The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

TRIM34  -  tripartite motif containing 34

Homo sapiens

Synonyms: IFP1, RNF21
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of TRIM34

  • The RING, B-box 2, and CC domains of the paralogous TRIM6 and TRIM34 proteins functionally replaced the corresponding TRIM5alpha(rh) domains, allowing HIV-1 restriction [1].
 

High impact information on TRIM34

  • Although TRIM6 and TRIM34 orthologs are found in other mammals, TRIM5 has to date been identified only in primates [2].
  • Here we investigated the abilities of domains from TRIM proteins (TRIM6, TRIM34, and TRIM21) that do not restrict HIV-1 infection to substitute for the domains of rhesus monkey TRIM5alpha (TRIM5alpha(rh)) [1].
  • The exceptions were TRIM1, TRIM5 and TRIM34 proteins [3].
  • As a structural feature, the RNF21 cDNA possessed at least three kinds of isoforms, due to alternative splicing, consisting of the long form with the RBCC-RBCC-B30.2 domain, the medium form with the RBCC-B30.2 domain, and the short form with only the RBCC domain [4].
  • Interestingly, the medium form of the RNF21 mRNA expressed most predominantly was dramatically up-regulated within 8-16 h by interferon stimulation of HeLa cells [4].
 

Analytical, diagnostic and therapeutic context of TRIM34

  • Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem [4].
  • All of the proteins in IFP-1 have been purified from isolated fibrils by electroelution after size separation on SDS-PAGE gels [5].

References

  1. Functional replacement of the RING, B-box 2, and coiled-coil domains of tripartite motif 5alpha (TRIM5alpha) by heterologous TRIM domains. Li, X., Li, Y., Stremlau, M., Yuan, W., Song, B., Perron, M., Sodroski, J. J. Virol. (2006) [Pubmed]
  2. Evolution of a cytoplasmic tripartite motif (TRIM) protein in cows that restricts retroviral infection. Si, Z., Vandegraaff, N., O'huigin, C., Song, B., Yuan, W., Xu, C., Perron, M., Li, X., Marasco, W.A., Engelman, A., Dean, M., Sodroski, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Antiretroviral potential of human tripartite motif-5 and related proteins. Zhang, F., Hatziioannou, T., Perez-Caballero, D., Derse, D., Bieniasz, P.D. Virology (2006) [Pubmed]
  4. Molecular cloning of ring finger protein 21 (RNF21)/interferon-responsive finger protein (ifp1), which possesses two RING-B box-coiled coil domains in tandem. Orimo, A., Tominaga, N., Yoshimura, K., Yamauchi, Y., Nomura, M., Sato, M., Nogi, Y., Suzuki, M., Suzuki, H., Ikeda, K., Inoue, S., Muramatsu, M. Genomics (2000) [Pubmed]
  5. Integral proteins of the extracellular matrix fibrils of Myxococcus xanthus. Behmlander, R.M., Dworkin, M. J. Bacteriol. (1994) [Pubmed]
 
WikiGenes - Universities