Tripartite motif-containing protein 14 (TRIM14)

Tripartite motif-containing protein 14 (TRIM14) is a member of the TRIM protein family, characterized by a B-box 2 domain, a coiled-coil domain, and a C-terminal PRY-SPRY domain, but uniquely lacking the classical N-terminal RING domain common in other TRIM proteins[1][2][3]. This distinguishes it as generally deficient in E3 ubiquitin ligase activity; however, emerging evidence suggests potential alternative modes of regulating ubiquitination. TRIM14 acts as a mitochondrial adaptor protein, crucial for assembling the antiviral MAVS signalosome upon detection of viral RNA, facilitating downstream activation of IRF3 and NF-κB and promoting the type I interferon response[1]. TRIM14 is inducible by interferon and participates in regulating the innate immune response, as well as pathways related to cell proliferation, differentiation, morphogenesis, and autophagy[3]. Pathologically, aberrant TRIM14 expression is associated with cancer, inflammatory, cardiovascular, and infectious diseases, making it a potential biomarker and emerging therapeutic target[2]. No approved drugs currently target TRIM14 directly.

Other names

Tripartite motif containing 14TRIM14KIAA0129tripartite motif protein TRIM14TRIM14 (Pub in mouse)