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Tripartite motif containing 34

TRIM34, RNF21, IFPI, ifp1
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, B-box type 1 and B-box type 2 domain, and a coiled-coil region. Expression of this gene is up-regulated by interferon. This gene is mapped to chromosome 11p15, where it resides within a TRIM gene cluster. Alternative splicing results in multiple transcript variants. A read-through transcript from the upstream TRIM6 gene has also been observed, which results in a fusion product from these neighboring family members. [provided by RefSeq, Oct 2010] (from NCBI)
Top mentioned proteins: Trim, TRIM5alpha, CAN, TRIM22, iMpact
Papers on TRIM34
Binding of the rhesus TRIM5α PRYSPRY domain to capsid is necessary but not sufficient for HIV-1 restriction.
Diaz-Griffero et al., United States. In Virology, 2014
In support of this hypothesis, we showed that some human tripartite motif proteins bind the HIV-1 capsid but do not restrict HIV-1 infection, such as human TRIM6 and TRIM34.
Elevated rate of fixation of endogenous retroviral elements in Haplorhini TRIM5 and TRIM22 genomic sequences: impact on transcriptional regulation.
Hunter et al., Atlanta, United States. In Plos One, 2012
All genes in the TRIM6/TRIM34/TRIM5/TRIM22 locus are type I interferon inducible, with TRIM5 and TRIM22 possessing antiviral properties.
Copy number variation influences gene expression and metabolic traits in mice.
Lusis et al., Los Angeles, United States. In Hum Mol Genet, 2009
Predicted CNV genes, such as Itlna, Defcr-1, Trim12 and Trim34 were highly correlated with these traits.
[Analysis of the dynamic change of TF, TFPI and IL-1beta in plasma of patients with acute leukemia].
Huang et al., Lishui, China. In Zhongguo Shi Yan Xue Ye Xue Za Zhi, 2008
This study was purposed to explore the significance of tissue factor (TF), tissue factor pathway inhibitor (IFPI) and interleukin-1beta (IL-1beta) in the evaluation of development, curative effect and prognosis of AL patients.
Discordant evolution of the adjacent antiretroviral genes TRIM22 and TRIM5 in mammals.
Malik et al., Seattle, United States. In Plos Pathog, 2007
Here, we present an evolutionary comparison of the TRIM5 gene to its closest human paralogs: TRIM22, TRIM34, and TRIM6.
Unique features of TRIM5alpha among closely related human TRIM family members.
Sodroski et al., Boston, United States. In Virology, 2007
TRIM5alpha, TRIM34 and TRIM6 associated with HIV-1 capsid-nucleocapsid complexes assembled in vitro; the TRIM5alpha and TRIM34 interactions with these complexes were dependent on their B30.2(SPRY)
Antiretroviral potential of human tripartite motif-5 and related proteins.
Bieniasz et al., New York City, United States. In Virology, 2006
The exceptions were TRIM1, TRIM5 and TRIM34 proteins.
Functional replacement of the RING, B-box 2, and coiled-coil domains of tripartite motif 5alpha (TRIM5alpha) by heterologous TRIM domains.
Sodroski et al., Boston, United States. In J Virol, 2006
heterologous RING, B-box 2, and CC domains from related TRIM proteins can functionally substitute for TRIM5alpha(rh) domains.
Evolution of a cytoplasmic tripartite motif (TRIM) protein in cows that restricts retroviral infection.
Sodroski et al., Boston, United States. In Proc Natl Acad Sci U S A, 2006
In humans, TRIM5 is located in a paralogous cluster that includes TRIM6, TRIM34, and TRIM22.
Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem.
Muramatsu et al., Saitama, Japan. In Genomics, 2000
We have cloned the full length of a novel cDNA, named ring finger protein 21 (RNF21), composed of the RING finger-B box-coiled coil (RBCC) domain and the B30.2 domain, which are characteristic of the RBCC-B30.2
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