MDM2 Antibody – Rabbit Polyclonal

This gene encodes a nuclear-localized E3 ubiquitin ligase. The encoded protein can promote tumor formation by targeting tumor suppressor proteins, such as p53, for proteasomal degradation. This gene is itself transcriptionally-regulated by p53. Overexpression or amplification of this locus is detected in a variety of different cancers. There is a pseudogene for this gene on chromosome 2. Alternative splicing results in a multitude of transcript variants, many of which may be expressed only in tumor cells. [provided by RefSeq, Jun 2013]

MDM2: 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.

Protein type: EC 6.3.2.-; EC 6.3.2.19; Inhibitor; Ligase; Nucleolus; Oncoprotein; Ubiquitin conjugating system; Ubiquitin ligase

Chromosomal Location of Human Ortholog: 12q15

Cellular Component: cytoplasm; cytosol; nuclear body; nucleolus; nucleoplasm; nucleus; plasma membrane; protein complex

Molecular Function: enzyme binding; identical protein binding; ligase activity; p53 binding; protein 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 sumoylation; protein ubiquitination; protein ubiquitination during ubiquitin-dependent protein catabolic process; regulation of protein catabolic process; response to antibiotic

Disease: Accelerated Tumor Formation, Susceptibility To