FBXW11

This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbws class and, in addition to an F-box, contains multiple WD40 repeats. This gene contains at least 14 exons, and its alternative splicing generates 3 transcript variants diverging at the presence/absence of two alternate exons. [provided by RefSeq]

F-box and WD repeat domain containing 11

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 regulation. 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. SCF(FBXW11) mediates the ubiquitination of CYTH1, and probably CYTH2 (PubMed:29420262).

(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.

Brain morphogenesis Source: GO_Central
Establishment of mitotic spindle orientation Source: GO_Central
Germ cell development Source: GO_Central
Microtubule organizing center organization Source: GO_Central
Negative regulation of transcription, DNA-templated Source: UniProtKB
Nuclear migration Source: GO_Central
Positive regulation of circadian rhythm Source: UniProtKB
Positive regulation of proteolysis Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
Protein dephosphorylation Source: UniProtKB
Protein destabilization Source: UniProtKB
Protein polyubiquitination Source: UniProtKB
Protein ubiquitination Source: UniProtKB
Regulation of microtubule motor activity Source: GO_Central
Retrograde axonal transport Source: GO_Central
Rhythmic process Source: UniProtKB-KW
SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
Vesicle transport along microtubule Source: GO_Central
Wnt signaling pathway Source: UniProtKB-KW

Nucleus; Cytoplasm

Neurodevelopmental, jaw, eye, and digital syndrome (NEDJED):
An autosomal dominant syndrome characterized by variable features including mild-to-severe developmental delay, speech delay, autistic and/or stereotypical behaviors, ocular anomalies, under- or overdeveloped jaw, and digital anomalies such as brachydactyly, clinodactyly, syndactyly, and contractures.