◀ Back to MDM2

MDM2 — MTBP

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: MTBP — MDM2 (direct interaction, pull down) Boyd et al., J Biol Chem 2000*
• IRef Biogrid Interaction: MTBP — MDM2 (physical association, affinity chromatography technology) Boyd et al., J Biol Chem 2000*
• IRef Biogrid Interaction: MTBP — MDM2 (direct interaction, two hybrid) Boyd et al., J Biol Chem 2000*
• IRef Biogrid Interaction: MTBP — MDM2 (physical association, affinity chromatography technology) Brady et al., Mol Cell Biol 2005*
• IRef Hprd Interaction: MTBP — MDM2 (in vitro) Boyd et al., J Biol Chem 2000*
• IRef Hprd Interaction: Complex of 36 proteins (in vivo) Maguire et al., Cancer Res 2008
• IRef Hprd Interaction: Complex of MDM4-MDM2-DHFR-MTBP-PSMD10-RB1 (in vivo) Maguire et al., Cancer Res 2008

Text-mined interactions from Literome

Brady et al., Mol Cell Biol 2005 : Regulation of p53 and MDM2 activity by MTBP ... Our findings suggest that MTBP differentially regulates the E3 ubiquitin ligase activity of MDM2 towards two of its most critical targets ( itself and p53 ) and in doing so significantly contributes to MDM2 dependent p53 homeostasis in unstressed cells
Odvody et al., Oncogene 2010 (Lymphoma, B-Cell) : Surprisingly, reduced levels of Mtbp did not lead to an increase in B-cell apoptosis or affect Mdm2