TRIM69
Domain
The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity and for nuclear localization and aggregation.
Function
E3 ubiquitin ligase that plays an important role in antiviral immunity by restricting different viral infections including dengue virus or vesicular stomatitis indiana virus (PubMed:23131556, PubMed:30142214, PubMed:31375575, PubMed:31578292). Ubiquitinates viral proteins such as dengue virus NS3 thereby limiting infection (PubMed:30844644). In addition, acts as a key mediator of type I interferon induced microtubule stabilization by directly associating to microtubules independently of its E3 ligase activity (PubMed:36251989). Plays also a role in cataract formation together with TP53 (PubMed:30844644). Mechanistically, inhibits UVB-induced cell apoptosis and reactive oxygen species (ROS) production by inducing TP53 ubiquitination (PubMed:30844644). Regulates centrosome dynamics and mitotic progression by ubiquitinating STK3/MST2; leading to its redistribution to the perinuclear cytoskeleton and subsequent phosphorylation by PLK1 (PubMed:37739411).
Pathway
Protein modification; protein ubiquitination.
Post-translational modifications
Phosphorylated. Phosphorylation is necessary for nuclear localization.
Sequence Similarities
Belongs to the TRIM/RBCC family.
Cellular localization
- Cytoplasm
- Nucleus
- Nucleus speckle
- Cytoplasm
- Cytoskeleton
- Microtubule organizing center
- Centrosome
- Adopts a filamentous distribution in the cell cytoplasm where it strongly colocalizes with stable microtubules.
Alternative names
RNF36, HSD-34, HSD34, TRIM69, E3 ubiquitin-protein ligase TRIM69, RFP-like domain-containing protein trimless, RING finger protein 36, RING-type E3 ubiquitin transferase TRIM69, Tripartite motif-containing protein 69