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Taking over the Atlas
Dear Colleagues,
The Atlas, once more, is in great danger, and I will have to proceed to a collective economic lay-off of all the team involved in the Atlas before the begining of April 2015 (a foundation having suddenly withdrawn its commitment to support the Atlas). I ask you herein if any Scientific Society (a Society of Cytogenetics, of Clinical Genetics, of Hematology, or a Cancer Society, or any other...), any University and/or Hospital, any Charity, or any database would be interested in taking over the Atlas, in whole or in part. If taking charge of the whole lot is too big, a consortium of various actors could be the solution (I am myself trying to find partners). Could you please spread the information, contact the relevant authorities, and find partners.
Survival of the Atlas will be critically dependant upon your ability to find solutions (and urgently!).
Kind regards.
Jean-Loup Huret
Donations are also welcome
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Don't let the Atlas imminent demise
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RCHY1 (ring finger and CHY zinc finger domain containing 1)


Other namesPIRH2
LocusID (NCBI) 25898
Location 4q21.1
Location_base_pair Starts at 76404247 and ends at 76439640 bp from pter ( according to hg19-Feb_2009)  [Mapping]


Description The gene encompasses 32 kb of DNA; 9 exons.
Transcription 4.3 kb nucleotides mRNA. 783 bp open reading frame.


  Immunohistochemical detection of human RCHY1 protein in non-small cell lung cancers. (A) squamous cell carcinoma, and (B) large cell carcinoma.
Description 261 amino acids; 32 kDa protein.
Expression RCHY1 expresses at higher level in liver, testis and heart. Lower expression is detected in lung, brain, muscle and spleen. RCHY1 is overexpressed in non-small cell lung cancers.
Localisation The localization of RCHY1 protein in human lung tumors was evaluated immunohistochemically. RCHY1 protein was found primarily in the cytoplasm and membrane and a small portion in the nucleus of malignant cells.
Function RCHY1 is an ubiquitin-protein E3 ligase that promotes p53 degradation. The RCHY1 gene encodes a RING-H2 domain-containing protein with intrinsic ubiquitin-protein ligase activity. It has been reported that RCHY1( Pirh2) physically interacts with p53 and promotes ubiquitination of p53 independently of Mdm2. RCHY1 was also reported to be transactivated by the p53 product in MEFs, murine proB cell BaF3 and human BJT fibroblasts cells. Therefore, like MDM2, RCHY1 participates in an autoregulatory feedback loop that controls p53 function. Expression of RCHY1 decreased the level of p53 protein, while abrogation of endogenous RCHY1 expression increased the level of p53. Furthermore, RCHY1 represses p53 functions, including p53-dependent transactivation and growth inhibition. RCHY1 is overexpressed in both human and murine lung cancers by comparing Pirh2 mRNA and protein level between lung neoplastic tissues and uninvolved adjacent lung tissue. The increased RCHY1 protein could cause degradation of wild type p53 and reduce the tumor suppression function in tumor cells.
It has been reported that coexpression of RCHY1(ARNIP) and androgen receptor (AR) in COS-1 cells reduces the interaction between AR N- and C-terminus. The RING-H2 domain of the RCHY1 functions as an ubiquitin-protein ligase in vitro in the presence of a specific ubiquitin-conjugating enzyme, Ubc4-1. Mutation of a single cysteine residue in the RCHY RING-H2 domain (Cys145Ala) abolished this E3 ubiquitin ligase activity. Fluorescent protein tagging studies revealed that AR-RCHY1 interaction was hormone-independent in COS-1 cells, and suggest that co-localization of both AR and RCHY1to the nucleus upon androgen addition may allow RCHY1 to play a role in nuclear processes.
It has been reported that wild-type RCHY1is an unstable protein with a short half-life and coexpression of TIP60 enhances RCHY1 protein stability and alters RCHY1 subcellular localization. In addition, MVP (measles virus phosphoprotein ) is able to specifically interact with and stabilize the RCHY1 by preventing its ubiquitination. It has been reported that the RCHY1 also interacts with NTKL-BP1 (N-terminal kinase-like protein-binding protein 1) protein
Homology It belongs to the ring finger ubiquitin protein E3 ligase family. Containing Conserved RING-finger Domain (residues 145 - 186 ) and CHY zinc finger (residues 20-94).


Note Unknown

Implicated in

Entity Non-Small Cell Lung Cancer
Disease Lung cancers are pathologically classified as small cell lung cancer and non-small cell lung cancer (non-small cell lung cancer includes large cell carcinomas, squamous cell carcinomas and adenocarcinomas).
Oncogenesis RCHY1 protein is overexpressed in about 84% human lung cancers compared to uninvolved lung tissue. The RCHY1 protein was also elevated in about 93% of murine lung tumors. Because RCHY1 is an ubiquitin-protein ligase that promotes p53 protein degradation, the increased RCHY1 expression could play an important role in lung tumorigenesis.

External links

HGNC (Hugo)RCHY1   17479
Entrez_Gene (NCBI)RCHY1  25898  ring finger and CHY zinc finger domain containing 1, E3 ubiquitin protein ligase
GeneCards (Weizmann)RCHY1
Ensembl hg19 (Hinxton)ENSG00000163743 [Gene_View]  chr4:76404247-76439640 [Contig_View]  RCHY1 [Vega]
Ensembl hg38 (Hinxton)ENSG00000163743 [Gene_View]  chr4:76404247-76439640 [Contig_View]  RCHY1 [Vega]
ICGC DataPortalENSG00000163743
Genatlas (Paris)RCHY1
SOURCE (Princeton)RCHY1
Genomic and cartography
GoldenPath hg19 (UCSC)RCHY1  -     chr4:76404247-76439640 -  4q21.1-q21.3   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)RCHY1  -     4q21.1-q21.3   [Description]    (hg38-Dec_2013)
EnsemblRCHY1 - 4q21.1-q21.3 [CytoView hg19]  RCHY1 - 4q21.1-q21.3 [CytoView hg38]
Mapping of homologs : NCBIRCHY1 [Mapview hg19]  RCHY1 [Mapview hg38]
Gene and transcription
Genbank (Entrez)AB209072 AF247041 AF255666 AF305424 AK091501
RefSeq transcript (Entrez)NM_001008925 NM_001009922 NM_001278536 NM_001278537 NM_001278538 NM_001278539 NM_015436
RefSeq genomic (Entrez)AC_000136 NC_000004 NC_018915 NG_029152 NT_016354 NW_001838915 NW_004929320
Consensus coding sequences : CCDS (NCBI)RCHY1
Cluster EST : UnigeneHs.48297 [ NCBI ]
CGAP (NCI)Hs.48297
Alternative Splicing : Fast-db (Paris)GSHG0023327
Alternative Splicing GalleryENSG00000163743
Gene ExpressionRCHY1 [ NCBI-GEO ]     RCHY1 [ SEEK ]   RCHY1 [ MEM ]
SOURCE (Princeton)Expression in : [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96PM5 (Uniprot)
NextProtQ96PM5  [Medical]
With graphics : InterProQ96PM5
Splice isoforms : SwissVarQ96PM5 (Swissvar)
Catalytic activity : Enzyme6.3.2.- [ Enzyme-Expasy ]   6.3.2.-6.3.2.- [ IntEnz-EBI ]   6.3.2.- [ BRENDA ]   6.3.2.- [ KEGG ]   
Domaine pattern : Prosite (Expaxy)ZF_CHY (PS51266)    ZF_CTCHY (PS51270)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)Rubredoxin-type_fold    Znf_CHY    Znf_CTCHY    Znf_RING    Znf_RING/FYVE/PHD   
Related proteins : CluSTrQ96PM5
Domain families : Pfam (Sanger)zf-CHY (PF05495)    zf-RING_2 (PF13639)   
Domain families : Pfam (NCBI)pfam05495    pfam13639   
Domain families : Smart (EMBL)RING (SM00184)  
DMDM Disease mutations25898
Blocks (Seattle)Q96PM5
PDB (SRS)2JRJ    2K2C    2K2D   
PDB (PDBSum)2JRJ    2K2C    2K2D   
PDB (IMB)2JRJ    2K2C    2K2D   
PDB (RSDB)2JRJ    2K2C    2K2D   
Human Protein AtlasENSG00000163743
Peptide AtlasQ96PM5
IPIIPI00289787   IPI00552384   IPI00021192   IPI00552504   IPI00967694   IPI00964860   IPI00966948   IPI00965022   IPI00965612   
Protein Interaction databases
IntAct (EBI)Q96PM5
Ontologies - Pathways
Ontology : AmiGOubiquitin ligase complex  p53 binding  ubiquitin-protein transferase activity  receptor binding  protein binding  nucleus  nucleolus  cytoplasm  zinc ion binding  protein ubiquitination  nuclear speck  ligase activity  positive regulation of protein ubiquitination  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  protein homodimerization activity  protein autoubiquitination  
Ontology : EGO-EBIubiquitin ligase complex  p53 binding  ubiquitin-protein transferase activity  receptor binding  protein binding  nucleus  nucleolus  cytoplasm  zinc ion binding  protein ubiquitination  nuclear speck  ligase activity  positive regulation of protein ubiquitination  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  protein homodimerization activity  protein autoubiquitination  
Pathways : KEGGp53 signaling pathway    Ubiquitin mediated proteolysis    Measles   
REACTOMEQ96PM5 [protein]
REACTOME PathwaysREACT_6900 Immune System [pathway]
Protein Interaction DatabaseRCHY1
DoCM (Curated mutations)RCHY1
Wikipedia pathwaysRCHY1
Gene fusion - rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerRCHY1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)RCHY1
Exome Variant ServerRCHY1
Genetic variants : HAPMAPRCHY1
Genomic Variants (DGV)RCHY1 [DGVbeta]
ICGC Data PortalENSG00000163743 
Somatic Mutations in Cancer : COSMICRCHY1 
CONAN: Copy Number AnalysisRCHY1 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
DECIPHER (Syndromes)4:76404247-76439640
Mutations and Diseases : HGMDRCHY1
NextProtQ96PM5 [Medical]
Disease Genetic AssociationRCHY1
Huge Navigator RCHY1 [HugePedia]  RCHY1 [HugeCancerGEM]
snp3D : Map Gene to Disease25898
DGIdb (Drug Gene Interaction db)RCHY1
General knowledge
Homologs : HomoloGeneRCHY1
Homology/Alignments : Family Browser (UCSC)RCHY1
Phylogenetic Trees/Animal Genes : TreeFamRCHY1
Chemical/Protein Interactions : CTD25898
Chemical/Pharm GKB GenePA38240
Clinical trialRCHY1
Cancer Resource (Charite)ENSG00000163743
Other databases
PubMed55 Pubmed reference(s) in Entrez


Cloning and characterization of an androgen receptor N-terminal-interacting protein with ubiquitin-protein ligase activity.
Beitel LK, Elhaji YA, Lumbroso R, Wing SS, Panet-Raymond V, Gottlieb B, Pinsky L, Trifiro MA
Journal of molecular endocrinology. 2002 ; 29 (1) : 41-60.
PMID 12200228
Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation.
Leng RP, Lin Y, Ma W, Wu H, Lemmers B, Chung S, Parant JM, Lozano G, Hakem R, Benchimol S
Cell. 2003 ; 112 (6) : 779-791.
PMID 12654245
Expression of Pirh2, a newly identified ubiquitin protein ligase, in lung cancer.
Duan W, Gao L, Druhan LJ, Zhu WG, Morrison C, Otterson GA, Villalona-Calero MA
Journal of the National Cancer Institute. 2004 ; 96 (22) : 1718-1721.
PMID 15547185
Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome.
Logan IR, Sapountzi V, Gaughan L, Neal DE, Robson CN
The Journal of biological chemistry. 2004 ; 279 (12) : 11696-11704.
PMID 14701804
A new human gene hNTKL-BP1 interacts with hPirh2.
Zhang L, Li J, Wang C, Ma Y, Huo K
Biochemical and biophysical research communications. 2005 ; 330 (1) : 293-297.
PMID 15781263
Inhibition of ubiquitination and stabilization of human ubiquitin E3 ligase PIRH2 by measles virus phosphoprotein.
Chen M, Cortay JC, Logan IR, Sapountzi V, Robson CN, Gerlier D
Journal of virology. 2005 ; 79 (18) : 11824-11836.
PMID 16140759
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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Written03-2006Wenrui Duan, Miguel A. Villalona-Calero


This paper should be referenced as such :
Duan, W ; Villalona-Calero, MA
RCHY1 (ring finger and CHY zinc finger domain containing 1)
Atlas Genet Cytogenet Oncol Haematol. 2006;10(3):173-174.
Free journal version : [ pdf ]   [ DOI ]

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indexed on : Tue Feb 17 20:04:05 CET 2015

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