Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Diversity in tissue expression, substrate binding, and SCF complex formation for a lectin family of ubiquitin ligases.
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FBXO17 is a member of the FBA lectin family of F-box proteins; it does NOT bind high-mannose glycans but binds complex-type glycoproteins (e.g. lactoferrin) and sulfated glycans (heparin strongly, chondroitin sulfate weakly) via a conserved hydrophobic pocket in the FBA/G domain, and it assembles into a canonical SCF complex with SKP1, CUL1 and RBX1.
Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics.
A proteome-scale map of the human interactome network.
A High-Density Map for Navigating the Human Polycomb Complexome.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
The SCF Complex Is Essential to Maintain Genome and Chromosome Stability.
Multimodal cell maps as a foundation for structural and functional genomics.
AcM-UBE2M transfers NEDD8 to CRL1 E3 ubiquitin ligase complex
NEDD8:AcM-UBE2M binds CRL1 E3 ubiquitin ligase complex
CAND1 binds cytosolic CRL E3 ubiquitin ligases
COMMDs displace CAND1 from cytosolic CRL E3 ubiquitin ligase complexes
COP9 signalosome deneddylates cytosolic CRL E3 ubiquitin ligase complexes
MyrG-DCUN1D3 binds CRL1 E3 ubiquitin ligase complex
Transfer of Ub from E2 to substrate and release of E2
Release of E3 from polyubiquitinated substrate
Polyubiquitination of substrate
Interaction of E3 with substrate and E2-Ub complex
Falcon deep research report for human FBXO17
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FBXO17 (also known as FBG4) is the substrate-recognition adaptor of an SCF-type E3 ubiquitin ligase (SCF^FBXO17), with the ~40-aa F-box domain binding SKP1 to link the substrate-recognition module to the CUL1-RBX1 catalytic core.
"SCF E3 ubiquitin ligases use F-box proteins as substrate adaptors**; the ~40-aa **F-box domain** binds **SKP1**, linking the variable substrate-recognition module to the CUL1-RBX1 catalytic core."
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The best-validated FBXO17 substrate is the protein kinase GSK3-beta; SCF^FBXO17 associates with GSK3-beta, promotes its polyubiquitination, and drives proteasome-dependent turnover in lung epithelial cells.
"A detailed biochemical study in lung epithelial cells shows that **FBXO17 associates with GSK3β**, promotes **polyubiquitination** of GSK3β, and drives **proteasome-dependent turnover** of GSK3β."
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By degrading GSK3-beta, FBXO17 dampens GSK3-beta-dependent pro-inflammatory cytokine production; FBXO17 overexpression reduces TNF-alpha/LPS-induced IL-6 and KC/CXCL1, partially rescued by GSK3-beta re-expression.
"FBXO17 overexpression reduces **TNFα- and LPS-induced IL-6 and KC/CXCL1**."
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FBXO17 has a non-canonical, SCF-independent mode that does not require the F-box domain - it binds IRF3 and recruits PP2A to promote IRF3 dephosphorylation, negatively regulating type I interferon signaling.
"FBXO17 can regulate signaling **independently of its canonical SCF function** by recruiting **PP2A** to the transcription factor **IRF3** to promote IRF3 dephosphorylation and suppress type I interferon signaling. This is explicitly described as not requiring the F-box domain and using the "F-box associated region.""
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FBXO17 and its demonstrated substrate GSK3-beta colocalize in the cytoplasm, consistent with a cytoplasmic site of action.
"Direct experimental localization in the mechanistic SCF substrate study indicates **cytoplasmic colocalization** of FBXO17 with its demonstrated substrate GSK3β."