FBXW11 Antibody (Center) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9UKB1 |
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Clone Names | 81028038 |
Gene ID | 23291 |
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Other Names | 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, FBXW11, BTRCP2, FBW1B, FBXW1B, KIAA0696 |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | FBXW11 {ECO:0000303|PubMed:26837067, ECO:0000312|HGNC:HGNC:13607} |
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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 (PubMed:10437795, PubMed:11158290, PubMed:10648623, PubMed:20347421, PubMed:19966869, PubMed:22017875, PubMed:22017876, PubMed:36608670). Probably recognizes and binds to phosphorylated target proteins: the interaction with substrates requires the phosphorylation of the two serine residues in the substrates' destruction motif D-S-G-X(2,3,4)-S (PubMed:10437795, PubMed:10648623, PubMed:20347421, PubMed:19966869, PubMed:22017875, PubMed:22017876, PubMed:36608670). SCF(FBXW11) mediates the ubiquitination of phosphorylated CTNNB1 and participates in Wnt signaling regulation (PubMed:10321728). SCF(FBXW11) plays a key role in NF-kappa-B activation by mediating ubiquitination of phosphorylated NFKBIA, leading to its degradation by the proteasome, thereby allowing the associated NF-kappa-B complex to translocate into the nucleus and to activate transcription (PubMed:10321728, PubMed:10644755, PubMed:10437795, PubMed:20347421). The SCF(FBXW11) complex also regulates NF-kappa-B by mediating ubiquitination of phosphorylated NFKB1: specifically ubiquitinates the p105 form of NFKB1, leading to its degradation (PubMed:11158290). SCF(FBXW11) mediates the ubiquitination of IFNAR1 (PubMed:14532120, PubMed:15337770). 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 (PubMed:18575781). 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 (PubMed:14603323). Has an essential role in the control of the clock-dependent transcription via degradation of phosphorylated PER1 and phosphorylated PER2 (PubMed:15917222). SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2 (PubMed:29420262). SCF(FBXW11) acts as a regulator of mTORC1 signaling pathway by catalyzing ubiquitination and subsequent proteasomal degradation of phosphorylated DEPTOR, TFE3 and MITF (PubMed:22017875, PubMed:22017876, PubMed:36608670). |
Cellular Location | Cytoplasm {ECO:0000250|UniProtKB:Q5SRY7}. Nucleus {ECO:0000250|UniProtKB:Q5SRY7} |
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Background
This gene encodes a member of the F-box protein familywhich is characterized by an approximately 40 amino acid motif, theF-box. The F-box proteins constitute one of the four subunits ofubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box),which function in phosphorylation-dependent ubiquitination. TheF-box proteins are divided into 3 classes: Fbws containing WD-40domains, Fbls containing leucine-rich repeats, and Fbxs containingeither different protein-protein interaction modules or norecognizable motifs. The protein encoded by this gene belongs tothe Fbws class and, in addition to an F-box, contains multiple WD40repeats. This gene contains at least 14 exons, and its alternativesplicing generates 3 transcript variants diverging at thepresence/absence of two alternate exons.
References
Peschiaroli, A., et al. Oncogene 29(9):1384-1393(2010)Lievens, S., et al. J. Proteome Res. 8(2):877-886(2009)Ewing, R.M., et al. Mol. Syst. Biol. 3, 89 (2007) :Peschiaroli, A., et al. Mol. Cell 23(3):319-329(2006)Sabile, A., et al. Mol. Cell. Biol. 26(16):5994-6004(2006)
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