◀ Back to ESR1
ESR1 — NCOA2
Pathways - manually collected, often from reviews:
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OpenBEL Selventa BEL large corpus:
ESR1
→
Complex of CREBBP-NCOA2
(directlyIncreases, CREBBP/NCOA2 Activity)
Evidence: The C-terminal region of the p160 proteins mediates interaction with other factors with a role in ER signaling including CBP (CREB-binding protein), p300 and arginine methyltransferase 1 (CARM-1) [32].
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OpenBEL Selventa BEL large corpus:
ESR1
→
Complex of EP300-NCOA2
(directlyIncreases, EP300/NCOA2 Activity)
Evidence: The C-terminal region of the p160 proteins mediates interaction with other factors with a role in ER signaling including CBP (CREB-binding protein), p300 and arginine methyltransferase 1 (CARM-1) [32].
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OpenBEL Selventa BEL large corpus:
ESR1
→
NCOA2
(directlyIncreases, NCOA2 Activity)
Evidence: There are three members of the p160 family of coactivators, NCoA-1 (SRC-1) [22], NCoA-2 (TIF2, GRIP1) [23,24], and NCoA-3 (AIB1, ACTR, RAC3, p/CIP, TRAM-1) [25-30],
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NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/P72 complex (ESR1-NCOA2-DDX17)
→
E2/ERA (dimer)/TIF2 complex (ESR1-NCOA2)
(modification, collaborate)
Watanabe et al., EMBO J 2001
Evidence: physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/P72 complex (ESR1-NCOA2-DDX17)
→
P72 (DDX17)
(modification, collaborate)
Watanabe et al., EMBO J 2001
Evidence: physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2 complex (ESR1-NCOA2)
→
P72 (DDX17)
(modification, collaborate)
Watanabe et al., EMBO J 2001
Evidence: physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/CoCoA complex (ESR1-NCOA2-CALCOCO1)
→
TFF1 (TFF1)
(transcription, activates)
Kim et al., Mol Cell 2003*
Evidence: physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/P72 complex (ESR1-NCOA2-DDX17)
→
TFF1 (TFF1)
(transcription, activates)
Watanabe et al., EMBO J 2001, Shao et al., Mol Cell Biol 2002*
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/P72 complex (ESR1-NCOA2-DDX17)
→
E2/ERA (dimer)/TIF2/P72/SRA1 complex (ESR1-NCOA2-DDX17-SRA1)
(modification, collaborate)
Watanabe et al., EMBO J 2001
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/P72 complex (ESR1-NCOA2-DDX17)
→
SRA1 (SRA1)
(modification, collaborate)
Watanabe et al., EMBO J 2001
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/P72/SRA1 complex (ESR1-NCOA2-DDX17-SRA1)
→
SRA1 (SRA1)
(modification, collaborate)
Watanabe et al., EMBO J 2001
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/CoCoA complex (ESR1-NCOA2-CALCOCO1)
→
CoCoA (CALCOCO1)
(modification, collaborate)
Kim et al., Mol Cell 2003*
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2/CoCoA complex (ESR1-NCOA2-CALCOCO1)
→
E2/ERA (dimer)/TIF2 complex (ESR1-NCOA2)
(modification, collaborate)
Kim et al., Mol Cell 2003*
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
CoCoA (CALCOCO1)
→
E2/ERA (dimer)/TIF2 complex (ESR1-NCOA2)
(modification, collaborate)
Kim et al., Mol Cell 2003*
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer) complex (ESR1)
→
E2/ERA (dimer)/TIF2 complex (ESR1-NCOA2)
(modification, collaborate)
Watanabe et al., EMBO J 2001, Katzenellenbogen et al., Ann N Y Acad Sci 2001
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer) complex (ESR1)
→
TIF2 (NCOA2)
(modification, collaborate)
Watanabe et al., EMBO J 2001, Katzenellenbogen et al., Ann N Y Acad Sci 2001
Evidence: mutant phenotype, physical interaction
-
NCI Pathway Database Validated nuclear estrogen receptor alpha network:
E2/ERA (dimer)/TIF2 complex (ESR1-NCOA2)
→
TIF2 (NCOA2)
(modification, collaborate)
Watanabe et al., EMBO J 2001, Katzenellenbogen et al., Ann N Y Acad Sci 2001
Evidence: mutant phenotype, physical interaction
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
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IRef Bind_translation Interaction:
ESR1
—
NCOA2
(two hybrid)
Poelzl et al., Proc Natl Acad Sci U S A 2000*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, pull down)
Voegel et al., EMBO J 1998*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(physical association, affinity chromatography technology)
Cui et al., Mol Endocrinol 2006*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, pull down)
Kindle et al., Mol Cell Biol 2005*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, two hybrid)
Jaber et al., J Mol Endocrinol 2004*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, pull down)
Torchia et al., Nature 1997
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, two hybrid)
Monroe et al., J Endocrinol 2003*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(physical association, affinity chromatography technology)
Kitagawa et al., Cell 2003
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, unspecified method)
Bramlett et al., Mol Endocrinol 2001*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, fluorescent resonance energy transfer)
Bai et al., Mol Endocrinol 2003*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, pull down)
Kraichely et al., Endocrinology 2000*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, two hybrid)
Kraichely et al., Endocrinology 2000*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(physical association, affinity chromatography technology)
Eng et al., J Biol Chem 1998*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, pull down)
Wärnmark et al., J Biol Chem 2002*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(association, x-ray crystallography)
Wärnmark et al., J Biol Chem 2002*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(physical association, affinity chromatography technology)
Watanabe et al., EMBO J 2001
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(physical association, affinity chromatography technology)
Fenne et al., Endocrinology 2008*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, two hybrid)
He et al., Mol Cell Biol 2003
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(physical association, affinity chromatography technology)
Yin et al., Molecular cancer 2007*
-
IRef Biogrid Interaction:
ESR1
—
NCOA2
(direct interaction, two hybrid)
Dutertre et al., Mol Endocrinol 2003*
-
IRef Dip Interaction:
ESR1
—
NCOA2
(physical association, biochemical)
Voegel et al., EMBO J 1998*
-
IRef Hprd Interaction:
ESR1
—
NCOA2
(in vitro)
Wärnmark et al., J Biol Chem 2002*
-
IRef Intact Interaction:
ESR1
—
NCOA2
(physical association, pull down)
Benecke et al., EMBO Rep 2000*
-
IRef Intact Interaction:
Complex of NCOA2-NCOA2-ESR1-ESR1-ESR1-ESR1-ESR1-ESR1-NCOA2
(association, transcriptional complementation assay)
Benecke et al., EMBO Rep 2000*
-
IRef Intact Interaction:
Complex of ESR1-NCOA2-DDX17-ESR1-DDX17-NCOA2-ESR1-NCOA2-DDX17
(association, anti tag coimmunoprecipitation)
Watanabe et al., EMBO J 2001
-
IRef Ophid Interaction:
ESR1
—
NCOA2
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Zheng et al., Mol Cell Biol 2005
:
Together these data demonstrate that E2-induced
SRC-3 phosphorylation is
dependent on a direct interaction between SRC-3 and
ERalpha and can occur outside of the nucleus
Hartmaier et al., Mol Endocrinol 2012
(Bone Demineralization, Pathologic...) :
The coregulator steroid receptor coactivator
(SRC)-1 increases transcriptional activity of the
estrogen receptor ( ER ) in a number of tissues including bone
Suen et al., J Biol Chem 1998
:
SRC-3 enhanced
ERalpha and progesterone receptor stimulated gene transcription in a ligand dependent manner, but stimulation of ERbeta mediated transcription was not observed