| + |
progesterone | up-regulates quantity 
precursor of
|
11-deoxycorticosterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268631 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25855791 |
Cytochrome P450 (P450)4 21A2 is the major steroid 21-hydroxylase, which catalyzes the 21-hydroxylation of progesterone and 17alpha-hydroxyprogesterone (17alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Glomerulosa |
| Pathways: | Sex Hormone Biosynthesis |
| + |
HSD3B2 | up-regulates quantity
chemical modification
|
progesterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268634 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 2243100 |
Three beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase (3 beta-HSD) catalyze the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration and is therefore essential for the biosynthesis of all classes of hormonal steroids, namely progesterone, glucocorticoids, mineralocorticoids, androgens, and estrogens. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Glomerulosa |
| Pathways: | Sex Hormone Biosynthesis |
| + |
progesterone | down-regulates activity 
chemical inhibition
|
NR3C2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258705 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 8282004 |
The sex steroid progesterone bound with an affinity (ki < 0.01 nM) even higher than that of aldosterone to the human mineralocorticoid receptor and effectively antagonized the effect of aldosterone via the human mineralocorticoid receptor in functional co-transfection assays. This indicates that progesterone has potent antimineralocorticoid properties, while its antiglucocorticoid effects were less pronounced. The partial agonistic activities of antihormones in this assay suggest a direct interaction of antihormone-receptor complexes with the response elements on the DNA. aldosterone shows a higher functional sensitivity for the human mineralocorticoid receptor than deoxycorticosterone (higher affinity) or cortisol (similar affinity). Moreover, the very high binding affinity of the human mineralocorticoid receptor for progesterone (k i < 0.0l nM) in combination with the very low agonistic activity indicates that progesterone may act as a potent human mineralocorticoid receptor antagonist that is even more effective than spironolactone (k~ = 5.7 nM), which displays no partial agonistic activity (fig. 4). |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
progesterone | up-regulates quantity 
|
CACNA2D3 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266856 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31746409 |
In vivo and in vitro, the addition of P4 upregulated the expression of CACNA2D3 and silencing of CACNA2D3 impaired the function of P4 on cell apoptosis and proliferation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
progesterone | down-regulates 
|
COMT |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251960 |
|
|
|
|
| pmid |
sentence |
| 17138778 |
Catechol-O-methyltransferase expression was down-regulated by progesterone or estrogen. |
|
| Publications: |
1 |
| + |
progesterone | down-regulates
|
Corticotropin |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268727 |
|
|
|
|
| pmid |
sentence |
| 24631756 |
ACTH and corticosterone responses to the same acute stress stimulus are higher in the pro-estrus phase of the cycle, when the serum concentrations of estrogen are the highest (Viau and Meaney, 1991). In the same study, it was shown that progesterone inhibits the sensitizing effects of estrogen on ACTH release during stress, as the ACTH levels and HPA output decreased with increasing amounts of progesterone in the estrous and diestrous phases. |
|
| Publications: |
1 |
| + |
progesterone | up-regulates quantity
precursor of
|
17alpha-hydroxyprogesterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268649 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17192295 |
THE MICROSOMAL ENZYME P450c17 catalyzes two reactions: the 17α-hydroxylation of progesterone and pregnenolone and the subsequent cleavage of the C17–20 carbon bond to produce dehydroepiandrosterone (DHEA) and androstenedione. Whereas only 17α-hydroxylase activity is necessary for the production of corticosteroids, both activities of P450c17 are required to synthesize sex hormones. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Testis, Zona Glomerulosa, Zona Fasciculata |
| Pathways: | Sex Hormone Biosynthesis |
| + |
HSD3B1 | up-regulates quantity
chemical modification
|
progesterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268635 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 2243100 |
Three beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase (3 beta-HSD) catalyze the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration and is therefore essential for the biosynthesis of all classes of hormonal steroids, namely progesterone, glucocorticoids, mineralocorticoids, androgens, and estrogens. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Glomerulosa |
| Pathways: | Sex Hormone Biosynthesis |
| + |
pregnenolone | up-regulates quantity
precursor of
|
progesterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268630 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 2243100 |
Three beta-hydroxysteroid dehydrogenase/delta 5-delta 4-isomerase (3 beta-HSD) catalyze the oxidative conversion of delta 5-3 beta-hydroxysteroids to the delta 4-3-keto configuration and is therefore essential for the biosynthesis of all classes of hormonal steroids, namely progesterone, glucocorticoids, mineralocorticoids, androgens, and estrogens. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Glomerulosa |
| Pathways: | Sex Hormone Biosynthesis |
| + |
CYP21A2 | down-regulates quantity
chemical modification
|
progesterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268646 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25855791 |
Cytochrome P450 (P450)4 21A2 is the major steroid 21-hydroxylase, which catalyzes the 21-hydroxylation of progesterone and 17alpha-hydroxyprogesterone (17alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Zona Glomerulosa |
| Pathways: | Sex Hormone Biosynthesis |
| + |
CYP17A1 | down-regulates quantity
chemical modification
|
progesterone |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268657 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17192295 |
THE MICROSOMAL ENZYME P450c17 catalyzes two reactions: the 17α-hydroxylation of progesterone and pregnenolone and the subsequent cleavage of the C17–20 carbon bond to produce dehydroepiandrosterone (DHEA) and androstenedione. Whereas only 17α-hydroxylase activity is necessary for the production of corticosteroids, both activities of P450c17 are required to synthesize sex hormones. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Testis, Zona Glomerulosa, Zona Fasciculata |
| Pathways: | Sex Hormone Biosynthesis |
3.0
progesterone