Ubiquitylation is commonly mediated by 3 enzymes: ubiquitin‐activating enzyme (E1), ubiquitin‐conjugating enzyme (E2), and ubiquitin ligase (E3).[59] Among the ubiquitin enzymes, E3s play a crucial role in attaching ub to target proteins and regulating various tumors by modulating the stability of key proteins.[60] Based on a comprehensive analysis of the previous experimental results, we found that the E3 ubiquitin ligase RNF25 may participate in the ubiquitination of FKBP8 by binding to circSATB1 and FKBP8, thereby regulating the biological functions of CRC cells. This evidence concerns the gene PRKN and colorectal carcinoma.