E3 ubiquitin-protein ligase TRIM45 (TRIM45)

E3 ubiquitin-protein ligase TRIM45 is an enzyme that catalyzes the transfer of ubiquitin to substrate proteins, specifically mediating K63-linked ubiquitination. It belongs to the tripartite motif (TRIM) family, characterized by a RING-finger domain, B-box domains, and a coiled-coil motif, plus a filamin-type immunoglobulin domain at its C-terminus[1][3]. TRIM45 is highly expressed in the brain and other tissues, and acts as a tumor suppressor by stabilizing p53 and inhibiting cell proliferation in cancers such as glioblastoma[1][2]. It negatively regulates MAPK and NF-κB signaling, contributes to cell cycle control, and modulates apoptosis and inflammation. TRIM45 may act as a transcriptional repressor and interacts with substrates such as p53 and TAB2[1][3][4]. Reduced TRIM45 function is linked to increased tumorigenicity and aggressive cancer phenotypes, making it a potential biomarker and emerging therapeutic target in oncology[2][5].

Other names

TRIM45RNF99RING finger protein 99FLJ13181

Not directly targeted by approved drugs; modulation of TRIM45 affects protein stability (especially p53), cell proliferation, and apoptosis. Drugs or tool compounds that influence ubiquitination could indirectly impact TRIM45 function