FBW1B_HUMAN
ID FBW1B_HUMAN Reviewed; 542 AA.
AC Q9UKB1; B2RC98; Q9P2S8; Q9P2S9; Q9Y4C6;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=F-box/WD repeat-containing protein 11;
DE AltName: Full=F-box and WD repeats protein beta-TrCP2;
DE AltName: Full=F-box/WD repeat-containing protein 1B;
DE AltName: Full=Homologous to Slimb protein;
DE Short=HOS;
GN Name=FBXW11; Synonyms=BTRCP2, FBW1B, FBXW1B, KIAA0696;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Fetal lung;
RX PubMed=10694485; DOI=10.1006/bbrc.2000.2241;
RA Koike J., Sagara N., Kirikoshi H., Takagi A., Miwa T., Hirai M., Katoh M.;
RT "Molecular cloning and genomic structure of the betaTRCP2 gene on
RT chromosome 5q35.1.";
RL Biochem. Biophys. Res. Commun. 269:103-109(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC TISSUE=Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Lymph;
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 [6]
RP IDENTIFICATION IN THE SCF(FBXW11) COMPLEX.
RX PubMed=10066435; DOI=10.1006/bbrc.1999.0289;
RA Suzuki H., Chiba T., Kobayashi M., Takeuchi M., Suzuki T., Ichiyama A.,
RA Ikenoue T., Omata M., Furuichi K., Tanaka K.;
RT "IkappaBalpha ubiquitination is catalyzed by an SCF-like complex containing
RT Skp1, cullin-1, and two F-box/WD40-repeat proteins, betaTrCP1 and
RT betaTrCP2.";
RL Biochem. Biophys. Res. Commun. 256:127-132(1999).
RN [7]
RP INTERACTION WITH NFKBIA AND CTNNB1, AND FUNCTION IN UBIQUITINATION OF
RP NFKBIA AND CTNNB1.
RX PubMed=10321728; DOI=10.1038/sj.onc.1202760;
RA Fuchs S.Y., Chen A., Xiong Y., Pan Z.Q., Ronai Z.;
RT "HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and Cullin1
RT and targets the phosphorylation-dependent degradation of IkappaB and beta-
RT catenin.";
RL Oncogene 18:2039-2046(1999).
RN [8]
RP SELF-ASSOCIATION, INTERACTION WITH BTRC AND NFKBIA, AND FUNCTION IN
RP UBIQUITINATION OF NFKBIA.
RX PubMed=10644755; DOI=10.1074/jbc.275.4.2877;
RA Suzuki H., Chiba T., Suzuki T., Fujita T., Ikenoue T., Omata M.,
RA Furuichi K., Shikama H., Tanaka K.;
RT "Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to
RT IkappaBalpha for signal-dependent ubiquitination.";
RL J. Biol. Chem. 275:2877-2884(2000).
RN [9]
RP INTERACTION WITH PHOSPHORYLATED IFNAR1, AND FUNCTION IN IFNAR1
RP UBIQUITINATION.
RX PubMed=14532120; DOI=10.1093/emboj/cdg524;
RA Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E., Fuchs S.Y.;
RT "SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation of
RT the interferon-alpha receptor.";
RL EMBO J. 22:5480-5490(2003).
RN [10]
RP IDENTIFICATION IN THE SCF(FBXW11) COMPLEX, INTERACTION WITH NFKBIA, AND
RP FUNCTION IN UBIQUITINATION OF NFKBIA.
RX PubMed=10437795; DOI=10.1016/s0014-5793(99)00895-9;
RA Vuillard L., Nicholson J., Hay R.T.;
RT "A complex containing betaTrCP recruits Cdc34 to catalyse ubiquitination of
RT IkappaBalpha.";
RL FEBS Lett. 455:311-314(1999).
RN [11]
RP INTERACTION WITH IFNAR1.
RX PubMed=15337770; DOI=10.1074/jbc.m407082200;
RA Kumar K.G., Krolewski J.J., Fuchs S.Y.;
RT "Phosphorylation and specific ubiquitin acceptor sites are required for
RT ubiquitination and degradation of the IFNAR1 subunit of type I interferon
RT receptor.";
RL J. Biol. Chem. 279:46614-46620(2004).
RN [12]
RP INTERACTION WITH TRIM21.
RX PubMed=16880511; DOI=10.1128/mcb.01630-05;
RA Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
RA Krek W.;
RT "Regulation of p27 degradation and S-phase progression by Ro52 RING finger
RT protein.";
RL Mol. Cell. Biol. 26:5994-6004(2006).
RN [13]
RP FUNCTION OF THE SCF(FBXW11) COMPLEX.
RX PubMed=10648623; DOI=10.1128/mcb.20.4.1382-1393.2000;
RA Wu K., Fuchs S.Y., Chen A., Tan P., Gomez C., Ronai Z., Pan Z.Q.;
RT "The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct
RT domains within CUL1 for substrate targeting and ubiquitin ligation.";
RL Mol. Cell. Biol. 20:1382-1393(2000).
RN [14]
RP INDUCTION.
RX PubMed=11850814; DOI=10.1038/sj.onc.1205132;
RA Spiegelman V.S., Tang W., Katoh M., Slaga T.J., Fuchs S.Y.;
RT "Inhibition of HOS expression and activities by Wnt pathway.";
RL Oncogene 21:856-860(2002).
RN [15]
RP FUNCTION, AND INTERACTION WITH CDC25A.
RX PubMed=14603323; DOI=10.1038/nature02082;
RA Busino L., Donzelli M., Chiesa M., Guardavaccaro D., Ganoth D.,
RA Dorrello N.V., Hershko A., Pagano M., Draetta G.F.;
RT "Degradation of Cdc25A by beta-TrCP during S phase and in response to DNA
RT damage.";
RL Nature 426:87-91(2003).
RN [16]
RP FUNCTION IN CIRCADIAN CLOCK, AND INTERACTION WITH PER1 AND PER3.
RX PubMed=15917222; DOI=10.1074/jbc.m502862200;
RA Shirogane T., Jin J., Ang X.L., Harper J.W.;
RT "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-
RT dependent degradation of the mammalian period-1 (Per1) protein.";
RL J. Biol. Chem. 280:26863-26872(2005).
RN [17]
RP FUNCTION, AND INTERACTION WITH RCAN1.
RX PubMed=18575781;
RA Asada S., Ikeda A., Nagao R., Hama H., Sudo T., Fukamizu A., Kasuya Y.,
RA Kishi T.;
RT "Oxidative stress-induced ubiquitination of RCAN1 mediated by SCFbeta-TrCP
RT ubiquitin ligase.";
RL Int. J. Mol. Med. 22:95-104(2008).
RN [18]
RP INTERACTION WITH REST.
RX PubMed=18354482; DOI=10.1038/nature06641;
RA Guardavaccaro D., Frescas D., Dorrello N.V., Peschiaroli A., Multani A.S.,
RA Cardozo T., Lasorella A., Iavarone A., Chang S., Hernando E., Pagano M.;
RT "Control of chromosome stability by the beta-TrCP-REST-Mad2 axis.";
RL Nature 452:365-369(2008).
RN [19]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH BST2.
RX PubMed=19730691; DOI=10.1371/journal.ppat.1000574;
RA Mangeat B., Gers-Huber G., Lehmann M., Zufferey M., Luban J., Piguet V.;
RT "HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it
RT and directing its beta-TrCP2-dependent degradation.";
RL PLoS Pathog. 5:E1000574-E1000574(2009).
RN [20]
RP FUNCTION OF THE SCF(FBXW11) COMPLEX, AND INTERACTION WITH NFKBIA.
RX PubMed=20347421; DOI=10.1016/j.molcel.2010.02.025;
RA Wu K., Kovacev J., Pan Z.Q.;
RT "Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for
RT polyubiquitination on a SCF substrate.";
RL Mol. Cell 37:784-796(2010).
RN [21]
RP FUNCTION, AND INTERACTION WITH USP47.
RX PubMed=19966869; DOI=10.1038/onc.2009.430;
RA Peschiaroli A., Skaar J.R., Pagano M., Melino G.;
RT "The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor
RT regulating cell survival.";
RL Oncogene 29:1384-1393(2010).
RN [22]
RP FUNCTION, AND INTERACTION WITH CEP68.
RX PubMed=25503564; DOI=10.1038/ncb3076;
RA Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V., Florens L.,
RA Washburn M.P., Pagano M.;
RT "Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM
RT to allow centriole separation, disengagement and licensing.";
RL Nat. Cell Biol. 17:31-43(2015).
RN [23]
RP FUNCTION, AND INTERACTION WITH HOST FBXW11 (MICROBIAL INFECTION).
RX PubMed=26837067; DOI=10.1371/journal.ppat.1005437;
RA Mudhasani R., Tran J.P., Retterer C., Kota K.P., Whitehouse C.A.,
RA Bavari S.;
RT "Protein Kinase R degradation is essential for Rift valley fever Virus
RT infection and is regulated by SKP1-CUL1-F-box (SCF)FBXW11-NSs E3 ligase.";
RL PLoS Pathog. 12:E1005437-E1005437(2016).
RN [24]
RP FUNCTION, AND INTERACTION WITH INAVA.
RX PubMed=29420262; DOI=10.1126/science.aan0814;
RA Mohanan V., Nakata T., Desch A.N., Levesque C., Boroughs A., Guzman G.,
RA Cao Z., Creasey E., Yao J., Boucher G., Charron G., Bhan A.K., Schenone M.,
RA Carr S.A., Reinecker H.C., Daly M.J., Rioux J.D., Lassen K.G., Xavier R.J.;
RT "C1orf106 is a colitis risk gene that regulates stability of epithelial
RT adherens junctions.";
RL Science 359:1161-1166(2018).
RN [25]
RP DEVELOPMENTAL STAGE, INVOLVEMENT IN NEDJED, AND VARIANTS NEDJED ARG-242;
RP TRP-363; ASP-364; THR-365; LYS-444; GLN-447 AND LEU-447.
RX PubMed=31402090; DOI=10.1016/j.ajhg.2019.07.005;
RA Holt R.J., Young R.M., Crespo B., Ceroni F., Curry C.J., Bellacchio E.,
RA Bax D.A., Ciolfi A., Simon M., Fagerberg C.R., van Binsbergen E.,
RA De Luca A., Memo L., Dobyns W.B., Mohammed A.A., Clokie S.J.H.,
RA Zazo Seco C., Jiang Y.H., Soerensen K.P., Andersen H., Sullivan J.,
RA Powis Z., Chassevent A., Smith-Hicks C., Petrovski S., Antoniadi T.,
RA Shashi V., Gelb B.D., Wilson S.W., Gerrelli D., Tartaglia M., Chassaing N.,
RA Calvas P., Ragge N.K.;
RT "De novo missense variants in FBXW11 cause diverse developmental phenotypes
RT including brain, eye, and digit anomalies.";
RL Am. J. Hum. Genet. 105:640-657(2019).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins. SCF(FBXW11) mediates the ubiquitination of phosphorylated
CC CTNNB1 and participates in Wnt signaling regulation. SCF(FBXW11)
CC mediates the ubiquitination of phosphorylated NFKBIA, which degradation
CC frees the associated NFKB1 to translocate into the nucleus and to
CC activate transcription. SCF(FBXW11) mediates the ubiquitination of
CC IFNAR1. SCF(FBXW11) mediates the ubiquitination of CEP68; this is
CC required for centriole separation during mitosis (PubMed:25503564).
CC Involved in the oxidative stress-induced a ubiquitin-mediated decrease
CC in RCAN1. Mediates the degradation of CDC25A induced by ionizing
CC radiation in cells progressing through S phase and thus may function in
CC the intra-S-phase checkpoint. Has an essential role in the control of
CC the clock-dependent transcription via degradation of phosphorylated
CC PER1 and phosphorylated PER2. SCF(FBXW11) mediates the ubiquitination
CC of CYTH1, and probably CYTH2 (PubMed:29420262).
CC {ECO:0000269|PubMed:10321728, ECO:0000269|PubMed:10437795,
CC ECO:0000269|PubMed:10644755, ECO:0000269|PubMed:10648623,
CC ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:14603323,
CC ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18575781,
CC ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:20347421,
CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:29420262}.
CC -!- FUNCTION: (Microbial infection) Target of human immunodeficiency virus
CC type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from
CC cells and antagonize its antiviral action.
CC {ECO:0000269|PubMed:19730691}.
CC -!- SUBUNIT: Self-associates. Component of the SCF(FBXW11) complex formed
CC of CUL1, SKP1, RBX1 and a FBXW11 dimer. Interacts with BTRC, BST2,
CC PER1, RCAN1 and USP47. Interacts with phosphorylated ubiquitination
CC substrates CTNNB1, NFKBIA, IFNAR1, PER1 and PER2; the interaction
CC requires the phosphorylation of the two serine residues in the
CC substrates' destruction motif D-S-G-X(2,3,4)-S. Interacts with TRIM21.
CC Interacts with PER3. Interacts with phosphorylated ubiquitination
CC substrate CEP68 (PubMed:25503564). Interacts with INAVA
CC (PubMed:29420262). Interacts with REST (PubMed:18354482).
CC {ECO:0000269|PubMed:10066435, ECO:0000269|PubMed:10321728,
CC ECO:0000269|PubMed:10437795, ECO:0000269|PubMed:10644755,
CC ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:14603323,
CC ECO:0000269|PubMed:15337770, ECO:0000269|PubMed:15917222,
CC ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:18354482,
CC ECO:0000269|PubMed:18575781, ECO:0000269|PubMed:19730691,
CC ECO:0000269|PubMed:19966869, ECO:0000269|PubMed:20347421,
CC ECO:0000269|PubMed:25503564, ECO:0000269|PubMed:29420262}.
CC -!- SUBUNIT: (Microbial infection) Interact with Rift valley fever virus
CC NSs (via omegaXaV motif); this interaction is important for EIF2AK2/PKR
CC degradation. {ECO:0000269|PubMed:26837067}.
CC -!- INTERACTION:
CC Q9UKB1; Q5JTC6: AMER1; NbExp=4; IntAct=EBI-355189, EBI-6169747;
CC Q9UKB1; O15169: AXIN1; NbExp=4; IntAct=EBI-355189, EBI-710484;
CC Q9UKB1; P35222: CTNNB1; NbExp=4; IntAct=EBI-355189, EBI-491549;
CC Q9UKB1; Q13616: CUL1; NbExp=11; IntAct=EBI-355189, EBI-359390;
CC Q9UKB1; P32314: FOXN2; NbExp=4; IntAct=EBI-355189, EBI-10706164;
CC Q9UKB1; P17181: IFNAR1; NbExp=8; IntAct=EBI-355189, EBI-1547250;
CC Q9UKB1; Q3KP66: INAVA; NbExp=2; IntAct=EBI-355189, EBI-7545562;
CC Q9UKB1; Q00987: MDM2; NbExp=4; IntAct=EBI-355189, EBI-389668;
CC Q9UKB1; Q16236: NFE2L2; NbExp=2; IntAct=EBI-355189, EBI-2007911;
CC Q9UKB1; P25963: NFKBIA; NbExp=2; IntAct=EBI-355189, EBI-307386;
CC Q9UKB1; Q13127: REST; NbExp=3; IntAct=EBI-355189, EBI-926706;
CC Q9UKB1; P63208: SKP1; NbExp=10; IntAct=EBI-355189, EBI-307486;
CC Q9UKB1; P30291: WEE1; NbExp=3; IntAct=EBI-355189, EBI-914695;
CC Q9UKB1; Q60793: Klf4; Xeno; NbExp=4; IntAct=EBI-355189, EBI-3043905;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C;
CC IsoId=Q9UKB1-1; Sequence=Displayed;
CC Name=A;
CC IsoId=Q9UKB1-2; Sequence=VSP_006765;
CC Name=B;
CC IsoId=Q9UKB1-3; Sequence=VSP_006766;
CC -!- DEVELOPMENTAL STAGE: In the embryo, it is expressed in the developing
CC eye, limbs and brain (PubMed:31402090). Expression is observed in the
CC lens, retina, lips of the optic fissure closure and regions of the
CC conjunctiva at Carnegie stages (CS) between CS15 and CS21. As eye
CC development progresses, the stronger signal observed in the retina
CC progressively shifts from the inner toward the outer retinal layers
CC (PubMed:31402090). In the developing hand, expression is strong at
CC CS15. At CS19 and CS21, after the digits have begun to form, strong
CC expression is seen in the mesenchyme surrounding the developing
CC cartilage (PubMed:31402090). In the brain, it is expressed in the
CC primitive ventricles at CS17 and CS19, hypothalamus and medulla at
CC CS17, and metencephalon at CS19 (PubMed:31402090). Strong expression is
CC also observed in the pharyngeal arches, including the mandibular
CC process and tongue at CS17 (PubMed:31402090).
CC {ECO:0000269|PubMed:31402090}.
CC -!- INDUCTION: Expression is negatively regulated by Wnt/beta-catenin
CC pathway. {ECO:0000269|PubMed:11850814}.
CC -!- DOMAIN: The N-terminal D domain mediates homodimerization.
CC {ECO:0000250|UniProtKB:Q9Y297}.
CC -!- DISEASE: Neurodevelopmental, jaw, eye, and digital syndrome (NEDJED)
CC [MIM:618914]: An autosomal dominant syndrome characterized by variable
CC features including mild-to-severe developmental delay, speech delay,
CC autistic and/or stereotypical behaviors, ocular anomalies, under- or
CC overdeveloped jaw, and digital anomalies such as brachydactyly,
CC clinodactyly, syndactyly, and contractures.
CC {ECO:0000269|PubMed:31402090}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31671.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF176022; AAF04528.1; -; mRNA.
DR EMBL; AB033279; BAA92329.1; -; mRNA.
DR EMBL; AB033280; BAA92330.1; -; mRNA.
DR EMBL; AB033281; BAA92331.1; -; mRNA.
DR EMBL; AB014596; BAA31671.1; ALT_INIT; mRNA.
DR EMBL; AK314999; BAG37495.1; -; mRNA.
DR EMBL; BC026213; AAH26213.1; -; mRNA.
DR CCDS; CCDS34289.1; -. [Q9UKB1-1]
DR CCDS; CCDS47340.1; -. [Q9UKB1-2]
DR CCDS; CCDS47341.1; -. [Q9UKB1-3]
DR RefSeq; NP_036432.2; NM_012300.2. [Q9UKB1-1]
DR RefSeq; NP_387448.2; NM_033644.2. [Q9UKB1-3]
DR RefSeq; NP_387449.2; NM_033645.2. [Q9UKB1-2]
DR PDB; 6WNX; X-ray; 2.50 A; A/D/G=114-542.
DR PDBsum; 6WNX; -.
DR AlphaFoldDB; Q9UKB1; -.
DR SMR; Q9UKB1; -.
DR BioGRID; 116887; 466.
DR CORUM; Q9UKB1; -.
DR DIP; DIP-27593N; -.
DR ELM; Q9UKB1; -.
DR IntAct; Q9UKB1; 113.
DR MINT; Q9UKB1; -.
DR STRING; 9606.ENSP00000265094; -.
DR iPTMnet; Q9UKB1; -.
DR PhosphoSitePlus; Q9UKB1; -.
DR BioMuta; FBXW11; -.
DR DMDM; 13124267; -.
DR EPD; Q9UKB1; -.
DR jPOST; Q9UKB1; -.
DR MassIVE; Q9UKB1; -.
DR MaxQB; Q9UKB1; -.
DR PaxDb; Q9UKB1; -.
DR PeptideAtlas; Q9UKB1; -.
DR PRIDE; Q9UKB1; -.
DR ProteomicsDB; 84760; -. [Q9UKB1-1]
DR ProteomicsDB; 84761; -. [Q9UKB1-2]
DR ProteomicsDB; 84762; -. [Q9UKB1-3]
DR Antibodypedia; 28871; 250 antibodies from 29 providers.
DR DNASU; 23291; -.
DR Ensembl; ENST00000265094.9; ENSP00000265094.5; ENSG00000072803.18. [Q9UKB1-1]
DR Ensembl; ENST00000296933.10; ENSP00000296933.6; ENSG00000072803.18. [Q9UKB1-3]
DR Ensembl; ENST00000393802.6; ENSP00000377391.2; ENSG00000072803.18. [Q9UKB1-2]
DR GeneID; 23291; -.
DR KEGG; hsa:23291; -.
DR UCSC; uc003mbl.2; human. [Q9UKB1-1]
DR CTD; 23291; -.
DR DisGeNET; 23291; -.
DR GeneCards; FBXW11; -.
DR HGNC; HGNC:13607; FBXW11.
DR HPA; ENSG00000072803; Low tissue specificity.
DR MalaCards; FBXW11; -.
DR MIM; 605651; gene.
DR MIM; 618914; phenotype.
DR neXtProt; NX_Q9UKB1; -.
DR OpenTargets; ENSG00000072803; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA28050; -.
DR VEuPathDB; HostDB:ENSG00000072803; -.
DR eggNOG; KOG0281; Eukaryota.
DR GeneTree; ENSGT00940000155898; -.
DR HOGENOM; CLU_000288_103_6_1; -.
DR InParanoid; Q9UKB1; -.
DR OMA; KMCEQHI; -.
DR OrthoDB; 666965at2759; -.
DR PhylomeDB; Q9UKB1; -.
DR TreeFam; TF105679; -.
DR PathwayCommons; Q9UKB1; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9UKB1; -.
DR SIGNOR; Q9UKB1; -.
DR BioGRID-ORCS; 23291; 378 hits in 1132 CRISPR screens.
DR ChiTaRS; FBXW11; human.
DR GeneWiki; FBXW11; -.
DR GenomeRNAi; 23291; -.
DR Pharos; Q9UKB1; Tbio.
DR PRO; PR:Q9UKB1; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UKB1; protein.
DR Bgee; ENSG00000072803; Expressed in corpus callosum and 213 other tissues.
DR ExpressionAtlas; Q9UKB1; baseline and differential.
DR Genevisible; Q9UKB1; HS.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
DR GO; GO:0070840; F:dynein complex binding; IBA:GO_Central.
DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; NAS:UniProtKB.
DR GO; GO:0048854; P:brain morphogenesis; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0031023; P:microtubule organizing center organization; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IBA:GO_Central.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR021977; Beta-TrCP_D.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12125; Beta-TrCP_D; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01028; Beta-TrCP_D; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 5.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Biological rhythms; Cell cycle;
KW Cytoplasm; Disease variant; Host-virus interaction; Nucleus;
KW Reference proteome; Repeat; Ubl conjugation pathway; WD repeat;
KW Wnt signaling pathway.
FT CHAIN 1..542
FT /note="F-box/WD repeat-containing protein 11"
FT /id="PRO_0000050981"
FT DOMAIN 129..167
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REPEAT 238..275
FT /note="WD 1"
FT REPEAT 278..315
FT /note="WD 2"
FT REPEAT 318..355
FT /note="WD 3"
FT REPEAT 361..398
FT /note="WD 4"
FT REPEAT 401..440
FT /note="WD 5"
FT REPEAT 442..478
FT /note="WD 6"
FT REPEAT 490..527
FT /note="WD 7"
FT REGION 67..116
FT /note="Homodimerization domain D"
FT /evidence="ECO:0000250|UniProtKB:Q9Y297"
FT VAR_SEQ 16..49
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006765"
FT VAR_SEQ 16..48
FT /note="CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL -> NTSVMEDQNEDESPK
FT KNTLW (in isoform B)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006766"
FT VARIANT 242
FT /note="G -> R (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084385"
FT VARIANT 363
FT /note="R -> W (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084386"
FT VARIANT 364
FT /note="A -> D (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084387"
FT VARIANT 365
FT /note="A -> T (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084388"
FT VARIANT 444
FT /note="E -> K (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084389"
FT VARIANT 447
FT /note="R -> L (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084390"
FT VARIANT 447
FT /note="R -> Q (in NEDJED)"
FT /evidence="ECO:0000269|PubMed:31402090"
FT /id="VAR_084391"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 129..136
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 202..225
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6WNX"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 272..276
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 300..306
FT /evidence="ECO:0007829|PDB:6WNX"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 340..351
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 353..360
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:6WNX"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 395..399
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 406..412
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 415..420
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:6WNX"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 463..469
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 470..474
FT /evidence="ECO:0007829|PDB:6WNX"
FT HELIX 480..482
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:6WNX"
FT STRAND 512..521
FT /evidence="ECO:0007829|PDB:6WNX"
SQ SEQUENCE 542 AA; 62091 MW; 7CD40087EFAA5C8A CRC64;
MEPDSVIEDK TIELMCSVPR SLWLGCANLV ESMCALSCLQ SMPSVRCLQI SNGTSSVIVS
RKRPSEGNYQ KEKDLCIKYF DQWSESDQVE FVEHLISRMC HYQHGHINSY LKPMLQRDFI
TALPEQGLDH IAENILSYLD ARSLCAAELV CKEWQRVISE GMLWKKLIER MVRTDPLWKG
LSERRGWDQY LFKNRPTDGP PNSFYRSLYP KIIQDIETIE SNWRCGRHNL QRIQCRSENS
KGVYCLQYDD EKIISGLRDN SIKIWDKTSL ECLKVLTGHT GSVLCLQYDE RVIVTGSSDS
TVRVWDVNTG EVLNTLIHHN EAVLHLRFSN GLMVTCSKDR SIAVWDMASA TDITLRRVLV
GHRAAVNVVD FDDKYIVSAS GDRTIKVWST STCEFVRTLN GHKRGIACLQ YRDRLVVSGS
SDNTIRLWDI ECGACLRVLE GHEELVRCIR FDNKRIVSGA YDGKIKVWDL QAALDPRAPA
STLCLRTLVE HSGRVFRLQF DEFQIISSSH DDTILIWDFL NVPPSAQNET RSPSRTYTYI
SR
