RCHY1

Protein-coding gene in the species Homo sapiens
RCHY1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2JRJ, 2K2C, 2K2D

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
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[1]
Chromosome 5 (mouse)
Genomic location for RCHY1
Genomic location for RCHY1
Band5|5 E2Start92,096,763 bp[1]
End92,110,927 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • sperm

  • secondary oocyte

  • endothelial cell

  • germinal epithelium

  • islet of Langerhans

  • right ventricle

  • biceps brachii

  • parietal pleura

  • Brodmann area 23

  • palpebral conjunctiva
Top expressed in
  • interventricular septum

  • zygote

  • granulocyte

  • secondary oocyte

  • endocardial cushion

  • seminal vesicula

  • parotid gland

  • medial ganglionic eminence

  • molar

  • temporal muscle
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • zinc ion binding
  • p53 binding
  • protein binding
  • protein homodimerization activity
  • metal ion binding
  • ubiquitin-protein transferase activity
  • transferase activity
  • signaling receptor binding
Cellular component
  • ubiquitin ligase complex
  • cytoplasm
  • nuclear speck
  • nucleus
  • nucleoplasm
  • cytosol
Biological process
  • error-free translesion synthesis
  • positive regulation of protein ubiquitination
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process
  • protein ubiquitination
  • protein autoubiquitination
  • ubiquitin-dependent protein catabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

25898

68098

Ensembl

n/a

ENSMUSG00000029397

UniProt

Q96PM5

Q9CR50

RefSeq (mRNA)
NM_001008925
NM_001009922
NM_001278536
NM_001278537
NM_001278538

NM_001278539
NM_015436
NM_001387136
NM_001387137

NM_001271797
NM_026557

RefSeq (protein)
NP_001009922
NP_001265465
NP_001265466
NP_001265467
NP_001265468

NP_056251

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

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

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

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000029397 – Ensembl, 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

  • Bonaldo MF, Lennon G, Soares MB (Sep 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • 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.
  • 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.
  • Logan IR, Sapountzi V, Gaughan L, Neal DE, Robson CN (Mar 2004). "Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome". The Journal of Biological Chemistry. 279 (12): 11696–704. doi:10.1074/jbc.M312712200. PMID 14701804.
  • Corcoran CA, Huang Y, Sheikh MS (Aug 2004). "The p53 paddy wagon: COP1, Pirh2 and MDM2 are found resisting apoptosis and growth arrest". Cancer Biology & Therapy. 3 (8): 721–5. doi:10.4161/cbt.3.8.1068. PMID 15280670.
  • Duan W, Gao L, Druhan LJ, Zhu WG, Morrison C, Otterson GA, Villalona-Calero MA (Nov 2004). "Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer". Journal of the National Cancer Institute. 96 (22): 1718–21. doi:10.1093/jnci/djh292. PMID 15547185.
  • Zhang L, Li J, Wang C, Ma Y, Huo K (Apr 2005). "A new human gene hNTKL-BP1 interacts with hPirh2". Biochemical and Biophysical Research Communications. 330 (1): 293–7. doi:10.1016/j.bbrc.2005.02.156. PMID 15781263.
  • Logan IR, Gaughan L, McCracken SR, Sapountzi V, Leung HY, Robson CN (Sep 2006). "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. doi:10.1128/MCB.00147-06. PMC 1592843. PMID 16914734.
  • Duan W, Gao L, Wu X, Zhang Y, Otterson GA, Villalona-Calero MA (Oct 2006). "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. doi:10.1016/j.yexcr.2006.07.005. PMID 16934800.
  • Duan S, Yao Z, Hou D, Wu Z, Zhu WG, Wu M (Jul 2007). "Phosphorylation of Pirh2 by calmodulin-dependent kinase II impairs its ability to ubiquitinate p53". The EMBO Journal. 26 (13): 3062–74. doi:10.1038/sj.emboj.7601749. PMC 1914097. PMID 17568776.
  • Hattori T, Isobe T, Abe K, Kikuchi H, Kitagawa K, Oda T, Uchida C, Kitagawa M (Nov 2007). "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1". Cancer Research. 67 (22): 10789–95. doi:10.1158/0008-5472.CAN-07-2033. PMID 18006823.
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