E3 ubiquitin-protein ligase (PubMed:27667714). Positively regulates the NF-kappa-B signaling pathway (PubMed:27667714, PubMed:28073078). (Microbial infection) Exhibits antiviral activity against Japanese encephalitis virus (JEV). Ubiquitinates the viral non-structural protein 2 (NS2A) and targets it for proteasome-mediated degradation. S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. Protein modification; protein ubiquitination. (Microbial infection) Interacts with Japanese encephalitis virus non-structural protein 2 (NS2A); mediates the ubiquitination of NS2A, targeting it for proteasome-mediated degradation. Up-regulated by Golgi stress-inducing agents such nigericin, trichostatin, tetoposide, campothecin and brefeldin A (PubMed:31133683). Up-regulated by IL1B/interleukin-1 beta and TNFA/TNF-alpha (PubMed:28073078). The RING-type zinc finger domain is essential for its E3 ubiquitin-protein ligase activity, ability to positively regulate the NF-kappa-B signaling pathway and its antiviral activity. Autoubiquitinated (PubMed:27667714). Polyubiquitinated (PubMed:20596523, PubMed:27667714). Undergoes extremely rapid proteolytic degradation by the proteasome (PubMed:31133683). Arose via a partial duplication of the TRIM41 gene, followed by independent loss or pseudogenization of TRIM52 in multiple mammalian and primate lineages. Belongs to the TRIM/RBCC family. Truncated N-terminus.