E3 ubiquitin-protein ligase TRIM31 (TRIM31)

E3 ubiquitin-protein ligase TRIM31 (TRIM31) is an enzyme of the tripartite motif (TRIM) family, containing RING, B-box, and coiled-coil domains. It mediates ubiquitin-dependent proteasomal degradation of specific substrates and plays a crucial role in the regulation of the immune response, inflammation (notably as a negative regulator of the NLRP3 inflammasome), hematopoietic stem cell quiescence, cell cycle control, and autophagy. Abnormal TRIM31 expression or function is associated with cancer, infection, inflammatory disorders, cardiovascular and metabolic diseases. The protein’s dualistic role in cancer—as either a tumor suppressor or promoter—depends on cellular context and the specific signaling pathways involved, notably impacting p53, mTORC1, PI3K-AKT, NF-κB, and Wnt/β-catenin. Its critical regulatory functions and disease associations position TRIM31 as a potential, yet complex, therapeutic target.

Other names

Tripartite motif-containing protein 31C6orf13HCG1HCGIRNFTripartite motif containing 31

Promotes ubiquitination and proteasomal degradation of target proteins (such as NLRP3, p53, CDK8). Regulates K48- and K63-linked ubiquitination pathways.