Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Identification of a family of human F-box proteins.
A Competitive binding mechanism between Skp1 and exportin 1 (CRM1) controls the localization of a subset of F-box proteins.
A proteome-scale map of the human interactome network.
A High-Density Map for Navigating the Human Polycomb Complexome.
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.
FBXO2/SCF ubiquitin ligase complex directs xenophagy through recognizing bacterial surface glycan.
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FBXO2, a glycoprotein-specific SCF substrate receptor, recognizes GlcNAc side chains of the group A Streptococcus surface carbohydrate and promotes ubiquitin-mediated xenophagy; FBXO2 knockout decreases ubiquitin accumulation and xenophagic degradation of bacteria. FBXO2/FBXO6/FBXO27 are FBA-family lectins that bind high-mannose N-glycoproteins and act as ERAD ubiquitin-ligase subunits.
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 FBXO2
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FBXO2/Fbs1 is the substrate-recognition adaptor of an SCF (SKP1-CUL1-RBX1-FBXO2) E3 ligase, not itself an enzyme; the F-box binds SKP1 and the C-terminal domain binds substrate while RBX1-associated E2 executes ubiquitin transfer.
"FBXO2 is best understood as a **substrate-recognition adaptor** that confers specificity to an SCF E3 ligase complex (SKP1–CUL1–RBX1–FBXO2). In this architecture, the **F-box** binds **SKP1**, which bridges to **CUL1/RBX1**, while FBXO2's C-terminal region binds the substrate; ubiquitin transfer is executed by the RBX1-associated E2 enzyme."
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FBXO2 recognizes a glycan-based degron, binding the innermost N-glycan core (Man3GlcNAc2) through a small hydrophobic pocket, preferring high-mannose N-glycans on denatured/misfolded glycoproteins.
"it binds the **innermost N-glycan core** (described as **Man3GlcNAc2** / innermost GlcNAc2 moiety) using a **small hydrophobic pocket** in its SBD, with preference for **high-mannose N-glycans** and **denatured/misfolded glycoproteins** (where the core glycan becomes accessible)."
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Lectin-type F-box proteins such as FBXO2 act in the nucleocytoplasmic compartment on retrotranslocated ER glycoproteins as part of ERAD.
"lectin-type F-box proteins such as FBXO2 are described as operating in the **nucleocytoplasmic compartment**, where they can recognize **retrotranslocated ER glycoproteins** and promote their ubiquitination as part of **ER-associated degradation (ERAD)** and broader proteostasis mechanisms."
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Glycoprotein quality-control substrates cited for the Fbs1/Fbs2 pathway include integrin beta-1, TCRalpha, asialoglycoprotein receptor H2a, and CFTR-deltaF508.
"Examples of glycoprotein targets/processes cited in the mechanistic literature include **integrin β1, TCRα, asialoglycoprotein receptor H2a**, and **CFTRΔF508** as glycoproteins in the orbit of Fbs1/Fbs2-mediated quality control."
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FBXO2 mediates clearance of damaged lysosomes (lysophagy) in CNS contexts; loss delays clearance and exacerbates neurodegeneration in a Niemann-Pick C model.
"Fbxo2 functions as part of an SCF complex and **mediates clearance of damaged lysosomes** in CNS contexts. Loss of Fbxo2 **delayed clearance of damaged lysosomes** and reduced viability after lysosomal damage in mouse primary cortical cultures; in an NPC disease model, Fbxo2 deficiency **exacerbated neurodegeneration and reduced survival**."