Isolation and identification of the human homolog of a new p53-binding protein, Mdmx

Avi Shvarts, Merlijn Bazuine, Patrick Dekker, Yolande F.M. Ramos, Wilma T. Steegenga, Gerard Merckx, Reinier C.A. Van Ham, Willemien Van Der Houven Van Oordt, Alex J. Van Der Eb, A. G. Jochemsen*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review


We recently reported the identification of a mouse eDNA encoding a new p53-associating protein that we called Mdmx because of its structural similarity to Mdm2, a well-known p53-binding protein. Here we report the isolation of a cDNA encoding the human homolog of Mdmx. The ORF of the cDNA encodes a protein of 490 amino acids, 90% similar to mouse Mdmx. The homology between Mdmx and Mdm2 is most prominent in the p53-binding domain and the putative metal-binding domains. The Mdmx protein, which, based on SDS-PAGE, has a MW of 80 kDa, can bind p53 in vitro. The human MDMX gene is transcribed in all tissues tested, with high levels in thymus. By fluorescence in situ hybridization analysis we mapped the mouse mdmx gene to chromosome 1 (region F-G) and the human MDMX gene to chromosome 1q32.

Original languageEnglish
Pages (from-to)34-42
Number of pages9
Issue number1
Publication statusPublished - 1 Jul 1997
Externally publishedYes

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