| + |
CDK2 |
phosphorylation
|
PGR |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84980 |
Ser20 |
HVAGGPPsPEVGSPL |
Homo sapiens |
|
| pmid |
sentence |
| 11110801 |
In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84984 |
Ser213 |
SGAPVKPsPQAAAVE |
Homo sapiens |
|
| pmid |
sentence |
| 11110801 |
In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84988 |
Ser25 |
PPSPEVGsPLLCRPA |
Homo sapiens |
|
| pmid |
sentence |
| 11110801 |
In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84992 |
Ser554 |
PDSEASQsPQYSFES |
Homo sapiens |
|
| pmid |
sentence |
| 11110801 |
In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84996 |
Ser676 |
LSQRFTFsPGQDIQL |
Homo sapiens |
|
| pmid |
sentence |
| 11110801 |
In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85000 |
Thr430 |
PPLPPRAtPSRPGEA |
Homo sapiens |
|
| pmid |
sentence |
| 11110801 |
In vitro phosphorylation of pr with cdk2 has revealed five additional in vitro cdk2 phosphorylation sites: ser(25), ser(213), thr(430), ser(554), and ser(676). |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates 
phosphorylation
|
PGR |
0.605 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74712 |
Ser294 |
APMAPGRsPLATTVM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10655479 |
Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26s proteasome |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates
phosphorylation
|
PGR |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74716 |
Ser294 |
APMAPGRsPLATTVM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10655479 |
Specifically, down-regulation of mature prs occurs by a mechanism in which ligand binding activates pr phosphorylation by mapks at a unique serine residue, which then targets the receptors for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | down-regulates
phosphorylation
|
PGR |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-74708 |
Ser294 |
APMAPGRsPLATTVM |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10655479 |
Phosphorylation of human progesterone receptors at serine-294 by mitogen-activated protein kinase signals their degradation by the 26s proteasome |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity by destabilization
phosphorylation
|
PGR |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276498 |
Ser554 |
PDSEASQsPQYSFES |
Homo sapiens |
|
| pmid |
sentence |
| 23880761 |
Here, we have found that glycogen synthase kinase (GSK)-3β phosphorylation of progesterone receptor-A (PR-A) facilitates its ubiquitination. GSK-3β-mediated phosphorylation of serine 390 in PR-A regulates its subsequent ubiquitination and protein stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 |
phosphorylation
|
PGR |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250926 |
Ser81 |
TQDQQSLsDVEGAYS |
in vitro |
|
| pmid |
sentence |
| 7983041 |
Although human PR contains 11 potential CKII consensus sequences, CKII in vitro phosphorylated purified PR-B only at Ser81 suggesting that this may be an authentic site for CKII in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ERK1/2 | down-regulates
phosphorylation
|
PGR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270157 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10655479 |
Specifically, down-regulation of mature prs occurs by a mechanism in which ligand binding activates pr phosphorylation by mapks at a unique serine residue, which then targets the receptors for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
tibolone | up-regulates activity 
chemical activation
|
PGR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257822 |
|
|
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 |
| + |
Gbeta | down-regulates
phosphorylation
|
PGR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270040 |
|
|
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 10655479 |
Specifically, down-regulation of mature prs occurs by a mechanism in which ligand binding activates pr phosphorylation by mapks at a unique serine residue, which then targets the receptors for degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NCOR2 | down-regulates
acetylation
|
PGR |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101289 |
|
|
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell |
| pmid |
sentence |
| 12771131 |
In this study we assessed the effect of smrt and dax-1 on ar and pr activity in the presence of both agonists and partial antagonists. We show that smrt and dax-1 repress agonist-dependent activity of both receptors, and the mechanism of repression includes disruption of the receptor dimer interactions rather than recruitment of histone deacetylases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ESR1 | down-regulates quantity by repression 
transcriptional regulation
|
PGR |
0.624 |
| 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 |
| + |
PGR | up-regulates quantity by expression 
transcriptional regulation
|
KLK4 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254913 |
|
|
Homo sapiens |
T-47D Cell |
| pmid |
sentence |
| 19147544 |
we have shown that K4.pPRE interacts directly with the PR to up-regulate KLK4 gene expression in T47D cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NCOA1 | up-regulates
|
PGR |
0.683 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70149 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10449719 |
Progesterone receptor (pr) functions as a transcription factor that modulates the transcription of target genes in response to progesterone and other signals. The transcriptional activity of pr requires the involvement of coactivators such as steroid receptor coactivator-1 (src-1). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PGR | up-regulates
binding
|
ESR1 |
0.624 |
| 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 |
4.0
PGR
- 
- 