| + |
GSK3B | up-regulates 
phosphorylation
|
ESR1 |
0.347 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139312 |
Ser102 |
GGFPPLNsVSPSPLM |
Homo sapiens |
|
| pmid |
sentence |
| 16076840 |
The gsk-3 inhibitor lithium chloride was used to determine the role of gsk-3 in phosphorylation of ser-102, -104, and -106 and ser-118 in vivo and to explore the role of these serines in the regulation of eralpha function. Treatment of cells with lithium chloride resulted in dephosphorylation of ser-104 and -106 and ser-118, which suggests these serine residues as targets for gsk-3 in vivo. Our results further suggest that eralpha phosphorylation by gsk-3 stabilizes eralpha under resting conditions and modulates eralpha transcriptional activity upon ligand binding. Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin a-cdk2 complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139316 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
|
| pmid |
sentence |
| 16076840 |
The gsk-3 inhibitor lithium chloride was used to determine the role of gsk-3 in phosphorylation of ser-102, -104, and -106 and ser-118 in vivo and to explore the role of these serines in the regulation of eralpha function. Treatment of cells with lithium chloride resulted in dephosphorylation of ser-104 and -106 and ser-118, which suggests these serine residues as targets for gsk-3 in vivo. Our results further suggest that eralpha phosphorylation by gsk-3 stabilizes eralpha under resting conditions and modulates eralpha transcriptional activity upon ligand binding. Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin a-cdk2 complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139320 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
|
| pmid |
sentence |
| 16076840 |
The gsk-3 inhibitor lithium chloride was used to determine the role of gsk-3 in phosphorylation of ser-102, -104, and -106 and ser-118 in vivo and to explore the role of these serines in the regulation of eralpha function. Treatment of cells with lithium chloride resulted in dephosphorylation of ser-104 and -106 and ser-118, which suggests these serine residues as targets for gsk-3 in vivo. Our results further suggest that eralpha phosphorylation by gsk-3 stabilizes eralpha under resting conditions and modulates eralpha transcriptional activity upon ligand binding. Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin a-cdk2 complex. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139324 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 16076840 |
The gsk-3 inhibitor lithium chloride was used to determine the role of gsk-3 in phosphorylation of ser-102, -104, and -106 and ser-118 in vivo and to explore the role of these serines in the regulation of eralpha function. Treatment of cells with lithium chloride resulted in dephosphorylation of ser-104 and -106 and ser-118, which suggests these serine residues as targets for gsk-3 in vivo. Our results further suggest that eralpha phosphorylation by gsk-3 stabilizes eralpha under resting conditions and modulates eralpha transcriptional activity upon ligand binding. Estradiol and phorbol ester cause phosphorylation of serine 118 in the human estrogen receptor. Potentiation of human estrogen receptor alpha transcriptional activation through phosphorylation of serines 104 and 106 by the cyclin a-cdk2 complex. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates
phosphorylation
|
ESR1 |
0.692 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178141 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
|
| pmid |
sentence |
| 18372406 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156860 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178145 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
|
| pmid |
sentence |
| 18372406 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156864 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156868 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| + |
CDK2 | up-regulates
phosphorylation
|
ESR1 |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69710 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
|
| pmid |
sentence |
| 10428798 |
Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69714 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
|
| pmid |
sentence |
| 10428798 |
Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69718 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10428798 |
Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200867 |
Ser294 |
RAANLWPsPLMIKRS |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 23390529 |
The pi3k/akt pathway is necessary to activate cdk2, which phosphorylates eralphaser294, and mediates the binding between pin1 and eralpha |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
AKT | up-regulates
phosphorylation
|
ESR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244243 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244247 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244255 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244251 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Luminal Breast Cancer |
| + |
CyclinA2/CDK2 | up-regulates
phosphorylation
|
ESR1 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217284 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
|
| pmid |
sentence |
| 10428798 |
Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217288 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
|
| pmid |
sentence |
| 10428798 |
Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217292 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10428798 |
Within er af-1, serines 104, 106, and 118 represent potential cdk phosphorylation sites, and in this current study, we ascertain their importance in mediating cyclin a-cdk2-dependent enhancement of er transcriptional activity. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates
phosphorylation
|
ESR1 |
0.757 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84963 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84967 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84971 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84975 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
|
| pmid |
sentence |
| 11108261 |
Studies using mutants of er-alpha demonstrated that akt increased estrogen receptor activity through the amino-terminal activation function-1 (af-1). Serines s104 s106, s118, and s167 appear to play a role in the activation of er-alpha by akt. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDK3 | up-regulates activity
phosphorylation
|
ESR1 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273189 |
Ser104 |
FPPLNSVsPSPLMLL |
|
|
| pmid |
sentence |
| 26202215 |
CDK3 was shown to be overexpressed in breast cancer and phosphorylate ERα at Ser104/116 and Ser118. Furthermore, we found that Mir-873 inhibits ER activity and cell growth via targeting CDK3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273188 |
Ser106 |
PLNSVSPsPLMLLHP |
|
|
| pmid |
sentence |
| 26202215 |
CDK3 was shown to be overexpressed in breast cancer and phosphorylate ERα at Ser104/116 and Ser118. Furthermore, we found that Mir-873 inhibits ER activity and cell growth via targeting CDK3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273187 |
Ser118 |
LHPPPQLsPFLQPHG |
|
|
| pmid |
sentence |
| 26202215 |
CDK3 was shown to be overexpressed in breast cancer and phosphorylate ERα at Ser104/116 and Ser118. Furthermore, we found that Mir-873 inhibits ER activity and cell growth via targeting CDK3 |
|
| Publications: |
3 |
| + |
MAPK1 | up-regulates
phosphorylation
|
ESR1 |
0.657 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178133 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 18372406 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156848 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178137 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 18372406 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156852 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96072 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 12466266 |
Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity;ser118 is phosphorylated by mitogen-activated protein kinase (mapk) in vitro and in cells treated with epidermal growth factor (egf) and insulin-like growth factor (igf) in vivo. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156856 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates
phosphorylation
|
ESR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244647 |
Ser104 |
FPPLNSVsPSPLMLL |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244651 |
Ser106 |
PLNSVSPsPLMLLHP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244655 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Luminal Breast Cancer, Oxytocin signaling |
| + |
GTF2H2 | up-regulates activity
phosphorylation
|
ESR1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260817 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10949034 |
TFIIH Phosphorylates Human Estrogen Receptor α at Serine 118 | We report here that Cdk7 overexpression stimulates transcription activation by ERα by stimulating phosphorylation of S118 in a ligand-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK7 | up-regulates
phosphorylation
|
ESR1 |
0.423 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81170 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10949034 |
Activation of estrogen receptor alpha by s118 phosphorylation involves a ligand-dependent interaction with tfiih and participation of cdk7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DUSP22 | down-regulates activity 
dephosphorylation
|
ESR1 |
0.264 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248827 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 17384676 |
These results strongly suggest that DUSP22 acts as a negative regulator of the ERalpha-mediated signaling pathway|whereas E2-induced phosphorylation and activation of ERalpha was suppressed by overexpression of DUSP22 but not catalytically inactive mutants. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 | up-regulates
phosphorylation
|
ESR1 |
0.609 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-136950 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 15879307 |
Conversely, constitutively active mkk6 induced p38 mapk activation that recapitulated the effects of polyphenols by inducing eralpha phosphorylation and downstream activation of akt, and enos. The key role of eralpha ser-118 phosphorylation was confirmed in enos-transfected cos-7 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90823 |
Thr311 |
NSLALSLtADQMVSA |
Homo sapiens |
|
| pmid |
sentence |
| 12138194 |
P38 mitogen-activated protein kinase was involved in estrogen receptor activation by estrogens and mekk1. Here, we report estrogen receptor-dependent p38 activation by estrogens in endometrial adenocarcinoma cells and in vitro and in vivo phosphorylation of the estrogen receptor alpha mediated through p38. The phosphorylation site was identified as threonine-311 (thr(311)), located in helix 1 of the hormone-binding domain. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MNAT1 | up-regulates activity
phosphorylation
|
ESR1 |
0.406 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260837 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10949034 |
Human Estrogen Receptor α Is Phosphorylated at Serine 118 In Vivo by Cdk7 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TFIIH | up-regulates
phosphorylation
|
ESR1 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269356 |
Ser118 |
LHPPPQLsPFLQPHG |
Homo sapiens |
|
| pmid |
sentence |
| 10949034 |
Activation of estrogen receptor alpha by s118 phosphorylation involves a ligand-dependent interaction with tfiih and participation of cdk7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT2 | up-regulates activity
phosphorylation
|
ESR1 |
0.524 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251490 |
Ser167 |
GGRERLAsTNDKGSM |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 11139588 |
AKT activate ERalpha in the absence of estrogen. The consensus AKT phosphorylation site Ser-167 of ERalpha is required for phosphorylation and activation by AKT. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
RPS6KA1 | up-regulates
phosphorylation
|
ESR1 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34113 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 7838153 |
Serine 167 is the major phosphorylation site on the human estrogen receptor. Phosphorylation is mediated by casein kinase ii. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IKBKE | up-regulates
phosphorylation
|
ESR1 |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161834 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19940156 |
Here, we show that ikkepsilon interacts with and phosphorylates estrogen receptor alpha (eralpha) on serine 167 in vitro and in vivo. As a result, ikkepsilon induces eralpha transactivation activity and enhances eralpha binding to dna. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KB1 | up-regulates
phosphorylation
|
ESR1 |
0.583 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34117 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
|
| pmid |
sentence |
| 7838153 |
Serine 167 is the major phosphorylation site on the human estrogen receptor. Phosphorylation is mediated by casein kinase ii. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA3 | up-regulates
phosphorylation
|
ESR1 |
0.412 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182958 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 19112174 |
S6k1 regulates estrogen receptor alpha (eralpha) by phosphorylating it on serine 167, leading to transcriptional activation of eralpha. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6K | up-regulates
phosphorylation
|
ESR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252807 |
Ser167 |
GGRERLAsTNDKGSM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 7838153 |
Serine 167 is the major phosphorylation site on the human estrogen receptor. Phosphorylation is mediated by casein kinase ii. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
ESR1 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-63984 |
Ser236 |
IDKNRRKsCQACRLR |
Homo sapiens |
|
| pmid |
sentence |
| 9891036 |
Phosphorylation of human estrogen receptor alpha by protein kinase a regulates dimerizationeralpha is phosphorylated by protein kinase a (pka) on serine-236 within the dna binding domain. Mutation of serine-236 to glutamic acid prevents dna binding by inhibiting dimerization by eralpha |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | down-regulates
phosphorylation
|
ESR1 |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162653 |
Ser282 |
EGRGEVGsAGDMRAA |
Homo sapiens |
Breast Cancer Cell, HeLa Cell |
| pmid |
sentence |
| 20043841 |
Additionally protein kinase ck2 was identified as a kinase that phosphorylated eralpha at s282 and s559 s282 and s559 represent the second and third sites of er_ regulation by ck2. Remarkably, mutation of s282 or s559 to alanine resulted in near opposite functional effects on er_ as compared to mutation of s167 to alanine. Er_ ligand independent transcriptional activity was markedly enhanced upon mutation of s282 and s559 to alanine |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162657 |
Ser559 |
PTSRGGAsVEETDQS |
Homo sapiens |
Breast Cancer Cell, HeLa Cell |
| pmid |
sentence |
| 20043841 |
Additionally protein kinase ck2 was identified as a kinase that phosphorylated eralpha at s282 and s559 s282 and s559 represent the second and third sites of er_ regulation by ck2. Remarkably, mutation of s282 or s559 to alanine resulted in near opposite functional effects on er_ as compared to mutation of s167 to alanine. Er_ ligand independent transcriptional activity was markedly enhanced upon mutation of s282 and s559 to alanine |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
ESR1 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94206 |
Ser305 |
IKRSKKNsLALSLTA |
Homo sapiens |
|
| pmid |
sentence |
| 12374744 |
Pak1 directly phosphorylated the activation function-2 domain of the er at the n-terminal residue ser305, and its mutation to ala (s305a) abolished the pak1-mediated phosphorylation and transactivation functions of the er |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
PRKACA | up-regulates
phosphorylation
|
ESR1 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-125779 |
Ser305 |
IKRSKKNsLALSLTA |
Homo sapiens |
|
| pmid |
sentence |
| 15193262 |
We show that phosphorylation of serine-305 in the hinge region of er_ by protein kinase a (pka) induced resistance to tamoxifenactivation of pka prevents tamoxifen-mediated inhibition of er transactivation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates
phosphorylation
|
ESR1 |
0.459 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163562 |
Tyr219 |
SIQGHNDyMCPATNQ |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20101225 |
Eralpha can be phosphorylated on two sites, tyrosine 52 (y-52) and tyrosine 219 (y-219). Eralpha phosphorylation by c-abl stabilizes eralpha, resulting in enhanced eralpha transcriptional activity and increased expression of endogenous eralpha target genes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163566 |
Tyr52 |
DSSKPAVyNYPEGAA |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20101225 |
Eralpha can be phosphorylated on two sites, tyrosine 52 (y-52) and tyrosine 219 (y-219). Eralpha phosphorylation by c-abl stabilizes eralpha, resulting in enhanced eralpha transcriptional activity and increased expression of endogenous eralpha target genes. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LCK | up-regulates
phosphorylation
|
ESR1 |
0.391 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72373 |
Tyr537 |
CKNVVPLyDLLLEML |
Homo sapiens |
|
| pmid |
sentence |
| 10571988 |
On the basis of these data and other reports describing the structure and activity of y537 mutations, as well as knowledge of the three-dimensional structure of the her ligand binding domain, we propose an alternate model wherein y537f mutation favors an open pocket conformation, affecting the estrogen binding kinetics and stability of the hormone-bound, transcriptionally active closed pocket conformation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55853 |
Tyr537 |
CKNVVPLyDLLLEML |
Homo sapiens |
Breast Cancer Cell, HeLa Cell |
| pmid |
sentence |
| 9500442 |
On the basis of these data and other reports describing the structure and activity of y537 mutations, as well as knowledge of the three-dimensional structure of the her ligand binding domain, we propose an alternate model wherein y537f mutation favors an open pocket conformation, affecting the estrogen binding kinetics and stability of the hormone-bound, transcriptionally active closed pocket conformation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates
phosphorylation
|
ESR1 |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-55857 |
Tyr537 |
CKNVVPLyDLLLEML |
Homo sapiens |
Breast Cancer Cell, HeLa Cell |
| pmid |
sentence |
| 9500442 |
Although the molecular mechanisms underlying ligand-independent activation of era are not completely understood, phosphorylation of a serine residue in af1 has been implicated in the response to epidermal growth factor. Era is also a target for tyrosine phosphorylation, anda single tyrosine residue located immediately adjacent to af2 has been identified as a substrate for src-family tyrosine kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN3 | up-regulates activity
dephosphorylation
|
ESR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277127 |
Tyr537 |
CKNVVPLyDLLLEML |
Homo sapiens |
|
| pmid |
sentence |
| 26079946 |
Our recent studies further demonstrated that PTPH1 dephosphorylates estrogen receptor at Y537, increases estrogen receptor stability and nuclear accumulation, and enhances breast cancer sensitivity to anti-estrogens [ ]. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DNMT1 | down-regulates quantity by repression 
transcriptional regulation
|
ESR1 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254027 |
|
|
Homo sapiens |
MDA-MB-468 Cell |
| pmid |
sentence |
| 23242655 |
Our previous studies demonstrated that mutant p53 along with repression complex proteins including DNMT1, HDAC1 and MeCP2 is associated with ER-negative promoter in MDA-MB-468 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNAI2 | down-regulates quantity by repression
transcriptional regulation
|
ESR1 |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255154 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20509143 |
SLUG up-regulation engenders breast cancer cells with stem cell-like properties including enhanced expression of CD44 and Jagged-1 in conjunction with estrogen receptor alpha down-regulation, growth as mammospheres, and extracellular matrix invasiveness. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
4,4'-sulfonyldiphenol | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268730 |
|
|
in vitro |
|
| pmid |
sentence |
| 31995776 |
This study investigated the endocrine-disrupting activity of BPA, BPF, and BPS alone or as a mixture and the agonistic and antagonistic activity of the BPs using an in vitro bioassay to detect ER-, AR-, and AhR-mediated activity. Here, we evaluated the endocrine-disrupting risks of the bisphenols by investigating their agonist and antagonist activities with the estrogen (ER), androgen (AR), and aryl hydrocarbon (AhR) receptors. Our results showed that BPA, BPS, and BPF (BPs) have estrogen agonist and androgen antagonist activities and decrease the ERα protein level. . |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ESR1 | up-regulates quantity by expression 
transcriptional regulation
|
GREB1 |
0.703 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254074 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 17666587 |
Long-range activation of GREB1 by estrogen receptor via three distal consensus estrogen-responsive elements in breast cancer cells. . GREB1 (gene regulated by estrogen in breast cancer 1) is an ER target gene that regulates estrogen-induced proliferation in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
diethylstilbestrol | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258598 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
HDAC1 | down-regulates quantity by repression
transcriptional regulation
|
ESR1 |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254029 |
|
|
Homo sapiens |
MDA-MB-468 Cell |
| pmid |
sentence |
| 23242655 |
Our previous studies demonstrated that mutant p53 along with repression complex proteins including DNMT1, HDAC1 and MeCP2 is associated with ER-negative promoter in MDA-MB-468 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OTUB1 | down-regulates activity
deubiquitination
|
ESR1 |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276529 |
|
|
|
|
| pmid |
sentence |
| 19383985 |
OTU Domain-containing ubiquitin aldehyde-binding protein 1 (OTUB1) deubiquitinates estrogen receptor (ER) alpha and affects ERalpha transcriptional activity.|We show that OTUB1 negatively regulates transcription mediated by ERalpha in transient reporter gene assays and transcription mediated by endogenous ERalpha in Ishikawa endometrial cancer cells. |
|
| Publications: |
1 |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
CYP19A1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271683 |
|
|
|
|
| pmid |
sentence |
| 11973645 |
By binding to S1, ERalpha down-regulates the aromatase promoter activity. |
|
| Publications: |
1 |
| Pathways: | Luminal Breast Cancer |
| + |
ESR1 | up-regulates
binding
|
ESR2 |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-64427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10022879 |
It was recently shown that er? And er? Could form a heterodimer complex both in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Oxytocin signaling |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
SCN5A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253467 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 24493753 |
The effects of β-oestradiol (E2), the biologically active form of oestrogen, are classically mediated by two types of oestrogen receptor (ER): ERα and ERβ. E2 has both non-genomic and genomic effects upon VGSC expression/activity; and (ii) transcriptionally, E2 (via ERα) downregulates functional VGSC (nNav1.5) expression in BCa cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Spinal Ganglion |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
UGT1A4 |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254075 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 19546240 |
our data indicate that up-regulation of UGT1A4 expression by E(2) is mediated by both ER alpha and Sp1 and is a potential mechanism contributing to the enhanced elimination of lamotrigine in pregnancy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tamoxifen citrate | down-regulates activity
chemical inhibition
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259301 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 20512796 |
Estrogen receptor-alpha (ER) antagonists have been widely used for breast cancer therapy. Despite initial responsiveness, hormone-sensitive ER-positive cancer cells eventually develop resistance to ER antagonists. It has been shown that in most of these resistant tumor cells, the ER is expressed and continues to regulate tumor growth. Recent studies indicate that tamoxifen initially acts as an antagonist, but later functions as an ER agonist, promoting tumor growth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates
binding
|
PIK3R2 |
0.525 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140473 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16169518 |
Recently, it has been known that er activates phosphatidylinositol-3-oh kinase (pi3k) through binding with the p85 regulatory subunit of pi3k. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
estrone | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258584 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
PGR |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82161 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11000528 |
We observed the transcriptional inhibition of the progesterone and glucocorticoid receptors when eralpha was cotransfected |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
perfluorohexanesulfonic acid | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268761 |
|
|
in vitro |
|
| pmid |
sentence |
| 23764977 |
Seven PFCs [perfluorohexane sulfonate (PFHxS), perfluorooctane sulfonate (PFOS), perfluorooctanoate (PFOA), perfluorononanoate (PFNA), perfluorodecanoate (PFDA), perfluoroundecanoate (PFUnA), and perfluorododecanoate (PFDoA)] were analyzed in vitro for their potential to affect estrogen receptor (ER) and androgen receptor (AR) transactivity as well as aromatase enzyme activity. The PFCs were assessed as single compounds and in an equimolar mixture. PFHxS, PFOS and PFOA significantly induced the ER transactivity, whereas PFHxS, PFOS, PFOA, PFNA and PFDA significantly antagonized the AR activity in a concentration-dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MLL2 complex | up-regulates
binding
|
ESR1 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145868 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16603732 |
Eralpha directly binds to the mll2 complex through two lxxll motifs in a region of mll2 near the c terminus in a ligand-dependent manner. Disrupting the interaction between eralpha and the mll2 complex with small interfering rnas specific against mll2 or an mll2 fragment representing the interacting region with eralpha significantly inhibited the eralpha transcription activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POU4F1 | up-regulates activity
binding
|
ESR1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241275 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9448000 |
The POU domain of Brn-3a and Brn-3b was shown to interact with the DNA-binding domain of the ER. Brn-3-ER interactions also affect transcriptional activity of an ERE-containing promoter, such that in estradiol-stimulated cells, Brn-3b strongly activated the promoter via the ERE, while Brn-3a had a mild inhibitory effect. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PGR | up-regulates
binding
|
ESR1 |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-98807 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12612073 |
Here we identify two domains of prb, erid-i and -ii, mediating a direct interaction with the ligand-binding domain of eralpha. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tamoxifen | down-regulates activity
chemical inhibition
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258587 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20512796 |
Estrogen receptor-alpha (ER) antagonists have been widely used for breast cancer therapy. Despite initial responsiveness, hormone-sensitive ER-positive cancer cells eventually develop resistance to ER antagonists. It has been shown that in most of these resistant tumor cells, the ER is expressed and continues to regulate tumor growth. Recent studies indicate that tamoxifen initially acts as an antagonist, but later functions as an ER agonist, promoting tumor growth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
TGFA |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253942 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 11517191 |
ER beta and ER alpha induced the expression of several endogenous genes such as pS2, TGF alpha, or the cyclin kinase inhibitor p21 but, in contrast to ER alpha, ER beta was unable to regulate c-myc proto-oncogene expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERBB2 | up-regulates
phosphorylation
|
ESR1 |
0.591 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124962 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15173068 |
The results presented here show for the first time that er redistribution to the cytoplasm and its interaction with her2 are important downstream effects of her2 overexpression, that erk1/2 is important for er cytoplasmic localization, and that subcellular localization of er may play a mechanistic role in determining the responsiveness of breast cancer cells to tamoxifen. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POU4F2 | up-regulates activity
binding
|
ESR1 |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241208 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 9448000 |
the POU domain of Brn-3a and Brn-3b was shown to interact with the DNA-binding domain of the ER. Brn-3-ER interactions also affect transcriptional activity of an ERE-containing promoter, such that in estradiol-stimulated cells, Brn-3b strongly activated the promoter via the ERE, while Brn-3a had a mild inhibitory effect. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NR2E3 | up-regulates quantity by expression
transcriptional regulation
|
ESR1 |
0.253 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266207 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 22174013 |
NR2E3 directly regulates expression of ESR1 | Furthermore, overexpression of exogenous NR2E3 further increased expression of ESR1 and its downstream targets as well as its transcriptional activity in MCF-7 cells (Fig S1 of Supporting Information), strongly demonstrating that NR2E3 regulates ESR1 expression and subsequent ESR1-mediated induction of target genes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
perfluorooctane-1-sulfonic acid | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268760 |
|
|
in vitro |
|
| pmid |
sentence |
| 23764977 |
Seven PFCs [perfluorohexane sulfonate (PFHxS), perfluorooctane sulfonate (PFOS), perfluorooctanoate (PFOA), perfluorononanoate (PFNA), perfluorodecanoate (PFDA), perfluoroundecanoate (PFUnA), and perfluorododecanoate (PFDoA)] were analyzed in vitro for their potential to affect estrogen receptor (ER) and androgen receptor (AR) transactivity as well as aromatase enzyme activity. The PFCs were assessed as single compounds and in an equimolar mixture. PFHxS, PFOS and PFOA significantly induced the ER transactivity, whereas PFHxS, PFOS, PFOA, PFNA and PFDA significantly antagonized the AR activity in a concentration-dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
hexestrol | down-regulates activity
chemical inhibition
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258593 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
Gbeta | up-regulates
phosphorylation
|
ESR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270023 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17615152 |
In several estrogen response element-containing genes, the s118a mutation strongly reduced induction by e(2), and u0126 did not further reduce expression. Here, we show that serines 104 (s104) and 106 (s106) are also phosphorylated by mapk in vitro and upon stimulation of mapk activity in vivo.Phosphorylation at serines 104 and 106 by erk1/2 mapk is important for estrogen receptor-alpha activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
estriol | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258586 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
GGNBP2 | down-regulates activity
binding
|
ESR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269076 |
|
|
Homo sapiens |
T-47D Cell |
| pmid |
sentence |
| 27357812 |
We further demonstrate that GGNBP2 protein physically interacts with ERα, inhibits E2-induced activation of estrogen response element-driven reporter activity, and attenuates ER target gene expression in T47D cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
bisphenol F | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268731 |
|
|
in vitro |
|
| pmid |
sentence |
| 31995776 |
This study investigated the endocrine-disrupting activity of BPA, BPF, and BPS alone or as a mixture and the agonistic and antagonistic activity of the BPs using an in vitro bioassay to detect ER-, AR-, and AhR-mediated activity. Here, we evaluated the endocrine-disrupting risks of the bisphenols by investigating their agonist and antagonist activities with the estrogen (ER), androgen (AR), and aryl hydrocarbon (AhR) receptors. Our results showed that BPA, BPS, and BPF (BPs) have estrogen agonist and androgen antagonist activities and decrease the ERα protein level. . |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
estramustine | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259296 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14755680 |
A variety of new estrogenic/anti‐estrogenic/selective estrogen receptor modulator (SERM)‐like compounds, including 2‐methoxyestradiol, genistein, resveratrol, licochalcone, Raloxifene, ICI 182,780, and estramustine are being evaluated for their potential in the next generation of PCa therapies. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NCOA1 | up-regulates
binding
|
ESR1 |
0.839 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-54442 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9427757 |
Steroid receptor co-activator (src1) is one of a number of transcriptional co-activators that are capable of potentiating the activity of nuclear receptors including the oestrogen receptor (er). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MECP2 | down-regulates quantity by repression
transcriptional regulation
|
ESR1 |
0.4 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254573 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 15870696 |
Valproate (VPA) induces silencing of the ERalpha, cyclin D1 and pS2 promoters. Chromatin immunoprecipitation (ChIP) analysis demonstrates that VPA induces recruitment of the 5-MeCpG binding protein MeCP2 to the ERalpha A promoter and also to the pS2 and cyclin D1 promoters |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254024 |
|
|
Homo sapiens |
MDA-MB-468 Cell |
| pmid |
sentence |
| 23242655 |
Our previous studies demonstrated that mutant p53 along with repression complex proteins including DNMT1, HDAC1 and MeCP2 is associated with ER-negative promoter in MDA-MB-468 cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
SNAI2 |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254230 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18588516 |
The down-regulation of slug in the ERalpha-positive MCF-7 cell line was mediated by direct repression of slug transcription by the formation of a co-repressor complex involving ligand-activated ERalpha protein, HDAC1 (histone deacetylase 1) and N-CoR (nuclear receptor co-repressor). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tibolone | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257821 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19464167 |
In this study, we have assessed the potential hormonal profile of tibolone and its primary metabolites on all human steroid receptors (PR, AR, GR, MR, ERα and ERβ) using HeLa or PC3 cells stably transfected with a given receptor and a luciferase reporter gene. We show that tibolone and its ∆ 4 -isomer predominantly bind and activate PR and AR whereas 3α and 3β-OH-tibolone predominantly bind and activate ERα (Table 1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
TFF1 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253938 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 11517191 |
ER beta and ER alpha induced the expression of several endogenous genes such as pS2, TGF alpha, or the cyclin kinase inhibitor p21 but, in contrast to ER alpha, ER beta was unable to regulate c-myc proto-oncogene expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
NCOA2 |
0.81 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-109520 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11477071 |
Er_ mutants unable to bind coactivators drastically decrease estradiol regulation of ap-1-mediated transcription and overexpression of the coactivator grip1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
bisphenol A | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268729 |
|
|
in vitro |
|
| pmid |
sentence |
| 31995776 |
This study investigated the endocrine-disrupting activity of BPA, BPF, and BPS alone or as a mixture and the agonistic and antagonistic activity of the BPs using an in vitro bioassay to detect ER-, AR-, and AhR-mediated activity. Here, we evaluated the endocrine-disrupting risks of the bisphenols by investigating their agonist and antagonist activities with the estrogen (ER), androgen (AR), and aryl hydrocarbon (AhR) receptors. Our results showed that BPA, BPS, and BPF (BPs) have estrogen agonist and androgen antagonist activities and decrease the ERα protein level. . |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268738 |
|
|
in vitro |
|
| pmid |
sentence |
| 9751507 |
Bisphenol A is an equally strong agonist for ERα as for ERβ, and the same is true for 4,4′-biphenol, which differs from bisphenol A in that it lacks the propane group between the phenolic rings. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
NR0B2 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74288 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10648597 |
We demonstrate that shp variants, carrying either interaction-defective nr box mutations or a deletion of the repressor domain, have lost the capacity to inhibit agonist-dependent transcriptional estrogen receptor activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
PSEN2 |
0.284 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271691 |
|
|
|
|
| pmid |
sentence |
| 14764652 |
Estrogen-induced transcriptional activities of both ERalpha and ERbeta and mRNA expression of estrogen-responsive genes, including pS2, c-myc, and cyclin D1, were suppressed by PP5 but enhanced by PP5 antisense oligonucleotide. |
|
| Publications: |
1 |
| + |
RBX1 | down-regulates quantity by destabilization
ubiquitination
|
ESR1 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271434 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 20130088 |
I3C-dependent activation of the aryl hydrocarbon receptor (AhR) initiates Rbx-1 E3 ligase-mediated ubiquitination and proteasomal degradation of ERalpha protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KMT2D | up-regulates
binding
|
ESR1 |
0.466 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-145865 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16603732 |
A novel estrogen receptor (er)alpha coactivator complex, the mll2 complex, which consists of mll2, ash2, rbq3, and wdr5, was identified / disrupting the interaction between eralpha and the mll2 complex with small interfering rnas specific against mll2 or an mll2 fragment representing the interacting region with eralpha significantly inhibited the eralpha transcription activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates activity
binding
|
AP1 |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263656 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18247370 |
The primary conclusion of the results reported here is that ERα and c‐jun, c‐fos and ATF‐2, but not Fra‐2 AP‐1 factors interact “in vivo” with specific estrogen‐responsive regulatory sequences and AP‐1 cis‐elements within the F promoter of the human ERα gene in osteoblast‐like SaOS‐2 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Luminal Breast Cancer |
| + |
biphenyl-4,4'-diol | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268740 |
|
|
in vitro |
|
| pmid |
sentence |
| 9751507 |
Bisphenol A is an equally strong agonist for ERα as for ERβ, and the same is true for 4,4′-biphenol, which differs from bisphenol A in that it lacks the propane group between the phenolic rings. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ESR1 | up-regulates
binding
|
PI3K |
0.648 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252675 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16169518 |
Recently, it has been known that er activates phosphatidylinositol-3-oh kinase (pi3k) through binding with the p85 regulatory subunit of pi3k. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
KDM4B |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263737 |
|
|
Homo sapiens |
T-47D Cell |
| pmid |
sentence |
| 20682797 |
Here, we show the histone demethylase JMJD2B is regulated by both ERalpha and HIF-1alpha, drives breast cancer cell proliferation in normoxia and hypoxia, and epigenetically regulates the expression of cell cycle genes such as CCND1, CCNA1, and WEE1. these data indicate that JMJD2B is a bona fide target of ERα and its expression in ER-positive breast cancer cells is mainly dependent on ERα. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EGFR | up-regulates
phosphorylation
|
ESR1 |
0.61 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115734 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 11887937 |
Activation of estrogen receptor-alpha (eralpha) by growth factors in the absence of estrogen is a well-documented phenomenon.Egfr tyrosine kinase in vitro stimulated the phosphorylation of recombinant er |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
AR |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-82158 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11000528 |
Inhibition of ar-induced transactivation that was er cdna dose-responsive and estradiol dependent |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
PPARG |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140233 |
|
|
Homo sapiens |
Breast Cancer Cell, MCF-7 Cell, HeLa Cell |
| pmid |
sentence |
| 16144913 |
Our data show for the first time that eralpha binds to ppar response element and represses its transactivation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
OXT |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268546 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 6153132 |
The human and rat OT promoters could be stimulated by the ligand-activated estrogen receptors ERalpha and ERbeta, the thyroid hormone receptor THRapha, and the retinoic acid receptors RARalpha and RARbeta in a variety of cells (3, 477, 478). However, it is important to note that these results were obtained from cotransfection experiments in cell lines, i.e., under nonphysiological circumstances. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Oxytocin signaling |
| + |
AIP | down-regulates activity
transcriptional regulation
|
ESR1 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253644 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 21984905 |
The immunophilin-like protein XAP2 is a negative regulator of estrogen signaling through interaction with estrogen receptor α. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
CRH |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268721 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 8408641 |
Evidence of direct estrogenic regulation of human corticotropin-releasing hormone gene expression. Potential implications for the sexual dimophism of the stress response and immune/inflammatory reaction.|Gel retardation and immunoprecipitation demonstrated specific association between the perfect half-palindromic EREs of hCRH gene and the DNA binding domain of hER in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Hypothalamus |
| + |
ESR1 | up-regulates
binding
|
PIK3R1 |
0.612 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140470 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 16169518 |
Recently, it has been known that er activates phosphatidylinositol-3-oh kinase (pi3k) through binding with the p85 regulatory subunit of pi3k. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
SCN8A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253476 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 22169964 |
In this study, quantitative real-time PCR analysis showed that the gene expression levels of TTX-S (Nav1.1 and Nav1.7) and TTX-R (Nav1.8 and Nav1.9) sodium channel subtypes were elevated in DRGs of αERKO and βERKO mice, whereas Nav1.6 mRNA decreased in αERKOs but showed no changes in βERKO mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
perfluorooctanoic acid | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268762 |
|
|
in vitro |
|
| pmid |
sentence |
| 23764977 |
Seven PFCs [perfluorohexane sulfonate (PFHxS), perfluorooctane sulfonate (PFOS), perfluorooctanoate (PFOA), perfluorononanoate (PFNA), perfluorodecanoate (PFDA), perfluoroundecanoate (PFUnA), and perfluorododecanoate (PFDoA)] were analyzed in vitro for their potential to affect estrogen receptor (ER) and androgen receptor (AR) transactivity as well as aromatase enzyme activity. The PFCs were assessed as single compounds and in an equimolar mixture. PFHxS, PFOS and PFOA significantly induced the ER transactivity, whereas PFHxS, PFOS, PFOA, PFNA and PFDA significantly antagonized the AR activity in a concentration-dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NR0B2 | down-regulates
binding
|
ESR1 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115033 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11861507 |
Our results identify shp as an inhibitor of 4-oht agonist activity in rl95-2 human endometrial carcinoma cells that express endogenous er?. We conclude that shp does not decrease er expression, but rather it is the direct interaction of shp with er that inhibits er transcriptional activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
ESR1 |
transcriptional regulation
|
MYC |
0.718 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253941 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 11517191 |
ER beta and ER alpha induced the expression of several endogenous genes such as pS2, TGF alpha, or the cyclin kinase inhibitor p21 but, in contrast to ER alpha, ER beta was unable to regulate c-myc proto-oncogene expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
CDKN1A |
0.491 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253940 |
|
|
Homo sapiens |
Breast Cancer Cell Line |
| pmid |
sentence |
| 11517191 |
ER beta and ER alpha induced the expression of several endogenous genes such as pS2, TGF alpha, or the cyclin kinase inhibitor p21 but, in contrast to ER alpha, ER beta was unable to regulate c-myc proto-oncogene expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
afimoxifene | down-regulates activity
chemical inhibition
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258595 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
CCND1 |
0.746 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135053 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15808510 |
Ikkalpha in conjunction with eralpha and aib1/src-3, is important in activating the transcription of estrogen-responsive genes, including cyclin d1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
raloxifene | down-regulates activity
chemical inhibition
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258582 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
SCN10A |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253470 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 22169964 |
17β-Estradiol regulates the gene expression of voltage-gated sodium channels. . In this study, we investigate the mRNA expressions of Nav channel subtypes mediated differentially by the ERs in the DRGs of wild-type (WT) and estrogen receptor knockout (αERKO and βERKO) mice. In the present study, by means of quantitative real-time PCR, we found that the expressions of Nav1.1, Nav1.7, Nav1.8, and Nav1.9 subtypes were elevated in αERKO and βERKO mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Ganglion |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
SCN11A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253471 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 22169964 |
17β-Estradiol regulates the gene expression of voltage-gated sodium channels. . In this study, we investigate the mRNA expressions of Nav channel subtypes mediated differentially by the ERs in the DRGs of wild-type (WT) and estrogen receptor knockout (αERKO and βERKO) mice. In the present study, by means of quantitative real-time PCR, we found that the expressions of Nav1.1, Nav1.7, Nav1.8, and Nav1.9 subtypes were elevated in αERKO and βERKO mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Ganglion |
| + |
BRCA1 | down-regulates activity
|
ESR1 |
0.745 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253974 |
|
|
Homo sapiens |
Breast Cancer Cell Line, Prostate Cancer Cell Line |
| pmid |
sentence |
| 11244506 |
The BRCA1 gene was previously found to inhibit the transcriptional activity of the estrogen receptor [ER-alpha] in human breast and prostate cancer cell lines. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
afimoxifene | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258594 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
SCN1A |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253468 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 22169964 |
17β-Estradiol regulates the gene expression of voltage-gated sodium channels. . In this study, we investigate the mRNA expressions of Nav channel subtypes mediated differentially by the ERs in the DRGs of wild-type (WT) and estrogen receptor knockout (αERKO and βERKO) mice. In the present study, by means of quantitative real-time PCR, we found that the expressions of Nav1.1, Nav1.7, Nav1.8, and Nav1.9 subtypes were elevated in αERKO and βERKO mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Ganglion |
| + |
17beta-estradiol | up-regulates activity
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258591 |
|
|
in vitro |
|
| pmid |
sentence |
| 9048584 |
In total 37 substances were tested for both ER subtypes (Fig. 3 and Table 1). In Fig. 3 several examples of typical competitor curves obtained are shown. In all cases monophasic curves were obtained for compounds with significant affinity. . The present study is the first in which the ligand binding properties of both ER subtypes are measured separately, and caution is needed when comparing RBAs from this study with the previous studies involving mixtures of ER subtypes. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Luminal Breast Cancer |
| + |
ESR1 | up-regulates quantity by expression
transcriptional regulation
|
F12 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254072 |
|
|
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 9794469 |
Transcription of the FXII gene is stimulated by estrogens through specific interaction of the estrogen receptor alpha (ER alpha) with an estrogen response element present on FXII promoter. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | down-regulates quantity by repression
transcriptional regulation
|
SCN9A |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253469 |
|
|
Mus musculus |
Neuron |
| pmid |
sentence |
| 22169964 |
17β-Estradiol regulates the gene expression of voltage-gated sodium channels. . In this study, we investigate the mRNA expressions of Nav channel subtypes mediated differentially by the ERs in the DRGs of wild-type (WT) and estrogen receptor knockout (αERKO and βERKO) mice. In the present study, by means of quantitative real-time PCR, we found that the expressions of Nav1.1, Nav1.7, Nav1.8, and Nav1.9 subtypes were elevated in αERKO and βERKO mice |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Tissue: |
Spinal Ganglion |
| + |
17beta-estradiol | up-regulates
chemical activation
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154660 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 17478088 |
Oestrogen receptors (er)alpha and beta modify the expression of genes involved in cell growth, proliferation and differentiation through binding to oestrogen response elements (eres) located in a number of gene promoters. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Luminal Breast Cancer |
| + |
fulvestrant | down-regulates activity
chemical inhibition
|
ESR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259305 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12113237 |
Fulvestrant (Faslodex, formerly ICI 182,780) is a potent steroidal antiestrogen that mediates its effects by estrogen receptor downregulation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ESR1
- 
- 