Has an E3 ubiquitin ligase activity (PubMed:19349376, PubMed:31123703). Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation (PubMed:19349376). May ubiquitinate BBS2 (PubMed:22500027). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation (PubMed:31123703). (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo (PubMed:7778269). Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo (PubMed:7778269). 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. It self-associates (PubMed:19349376). Interacts with DTNBP1 (PubMed:19349376). Interacts with PIAS4/PIASY upon treatment with UVB and TNF-alpha (By similarity). Interacts with AMBRA1; promoting activation of ULK1 through unanchored 'Lys-63'-linked polyubiquitin chains (PubMed:31123703). (Microbial infection) Interacts with S.typhimurium protein SseK3; SseK3 does not glycosylate TRIM32. Localized in cytoplasmic bodies, often located around the nucleus. Spleen, thymus, prostate, testis, ovary, intestine, colon and skeletal muscle. Ubiquitinated. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. It has been suggested that TRIM32 might be the E3 ubiquitin ligase for BBS2, a component of the BBSome complex involved in ciliogenesis, that is ubiquitinated and degraded by the proteasome (PubMed:22500027). Belongs to the TRIM/RBCC family. TRIM32