E3 ubiquitin-protein ligase TRIM47 (TRIM47)

E3 ubiquitin-protein ligase TRIM47 is a member of the tripartite motif (TRIM) family characterized by a RING finger, B-box, and coiled-coil domains. It acts as an E3 ubiquitin ligase, mediating the ubiquitination and proteasomal degradation of substrate proteins such as CYLD, BRCA1, and those involved in NF-κB signaling[3][4][6]. TRIM47 regulates cellular processes like protein turnover, synaptic development (as a negative regulator of excitatory synapse formation), and cell proliferation. Overexpression or aberrant regulation of TRIM47 has been linked to several cancers, including breast, glioma, and pancreatic cancers, often correlating with therapy resistance and poor prognosis[1][4][6]. It is expressed in developing neurons, where its levels are activity- and NMDA receptor-dependent, indicating important functions in the nervous system, particularly during periods of synaptogenesis[1][2].

Other names

Tripartite motif-containing 47E3 ubiquitin-protein ligase TRIM47GOARNF100Gene overexpressed in astrocytoma proteinRING finger protein 100

Drugs (potential or experimental) would likely act by inhibiting TRIM47’s E3 ligase activity, interfering with its ability to mediate ubiquitination and proteasomal degradation of substrates such as CYLD, BRCA1, SMAD4, and PKC-ε[3][4][6]. Downregulation may restore expression or activity of tumor suppressors (e.g., BRCA1) or hinder oncogenic signaling (e.g., NF-κB pathway)[4][6].