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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Tripartite motif containing 11

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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, Trim, RBCC, Pax6, ACID
Papers on TRIM11
Activation of AKT1/GSK-3β/β-Catenin-TRIM11/Survivin Pathway by Novel GSK-3β Inhibitor Promotes Neuron Cell Survival: Study in Differentiated SH-SY5Y Cells in OGD Model.
Ramanathan et al., Coimbatore, India. In Mol Neurobiol, Jan 2016
During differentiation, upregulation of the growth-associated protein 43 (GAP43), neurogenin1 (NGN1), neuronal differentiation 2 (NeuroD2), and tripartite motif containing 11 (TRIM11) genes were observed.
The human antiviral factor TRIM11 is under the regulation of HIV-1 Vpr.
Yang et al., Wuhan, China. In Plos One, 2013
TRIM11 has been reported to be able to restrict HIV-1 replication, but the detailed aspects of the interfering mechanisms remain unclear.
Effects of cellular activation on anti-HIV-1 restriction factor expression profile in primary cells.
Pillai et al., San Francisco, United States. In J Virol, 2013
Expression of RTF1, RNA polymerase II-associated factor 1 (PAF1), TRIM11, TRIM26, and BST-2/tetherin correlated with decreased HIV-1 infectivity.
TRIM11 is overexpressed in high-grade gliomas and promotes proliferation, invasion, migration and glial tumor growth.
Bota et al., Orange, United States. In Oncogene, 2013
TRIM11 (tripartite motif-containing protein 11), an E3 ubiquitin ligase, is known to be involved in the development of the central nervous system.
TRIM11 negatively regulates IFNβ production and antiviral activity by targeting TBK1.
Kwon et al., Taejŏn, South Korea. In Plos One, 2012
In this study, we identified TRIM11 (tripartite motif containing 11) as a novel negative regulator of IFNβ production.
The E3 ubiquitin ligase TRIM11 mediates the degradation of congenital central hypoventilation syndrome-associated polyalanine-expanded PHOX2B.
Ceccherini et al., Genova, Italy. In J Mol Med (berl), 2012
Finally, we show that the E3 ubiquitin ligase TRIM11 plays a critical role in the clearance of mutant PHOX2B through the proteasome.
Trim11 modulates the function of neurogenic transcription factor Pax6 through ubiquitin-proteosome system.
Stoykova et al., Göttingen, Germany. In Genes Dev, 2008
Here, we report that Trim11, a member of the TRIM/RBCC protein family of E3 ubiquitin ligases, interacts with Pax6 and mediates Pax6 degradation via the ubiquitin-proteasome system.
Trim11 increases expression of dopamine beta-hydroxylase gene by interacting with Phox2b.
Kim et al., Belmont, United States. In Biochem Biophys Res Commun, 2008
This study suggests a potential role for Trim11 in the specification of NA phenotype by interaction with Phox2b.
TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.
Mothes et al., New Haven, United States. In Plos Pathog, 2008
Downregulation of TRIM11 and TRIM15 enhanced virus release suggesting that these proteins contribute to the endogenous restriction of retroviruses in cells.
TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system.
Takahashi et al., Fuchū, Japan. In Febs Lett, 2006
These results suggest that TRIM11, with the ubiquitin-proteasome pathway, regulates ARC105 function in TGFbeta signaling.
A screen for proteins that interact with PAX6: C-terminal mutations disrupt interaction with HOMER3, DNCL1 and TRIM11.
Hanson et al., Edinburgh, United Kingdom. In Bmc Genet, 2004
PAX6 interacts with HOMER3, DNCL1, and TRIM11. Three C-terminal PAX6 mutations, previously identified in patients with eye malformations, all reduced or abolished the interactions.
A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease-relevant insults.
Nishimoto et al., Tokyo, Japan. In Eur J Neurosci, 2003
The results suggest that TRIM11 plays a role in the regulation of intracellular humanin level through ubiquitin-mediated protein degradation pathways.
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