a ubiquitin ligase for p53, plays a central role in regulation of the stability of p53 via Akt-mediated MDM2 phosphorylation. Phosphorylation of MDM2 increases its interaction with p300, providing a platform to allow the assembly of the protein complex necessary for MDM2-mediated ubiquitination and degradation of p53. Phosphorylation of MDM2 also blocks its binding to p19ARF, increasing the degradation of p53. Facilitates the nuclear export of p53 and targets it for proteasome-mediated proteolysis. Eight alternatively spliced isoforms have been reported. Note: This description may include information from UniProtKB.
Molecular Function: 5S rRNA binding; enzyme binding; identical protein binding; ligase activity; p53 binding; protein binding; protein N-terminus binding; ribonucleoprotein binding; SUMO ligase activity; ubiquitin protein ligase binding; ubiquitin-protein ligase activity; zinc ion binding
Biological Process: DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; establishment of protein localization; negative regulation of DNA damage response, signal transduction by p53 class mediator; negative regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; peptidyl-lysine modification; positive regulation of cell proliferation; positive regulation of mitotic cell cycle; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; protein autoubiquitination; protein complex assembly; protein destabilization; protein deubiquitination; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; proteolysis involved in cellular protein catabolic process; regulation of protein catabolic process; response to antibiotic