F-box domain found in F-box only protein 38 (FBXO38) and similar proteins
FBXO38, also called FBX38, or modulator of KLF7 activity (MoKA), is part of an SCF (SKP1-cullin-F-box) protein ligase complex. It may coactivate the transcription factor Kruppel-like factor 7 (KLF7), but does not seem to promote KLF7 ubiquitination. FBXO38 acts as a crucial regulator of programmed cell death protein-1 (PD-1) protein turnover in T cells by mediating PD-1 ubiquitination and regulating anti-tumor immunity of T cells. 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:putative Skp1 binding site [polypeptide binding site]
Evidence:
Comment:based on the structure evidences that other F-box superfamily members interact with Skp1
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.
Jiyao W et al.(2023). "The conserved domain database in 2023.",