OpenTargets; ENSG00000159069; -.
DR PharmGKB; PA134928070; -.
DR VEuPathDB; HostDB:ENSG00000159069; -.
DR eggNOG; ENOG502QTGQ; Eukaryota.
DR GeneTree; ENSGT00730000111276; -.
DR HOGENOM; CLU_021121_0_0_1; -.
DR InParanoid; Q969U6; -.
DR OMA; LYKFYNR; -.
DR OrthoDB; 771384at2759; -.
DR PhylomeDB; Q969U6; -.
DR TreeFam; TF324320; -.
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 BioGRID-ORCS; 54461; 6 hits in 1116 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 147 other tissues.
DR ExpressionAtlas; Q969U6; baseline and differential.
DR Genevisible; Q969U6; HS.
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: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 Gene3D; 2.130.10.10; -; 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; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR20995; PTHR20995; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 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; Reference proteome;
KW Repeat; Ubl conjugation; Ubl conjugation pathway; 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
