Biology:RCHY1
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 Generic protein structure example |
RING finger and CHY zinc finger domain-containing protein 1 is a protein that in humans is encoded by the RCHY1 gene.[1]
Function
The protein encoded by this gene has ubiquitin-protein ligase activity. This protein binds with p53 and promotes the ubiquitin-mediated proteosomal degradation of p53. This gene is oncogenic because loss of p53 function contributes directly to malignant tumor development. Transcription of this gene is regulated by p53. Alternative splicing results in multiple transcript variants encoding different isoforms.[1]
Interactions
RCHY1 has been shown to interact with P53[2][3] and Androgen receptor.[4]
References
- ↑ 1.0 1.1 "Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25898.
- ↑ "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation". Cell 112 (6): 779–91. Mar 2003. doi:10.1016/S0092-8674(03)00193-4. PMID 12654245.
- ↑ "Molecular basis of Pirh2-mediated p53 ubiquitylation". Nature Structural & Molecular Biology 15 (12): 1334–42. Dec 2008. doi:10.1038/nsmb.1521. PMID 19043414.
- ↑ "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". Journal of Molecular Endocrinology 29 (1): 41–60. Aug 2002. doi:10.1677/jme.0.0290041. PMID 12200228.
Further reading
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research 6 (9): 791–806. Sep 1996. doi:10.1101/gr.6.9.791. PMID 8889548.
- "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". Journal of Molecular Endocrinology 29 (1): 41–60. Aug 2002. doi:10.1677/jme.0.0290041. PMID 12200228.
- "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation". Cell 112 (6): 779–91. Mar 2003. doi:10.1016/S0092-8674(03)00193-4. PMID 12654245.
- "Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome". The Journal of Biological Chemistry 279 (12): 11696–704. Mar 2004. doi:10.1074/jbc.M312712200. PMID 14701804.
- "The p53 paddy wagon: COP1, Pirh2 and MDM2 are found resisting apoptosis and growth arrest". Cancer Biology & Therapy 3 (8): 721–5. Aug 2004. doi:10.4161/cbt.3.8.1068. PMID 15280670.
- "Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer". Journal of the National Cancer Institute 96 (22): 1718–21. Nov 2004. doi:10.1093/jnci/djh292. PMID 15547185.
- "A new human gene hNTKL-BP1 interacts with hPirh2". Biochemical and Biophysical Research Communications 330 (1): 293–7. Apr 2005. doi:10.1016/j.bbrc.2005.02.156. PMID 15781263.
- "Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer". Molecular and Cellular Biology 26 (17): 6502–10. Sep 2006. doi:10.1128/MCB.00147-06. PMID 16914734.
- "Differential response between the p53 ubiquitin-protein ligases Pirh2 and MdM2 following DNA damage in human cancer cells". Experimental Cell Research 312 (17): 3370–8. Oct 2006. doi:10.1016/j.yexcr.2006.07.005. PMID 16934800.
- "Phosphorylation of Pirh2 by calmodulin-dependent kinase II impairs its ability to ubiquitinate p53". The EMBO Journal 26 (13): 3062–74. Jul 2007. doi:10.1038/sj.emboj.7601749. PMID 17568776.
- "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1". Cancer Research 67 (22): 10789–95. Nov 2007. doi:10.1158/0008-5472.CAN-07-2033. PMID 18006823.
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