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ESR1 — NCOA1

Pathways - manually collected, often from reviews:

• OpenBEL Selventa BEL large corpus: Complex of ESR1-NCOA1 → estradiol/ESR1 complex (ESR1) (increases)
  
  Evidence: oestrogenic conditions SRC-1 preferentially binds to the ER which effectively sequesters it thereby reducing enhancer activity
• OpenBEL Selventa BEL large corpus: Complex of ESR1-NCOA1 → estradiol/ESR1 complex (ESR1) (increases)
  
  Evidence: in a substantial proportion of patients with primary breast cancer, and in all patients with ER positive metastatic disease, resistance eventually develops to all strategies that are designed to limit ER activation by oestrogen. ER binds as a dimer to small palindromic DNA motifs - known as oestrogen response elements (EREs) - in the promoters of these genes, through the action of two ZINC FINGERS 29. AF1 and AF2 activate transcription independently and/or synergistically. There is evidence that...
• OpenBEL Selventa BEL large corpus: ESR1 → Complex of CARM1-NCOA1 (directlyIncreases, CARM1/NCOA1 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].
• OpenBEL Selventa BEL large corpus: ESR1 → Complex of CREBBP-NCOA1 (directlyIncreases, CREBBP/NCOA1 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].
• OpenBEL Selventa BEL large corpus: ESR1 → Complex of CREBBP-NCOA1 (directlyIncreases, CREBBP/NCOA1 Activity)
  Evidence: ER coregulators are also targets of many of the same signaling pathways that affect ER directly. MAPK can phosphorylate p160 coactivators NCoA-1 and NCoA-3, and can enhance their transcriptional activities partly by facilitating their interaction with CBP/p300 [87,88].
• OpenBEL Selventa BEL large corpus: ESR1 → Complex of ESR1-NCOA1 (directlyIncreases, ESR1/NCOA1 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],
• OpenBEL Selventa BEL large corpus: ESR1 → Complex of ESR1-NCOA1 (directlyIncreases, ESR1/NCOA1 Activity)
  Evidence: in a substantial proportion of patients with primary breast cancer, and in all patients with ER positive metastatic disease, resistance eventually develops to all strategies that are designed to limit ER activation by oestrogen. ER binds as a dimer to small palindromic DNA motifs - known as oestrogen response elements (EREs) - in the promoters of these genes, through the action of two ZINC FINGERS 29. AF1 and AF2 activate transcription independently and/or synergistically. There is evidence that...
• OpenBEL Selventa BEL large corpus: ESR1 → Complex of NCOA1-SRA1 (increases, NCOA1/SRA1 Activity)
  Evidence: The growing family of nuclear receptor coactivators has recently acquired a unique member, steroid receptor RNA activator (SRA) [22]. Differing from the other coactivators, SRA functions as a RNA transcript instead of as a protein. SRA specifically coactivates the transcriptional activity of steroid receptors, including the PR, the ER, the glucocorticoid receptor, and the androgen receptor.
• OpenBEL Selventa BEL large corpus: Complex of ESR1-NCOA1 → CCND1 (increases)
  Evidence: Cyclin D1, a protein frequently overexpressed in breast cancer, has been shown to activate unliganded ER through recruiting p160 coactivators and p/CAF [52-55]. The calcium binding protein calmodulin and the activating enzyme of NEDD8, Uba3, both regulate ER activity by modulating the steady-state level of the receptor [56,57].
• OpenBEL Selventa BEL large corpus: ESR1 → NCOA1 (directlyIncreases, NCOA1 Activity)
  Evidence: ER coregulators are also targets of many of the same signaling pathways that affect ER directly. MAPK can phosphorylate p160 coactivators NCoA-1 and NCoA-3, and can enhance their transcriptional activities partly by facilitating their interaction with CBP/p300 [87,88].
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → E2/ERA (dimer)/Src-1/p300 complex (ESR1-NCOA1-EP300) (modification, collaborate)
  Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → p300 (EP300) (modification, collaborate) Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → MPG (MPG) (modification, collaborate) Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → E2/ERA (dimer)/Src-1/MPG complex (ESR1-NCOA1-MPG) (modification, collaborate)
  Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1/p300 complex (ESR1-NCOA1-EP300) → p300 (EP300) (modification, collaborate) Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1/p300 complex (ESR1-NCOA1-EP300) → MPG (MPG) (modification, collaborate) Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1/p300 complex (ESR1-NCOA1-EP300) → E2/ERA (dimer)/Src-1/MPG complex (ESR1-NCOA1-MPG) (modification, collaborate)
  Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: p300 (EP300) → E2/ERA (dimer)/Src-1/MPG complex (ESR1-NCOA1-MPG) (modification, collaborate)
  Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: MPG (MPG) → E2/ERA (dimer)/Src-1/MPG complex (ESR1-NCOA1-MPG) (modification, collaborate)
  Likhite et al., J Biol Chem 2004, Hanstein et al., Proc Natl Acad Sci U S A 1996*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → Prolactin (PRL) (transcription, activates) Zwart et al., J Cell Sci 2010*
  Evidence: mutant phenotype, reporter gene, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → E2/ERA (dimer) complex (ESR1) (modification, collaborate)
  Métivier et al., Mol Endocrinol 2001*, Katzenellenbogen et al., Ann N Y Acad Sci 2001, Zwart et al., J Cell Sci 2010*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer)/Src-1 complex (ESR1-NCOA1) → Src-1 (NCOA1) (modification, collaborate) Métivier et al., Mol Endocrinol 2001*, Katzenellenbogen et al., Ann N Y Acad Sci 2001, Zwart et al., J Cell Sci 2010*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer) complex (ESR1) → Src-1 (NCOA1) (modification, collaborate) Métivier et al., Mol Endocrinol 2001*, Katzenellenbogen et al., Ann N Y Acad Sci 2001, Zwart et al., J Cell Sci 2010*
  Evidence: mutant phenotype, physical interaction
• NCI Pathway Database Validated nuclear estrogen receptor alpha network: E2/ERA (dimer) complex (ESR1) → E2/ERA (dimer)/Src-1/MPG complex (ESR1-NCOA1-MPG) (transcription, activates)
  Likhite et al., J Biol Chem 2004
  Evidence: reporter gene

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

Studies that report less than 10 interactions are marked with *

• IRef Bind_translation Interaction: NCOA1 — ESR1 (competition binding) Martini et al., Mol Cell Biol 2000*
• IRef Bind_translation Interaction: NCOA1 — ESR1 (two hybrid) Martini et al., Mol Cell Biol 2000*
• IRef Bind_translation Interaction: NCOA1 — ESR1 (two hybrid) Albers et al., Mol Cell Proteomics 2005
• IRef Bind_translation Interaction: NCOA1 — ESR1 (unspecified method) Needham et al., J Steroid Biochem Mol Biol 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (physical association, affinity chromatography technology) Eng et al., J Biol Chem 1998*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Needham et al., J Steroid Biochem Mol Biol 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Needham et al., J Steroid Biochem Mol Biol 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) DiRenzo et al., Mol Cell Biol 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Sheppard et al., Mol Cell Biol 2001*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Kalkhoven et al., EMBO J 1998*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Kang et al., Proc Natl Acad Sci U S A 2002
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Watanabe et al., EMBO J 2001
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Dutertre et al., Mol Endocrinol 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Dutertre et al., Mol Endocrinol 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (physical association, affinity chromatography technology) Shiozawa et al., J Clin Endocrinol Metab 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Tremblay et al., J Steroid Biochem Mol Biol 2001*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, fluorescent resonance energy transfer) Llopis et al., Proc Natl Acad Sci U S A 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Chien et al., Mol Endocrinol 1999*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Webb et al., Mol Endocrinol 1998*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Webb et al., Mol Endocrinol 1998*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Lazennec et al., Mol Endocrinol 1997*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Heery et al., Nature 1997*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Heery et al., Nature 1997*
• IRef Biogrid Interaction: NCOA1 — ESR1 (physical association, affinity chromatography technology) Torchia et al., Nature 1997
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Torchia et al., Nature 1997
• IRef Biogrid Interaction: NCOA1 — ESR1 (physical association, affinity chromatography technology) Fleming et al., J Clin Endocrinol Metab 2004*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Fujita et al., J Biol Chem 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Fujita et al., J Biol Chem 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Monroe et al., J Endocrinol 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, fluorescent resonance energy transfer) Bai et al., Mol Endocrinol 2003*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, unspecified method) Bramlett et al., Mol Endocrinol 2001*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, two hybrid) Kraichely et al., Endocrinology 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (direct interaction, pull down) Kraichely et al., Endocrinology 2000*
• IRef Biogrid Interaction: NCOA1 — ESR1 (physical association, affinity chromatography technology) Gong et al., Cancer Sci 2010*
• IRef Hprd Interaction: ESR1 — NCOA1 (in vitro) Zhang et al., Mol Cell Endocrinol 2001*, Kalkhoven et al., EMBO J 1998*
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, pull down) Endoh et al., Mol Cell Biol 1999*
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, pull down) Métivier et al., Mol Endocrinol 2001*
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, two hybrid) Cho et al., J Biol Chem 2006*
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, pull down) Zhang et al., EMBO J 2006
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, two hybrid) Zwart et al., EMBO J 2007*
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, fluorescent resonance energy transfer) Zwart et al., EMBO J 2007*
• IRef Intact Interaction: NCOA1 — ESR1 (physical association, pull down) Okada et al., EMBO Rep 2008
• IRef Intact Interaction: Complex of DDX17-ESR1-NCOA1 (association, pull down) Watanabe et al., EMBO J 2001
• IRef Mppi Interaction: NCOA1 — ESR1 (two hybrid) Needham et al., J Steroid Biochem Mol Biol 2000*
• IRef Ophid Interaction: NCOA1 — ESR1 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Métivier et al., Mol Endocrinol 2001 : This interaction of SRC-1 with the AF-1 alpha-helical core is essential for both E2- and OHT induced ERalpha activity
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
Zhou et al., Mol Endocrinol 1998 : Using estrogen receptor ( ERalpha ) as an alternative system, known agonists induced an interaction between ERalpha LBD and SRC-1 , whereas ER antagonists disrupted agonist induced interaction of ERalpha with SRC-1