MDM2 Proto-Oncogene Peptide 1
Rabbit Recombinant Cloned Antibody
Peptide, Recombinant Full-length, Native Protein, Phosphorylation
This PDF contains the evaluation results provided by the Human Protein Atlas (www.proteinatlas.org)
This antibody is not suitable for use in an Immunohistochemistry format as described in SOP M-106.
NCI Identification Number:
MDM2 Proto-Oncogene Peptide 1
CPTC-MDM2 Peptide 1
MDM2 Proto-Oncogene; MDM2 Proto-Oncogene, E3 Ubiquitin Protein Ligase; E3 Ubiquitin-Protein Ligase Mdm2; Oncoprotein Mdm2; Hdm2; Mdm2, Transformed 3T3 Cell Double Minute 2, P53 Binding Protein (Mouse); Mdm2, Transformed 3T3 Cell Double Minute 2, P53 Binding Protein; Mouse Double Minute 2, Human Homolog Of; P53-Binding Protein; Double Minute 2, Human Homolog Of; P53-Binding Protein; Mdm2, P53 E3 Ubiquitin Protein Ligase Homolog; MDM2 Oncogene, E3 Ubiquitin Protein Ligase; Mdm2 P53 Binding Protein Homolog (Mouse); RING-Type E3 Ubiquitin Transferase Mdm2; P53-Binding Protein Mdm2; Double Minute 2 Protein; EC 220.127.116.11; EC 6.3.2; ACTFS; HDMX
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.MDM2 (MDM2 Proto-Oncogene) is a Protein Coding gene. Diseases associated with MDM2 include Accelerated Tumor Formation and Dedifferentiated Liposarcoma. Among its related pathways are RET signaling and Bladder cancer. Gene Ontology (GO) annotations related to this gene include identical protein binding and ligase activity. An important paralog of this gene is MDM4.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 (PubMed:12821780, PubMed:15053880, PubMed:15195100, PubMed:15632057, PubMed:16337594, PubMed:17290220, PubMed:19098711, PubMed:19219073, PubMed:19837670, PubMed:19965871, PubMed:20173098, PubMed:20385133, PubMed:20858735, PubMed:22128911). Ubiquitinates DCX, leading to DCX degradation and reduction of the dendritic spine density of olfactory bulb granule cells (By similarity). Ubiquitinates DLG4, leading to proteasomal degradation of DLG4 which is required for AMPA receptor endocytosis (By similarity). Ligases are enzymes which 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 of enzymes, which also includes synthases and carboxylases.
NCBI Accession Number:
UniProt Accession Number:
Calculated Isoelectric Point:
No SOPs available.
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