TRIM11
Description
The TRIM11 (tripartite motif containing 11) is a protein-coding gene located on chromosome 1.
Tripartite motif-containing protein 11 is a protein found in humans that is encoded by the TRIM11 gene. The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This protein localizes to the nucleus and the cytoplasm. Its function has not been identified.
TRIM11, also known as Protein BIA1, RING finger protein 92, and Tripartite motif-containing protein 11, is an E3 ubiquitin-protein ligase. It promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. It mediates PAX6 ubiquitination, leading to proteasomal degradation and modulating cortical neurogenesis. TRIM11 may also inhibit PAX6 transcriptional activity by preventing PAX6 from binding to its consensus sequences. TRIM11 contributes to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. It mediates MED15 ubiquitination, leading to proteasomal degradation. TRIM11 may contribute to the innate restriction of retroviruses. Overexpression of TRIM11 reduces HIV-1 and murine leukemia virus infectivity by suppressing viral gene expression. This antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. TRIM11 may regulate TRIM5 turnover via the proteasome pathway, counteracting TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. TRIM11 acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2. Upon DNA stimulation, TRIM11 undergoes autoubiquitination, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes.
TRIM11 is also known as BIA1, RNF92.
