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MECOM — SMAD3

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

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: SMAD3 — MECOM (coimmunoprecipitation) Nitta et al., Oncogene 2005*
• IRef Biogrid Interaction: SMAD3 — MECOM (physical association, affinity chromatography technology) Kurokawa et al., Nature 1998*
• IRef Biogrid Interaction: SMAD3 — MECOM (direct interaction, pull down) Kurokawa et al., Nature 1998*
• IRef Biogrid Interaction: SMAD3 — MECOM (physical association, affinity chromatography technology) Alliston et al., J Biol Chem 2005*
• IRef Biogrid Interaction: SMAD3 — MECOM (direct interaction, pull down) Alliston et al., J Biol Chem 2005*
• IRef Hprd Interaction: MECOM — SMAD3 (in vitro) Kurokawa et al., Nature 1998*
• IRef Hprd Interaction: MECOM — SMAD3 (in vivo) Kurokawa et al., Nature 1998*
• IRef Ophid Interaction: SMAD3 — MECOM (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Su et al., Tumori 2010 (Leukemia, Myelogenous, Chronic, BCR-ABL Positive) : However, specific histone deacetylase inhibitors can interrupt the effect of histone deacetylase to alleviate EVI1 mediated suppression of TGF-beta1/SMAD signaling
Kurokawa et al., Blood 1998 (Leukemia, Myeloid...) : AML1/Evi-1 interacts with Smad3, an intracellular mediator of TGF-beta signaling, through the first zinc finger domain, and represses the Smad3 activity, as Evi-1 does