Tripartite motif-containing protein 3 (TRIM3)

Tripartite motif-containing protein 3 (TRIM3) is a cytoplasmic E3 ubiquitin ligase belonging to the TRIM-NHL protein family and characterized by a RING finger, two B-box domains, and a coiled-coil region[3][5]. TRIM3 acts as a tumor suppressor and is the human ortholog of the Drosophila 'brain tumor' (brat) protein[4]. It is involved in ubiquitination and degradation or stabilization of various substrate proteins, impacting cell cycle progression, growth suppression, and apoptosis regulation[2][3][4]. TRIM3 targets and ubiquitinates proteins such as P53, Estrogen receptor alpha, SLC7A11, and LDHA, thereby regulating tumorigenesis and metabolic adaptation in cancer cells[3][4]. Loss of TRIM3 expression is associated with increased cell proliferation, cancer stem cell phenotypes, resistance to apoptosis, and poor prognosis in several human cancers[4]. Additionally, TRIM3 may play a role in intracellular cargo transport via interaction with myosin V and alpha-actinin-4, and its domain structure allows complex regulation and protein-protein interactions typical of the diversified TRIM protein family[3][5][1].

Other names

BERPHAC1RNF22RNF97Brain-expressed RING finger proteinRING finger protein 22RING finger protein 97brain expressed ring fingertripartite motif protein TRIM3

Targeted protein ubiquitination (E3 ligase activity), Ubiquitination and degradation of specific substrates (e.g., P53, Estrogen receptor alpha, SLC7A11, lactate dehydrogenase A), Stabilization of target proteins via non-proteolytic ubiquitination