This short domain is commonly found at the N-terminus of various proteins, and typically co-occurs with one or more other conserved domains or motifs, such as leucine rich repeats, WD40 repeats, kelch, tub, spry, and others. The F-box domain has a role in mediating protein-protein interactions in a variety of contexts, such as polyubiquitination, transcription elongation, centromere binding and translational repression. One of the best researched roles of F-box proteins is their participation in SCF (Skp1-Cul1-F-box protein), a multi-protein complex that functions as a ubiquitin E3 ligase, where the role of the F-box protein is to recruit target substrates. Gene families containing the F-box are found greatly expanded in narrow taxonomic lineages, such as flowering plants and nematodes. In this hierarchical classification, many of the subfamilies are named according to their domain architectures.
Feature 1:Skp1 binding site [polypeptide binding site]
Evidence:
Comment:F-box proteins participate in SCF (Skp1-Cul1-F-box protein) complexes that function as ubiquitin E3 ligases, where the role of the F-box protein is to recruit target substrates.
Structure:2E31; Mus musculus FBXO2 in complex with Skp1, contacts at 4A
Jiyao W et al.(2023). "The conserved domain database in 2023.",