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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: F-box/WD repeat-containing protein 11

UniprotKB/SwissProt ID: Q9UKB1 (Q9UKB1)

Gene Name: FBXW11

Organism: Homo sapiens (Human)

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:10648623, PubMed:11158290, PubMed:19966869, PubMed:20347421, 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:19966869, PubMed:20347421, 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:10437795, PubMed:10644755, 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) (Microbial infection) Target of human immunodeficiency virus type 1 (HIV-1) protein VPU to polyubiquitinate and deplete BST2 from cells and antagonize its antiviral action

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR021977 Beta-TrCP_D
IPR036047 F-box-like_dom_sf
IPR001810 F-box_dom
IPR020472 G-protein_beta_WD-40_rep
IPR050995 WD-F-box_domain-protein
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR019775 WD40_repeat_CS
IPR036322 WD40_repeat_dom_sf
IPR001680 WD40_rpt

The S-nitrosylation sites of Q9UKB1

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 484 LDPRAPASTL C LRTLVEHSGR