Tripartite motif-containing protein 7 (TRIM7)

Tripartite motif-containing protein 7 (TRIM7) is a member of the E3 ubiquitin ligase family and the TRIM protein family, characterized by a conserved RING-B-box-coiled-coil (RBCC) motif and a C-terminal PRY-SPRY (B30.2) domain[1][3][5]. TRIM7 localizes to both the nucleus and cytoplasm and acts as an enzyme that tags specific protein substrates with ubiquitin, leading to their degradation or functional modulation. It plays complex roles in antiviral immunity by targeting viral proteins for degradation and modulating innate immune pathways such as TLR4, NF-κB, and STING signaling[1][5]. TRIM7 also regulates processes including tumorigenesis (both suppressing and promoting, depending on cellular context), cell proliferation, apoptosis, and ferroptosis, with emerging evidence for roles in fibrosis and atherosclerosis[1][3][5]. TRIM7 is being investigated as a context-dependent biomarker and a potential therapeutic target in certain cancers, viral infections, and fibrotic diseases[3][5].

Other names

TRIM7GNIP1GNIP2GNIP3Tripartite motif containing 7E3 ubiquitin-protein ligase TRIM7

Mediates polyubiquitination (Lys-48, Lys-63 linked) of substrates leading to proteasomal degradation or stabilization. Targets viral proteins for ubiquitination, restricting or promoting viral replication depending on substrate.