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ESR1 — SAFB
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
ESR1
—
SAFB
(unspecified method)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Biogrid Interaction:
ESR1
—
SAFB
(direct interaction, pull down)
Townson et al., J Biol Chem 2004*
-
IRef Biogrid Interaction:
ESR1
—
SAFB
(physical association, affinity chromatography technology)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Biogrid Interaction:
ESR1
—
SAFB
(direct interaction, pull down)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Biogrid Interaction:
ESR1
—
SAFB
(physical association, affinity chromatography technology)
Garee et al., Biochem Biophys Res Commun 2011*
-
IRef Hprd Interaction:
ESR1
—
SAFB
(in vitro)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Hprd Interaction:
ESR1
—
SAFB
(in vivo)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Mppi Interaction:
ESR1
—
SAFB
(coimmunoprecipitation)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Mppi Interaction:
ESR1
—
SAFB
(copurification)
Oesterreich et al., Mol Endocrinol 2000*
-
IRef Ophid Interaction:
ESR1
—
SAFB
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Townson et al., J Biol Chem 2004
:
We have previously shown that
SAFB1 can
repress estrogen receptor ( ERalpha ) -mediated transactivation ... We propose a model in which
SAFB1 represses
ERalpha activity via indirect association with histone deacetylation and interaction with the basal transcription machinery
Jiang et al., Mol Endocrinol 2006
(Breast Neoplasms) :
Scaffold attachment factor
SAFB1 suppresses
estrogen receptor alpha mediated transcription in part via interaction with nuclear receptor corepressor