RCHY1

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RCHY1
Protein RCHY1 PDB 2JRJ.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases RCHY1, ARNIP, CHIMP, PIRH2, PRO1996, RNF199, ZCHY, ZNF363, ring finger and CHY zinc finger domain containing 1
External IDs MGI: 1915348 HomoloGene: 22894 GeneCards: 25898
Genetically Related Diseases
Disease Name References
Rheumatoid Arthritis
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
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001271797
NM_026557

RefSeq (protein)

NP_001009922.1
NP_001265465.1
NP_001265466.1
NP_001265467.1
NP_056251.2

NP_001258726.1
NP_080833.1

Location (UCSC) Chr 4: 75.48 – 75.51 Mb Chr 5: 91.95 – 91.96 Mb
PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

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

Function[edit]

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[edit]

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

References[edit]

  1. ^ a b "Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1". 
  2. ^ Leng RP, Lin Y, Ma W, Wu H, Lemmers B, Chung S, Parant JM, Lozano G, Hakem R, Benchimol S (Mar 2003). "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation". Cell 112 (6): 779–91. doi:10.1016/S0092-8674(03)00193-4. PMID 12654245. 
  3. ^ Sheng Y, Laister RC, Lemak A, Wu B, Tai E, Duan S, Lukin J, Sunnerhagen M, Srisailam S, Karra M, Benchimol S, Arrowsmith CH (Dec 2008). "Molecular basis of Pirh2-mediated p53 ubiquitylation". Nature Structural & Molecular Biology 15 (12): 1334–42. doi:10.1038/nsmb.1521. PMID 19043414. 
  4. ^ Beitel LK, Elhaji YA, Lumbroso R, Wing SS, Panet-Raymond V, Gottlieb B, Pinsky L, Trifiro MA (Aug 2002). "Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity". Journal of Molecular Endocrinology 29 (1): 41–60. doi:10.1677/jme.0.0290041. PMID 12200228. 

Further reading[edit]