F-box domain found in the F-box associated (FBA) family of F-box proteins
The F-box associated (FBA) family is composed of FBXO2, FBXO6, FBXO17, FBXO27, and FBXO44, which contain a conserved G domain that mediates substrate binding. Members of this family play diverse roles in glycoprotein quality control. They bind high mannose and sulfated glycoproteins, with one FBA protein, FBXO44, failing to bind any glycans on the tested arrays. FBA proteins are components of canonical SCF (Skp1, Cullin1, and Rbx1) complexes, yet FBXO2 bound very little Cullin1, suggesting that FBXO2 may exist primarily as a heterodimer with Skp1. 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.
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:3WSO; Homo sapiens FBXO44 in complex with Skp1, contacts at 4A