MDM4

From Wikipedia, the free encyclopedia
MDM4
Protein MDM4 PDB 2cr8.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesMDM4, HDMX, MDMX, MRP1, p53 regulator, MDM4 regulator of p53, BMFS6
External IDsOMIM: 602704 MGI: 107934 HomoloGene: 1794 GeneCards: MDM4
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_008575
NM_001302801
NM_001302802
NM_001302803
NM_001302804

RefSeq (protein)

NP_001289730
NP_001289731
NP_001289732
NP_001289733
NP_032601

Location (UCSC)Chr 1: 204.52 – 204.56 MbChr 1: 132.89 – 132.96 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein Mdm4 is a protein that in humans is encoded by the MDM4 gene.[5][6]

Function[]

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[6]

Interactions[]

MDM4 has been shown to interact with E2F1,[7] Mdm2[8][9][10][11] and P53.[5][10]

References[]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198625 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000054387 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. hdl:2066/26148. PMID 9226370.
  6. ^ a b "Entrez Gene: MDM4 Mdm4, transformed 3T3 cell double minute 4, p53 binding protein (mouse)".
  7. ^ 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. S2CID 38805122.
  8. ^ 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.
  9. ^ 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. S2CID 20021952.
  10. ^ 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.
  11. ^ 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[]


Retrieved from ""