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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