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Ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase
Protein RCHY1 PDB 2JRJ.png
Rendering based on PDB 2JRJ.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols RCHY1 ; ARNIP; CHIMP; PIRH2; PRO1996; RNF199; ZCHY; ZNF363
External IDs OMIM607680 MGI1915348 HomoloGene22894 GeneCards: RCHY1 Gene
RNA expression pattern
PBB GE RCHY1 212743 at tn.png
PBB GE RCHY1 212749 s at tn.png
PBB GE RCHY1 214281 s at tn.png
More reference expression data
Species Human Mouse
Entrez 25898 68098
Ensembl ENSG00000163743 ENSMUSG00000029397
UniProt Q96PM5 Q9CR50
RefSeq (mRNA) NM_001008925 NM_001271797
RefSeq (protein) NP_001009922 NP_001258726
Location (UCSC) Chr 4:
76.4 – 76.44 Mb
Chr 5:
91.95 – 91.96 Mb
PubMed search [1] [2]

RING finger and CHY zinc finger domain-containing protein 1 is a protein that in humans is encoded by the RCHY1 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]


RCHY1 has been shown to interact with P53[2][3] and Androgen receptor.[4]


  1. ^ a b "Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1". 
  2. ^ Leng, Roger P; Lin Yunping; Ma Weili; Wu Hong; Lemmers Benedicte; Chung Stephen; Parant John M; Lozano Guillermina; Hakem Razqallah; Benchimol Samuel (Mar 2003). "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation". Cell (United States) 112 (6): 779–91. doi:10.1016/S0092-8674(03)00193-4. ISSN 0092-8674. PMID 12654245. 
  3. ^ Sheng, Yi; Laister Rob C, Lemak Alexander, Wu Bin, Tai Elizabeth, Duan Shili, Lukin Jonathan, Sunnerhagen Maria, Srisailam Sampath, Karra Murthy, Benchimol Sam, Arrowsmith Cheryl H (Dec 2008). "Molecular basis of Pirh2-mediated p53 ubiquitylation". Nat. Struct. Mol. Biol. (United States) 15 (12): 1334–42. doi:10.1038/nsmb.1521. PMID 19043414. 
  4. ^ Beitel, L K; Elhaji Y A; Lumbroso R; Wing S S; Panet-Raymond V; Gottlieb B; Pinsky L; Trifiro M A (Aug 2002). "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". J. Mol. Endocrinol. (England) 29 (1): 41–60. doi:10.1677/jme.0.0290041. ISSN 0952-5041. PMID 12200228. 

Further reading[edit]