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F-box/WD repeat-containing protein 11 (F-box and WD repeats protein beta-TrCP2) (F-box/WD repeat-containing protein 1B) (Homologous to Slimb protein) (HOS)

 FBW1B_HUMAN             Reviewed;         542 AA.
Q9UKB1; B2RC98; Q9P2S8; Q9P2S9; Q9Y4C6;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 178.
RecName: Full=F-box/WD repeat-containing protein 11;
AltName: Full=F-box and WD repeats protein beta-TrCP2;
AltName: Full=F-box/WD repeat-containing protein 1B;
AltName: Full=Homologous to Slimb protein;
Short=HOS;
Name=FBXW11; Synonyms=BTRCP2, FBW1B, FBXW1B, KIAA0696;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10531035; DOI=10.1016/S0960-9822(00)80020-2;
Cenciarelli C., Chiaur D.S., Guardavaccaro D., Parks W., Vidal M.,
Pagano M.;
"Identification of a family of human F-box proteins.";
Curr. Biol. 9:1177-1179(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Fetal lung;
PubMed=10694485; DOI=10.1006/bbrc.2000.2241;
Koike J., Sagara N., Kirikoshi H., Takagi A., Miwa T., Hirai M.,
Katoh M.;
"Molecular cloning and genomic structure of the betaTRCP2 gene on
chromosome 5q35.1.";
Biochem. Biophys. Res. Commun. 269:103-109(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION IN THE SCF(FBXW11) COMPLEX.
PubMed=10066435; DOI=10.1006/bbrc.1999.0289;
Suzuki H., Chiba T., Kobayashi M., Takeuchi M., Suzuki T.,
Ichiyama A., Ikenoue T., Omata M., Furuichi K., Tanaka K.;
"IkappaBalpha ubiquitination is catalyzed by an SCF-like complex
containing Skp1, cullin-1, and two F-box/WD40-repeat proteins,
betaTrCP1 and betaTrCP2.";
Biochem. Biophys. Res. Commun. 256:127-132(1999).
[7]
INTERACTION WITH NFKBIA AND CTNNB1, AND FUNCTION IN UBIQUITINATION OF
NFKBIA AND CTNNB1.
PubMed=10321728; DOI=10.1038/sj.onc.1202760;
Fuchs S.Y., Chen A., Xiong Y., Pan Z.Q., Ronai Z.;
"HOS, a human homolog of Slimb, forms an SCF complex with Skp1 and
Cullin1 and targets the phosphorylation-dependent degradation of
IkappaB and beta-catenin.";
Oncogene 18:2039-2046(1999).
[8]
SELF-ASSOCIATION, INTERACTION WITH BTRC AND NFKBIA, AND FUNCTION IN
UBIQUITINATION OF NFKBIA.
PubMed=10644755; DOI=10.1074/jbc.275.4.2877;
Suzuki H., Chiba T., Suzuki T., Fujita T., Ikenoue T., Omata M.,
Furuichi K., Shikama H., Tanaka K.;
"Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to
IkappaBalpha for signal-dependent ubiquitination.";
J. Biol. Chem. 275:2877-2884(2000).
[9]
INTERACTION WITH PHOSPHORYLATED IFNAR1, AND FUNCTION IN IFNAR1
UBIQUITINATION.
PubMed=14532120; DOI=10.1093/emboj/cdg524;
Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E.,
Fuchs S.Y.;
"SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation
of the interferon-alpha receptor.";
EMBO J. 22:5480-5490(2003).
[10]
IDENTIFICATION IN THE SCF(FBXW11) COMPLEX, INTERACTION WITH NFKBIA,
AND FUNCTION IN UBIQUITINATION OF NFKBIA.
PubMed=10437795; DOI=10.1016/S0014-5793(99)00895-9;
Vuillard L., Nicholson J., Hay R.T.;
"A complex containing betaTrCP recruits Cdc34 to catalyse
ubiquitination of IkappaBalpha.";
FEBS Lett. 455:311-314(1999).
[11]
INTERACTION WITH IFNAR1.
PubMed=15337770; DOI=10.1074/jbc.M407082200;
Kumar K.G., Krolewski J.J., Fuchs S.Y.;
"Phosphorylation and specific ubiquitin acceptor sites are required
for ubiquitination and degradation of the IFNAR1 subunit of type I
interferon receptor.";
J. Biol. Chem. 279:46614-46620(2004).
[12]
INTERACTION WITH TRIM21.
PubMed=16880511; DOI=10.1128/MCB.01630-05;
Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M.,
Krek W.;
"Regulation of p27 degradation and S-phase progression by Ro52 RING
finger protein.";
Mol. Cell. Biol. 26:5994-6004(2006).
[13]
FUNCTION OF THE SCF(FBXW11) COMPLEX.
PubMed=10648623; DOI=10.1128/MCB.20.4.1382-1393.2000;
Wu K., Fuchs S.Y., Chen A., Tan P., Gomez C., Ronai Z., Pan Z.Q.;
"The SCF(HOS/beta-TRCP)-ROC1 E3 ubiquitin ligase utilizes two distinct
domains within CUL1 for substrate targeting and ubiquitin ligation.";
Mol. Cell. Biol. 20:1382-1393(2000).
[14]
INDUCTION.
PubMed=11850814; DOI=10.1038/sj.onc.1205132;
Spiegelman V.S., Tang W., Katoh M., Slaga T.J., Fuchs S.Y.;
"Inhibition of HOS expression and activities by Wnt pathway.";
Oncogene 21:856-860(2002).
[15]
FUNCTION, AND INTERACTION WITH CDC25A.
PubMed=14603323; DOI=10.1038/nature02082;
Busino L., Donzelli M., Chiesa M., Guardavaccaro D., Ganoth D.,
Dorrello N.V., Hershko A., Pagano M., Draetta G.F.;
"Degradation of Cdc25A by beta-TrCP during S phase and in response to
DNA damage.";
Nature 426:87-91(2003).
[16]
FUNCTION IN CIRCADIAN CLOCK, AND INTERACTION WITH PER1 AND PER3.
PubMed=15917222; DOI=10.1074/jbc.M502862200;
Shirogane T., Jin J., Ang X.L., Harper J.W.;
"SCFbeta-TRCP controls clock-dependent transcription via casein kinase
1-dependent degradation of the mammalian period-1 (Per1) protein.";
J. Biol. Chem. 280:26863-26872(2005).
[17]
FUNCTION, AND INTERACTION WITH RCAN1.
PubMed=18575781;
Asada S., Ikeda A., Nagao R., Hama H., Sudo T., Fukamizu A.,
Kasuya Y., Kishi T.;
"Oxidative stress-induced ubiquitination of RCAN1 mediated by SCFbeta-
TrCP ubiquitin ligase.";
Int. J. Mol. Med. 22:95-104(2008).
[18]
FUNCTION, AND INTERACTION WITH BST2.
PubMed=19730691; DOI=10.1371/journal.ppat.1000574;
Mangeat B., Gers-Huber G., Lehmann M., Zufferey M., Luban J.,
Piguet V.;
"HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding
it and directing its beta-TrCP2-dependent degradation.";
PLoS Pathog. 5:E1000574-E1000574(2009).
[19]
FUNCTION OF THE SCF(FBXW11) COMPLEX, AND INTERACTION WITH NFKBIA.
PubMed=20347421; DOI=10.1016/j.molcel.2010.02.025;
Wu K., Kovacev J., Pan Z.Q.;
"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for
polyubiquitination on a SCF substrate.";
Mol. Cell 37:784-796(2010).
[20]
FUNCTION, AND INTERACTION WITH USP47.
PubMed=19966869; DOI=10.1038/onc.2009.430;
Peschiaroli A., Skaar J.R., Pagano M., Melino G.;
"The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor
regulating cell survival.";
Oncogene 29:1384-1393(2010).
[21]
FUNCTION, AND INTERACTION WITH CEP68.
PubMed=25503564; DOI=10.1038/ncb3076;
Pagan J.K., Marzio A., Jones M.J., Saraf A., Jallepalli P.V.,
Florens L., Washburn M.P., Pagano M.;
"Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from
the PCM to allow centriole separation, disengagement and licensing.";
Nat. Cell Biol. 17:31-43(2015).
-!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-
box protein) E3 ubiquitin-protein ligase complex which mediates
the ubiquitination and subsequent proteasomal degradation of
target proteins. Probably recognizes and binds to phosphorylated
target proteins. SCF(FBXW11) mediates the ubiquitination of
phosphorylated CTNNB1 and participates in Wnt signaling.
SCF(FBXW11) mediates the ubiquitination of phosphorylated NFKBIA,
which degradation frees the associated NFKB1 to translocate into
the nucleus and to activate transcription. SCF(FBXW11) mediates
the ubiquitination of IFNAR1. SCF(FBXW11) mediates the
ubiquitination of CEP68; this is required for centriole separation
during mitosis (PubMed:25503564). Involved in the oxidative
stress-induced a ubiquitin-mediated decrease in RCAN1. Mediates
the degradation of CDC25A induced by ionizing radiation in cells
progressing through S phase and thus may function in the intra-S-
phase checkpoint. Has an essential role in the control of the
clock-dependent transcription via degradation of phosphorylated
PER1 and phosphorylated PER2. Is target of human immunodeficiency
virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete
BST2 from cells and antagonize its antiviral action.
{ECO:0000269|PubMed:10321728, ECO:0000269|PubMed:10437795,
ECO:0000269|PubMed:10644755, ECO:0000269|PubMed:10648623,
ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:14603323,
ECO:0000269|PubMed:15917222, ECO:0000269|PubMed:18575781,
ECO:0000269|PubMed:19730691, ECO:0000269|PubMed:19966869,
ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:25503564}.
-!- SUBUNIT: Self-associates. Component of the SCF(FBXW11) complex
formed of CUL1, SKP1, RBX1 and a FBXW11 dimer. Interacts with
BTRC, BST2, PER1, RCAN1 and USP47. Interacts with phosphorylated
ubiquitination substrates CTNNB1, NFKBIA, IFNAR1, PER1 and PER2;
the interaction requires the phosphorylation of the two serine
residues in the substrates' destruction motif D-S-G-X(2,3,4)-S.
Interacts with TRIM21. Interacts with PER3. Interacts with
phosphorylated ubiquitination substrate CEP68 (PubMed:25503564).
{ECO:0000269|PubMed:10066435, ECO:0000269|PubMed:10321728,
ECO:0000269|PubMed:10437795, ECO:0000269|PubMed:10644755,
ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:14603323,
ECO:0000269|PubMed:15337770, ECO:0000269|PubMed:15917222,
ECO:0000269|PubMed:16880511, ECO:0000269|PubMed:18575781,
ECO:0000269|PubMed:19730691, ECO:0000269|PubMed:19966869,
ECO:0000269|PubMed:20347421, ECO:0000269|PubMed:25503564}.
-!- INTERACTION:
Q5JTC6:AMER1; NbExp=4; IntAct=EBI-355189, EBI-6169747;
O15169:AXIN1; NbExp=4; IntAct=EBI-355189, EBI-710484;
P35222:CTNNB1; NbExp=4; IntAct=EBI-355189, EBI-491549;
Q13616:CUL1; NbExp=4; IntAct=EBI-355189, EBI-359390;
P32314:FOXN2; NbExp=4; IntAct=EBI-355189, EBI-10706164;
P17181:IFNAR1; NbExp=8; IntAct=EBI-355189, EBI-1547250;
Q60793:Klf4 (xeno); NbExp=4; IntAct=EBI-355189, EBI-3043905;
Q00987:MDM2; NbExp=4; IntAct=EBI-355189, EBI-389668;
P25963:NFKBIA; NbExp=2; IntAct=EBI-355189, EBI-307386;
Q15653:NFKBIB; NbExp=2; IntAct=EBI-355189, EBI-352889;
Q13127:REST; NbExp=3; IntAct=EBI-355189, EBI-926706;
P63208:SKP1; NbExp=7; IntAct=EBI-355189, EBI-307486;
P30291:WEE1; NbExp=3; IntAct=EBI-355189, EBI-914695;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=C;
IsoId=Q9UKB1-1; Sequence=Displayed;
Name=A;
IsoId=Q9UKB1-2; Sequence=VSP_006765;
Name=B;
IsoId=Q9UKB1-3; Sequence=VSP_006766;
-!- INDUCTION: Expression is negatively regulated by Wnt/beta-catenin
pathway. {ECO:0000269|PubMed:11850814}.
-!- DOMAIN: The N-terminal D domain mediates homodimerization.
{ECO:0000250}.
-!- SEQUENCE CAUTION:
Sequence=BAA31671.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF176022; AAF04528.1; -; mRNA.
EMBL; AB033279; BAA92329.1; -; mRNA.
EMBL; AB033280; BAA92330.1; -; mRNA.
EMBL; AB033281; BAA92331.1; -; mRNA.
EMBL; AB014596; BAA31671.1; ALT_INIT; mRNA.
EMBL; AK314999; BAG37495.1; -; mRNA.
EMBL; BC026213; AAH26213.1; -; mRNA.
CCDS; CCDS34289.1; -. [Q9UKB1-1]
CCDS; CCDS47340.1; -. [Q9UKB1-2]
CCDS; CCDS47341.1; -. [Q9UKB1-3]
RefSeq; NP_036432.2; NM_012300.2. [Q9UKB1-1]
RefSeq; NP_387448.2; NM_033644.2. [Q9UKB1-3]
RefSeq; NP_387449.2; NM_033645.2. [Q9UKB1-2]
UniGene; Hs.484138; -.
ProteinModelPortal; Q9UKB1; -.
SMR; Q9UKB1; -.
BioGrid; 116887; 413.
CORUM; Q9UKB1; -.
DIP; DIP-27593N; -.
ELM; Q9UKB1; -.
IntAct; Q9UKB1; 51.
MINT; MINT-120522; -.
STRING; 9606.ENSP00000265094; -.
iPTMnet; Q9UKB1; -.
PhosphoSitePlus; Q9UKB1; -.
BioMuta; FBXW11; -.
DMDM; 13124267; -.
EPD; Q9UKB1; -.
PaxDb; Q9UKB1; -.
PeptideAtlas; Q9UKB1; -.
PRIDE; Q9UKB1; -.
DNASU; 23291; -.
Ensembl; ENST00000265094; ENSP00000265094; ENSG00000072803. [Q9UKB1-1]
Ensembl; ENST00000296933; ENSP00000296933; ENSG00000072803. [Q9UKB1-3]
Ensembl; ENST00000393802; ENSP00000377391; ENSG00000072803. [Q9UKB1-2]
GeneID; 23291; -.
KEGG; hsa:23291; -.
UCSC; uc003mbl.2; human. [Q9UKB1-1]
CTD; 23291; -.
DisGeNET; 23291; -.
EuPathDB; HostDB:ENSG00000072803.17; -.
GeneCards; FBXW11; -.
HGNC; HGNC:13607; FBXW11.
HPA; HPA062578; -.
HPA; HPA072204; -.
MIM; 605651; gene.
neXtProt; NX_Q9UKB1; -.
OpenTargets; ENSG00000072803; -.
PharmGKB; PA28050; -.
eggNOG; KOG0281; Eukaryota.
eggNOG; ENOG410XTA8; LUCA.
GeneTree; ENSGT00760000119106; -.
HOGENOM; HOG000006638; -.
HOVERGEN; HBG002521; -.
InParanoid; Q9UKB1; -.
KO; K03362; -.
OMA; RLISRMC; -.
OrthoDB; EOG091G0437; -.
PhylomeDB; Q9UKB1; -.
TreeFam; TF105679; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; Q9UKB1; -.
SIGNOR; Q9UKB1; -.
ChiTaRS; FBXW11; human.
GeneWiki; FBXW11; -.
GenomeRNAi; 23291; -.
PRO; PR:Q9UKB1; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000072803; -.
CleanEx; HS_FBXW11; -.
ExpressionAtlas; Q9UKB1; baseline and differential.
Genevisible; Q9UKB1; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; NAS:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR021977; Beta-TrCP_D.
InterPro; IPR001810; F-box_dom.
InterPro; IPR036047; F-box_dom_like.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12125; Beta-TrCP_D; 1.
Pfam; PF12937; F-box-like; 1.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM01028; Beta-TrCP_D; 1.
SMART; SM00256; FBOX; 1.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
SUPFAM; SSF81383; SSF81383; 1.
PROSITE; PS50181; FBOX; 1.
PROSITE; PS00678; WD_REPEATS_1; 5.
PROSITE; PS50082; WD_REPEATS_2; 7.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Alternative splicing; Biological rhythms; Cell cycle;
Complete proteome; Cytoplasm; Nucleus; Reference proteome; Repeat;
Ubl conjugation pathway; WD repeat; Wnt signaling pathway.
CHAIN 1 542 F-box/WD repeat-containing protein 11.
/FTId=PRO_0000050981.
DOMAIN 129 167 F-box. {ECO:0000255|PROSITE-
ProRule:PRU00080}.
REPEAT 238 275 WD 1.
REPEAT 278 315 WD 2.
REPEAT 318 355 WD 3.
REPEAT 361 398 WD 4.
REPEAT 401 440 WD 5.
REPEAT 442 478 WD 6.
REPEAT 490 527 WD 7.
REGION 67 116 Homodimerization domain D. {ECO:0000250}.
VAR_SEQ 16 49 Missing (in isoform A).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_006765.
VAR_SEQ 16 48 CSVPRSLWLGCANLVESMCALSCLQSMPSVRCL -> NTSV
MEDQNEDESPKKNTLW (in isoform B).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_006766.
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


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