Atlas of Genetics and Cytogenetics in Oncology and Haematology


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MDM2 (transformed mouse 3T3 cell double minute 2, p53 binding protein)

Identity

Other namesHDMX
hdm2
HGNC (Hugo) MDM2
LocusID (NCBI) 4193
Location 12q15
Location_base_pair Starts at 69202797 and ends at 69239324 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

Description The gene encompasses 33 kb of DNA; 12 exons.
Transcription 2.3 kb nucleotides mRNA. 1476 b open reading frame.

Protein

Description 491 amino acids; 90 kDa protein.
Expression Expression of MDM2 during embryogenesis was studied in mice. During 14.5 to 18.5 days of prenatal development, the nasal respiratory epithelium expresses high levels of MDM2 RNA and protein in both wild type and p53 null embryos. MDM2 expression during development is tissue-specific and is independent of p53. The mdm2 basal mRNA expression appears relatively moderate in most organs in adult mice.
MDM2 gene was overexpressed in some types of leukemias and lymphomas. Overexpression was significantly more frequent in the low-grade type of B-cell non-Hodgkin's lymphoma (B-NHL) than in the intermediate/high grade types of lymphoma and the overexpression was also significantly more frequent in the advanced rather than the earlier stages of B-cell chronic lymphocytic leukemia (B-CLL).
Localisation MDM2 protein was found in nucleus and cytoplasm.
Function MDM2 was originally cloned from transformed Balb/c3T3 cell line called 3T3DM and was identified as an amplified oncogene in murine cell lines. MDM2 was shown to be amplified in approximately 30% of osteosarcomas and soft tissue tumors and was subsequently found to act as an ubiquitin ligase promoting proteasome dependent degradation of p53. MDM2 is also a transcriptional target of p53 such that p53 activity controls the expression and protein level of its own negative regulator, providing for an elegant feedback loop. MDM2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein. The MDM2-p53 complex also inhibits p53 mediated transactivation.
MDM2 knockout mouse embryos died during development and deletion of the p53 gene rescues MDM2 null embryos. These studies suggested that p53 is lethal in the absence of MDM2 during mouse development and MDM2 is a critical regulator to control p53 activity.
In addition, MDM2 involves nuclear export of p53 protein. Interaction between the p53 and MDM2 is not sufficient to mediate p53 degradation. The p53­MDM2 complex must be shuttled from the nucleus to the cytoplasm in order for p53 degradation.
Besides, the MDM2 protein also promotes RB (retinoblastoma) protein degradation in a proteasome-dependent manner in human tumor cell lines. MDM2 overexpression contributes to cancer development in part by destabilizing RB.
Interaction between MDM2 and the tumor suppressor genes p53 and Rb lead to deregulate cell proliferation and apoptosis. MDM2 is a key factor in human tumorigenesis.
Both MDM2 and Pirh2 (RCHY1) proteins are p53 ubiquitin-protein E3 ligases promoting for degradation of p53 protein. However, MDM2 operates in a distinct manner from Pirh2 in response to DNA damage in cancer cells. MDM2 protein is reduced or absent in the p53 null cells compared to the p53 positive cells, Whereas, Pirh2 expression is not affected by the status of p53.
A single nucleotide polymorphism (SNP309) found in the MDM2 promoter is shown to increase the affinity of the transcriptional activator Sp1, resulting in higher levels of MDM2 RNA and protein and the subsequent attenuation of the p53 pathway. In humans, SNP309 is shown to associate with accelerated tumor formation in both hereditary and sporadic cancers.
Homology The MDM2 gene has been identified in various organisms including mammals, amphibians and fishes. It belongs to the ring finger ubiquitin protein E3 ligase family, containing Conserved RING-finger Domain.

Mutations

Note MDM2 mutations are uncommon. Point mutations were reported in human cancers.

Implicated in

Entity Soft tissue tumors and osteosarcomas.
Disease A set of data of MDM2 amplification based on 3889 samples from tumors or xenografts from 28 tumor types from previously published sources was collected. The overall frequency of MDM2 amplification in these human tumors was 7%. Gene amplification was observed in 19 tumor types, with the highest frequency observed in soft tissue tumors (20%), osteosarcomas (16%) and esophageal carcinomas (13%).
Oncogenesis MDM2 is amplified in many cancers. Because the MDM2 is an ubiquitin-protein ligase that promotes p53 protein degradation, the increased MDM2 protein could play an important role in tumorigenesis, especially in the development of soft tissue tumors, osteosarcomas and esophageal carcinomas.
  

Other Leukemias implicated (Data extracted from papers in the Atlas)

Leukemias t0817q24q22ID1494

Other Solid tumors implicated (Data extracted from papers in the Atlas)

Solid Tumors ProstateOverviewID5041 ProstateOverviewID5041 ProstateOverviewID5041 ProstateOverviewID5041 ProstateOverviewID5041
softissuTumID5042 ProstateOverviewID5041 breastID5018 softissuTumID5042 AmeloblastomID5945
MedulloblastomaID5065 rhab5004 EmbryoRhabdomyoID5193

External links

Nomenclature
HGNC (Hugo)MDM2   6973
Cards
AtlasMDM2ID115ch12q15
Entrez_Gene (NCBI)MDM2  4193  MDM2 proto-oncogene, E3 ubiquitin protein ligase
GeneCards (Weizmann)MDM2
Ensembl (Hinxton)ENSG00000135679 [Gene_View]  chr12:69202797-69239324 [Contig_View]  MDM2 [Vega]
ICGC DataPortalENSG00000135679
cBioPortalMDM2
AceView (NCBI)MDM2
Genatlas (Paris)MDM2
WikiGenes4193
SOURCE (Princeton)NM_001145336 NM_001145337 NM_001145339 NM_001145340 NM_001278462 NM_002392 NM_006878 NM_006879 NM_006880 NM_006881 NM_006882 NM_032739
Genomic and cartography
GoldenPath (UCSC)MDM2  -  12q15   chr12:69202797-69239324 +  12q13-q14   [Description]    (hg19-Feb_2009)
EnsemblMDM2 - 12q13-q14 [CytoView]
Mapping of homologs : NCBIMDM2 [Mapview]
OMIM164785   614401   
Gene and transcription
Genbank (Entrez)AA708958 AF092843 AF092844 AF092845 AF201370
RefSeq transcript (Entrez)NM_001145336 NM_001145337 NM_001145339 NM_001145340 NM_001278462 NM_002392 NM_006878 NM_006879 NM_006880 NM_006881 NM_006882 NM_032739
RefSeq genomic (Entrez)AC_000144 NC_000012 NC_018923 NG_016708 NT_029419 NW_001838060 NW_004929384
Consensus coding sequences : CCDS (NCBI)MDM2
Cluster EST : UnigeneHs.733536 [ NCBI ]
CGAP (NCI)Hs.733536
Alternative Splicing : Fast-db (Paris)GSHG0006826
Alternative Splicing GalleryENSG00000135679
Gene ExpressionMDM2 [ NCBI-GEO ]     MDM2 [ SEEK ]   MDM2 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ00987 (Uniprot)
NextProtQ00987  [Medical]
With graphics : InterProQ00987
Splice isoforms : SwissVarQ00987 (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_RANBP2_1 (PS01358)    ZF_RANBP2_2 (PS50199)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)Mdm2 [organisation]   MDM2_E3_ligase [organisation]   p53_neg-reg_MDM_2/4 [organisation]   SWIB_MDM2_domain [organisation]   Znf_RanBP2 [organisation]   Znf_RING [organisation]   Znf_RING/FYVE/PHD [organisation]  
Related proteins : CluSTrQ00987
Domain families : Pfam (Sanger)SWIB (PF02201)    zf-RanBP (PF00641)   
Domain families : Pfam (NCBI)pfam02201    pfam00641   
Domain families : Smart (EMBL)RING (SM00184)  
DMDM Disease mutations4193
Blocks (Seattle)Q00987
PDB (SRS)1RV1    1T4E    1T4F    1YCR    1Z1M    2AXI    2C6A    2C6B    2F1Y    2FOP    2GV2    2HDP    2LZG    2M86    2VJE    2VJF    3EQS    3G03    3IUX    3IWY    3JZK    3JZR    3JZS    3LBK    3LBL    3LNJ    3LNZ    3MQS    3TJ2    3TPX    3TU1    3V3B    3VBG    3VZV    3W69    4DIJ    4ERE    4ERF    4HBM    4HFZ    4HG7    4JV7    4JV9    4JVE    4JVR    4JWR    4MDN    4MDQ    4OAS    4OBA    4OCC    4ODE    4ODF    4OGN    4OGT    4OGV    4OQ3   
PDB (PDBSum)1RV1    1T4E    1T4F    1YCR    1Z1M    2AXI    2C6A    2C6B    2F1Y    2FOP    2GV2    2HDP    2LZG    2M86    2VJE    2VJF    3EQS    3G03    3IUX    3IWY    3JZK    3JZR    3JZS    3LBK    3LBL    3LNJ    3LNZ    3MQS    3TJ2    3TPX    3TU1    3V3B    3VBG    3VZV    3W69    4DIJ    4ERE    4ERF    4HBM    4HFZ    4HG7    4JV7    4JV9    4JVE    4JVR    4JWR    4MDN    4MDQ    4OAS    4OBA    4OCC    4ODE    4ODF    4OGN    4OGT    4OGV    4OQ3   
PDB (IMB)1RV1    1T4E    1T4F    1YCR    1Z1M    2AXI    2C6A    2C6B    2F1Y    2FOP    2GV2    2HDP    2LZG    2M86    2VJE    2VJF    3EQS    3G03    3IUX    3IWY    3JZK    3JZR    3JZS    3LBK    3LBL    3LNJ    3LNZ    3MQS    3TJ2    3TPX    3TU1    3V3B    3VBG    3VZV    3W69    4DIJ    4ERE    4ERF    4HBM    4HFZ    4HG7    4JV7    4JV9    4JVE    4JVR    4JWR    4MDN    4MDQ    4OAS    4OBA    4OCC    4ODE    4ODF    4OGN    4OGT    4OGV    4OQ3   
PDB (RSDB)1RV1    1T4E    1T4F    1YCR    1Z1M    2AXI    2C6A    2C6B    2F1Y    2FOP    2GV2    2HDP    2LZG    2M86    2VJE    2VJF    3EQS    3G03    3IUX    3IWY    3JZK    3JZR    3JZS    3LBK    3LBL    3LNJ    3LNZ    3MQS    3TJ2    3TPX    3TU1    3V3B    3VBG    3VZV    3W69    4DIJ    4ERE    4ERF    4HBM    4HFZ    4HG7    4JV7    4JV9    4JVE    4JVR    4JWR    4MDN    4MDQ    4OAS    4OBA    4OCC    4ODE    4ODF    4OGN    4OGT    4OGV    4OQ3   
Human Protein AtlasENSG00000135679 [gene] [tissue] [antibody] [cell] [cancer]
Peptide AtlasQ00987
HPRD01272
IPIIPI00789663   IPI00944540   IPI00218551   IPI00218552   IPI00218553   IPI00295694   IPI00791322   IPI00969213   IPI00410597   IPI00168602   IPI00383012   IPI00472854   IPI01021805   IPI01018751   IPI00386544   IPI00386041   IPI00472971   IPI00103724   IPI00041320   IPI00103723   IPI00984631   IPI00853596   IPI00978667   IPI00386541   IPI00748589   IPI00386543   IPI00973836   IPI00973912   IPI00025490   IPI01015017   IPI00384422   IPI01011784   IPI00798285   IPI01011407   IPI01010971   IPI00981581   
Protein Interaction databases
DIP (DOE-UCLA)Q00987
IntAct (EBI)Q00987
FunCoupENSG00000135679
BioGRIDMDM2
InParanoidQ00987
Interologous Interaction database Q00987
IntegromeDBMDM2
STRING (EMBL)MDM2
Ontologies - Pathways
Ontology : AmiGOnegative regulation of transcription from RNA polymerase II promoter  p53 binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  nucleolus  cytoplasm  cytosol  plasma membrane  protein complex assembly  DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest  DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest  traversing start control point of mitotic cell cycle  epidermal growth factor receptor signaling pathway  synaptic transmission  zinc ion binding  positive regulation of cell proliferation  fibroblast growth factor receptor signaling pathway  response to carbohydrate  response to iron ion  positive regulation of gene expression  negative regulation of protein processing  viral process  protein ubiquitination  nuclear body  ligase activity  peptidyl-lysine modification  enzyme binding  endocytic vesicle membrane  ubiquitin protein ligase binding  protein destabilization  response to magnesium ion  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  protein localization to nucleus  Fc-epsilon receptor signaling pathway  regulation of protein catabolic process  response to cocaine  response to drug  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  identical protein binding  peroxisome proliferator activated receptor binding  negative regulation of apoptotic process  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  protein complex  response to morphine  negative regulation of DNA damage response, signal transduction by p53 class mediator  innate immune response  establishment of protein localization  synapse  response to ether  negative regulation of transcription, DNA-templated  positive regulation of mitotic cell cycle  response to antibiotic  positive regulation of protein export from nucleus  neurotrophin TRK receptor signaling pathway  phosphatidylinositol-mediated signaling  cellular response to hydrogen peroxide  negative regulation of cell cycle arrest  cellular response to acid  cellular response to antibiotic  cellular response to vitamin B1  cellular response to alkaloid  cellular response to peptide hormone stimulus  cellular response to estrogen stimulus  cellular response to hypoxia  cellular response to UV-C  scaffold protein binding  
Ontology : EGO-EBInegative regulation of transcription from RNA polymerase II promoter  p53 binding  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  nucleolus  cytoplasm  cytosol  plasma membrane  protein complex assembly  DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest  DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest  traversing start control point of mitotic cell cycle  epidermal growth factor receptor signaling pathway  synaptic transmission  zinc ion binding  positive regulation of cell proliferation  fibroblast growth factor receptor signaling pathway  response to carbohydrate  response to iron ion  positive regulation of gene expression  negative regulation of protein processing  viral process  protein ubiquitination  nuclear body  ligase activity  peptidyl-lysine modification  enzyme binding  endocytic vesicle membrane  ubiquitin protein ligase binding  protein destabilization  response to magnesium ion  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  protein localization to nucleus  Fc-epsilon receptor signaling pathway  regulation of protein catabolic process  response to cocaine  response to drug  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  identical protein binding  peroxisome proliferator activated receptor binding  negative regulation of apoptotic process  negative regulation of cysteine-type endopeptidase activity involved in apoptotic process  protein complex  response to morphine  negative regulation of DNA damage response, signal transduction by p53 class mediator  innate immune response  establishment of protein localization  synapse  response to ether  negative regulation of transcription, DNA-templated  positive regulation of mitotic cell cycle  response to antibiotic  positive regulation of protein export from nucleus  neurotrophin TRK receptor signaling pathway  phosphatidylinositol-mediated signaling  cellular response to hydrogen peroxide  negative regulation of cell cycle arrest  cellular response to acid  cellular response to antibiotic  cellular response to vitamin B1  cellular response to alkaloid  cellular response to peptide hormone stimulus  cellular response to estrogen stimulus  cellular response to hypoxia  cellular response to UV-C  scaffold protein binding  
Pathways : BIOCARTACell Cycle: G2/M Checkpoint [Genes]    Hypoxia and p53 in the Cardiovascular system [Genes]    ATM Signaling Pathway [Genes]    Tumor Suppressor Arf Inhibits Ribosomal Biogenesis [Genes]    Sumoylation by RanBP2 Regulates Transcriptional Repression [Genes]    HIV-I Nef: negative effector of Fas and TNF [Genes]    CTCF: First Multivalent Nuclear Factor [Genes]    p53 Signaling Pathway [Genes]   
Pathways : KEGGFoxO signaling pathway    Cell cycle    p53 signaling pathway    Ubiquitin mediated proteolysis    Endocytosis    PI3K-Akt signaling pathway    Thyroid hormone signaling pathway    Epstein-Barr virus infection    Pathways in cancer    Transcriptional misregulation in cancer    Viral carcinogenesis    Proteoglycans in cancer    MicroRNAs in cancer    Glioma    Prostate cancer    Melanoma    Bladder cancer    Chronic myeloid leukemia   
Protein Interaction DatabaseMDM2
Wikipedia pathwaysMDM2
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)MDM2
snp3D : Map Gene to Disease4193
SNP (GeneSNP Utah)MDM2
SNP : HGBaseMDM2
Genetic variants : HAPMAPMDM2
Exome VariantMDM2
1000_GenomesMDM2 
ICGC programENSG00000135679 
Cancer Gene: CensusMDM2 
Somatic Mutations in Cancer : COSMICMDM2 
CONAN: Copy Number AnalysisMDM2 
Mutations and Diseases : HGMDMDM2
Genomic VariantsMDM2  MDM2 [DGVbeta]
dbVarMDM2
ClinVarMDM2
Pred. of missensesPolyPhen-2  SIFT(SG)  SIFT(JCVI)  Align-GVGD  MutAssessor  Mutanalyser  
Pred. splicesGeneSplicer  Human Splicing Finder  MaxEntScan  
Diseases
OMIM164785    614401   
MedgenMDM2
GENETestsMDM2
Disease Genetic AssociationMDM2
Huge Navigator MDM2 [HugePedia]  MDM2 [HugeCancerGEM]
General knowledge
Homologs : HomoloGeneMDM2
Homology/Alignments : Family Browser (UCSC)MDM2
Phylogenetic Trees/Animal Genes : TreeFamMDM2
Chemical/Protein Interactions : CTD4193
Chemical/Pharm GKB GenePA30718
Drug Sensitivity MDM2
Clinical trialMDM2
Cancer Resource (Charite)ENSG00000135679
Other databases
Probes
Litterature
PubMed499 Pubmed reference(s) in Entrez
CoreMineMDM2
iHOPMDM2
OncoSearchMDM2

Bibliography

Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line.
Cahilly-Snyder L, Yang-Feng T, Francke U, George DL
Somatic cell and molecular genetics. 1987 ; 13 (3) : 235-244.
PMID 3474784
 
Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line.
Fakharzadeh SS, Trusko SP, George DL
The EMBO journal. 1991 ; 10 (6) : 1565-1569.
PMID 2026149
 
The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation.
Momand J, Zambetti GP, Olson DC, George D, Levine AJ
Cell. 1992 ; 69 (7) : 1237-1245.
PMID 1535557
 
Amplification of a gene encoding a p53-associated protein in human sarcomas.
Oliner JD, Kinzler KW, Meltzer PS, George DL, Vogelstein B
Nature. 1992 ; 358 (6381) : 80-83.
PMID 1614537
 
mdm2 expression is induced by wild type p53 activity.
Barak Y, Juven T, Haffner R, Oren M
The EMBO journal. 1993 ; 12 (2) : 461-468.
PMID 8440237
 
Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53.
Oliner JD, Pietenpol JA, Thiagalingam S, Gyuris J, Kinzler KW, Vogelstein B
Nature. 1993 ; 362 (6423) : 857-860.
PMID 8479525
 
The mdm-2 gene is induced in response to UV light in a p53-dependent manner.
Perry ME, Piette J, Zawadzki JA, Harvey D, Levine AJ
Proceedings of the National Academy of Sciences of the United States of America. 1993 ; 90 (24) : 11623-11627.
PMID 8265599
 
Interactions between p53 and MDM2 in a mammalian cell cycle checkpoint pathway.
Chen CY, Oliner JD, Zhan Q, Fornace AJ Jr, Vogelstein B, Kastan MB
Proceedings of the National Academy of Sciences of the United States of America. 1994 ; 91 (7) : 2684-2688.
PMID 8146175
 
Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53.
Jones SN, Roe AE, Donehower LA, Bradley A
Nature. 1995 ; 378 (6553) : 206-208.
PMID 7477327
 
Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53.
Montes de Oca Luna R, Wagner DS, Lozano G
Nature. 1995 ; 378 (6553) : 203-206.
PMID 7477326
 
mdm-2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein.
Chen J, Wu X, Lin J, Levine AJ
Molecular and cellular biology. 1996 ; 16 (5) : 2445-2452.
PMID 8628312
 
Overexpression of the MDM2 oncogene in leukemia and lymphoma.
Watanabe T, Ichikawa A, Saito H, Hotta T
Leukemia & lymphoma. 1996 ; 21 (5-6) : 391-397.
PMID 9172803
 
Mdm2 promotes the rapid degradation of p53.
Haupt Y, Maya R, Kazaz A, Oren M
Nature. 1997 ; 387 (6630) : 296-299.
PMID 9153395
 
Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53.
Honda R, Tanaka H, Yasuda H
FEBS letters. 1997 ; 420 (1) : 25-27.
PMID 9450543
 
Regulation of p53 stability by Mdm2.
Kubbutat MH, Jones SN, Vousden KH
Nature. 1997 ; 387 (6630) : 299-303.
PMID 9153396
 
Point mutations and nucleotide insertions in the MDM2 zinc finger structure of human tumours.
Schlott T, Reimer S, Jahns A, Ohlenbusch A, Ruschenburg I, Nagel H, Droese M
The Journal of pathology. 1997 ; 182 (1) : 54-61.
PMID 9227342
 
Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6.
Freedman DA, Levine AJ
Molecular and cellular biology. 1998 ; 18 (12) : 7288-7293.
PMID 9819415
 
MDM2 expression during mouse embryogenesis and the requirement of p53.
Lˆ©veillard T, Gorry P, Niederreither K, Wasylyk B
Mechanisms of development. 1998 ; 74 (1-2) : 189-193.
PMID 9651526
 
The MDM2 gene amplification database.
Momand J, Jung D, Wilczynski S, Niland J
Nucleic acids research. 1998 ; 26 (15) : 3453-3459.
PMID 9671804
 
P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2.
Tao W, Levine AJ
Proceedings of the National Academy of Sciences of the United States of America. 1999 ; 96 (12) : 6937-6941.
PMID 10359817
 
A single nucleotide polymorphism in the MDM2 promoter attenuates the p53 tumor suppressor pathway and accelerates tumor formation in humans.
Bond GL, Hu W, Bond EE, Robins H, Lutzker SG, Arva NC, Bargonetti J, Bartel F, Taubert H, Wuerl P, Onel K, Yip L, Hwang SJ, Strong LC, Lozano G, Levine AJ
Cell. 2004 ; 119 (5) : 591-602.
PMID 15550242
 
MDM2 promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma protein.
Sdek P, Ying H, Chang DL, Qiu W, Zheng H, Touitou R, Allday MJ, Xiao ZX
Molecular cell. 2005 ; 20 (5) : 699-708.
PMID 16337594
 
Differential response between the p53 ubiquitin-protein ligases Pirh2 and MdM2 following DNA damage in human cancer cells.
Duan W, Gao L, Wu X, Zhang Y, Otterson GA, Villalona-Calero MA
Experimental cell research. 2006 ; 312 (17) : 3370-3378.
PMID 16934800
 
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Contributor(s)

Written12-2006Wenrui Duan, Miguel A Villalona-Calero

Citation

This paper should be referenced as such :
Villalona-Calero, MA ; Duan, W
MDM2 (transformed mouse 3T3 cell double minute 2, p53 binding protein)
Atlas Genet Cytogenet Oncol Haematol. 2007;11(2):102-104.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/MDM2ID115ch12q15.html

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indexed on : Sat Jul 26 15:17:25 CEST 2014

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