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The protein encoded by TRIM11 is a member of the tripartite motif (TRIM) family. Additionally we are shipping Tripartite Motif Containing 11 Antibodies (82) and many more products for this protein.
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Results show that TRIM11 was highly expressed in lung cancer tissues and cell lines and suggest that it acts as an oncogene (show RAB1A Proteins) in lung cancer through promoting cell growth, migration and invasion.
TRIM11 suppresses AIM2 inflammasome by degrading AIM2 via p62-dependent selective autophagy.
TRIM11 to be overexpressed in HCC (show FAM126A Proteins) tissues and cell lines. Downregulation of TRIM11 inhibited HCC (show FAM126A Proteins) cell proliferation and invasion in vitro and in vivo as well as suppressed the epithelial-mesenchymal transition (EMT (show ITK Proteins)) process.
study identified TRIM11 as a new HIV-1 capsid binding protein; data also reveal that TRIM11 restricts HIV-1 reverse transcription by accelerating viral uncoating, and microtubule dynamics is implicated in TRIM11-imposed block to early events of HIV-1 replication
TRIM11 is a host cellular factor that interferes with the early steps of HIV-1 replication and provides a connection between viral protein and host antiviral factors.
TRIM11 is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth.
TRIM11 negatively regulates IFN-beta (show IFNB1 Proteins) production and antiviral activity by targeting TBK1 (show TBK1 Proteins).
Study shows that the E3 ubiquitin ligase (show MUL1 Proteins) TRIM11 plays a critical role in the clearance of mutant PHOX2B (show PHOX2B Proteins), which causes congenital central hypoventilation syndrome, through the proteasome.
PAX6 (show PAX6 Proteins) interacts with HOMER3 (show HOMER3 Proteins), DNCL1 (show DYNLL1 Proteins), and TRIM11. Three C-terminal PAX6 (show PAX6 Proteins) mutations, previously identified in patients with eye malformations, all reduced or abolished the interactions.
These results suggest that TRIM11, with the ubiquitin-proteasome pathway, regulates ARC105 (show MED15 Proteins) function in TGFbeta (show TGFB1 Proteins) signaling.
The results suggest that TRIM11 plays a role in the regulation of intracellular humanin level through ubiquitin-mediated protein degradation pathways.
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.
tripartite motif-containing 11
, tripartite motif containing 11
, E3 ubiquitin-protein ligase TRIM11
, RING finger protein 92
, tripartite motif-containing protein 11
, tripartite motif protein 11