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RCHY1

From Wikipedia, the free encyclopedia
RCHY1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRCHY1, ARNIP, CHIMP, PIRH2, PRO1996, RNF199, ZCHY, ZNF363, ring finger and CHY zinc finger domain containing 1
External IDsOMIM: 607680; MGI: 1915348; HomoloGene: 22894; GeneCards: RCHY1; OMA:RCHY1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001271797
NM_026557

RefSeq (protein)

NP_001258726
NP_080833

Location (UCSC)n/aChr 5: 92.1 – 92.11 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

RING finger and CHY zinc finger domain-containing protein 1 is a protein that in humans is encoded by the RCHY1 gene.[4]

Function

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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.[4]

Interactions

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RCHY1 has been shown to interact with P53[5][6] and Androgen receptor.[7]

References

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  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029397Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ a b "Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1".
  5. ^ 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. S2CID 9316769.
  6. ^ 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. PMC 4075976. PMID 19043414.
  7. ^ 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

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