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MDM4, p53 regulator
Protein MDM4 PDB 2cr8.png
PDB rendering based on 2cr8.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols MDM4 ; HDMX; MDMX; MRP1
External IDs OMIM602704 MGI107934 HomoloGene1794 ChEMBL: 1255126 GeneCards: MDM4 Gene
RNA expression pattern
PBB GE MDM4 205655 at tn.png
More reference expression data
Species Human Mouse
Entrez 4194 17248
Ensembl ENSG00000198625 ENSMUSG00000054387
UniProt O15151 O35618
RefSeq (mRNA) NM_001204171 NM_008575
RefSeq (protein) NP_001191100 NP_032601
Location (UCSC) Chr 1:
204.49 – 204.54 Mb
Chr 1:
132.99 – 133.03 Mb
PubMed search [1] [2]

Protein Mdm4 is a protein that in humans is encoded by the MDM4 gene.[1][2]


The human MDM4 gene, which plays a role in apoptosis, encodes a 490-amino acid protein containing a RING finger domain and a putative nuclear localization signal. The MDM4 putative nuclear localization signal, which all Mdm proteins contain, is located in the C-terminal region of the protein. The mRNA is expressed at a high level in thymus and at lower levels in all other tissues tested. MDM4 protein produced by in vitro translation interacts with p53 via a binding domain located in the N-terminal region of the MDM4 protein. MDM4 shows significant structural similarity to p53-binding protein MDM2[2]


MDM4 has been shown to interact with E2F1,[3] Mdm2[4][5][6][7] and P53.[1][6]


  1. ^ a b Shvarts A, Bazuine M, Dekker P, Ramos YF, Steegenga WT, Merckx G et al. (Sep 1997). "Isolation and identification of the human homolog of a new p53-binding protein, Mdmx". Genomics 43 (1): 34–42. doi:10.1006/geno.1997.4775. PMID 9226370. 
  2. ^ a b "Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)". 
  3. ^ Strachan GD, Jordan-Sciutto KL, Rallapalli R, Tuan RS, Hall DJ (Feb 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. 88 (3): 557–68. doi:10.1002/jcb.10318. PMID 12532331. 
  4. ^ Kadakia M, Brown TL, McGorry MM, Berberich SJ (Dec 2002). "MdmX inhibits Smad transactivation". Oncogene 21 (57): 8776–85. doi:10.1038/sj.onc.1205993. PMID 12483531. 
  5. ^ Tanimura S, Ohtsuka S, Mitsui K, Shirouzu K, Yoshimura A, Ohtsubo M (Mar 1999). "MDM2 interacts with MDMX through their RING finger domains". FEBS Lett. 447 (1): 5–9. doi:10.1016/S0014-5793(99)00254-9. PMID 10218570. 
  6. ^ a b Badciong JC, Haas AL (Dec 2002). "MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination". J. Biol. Chem. 277 (51): 49668–75. doi:10.1074/jbc.M208593200. PMID 12393902. 
  7. ^ Linke K, Mace PD, Smith CA, Vaux DL, Silke J, Day CL (May 2008). "Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans". Cell Death Differ. 15 (5): 841–8. doi:10.1038/sj.cdd.4402309. PMID 18219319. 

Further reading[edit]