MDM4

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Mdm4 p53 binding protein homolog (mouse)
Protein MDM4 PDB 2cr8.png
PDB rendering based on 2cr8.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
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
Orthologs
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]

Interactions[edit]

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

References[edit]

  1. ^ 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. 
  2. ^ a b "Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)". 
  3. ^ Strachan, Gordon D; Jordan-Sciutto Kelly L, Rallapalli Ravikumar, Tuan Rocky S, Hall David J (Feb 2003). "The E2F-1 transcription factor is negatively regulated by its interaction with the MDMX protein". J. Cell. Biochem. (United States) 88 (3): 557–68. doi:10.1002/jcb.10318. ISSN 0730-2312. PMID 12532331. 
  4. ^ Kadakia, Madhavi; Brown Thomas L, McGorry Molly M, Berberich Steven J (Dec 2002). "MdmX inhibits Smad transactivation". Oncogene (England) 21 (57): 8776–85. doi:10.1038/sj.onc.1205993. ISSN 0950-9232. 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. (NETHERLANDS) 447 (1): 5–9. doi:10.1016/S0014-5793(99)00254-9. ISSN 0014-5793. PMID 10218570. 
  6. ^ a b Badciong, James C; Haas Arthur L (Dec 2002). "MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination". J. Biol. Chem. (United States) 277 (51): 49668–75. doi:10.1074/jbc.M208593200. ISSN 0021-9258. PMID 12393902. 
  7. ^ Linke, K; Mace P D, Smith C A, Vaux D L, Silke J, Day C L (May 2008). "Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans". Cell Death Differ. (England) 15 (5): 841–8. doi:10.1038/sj.cdd.4402309. ISSN 1350-9047. PMID 18219319. 

Further reading[edit]