TRIM3 Gene: Function, Expression, and Role in Cancer | NCBI, UniProt

TRIM3 (tripartite motif containing 3) encodes a member of the tripartite motif (TRIM) family, characterized by a RING finger domain, B-box zinc finger, and coiled-coil region. The protein functions as an E3 ubiquitin ligase involved in protein ubiquitination and degradation. TRIM3 acts as a tumor suppressor by regulating cell proliferation, migration, and invasion, particularly in gliomas and breast cancer. It also plays a role in neuronal development and synaptic function.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Ubiquitin mediated proteolysis (KEGG: hsa04120)

• p53 signaling pathway (KEGG: hsa04115) - indirect regulation

• PI3K-Akt signaling pathway (KEGG: hsa04151) - via AKT modulation

TRIM3 is a 744-amino acid protein with a molecular weight of approximately 84 kDa. It contains an N-terminal RING finger domain (required for E3 ubiquitin ligase activity), two B-box zinc fingers, a coiled-coil region, and a C-terminal NHL repeat domain. The protein localizes to both cytoplasm and nucleus. TRIM3 ubiquitinates target proteins such as p53 and β-catenin, promoting their degradation and thereby inhibiting cell cycle progression and migration. It is highly expressed in brain and testis, with lower levels in other tissues. Loss of TRIM3 expression is frequently observed in gliomas and various cancers, correlating with aggressive tumor behavior.