MDM2 (GeneName), E3 ubiquitin-protein ligase Mdm2 (ProteinName), MDM2_HUMAN.
Human MDM2/ E3 ubiquitin-protein ligase Mdm2 ELISA Kit
Double minute 2 protein, Hdm2, Oncoprotein Mdm2, RING-type E3 ubiquitin transferase Mdm2, p53-binding protein Mdm2
Natural and recombinant human E3 ubiquitin-protein ligase Mdm2
Serum, plasma, tissue homogenates, cell culture supernates and other biological fluids
Interacts with p53/TP53, TP73/p73, RBL5 and RP11. Binds specifically to RNA. Can interact with RB1, E1A-associated protein EP300 and the E2F1 transcription factor. Forms a ternary complex with p53/TP53 and WWOX. Interacts with CDKN2AIP, RFWD3, USP7, PYHIN1, UBXN6, and RBBP6. Interacts with ARRB1 and ARRB2. Interacts with PSMA3. Found in a trimeric complex with MDM2, MDM4 and USP2. Interacts with USP2 (via N-terminus and C-terminus). Interacts with MDM4. Part of a complex with MDM2, DAXX, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts directly with DAXX and USP7. Interacts (via C-terminus) with RASSF1 isoform A (via N-terminus); the interaction is independent of TP53. Interacts with APEX1; leading to its ubiquitination and degradation. Interacts with RYBP; this inhibits ubiquitination of TP53. Identified in a complex with RYBP and p53/TP53. Also component of the TRIM28/KAP1-MDM2-p53/TP53 complex involved in regulating p53/TP53 stabilization and activity. Binds directly both p53/TP53 and TRIM28. Component of the TRIM28/KAP1-ERBB4-MDM2 complex involved in connecting growth factor responses with DNA damage. Interacts directly with both TRIM28 and ERBB4 in the complex. Interacts with DYRK2. Interacts with IGF1R. Interacts with TRIM13; the interaction ubiquitinates MDM2 leading to its proteasomal degradation. Interacts with SNAI1; this interaction promotes SNAI1 ubiquitination. Interacts with NOTCH1 (via intracellular domain). Interacts with FHIT. Interacts with RFFL and RNF34; the interaction stabilizes MDM2. Interacts with CDK5RAP3 and CDKN2A/ARF; form a ternary complex involved in regulation of p53/TP53 (PubMed:16173922). Interacts with MTA1. Interacts with AARB2. Interacts with MTBP. Interacts with PML. Interacts with RPL11. Interacts with TBRG1. Interacts with herpes virus 8 protein v-IRF4. Interacts with and ubiquitinates HIV-1 Tat.
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.
Nucleus Nucleoplasm Cytoplasm Nucleus Nucleolus Expressed predominantly in the nucleoplasm. Interaction with ARF(P14) results in the localization of both proteins to the nucleolus. The nucleolar localization signals in both ARF(P14) and MDM2 may be necessary to allow efficient nucleolar localization of both proteins. Colocalizes with RASSF1 isoform A in the nucleus.
MCNTNMSVPT | DGAVTTSQIP | ASEQETLVRP | KPLLLKLLKS | VGAQKDTYTM |
KEVLFYLGQY | IMTKRLYDEK | QQHIVYCSND | LLGDLFGVPS | FSVKEHRKIY |
TMIYRNLVVV | NQQESSDSGT | SVSENRCHLE | GGSDQKDLVQ | ELQEEKPSSS |
HLVSRPSTSS | RRRAISETEE | NSDELSGERQ | RKRHKSDSIS | LSFDESLALC |
VIREICCERS | SSSESTGTPS | NPDLDAGVSE | HSGDWLDQDS | VSDQFSVEFE |
VESLDSEDYS | LSEEGQELSD | EDDEVYQVTV | YQAGESDTDS | FEEDPEISLA |
DYWKCTSCNE | MNPPLPSHCN | RCWALRENWL | PEDKGKDKGE | ISEKAKLENS |
TQAEEGFDVP | DCKKTIVNDS | RESCVEENDD | KITQASQSQE | SEDYSQPSTS |
SSIIYSSQED | VKEFEREETQ | DKEESVESSL | PLNAIEPCVI | CQGRPKNGCI |
VHGKTGHLMA | CFTCAKKLKK | RNKPCPVCRQ | PIQMIVLTYF | P
This product has not yet been referenced specifically in any publications.
"Iron-dependent regulation of MDM2 influences p53 activity and hepatic carcinogenesis."
"ATM activates p53 by regulating MDM2 oligomerization and E3 processivity."
"Risk of MDM2 SNP309 alone or in combination with the p53 codon 72 polymorphism in acute myeloid leukemia."
"Germline analysis of thymidine/guanidine polymorphism at position 309 of the Mdm2 promoter in malignant melanoma patients."
"Hypophosphorylation of Mdm2 augments p53 stability."
"Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase."
"Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53."
"Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53."
"Amplification of a gene encoding a p53-associated protein in human sarcomas."
"Inactivation of the MDM2 RING domain enhances p53 transcriptional activity in mice."
Displaying results : 0
No feedback yet, let's comment.
Product Name *
Size Quantity Price ($) Subtotal 1 ($)
Subtotal 2: $
Size Quantity Price ($)
Do you want to be our agent and get a lower discount?
Please contact us:
Please contact us: