E3 ubiquitin-protein ligase TRIM17 (TRIM17)

E3 ubiquitin-protein ligase TRIM17 is a member of the tripartite motif (TRIM) family, characterized by an N-terminal RING finger domain, two B-box zinc fingers, and a coiled-coil region, often followed by a C-terminal PRY-SPRY domain[2][5]. TRIM17 is primarily expressed in the testis and certain brain regions, and it is strongly induced under cellular stress[1][2]. As an E3 ligase, TRIM17 promotes proteasome-dependent substrate degradation, regulates key processes such as cell proliferation (by targeting kinetochore proteins like ZWINT), initiates neuronal apoptosis (notably through MCL1 degradation), and controls autophagy and transcription factor stability (NFATc3, ZSCAN21)[2][3][4][5]. Notably, TRIM17 can form hetero-oligomers with other TRIM proteins, either antagonizing or enhancing their ubiquitin ligase activities, adding a layer of regulatory flexibility to ubiquitin signaling[2][5]. Pathologically, TRIM17 upregulation is associated with neurodegeneration, autism, and tumor chemoresistance, and it may contribute to Parkinson’s disease by modulating alpha-synuclein transcription[1][2][6]. No approved drugs directly target TRIM17, but it is considered a potential therapeutic target due to its central roles in cell death and disease mechanisms[2][3].

Other names

TRIM17RBCCRNF16TERFRING finger protein 16Testis RING finger proteinTripartite motif-containing protein 17ring finger protein terf

Targeted protein degradation (modulates proteasomal degradation of substrate proteins via ubiquitination); Dual E3 ligase modulation (can stabilize or degrade substrates depending on context and partner proteins)