RCHY1

RCHY1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2JRJ, 2K2C, 2K2D

Identifiers

Aliases

RCHY1, ARNIP, CHIMP, PIRH2, PRO1996, RNF199, ZCHY, ZNF363, ring finger and CHY zinc finger domain containing 1

External IDs

OMIM: 607680 MGI: 1915348 HomoloGene: 22894 GeneCards: RCHY1

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[1]

Band	5\|5 E2	Start	92,096,763 bp^[1]
Band	5\|5 E2	End	92,110,927 bp^[1]

RNA expression pattern

Bgee

Human

Mouse (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

secondary oocyte

endocardial cushion

seminal vesicula

parotid gland

medial ganglionic eminence

molar

temporal muscle

atrioventricular valve

sternocleidomastoid 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

Species

Human

Mouse

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/a

Chr 5: 92.1 – 92.11 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.^[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

^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000029397 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: RCHY1 ring finger and CHY zinc finger domain containing 1".
^ 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.
^ 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.
^ 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.

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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This page was last edited on 3 March 2023, at 20:22

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Function

Interactions

References

Further reading