RC3H1
Appearance
This article may be too technical for most readers to understand.(October 2014) |
Ring finger and CCCH-type domains 1, also known as Roquin-1, is a protein that in humans is encoded by the RC3H1 gene. [5]
Function
This gene encodes a protein containing RING-type and C3H1-type zinc finger motifs. The encoded protein recognizes and binds to a constitutive decay element (CDE) in the 3' UTR of mRNAs, leading to mRNA deadenylation and degradation. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2014].
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000135870 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040423 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Entrez Gene: Ring finger and CCCH-type domains 1". Retrieved 2014-10-08.
Further reading
- Bertossi, A; Aichinger, M; Sansonetti, P; Lech, M; Neff, F; Pal, M; Wunderlich, F. T.; Anders, H. J.; Klein, L; Schmidt-Supprian, M (2011). "Loss of Roquin induces early death and immune deregulation but not autoimmunity". Journal of Experimental Medicine. 208 (9): 1749–56. doi:10.1084/jem.20110578. PMC 3171092. PMID 21844204.
- Leppek, K; Schott, J; Reitter, S; Poetz, F; Hammond, M. C.; Stoecklin, G (2013). "Roquin promotes constitutive mRNA decay via a conserved class of stem-loop recognition motifs". Cell. 153 (4): 869–81. doi:10.1016/j.cell.2013.04.016. PMID 23663784.
- Heissmeyer, V; Vogel, K. U. (2013). "Molecular control of Tfh-cell differentiation by Roquin family proteins". Immunological Reviews. 253 (1): 273–89. doi:10.1111/imr.12056. PMID 23550652.
- Chang, P. P.; Lee, S. K.; Hu, X; Davey, G; Duan, G; Cho, J. H.; Karupiah, G; Sprent, J; Heath, W. R.; Bertram, E. M.; Vinuesa, C. G. (2012). "Breakdown in repression of IFN-γ mRNA leads to accumulation of self-reactive effector CD8+ T cells". The Journal of Immunology. 189 (2): 701–10. doi:10.4049/jimmunol.1102432. PMID 22685317.
- Athanasopoulos, V; Barker, A; Yu, D; Tan, A. H.; Srivastava, M; Contreras, N; Wang, J; Lam, K. P.; Brown, S. H.; Goodnow, C. C.; Dixon, N. E.; Leedman, P. J.; Saint, R; Vinuesa, C. G. (2010). "The ROQUIN family of proteins localizes to stress granules via the ROQ domain and binds target mRNAs". FEBS Journal. 277 (9): 2109–27. doi:10.1111/j.1742-4658.2010.07628.x. PMID 20412057.
- Yu, D; Tan, A. H.; Hu, X; Athanasopoulos, V; Simpson, N; Silva, D. G.; Hutloff, A; Giles, K. M.; Leedman, P. J.; Lam, K. P.; Goodnow, C. C.; Vinuesa, C. G. (2007). "Roquin represses autoimmunity by limiting inducible T-cell co-stimulator messenger RNA". Nature. 450 (7167): 299–303. doi:10.1038/nature06253. PMID 18172933.
- Pratama, A; Ramiscal, R. R.; Silva, D. G.; Das, S. K.; Athanasopoulos, V; Fitch, J; Botelho, N. K.; Chang, P. P.; Hu, X; Hogan, J. J.; Maña, P; Bernal, D; Korner, H; Yu, D; Goodnow, C. C.; Cook, M. C.; Vinuesa, C. G. (2013). "Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation". Immunity. 38 (4): 669–80. doi:10.1016/j.immuni.2013.01.011. PMID 23583642.
- Vinuesa, C. G.; Cook, M. C.; Angelucci, C; Athanasopoulos, V; Rui, L; Hill, K. M.; Yu, D; Domaschenz, H; Whittle, B; Lambe, T; Roberts, I. S.; Copley, R. R.; Bell, J. I.; Cornall, R. J.; Goodnow, C. C. (2005). "A RING-type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity". Nature. 435 (7041): 452–8. doi:10.1038/nature03555. PMID 15917799.
- Linterman, M. A.; Rigby, R. J.; Wong, R; Silva, D; Withers, D; Anderson, G; Verma, N. K.; Brink, R; Hutloff, A; Goodnow, C. C.; Vinuesa, C. G. (2009). "Roquin differentiates the specialized functions of duplicated T cell costimulatory receptor genes CD28 and ICOS". Immunity. 30 (2): 228–41. doi:10.1016/j.immuni.2008.12.015. PMID 19217324.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.