SCUBA

FBXL17 — F-box and leucine rich repeat protein 17

FBXL17 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

FBXL17's module in each cell type

Cell typeModuleShares the module with
MacrophagesEndosomal Rab Trafficking
Vesicular traficking
ABL1, ANKS1A, ARB2A, CAMK1D, CPEB3, DENND4C, DISC1, FTO +15 moreView in SCUBA
NeutrophilsGeneral Homeostatic Regulation
Housekeeping
ARID2, EXOC4, LARP4B, MCU, MGAT5, RAD51B, RASA1

About the gene

SynonymsDKFZP434C1715, Fbl17, Fbx13, FBXO13
Chromosome5: 107859035-108382098
Predicted locationIntracellular, Membrane
Essential geneNo
Protein classPredicted intracellular proteins, Predicted membrane proteins
Biological processNeurogenesis, Ubl conjugation pathway

Function

Substrate-recognition component of the SCF(FBXL17) E3 ubiquitin ligase complex, a key component of a quality control pathway required to ensure functional dimerization of BTB domain-containing proteins (dimerization quality control, DQC). FBXL17 specifically recognizes and binds a conserved degron of non-consecutive residues present at the interface of BTB dimers of aberrant composition: aberrant BTB dimer are then ubiquitinated by the SCF(FBXL17) complex and degraded by the proteasome. The ability of the SCF(FBXL17) complex to eliminate compromised BTB dimers is required for the differentiation and survival of neural crest and neuronal cells (By similarity). The SCF(FBXL17) complex mediates ubiquitination and degradation of BACH1. The SCF(FBXL17) complex is also involved in the regulation of the hedgehog/smoothened (Hh) signaling pathway by mediating the ubiquitination and degradation of SUFU, allowing the release of GLI1 from SUFU for proper Hh signal transduction. The SCF(FBXL17) complex mediates ubiquitination and degradation of PRMT1 (By similarity).

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.