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Tripartite motif containing 22

TRIM22, Staf50, tripartite motif-containing 22, stimulated trans-acting factor
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 cytoplasm and its expression is induced by interferon. The protein down-regulates transcription from the HIV-1 LTR promoter region, suggesting that function of this protein may be to mediate interferon's antiviral effects. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2010] (from NCBI)
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Papers on TRIM22
BRG1 is indispensable for IFN-γ-induced TRIM22 expression, which is dependent on the recruitment of IRF-1.
Xiong et al., Shanghai, China. In Biochem Biophys Res Commun, 2011
BRG1-mediated chromatin remodeling is critical for the IFN-gamma-inducibility of TRIM22 gene.
Identification of tripartite motif-containing 22 (TRIM22) as a novel NF-κB activator.
Xiong et al., Shanghai, China. In Biochem Biophys Res Commun, 2011
These data suggested that TRIM22 was a positive regulator of NF-kappaB-mediated transcription.
TRIM22 inhibits HIV-1 transcription independently of its E3 ubiquitin ligase activity, Tat, and NF-kappaB-responsive long terminal repeat elements.
Vicenzi et al., Milano, Italy. In J Virol, 2011
Nuclear TRIM22 significantly impairs HIV-1 replication, likely by interfering with Tat- and NF-kappaB-independent long-terminal-repeat-driven transcription.
Association of TRIM22 with the type 1 interferon response and viral control during primary HIV-1 infection.
CAPRISA Acute Infection Study Team et al., Durban, South Africa. In J Virol, 2011
These data suggest concordance between type 1 IFN and TRIM22 in PBMCs and that TRIM22 likely acts as an antiviral effector in HIV-1 infection.
The human IFN-inducible p53 target gene TRIM22 colocalizes with the centrosome independently of cell cycle phase.
Drott et al., Lund, Sweden. In Exp Cell Res, 2010
endogenous TRIM22 is localized to both nucleus and cytosol in primary human mononuclear cells, as well as in the human osteosarcoma cell line U2OS
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