RCHY1

From Wikipedia, the free encyclopedia


Ring finger and CHY zinc finger domain containing 1
Identifiers
Symbol(s) RCHY1; ARNIP; CHIMP; DKFZp586C1620; PIRH2; PRO1996; RNF199; ZNF363; hARNIP
External IDs OMIM: 607680 MGI: 1915348 HomoloGene: 22894
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 25898 68098
Ensembl ENSG00000163743 ENSMUSG00000029397
Uniprot Q96PM5 Q8R593
Refseq NM_001008925 (mRNA)
NP_001008925 (protein)		 NM_026557 (mRNA)
NP_080833 (protein)
Location Chr 4: 76.62 - 76.66 Mb Chr 5: 93.02 - 93.04 Mb
Pubmed search [1] [2]

Ring finger and CHY zinc finger domain containing 1, also known as RCHY1, is a human gene.[1]

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]

[edit] References

  1. ^ a b Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1.

[edit] Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548. 
  • Beitel LK, Elhaji YA, Lumbroso R, et al. (2002). "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity.". J. Mol. Endocrinol. 29 (1): 41-60. PMID 12200228. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Leng RP, Lin Y, Ma W, et al. (2003). "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation.". Cell 112 (6): 779-91. PMID 12654245. 
  • Logan IR, Sapountzi V, Gaughan L, et al. (2004). "Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome.". J. Biol. Chem. 279 (12): 11696-704. doi:10.1074/jbc.M312712200. PMID 14701804. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Corcoran CA, Huang Y, Sheikh MS (2005). "The p53 paddy wagon: COP1, Pirh2 and MDM2 are found resisting apoptosis and growth arrest.". Cancer Biol. Ther. 3 (8): 721-5. PMID 15280670. 
  • Duan W, Gao L, Druhan LJ, et al. (2004). "Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer.". J. Natl. Cancer Inst. 96 (22): 1718-21. doi:10.1093/jnci/djh292. PMID 15547185. 
  • Zhang L, Li J, Wang C, et al. (2005). "A new human gene hNTKL-BP1 interacts with hPirh2.". Biochem. Biophys. Res. Commun. 330 (1): 293-7. doi:10.1016/j.bbrc.2005.02.156. PMID 15781263. 
  • Logan IR, Gaughan L, McCracken SR, et al. (2006). "Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer.". Mol. Cell. Biol. 26 (17): 6502-10. doi:10.1128/MCB.00147-06. PMID 16914734. 
  • Duan W, Gao L, Wu X, et al. (2006). "Differential response between the p53 ubiquitin-protein ligases Pirh2 and MdM2 following DNA damage in human cancer cells.". Exp. Cell Res. 312 (17): 3370-8. doi:10.1016/j.yexcr.2006.07.005. PMID 16934800. 
  • Duan S, Yao Z, Hou D, et al. (2007). "Phosphorylation of Pirh2 by calmodulin-dependent kinase II impairs its ability to ubiquitinate p53.". EMBO J. 26 (13): 3062-74. doi:10.1038/sj.emboj.7601749. PMID 17568776. 
  • Hattori T, Isobe T, Abe K, et al. (2007). "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1.". Cancer Res. 67 (22): 10789-95. doi:10.1158/0008-5472.CAN-07-2033. PMID 18006823. 
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