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RAF1 — STK3
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind Interaction:
RAF1
—
STK3
O'Neill et al., Science 2004*
-
IRef Bind_translation Interaction:
RAF1
—
STK3
(affinity chromatography technology)
O'Neill et al., Science 2004*
-
IRef Bind_translation Interaction:
RAF1
—
STK3
(coimmunoprecipitation)
O'Neill et al., Science 2004*
-
IRef Biogrid Interaction:
RAF1
—
STK3
(physical association, affinity chromatography technology)
Kilili et al., J Biol Chem 2010*
-
IRef Biogrid Interaction:
RAF1
—
STK3
(physical association, affinity chromatography technology)
Matallanas et al., Mol Cell 2007*
-
IRef Biogrid Interaction:
RAF1
—
STK3
(physical association, affinity chromatography technology)
O'Neill et al., Science 2004*
-
IRef Biogrid Interaction:
RAF1
—
STK3
(direct interaction, pull down)
O'Neill et al., Science 2004*
-
IRef Biogrid Interaction:
RAF1
—
STK3
(physical association, affinity chromatography technology)
Romano et al., Cancer Res 2010*
-
IRef Hprd Interaction:
RAF1
—
STK3
(in vitro)
O'Neill et al., Science 2004*
-
IRef Hprd Interaction:
RAF1
—
STK3
(in vivo)
O'Neill et al., Science 2004*
-
IRef Intact Interaction:
Complex of 143 proteins
(association, anti tag coimmunoprecipitation)
Text-mined interactions from Literome
Baccarini et al., J Biol Chem 1991
:
Phosphorylation of the
RAF-1 protooncogene product and
activation of its associated
serine/threonine kinase are common features of the response of cells to peptide growth factors
Morrison et al., Proc Natl Acad Sci U S A 1988
:
These findings suggest that proliferative signals generated at the membrane result in the phosphorylation of the
Raf-1 protein and the
activation of its
serine/threonine kinase activity