Tripartite motif-containing protein 61 (TRIM61)

Tripartite motif-containing protein 61 (TRIM61) is a member of the TRIM family of proteins, characterized by an N-terminal tripartite motif featuring a RING-type zinc finger, one or two B-box domains, and a coiled-coil region[1][7]. TRIM61 is predicted to function as an E3 ubiquitin-protein ligase, participating in protein ubiquitination and regulation of gene expression, particularly in the context of innate immune responses[2][6][7]. It is encoded by the TRIM61 gene (also known as RNF35) and shares structural features common to the TRIM protein family, which is involved in various cellular processes including transcriptional regulation and antiviral defense[1][2][7]. Genetic associations have linked TRIM61 with Bardet-Biedl syndrome 11 and Leber Plus disease, though there is limited evidence for direct disease causation[2]. Currently, there are no drugs known to specifically target TRIM61, nor is it established as a biomarker or drug safety risk.

Other names

RNF35RING finger protein 35Putative tripartite motif-containing protein 61