TRIM1s

TRIM1s, also known as Tripartite Motif 1s, refers to a specific subfamily within the larger TRIM (Tripartite Motif) protein family. These proteins are characterized by the presence of three conserved domains: a RING domain, a B-box domain, and a coiled-coil domain. The TRIM1s subfamily is distinguished by variations in the C-terminal domain following the coiled-coil. TRIM proteins are involved in a wide range of cellular processes, including immunity, cell cycle regulation, and DNA damage response.

The precise functions of TRIM1s are still under active investigation, but they are thought to act as E3 ubiquitin ligases, meaning they play a role in the ubiquitization of target proteins. This process of adding ubiquitin molecules can alter the function, localization, or degradation of the target protein. Research has implicated TRIM1s in various cellular pathways, and their dysregulation has been linked to certain diseases, though specific causal relationships are still being elucidated. Studies exploring the roles of individual TRIM1s proteins continue to expand our understanding of their contribution to cellular homeostasis and disease pathogenesis.