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Protein MDM4 PDB 2cr8.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases MDM4, HDMX, MDMX, MRP1, p53 regulator
External IDs MGI: 107934 HomoloGene: 1794 GeneCards: MDM4
Genetically Related Diseases
breast cancer[1]
RNA expression pattern
PBB GE MDM4 205655 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)
Location (UCSC) Chr 1: 204.52 – 204.56 Mb Chr 1: 132.96 – 133.03 Mb
PubMed search [2] [3]
View/Edit Human View/Edit Mouse

Protein Mdm4 is a protein that in humans is encoded by the MDM4 gene.[4][5]


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[5]


MDM4 has been shown to interact with E2F1,[6] Mdm2[7][8][9][10] and P53.[4][9]


  1. ^ "Diseases that are genetically associated with MDM4 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ a b Shvarts A, Bazuine M, Dekker P, Ramos YF, Steegenga WT, Merckx G, van Ham RC, van der Houven van Oordt W, van der Eb AJ, Jochemsen AG (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. 
  5. ^ a b "Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)". 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ 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. 
  9. ^ 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. 
  10. ^ 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]