Aliases for MDM2 Gene
- MDM2 Proto-Oncogene, E3 Ubiquitin Protein Ligase 2 3
- Oncoprotein Mdm2 3 4
- ACTFS 3 6
- Hdm2 3 4
- Mdm2, Transformed 3T3 Cell Double Minute 2, P53 Binding Protein (Mouse) 2
- Mdm2, Transformed 3T3 Cell Double Minute 2, P53 Binding Protein 3
- Mouse Double Minute 2, Human Homolog Of; P53-Binding Protein 2
- Double Minute 2, Human Homolog Of; P53-Binding Protein 3
- Mdm2, P53 E3 Ubiquitin Protein Ligase Homolog 3
External Ids for MDM2 Gene
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]
GeneCards Summary for MDM2 Gene
MDM2 (MDM2 Proto-Oncogene, E3 Ubiquitin Protein Ligase) is a Protein Coding gene. Diseases associated with MDM2 include malignant fibrous histiocytoma of bone and anal squamous cell carcinoma. Among its related pathways are PI3K-Akt signaling pathway and PI-3K cascade. GO annotations related to this gene include identical protein binding and enzyme binding. An important paralog of this gene is MDM4.
UniProtKB/Swiss-Prot for MDM2 Gene
E3 ubiquitin-protein ligase that mediates ubiquitination of p53/TP53, leading to its degradation by the proteasome. Inhibits p53/TP53- and p73/TP73-mediated cell cycle arrest and apoptosis by binding its transcriptional activation domain. Also acts as a ubiquitin ligase E3 toward itself and ARRB1. Permits the nuclear export of p53/TP53. Promotes proteasome-dependent ubiquitin-independent degradation of retinoblastoma RB1 protein. Inhibits DAXX-mediated apoptosis by inducing its ubiquitination and degradation. Component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in stabilizing p53/TP53. Also component of the TRIM28/KAP1-ERBB4-MDM2 complex which links growth factor and DNA damage response pathways. Mediates ubiquitination and subsequent proteasome degradation of DYRK2 in nucleus. Ubiquitinates IGF1R and SNAI1 and promotes them to proteasomal degradation.
Ligases catalyze the joining of two molecules with concomitant hydrolysis of the diphosphate bond in ATP or a similar triphosphate. They belong to the E.C. 6 class, which also includes synthases and carboxylases. Ubiquitin ligases, such as MDM2, E3A and anaphase-promoting complex, attach ubiquitin molecules onto lysine residues of target proteins. Ubiquitin ligases function as a complex of an E1-activating enzyme, an E2-conjugating enzyme and an E3-ubiquiting enzyme. Using ATP, E1 activates the ubiquitin molecule and transfer it to E2. E2 interacts with E3 partners to transfer the ubiquitin moeity to the target protein. Generally multiple ubiquitin molecules are attached (polyubiquitination), which marks the target protein for proteasomal degradation.