+ |
PTH1R | up-regulates activity
binding
|
GNAS |
0.485 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270551 |
|
|
|
|
pmid |
sentence |
28363951 |
This calciotropic hormone exerts its actions via binding to the PTH/PTH-related peptide receptor (PTH1R), which couples to multiple heterotrimeric G proteins, including Gs and Gq/11. |
|
Publications: |
1 |
+ |
PTH1R | down-regulates quantity
|
SLC34A3 |
0.349 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270557 |
|
|
|
|
pmid |
sentence |
28363951 |
PTH inhibits reabsorption of phosphate from the glomerular filtrate in RPT by decreasing the abundance of sodium-phosphate co-transporters NPT2a and NPT2c on the apical membrane, thus enhancing renal phosphate excretion |
|
Publications: |
1 |
+ |
PTHLH | up-regulates activity
binding
|
PTH1R |
0.752 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270549 |
|
|
in vitro |
|
pmid |
sentence |
8683730 |
Prostate-specific antigen was found to specifically cleave PTHrP 1-141 in a time- and dose-dependent manner.|The preferred PSA cleavage site of PTHrP 1-141 was determined to be at the carboxyl-terminus of phenylalanine 23, consistent with chymotryptic-like enzymatic activity of PSA. Cleavage of PTHrP by PSA completely abolished the ability of PTHrP to stimulate cAMP production. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
Parathyroid hormone-related peptide (1-36) | up-regulates activity
chemical activation
|
PTH1R |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-257575 |
|
|
Homo sapiens |
HEK-293A Cell |
pmid |
sentence |
31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTH1R | up-regulates activity
binding
|
GNAQ |
0.278 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270550 |
|
|
|
|
pmid |
sentence |
28363951 |
This calciotropic hormone exerts its actions via binding to the PTH/PTH-related peptide receptor (PTH1R), which couples to multiple heterotrimeric G proteins, including Gs and Gq/11. |
|
Publications: |
1 |
+ |
PTH1R | down-regulates quantity
|
DKK1 |
0.315 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270553 |
|
|
|
|
pmid |
sentence |
28363951 |
Furthermore, PTH acts on osteocytes to suppress the expression of sclerostin, an inhibitor of canonical Wnt signaling (Li, et al. 2005; Semenov, et al. 2005)). PTH action on sclerostin is primarily through cAMP signaling (Keller and Kneissel 2005) and mediated by Myocyte enhancer factor-2 (MEF2) transcriptional regulators (Leupin, et al. 2007). Using the cAMP signaling pathway in osteoblasts, PTH also inhibits the expression of Dickkopf 1 (Dkk1) (Guo et al. 2010a), which is another Wnt pathway inhibitor |
|
Publications: |
1 |
+ |
PTH1R | up-regulates quantity
|
CYP24A1 |
0.292 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270555 |
|
|
|
|
pmid |
sentence |
28363951 |
These PTH actions are mainly mediated by Gsalpha signaling, which induces the expression of the gene encoding 25-hydroxyvitamin D 1alpha-hydroxylase (Cyp27b1) and destabilizes the transcript encoding vitamin D 24-hydroxylase (Cyp24a1) |
|
Publications: |
1 |
+ |
PTH1R | down-regulates quantity
|
SLC34A1 |
0.313 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270556 |
|
|
|
|
pmid |
sentence |
28363951 |
PTH inhibits reabsorption of phosphate from the glomerular filtrate in RPT by decreasing the abundance of sodium-phosphate co-transporters NPT2a and NPT2c on the apical membrane, thus enhancing renal phosphate excretion |
|
Publications: |
1 |
+ |
PTH1R | down-regulates quantity
|
SOST |
0.389 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270552 |
|
|
|
|
pmid |
sentence |
28363951 |
Furthermore, PTH acts on osteocytes to suppress the expression of sclerostin, an inhibitor of canonical Wnt signaling (Li, et al. 2005; Semenov, et al. 2005)). PTH action on sclerostin is primarily through cAMP signaling (Keller and Kneissel 2005) and mediated by Myocyte enhancer factor-2 (MEF2) transcriptional regulators (Leupin, et al. 2007). Using the cAMP signaling pathway in osteoblasts, PTH also inhibits the expression of Dickkopf 1 (Dkk1) (Guo et al. 2010a), which is another Wnt pathway inhibitor |
|
Publications: |
1 |
+ |
PTH1R | up-regulates
binding
|
LRP6 |
0.343 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-199533 |
|
|
Homo sapiens |
|
pmid |
sentence |
23151663 |
Parathyroid hormone (pth) binding to its receptor pth1r induces association of the pthpth1r complex with lrp6and phosphorylation of pppsp sites by protein kinase_ a, which in turn triggers wnt. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTH1R | up-regulates quantity
|
CYP27B1 |
0.306 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-270554 |
|
|
|
|
pmid |
sentence |
28363951 |
These PTH actions are mainly mediated by Gsalpha signaling, which induces the expression of the gene encoding 25-hydroxyvitamin D 1alpha-hydroxylase (Cyp27b1) and destabilizes the transcript encoding vitamin D 24-hydroxylase (Cyp24a1) |
|
Publications: |
1 |
+ |
PTH | up-regulates
binding
|
PTH1R |
0.763 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182039 |
|
|
Homo sapiens |
|
pmid |
sentence |
18981475 |
Here we show that binding of pth to its receptor pth1r induced association of lrp6, a coreceptor of wnt, with pth1r. The formation of the ternary complex containing pth, pth1r, and lrp6 promoted rapid phosphorylation of lrp6, which resulted in the recruitment of axin to lrp6, and stabilization of beta-catenin. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |