TRIM15
Description
The TRIM15 (tripartite motif containing 15) is a protein-coding gene located on chromosome 6.
TRIM15 is a protein encoded by the TRIM15 gene in humans. It belongs to the tripartite motif (TRIM) family, characterized by three zinc-binding domains: a RING, a B-box type 1, and a B-box type 2, as well as a coiled-coil region. TRIM15 localizes to the cytoplasm. Its specific function remains unknown. Alternative splicing of the TRIM15 gene leads to two transcript variants encoding different isoforms.
TRIM15 is an E3 ubiquitin ligase that plays a role in various biological processes, including innate antiviral immunity, cell migration, and chemotaxis. It specifically modifies MAPK1/ERK2 and MAPK3/ERK1 via Lys-63 ubiquitination, promoting their activation by facilitating their interaction with MAP2K1 and MAP2K2. Additionally, TRIM15 contributes to cell migration and chemotaxis by acting as a stable component of focal adhesions, recruited by the multi-adapter protein paxillin. It functions in the RIG-I mediated interferon induction pathway, upstream or at the level of MAVS. TRIM15 inhibits NF-κB activation by regulating Lys-63 ubiquitination of MAP3K7/TAK1, preventing TRIM8 cytoplasmic translocation and thereby inhibiting TRIM8-mediated Lys-63-linked polyubiquitination of MAP3K7/TAK1 in the cytoplasm. Furthermore, TRIM15 plays a significant role in regulating the activation of hepatic stellate cells.
TRIM15 is also known as RNF93, ZNF178, ZNFB7.
