TRIM14 (tripartite motif containing 14) is a multifunctional protein that plays essential roles in innate immune defense and cellular regulation. As an antiviral factor, TRIM14 restricts flavivirus replication by colocalizing with viral proteins and acts as an interferon-stimulated gene mediating type I interferon responses against Langat and Zika viruses 1. The protein functions through multiple mechanisms involving protein-protein interactions and ubiquitin regulation. TRIM14 recruits the deubiquitinase USP14 to stabilize target proteins by removing K63-linked ubiquitin chains, thereby preventing their autophagic degradation 2. This TRIM14/USP14 axis is particularly important in cancer contexts, where it stabilizes PD-L1 to promote immune evasion 2 and protects GPX4 from ferroptotic degradation in hepatocellular carcinoma, contributing to radiotherapy resistance 3. In inflammatory conditions like psoriasis, TRIM14 is highly expressed and activates the NF-κB pathway by binding TRAF3 and mediating its autophagic degradation 4. TRIM14 also regulates cellular differentiation and apoptosis, with overexpression promoting apoptosis in embryonic development through activation of proapoptotic genes 5. The protein demonstrates consistent transcriptional regulatory effects across different mammalian cell types 6.