| + |
THR | up-regulates activity 
binding
|
RARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267779 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RXRB | up-regulates
binding
|
THR |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269880 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10976919 |
Like many receptors belonging to the superfamily of steroid/thyroid nuclear receptors, thyroid hormone receptors (trs) bind to specific th-dna responsive elements (tre) upstream of target gene in heterodimeric complex with the 9-cis retinoid acid receptor (rxr |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270297 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10976919 |
Like many receptors belonging to the superfamily of steroid/thyroid nuclear receptors, thyroid hormone receptors (trs) bind to specific th-dna responsive elements (tre) upstream of target gene in heterodimeric complex with the 9-cis retinoid acid receptor (rxr |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
THR | down-regulates activity 
binding
|
GATA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267275 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29407449 |
We found that the T3-bound TR inhibits this reporter construct driven by GATA2 alone, indicating that the target of T3-bound TR repression is GATA2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Hypophysis |
| Pathways: | Thyroid Hormone Metabolism |
| + |
RARA | up-regulates
binding
|
THR |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270293 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RARB | up-regulates activity
binding
|
THR |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267807 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
THR | up-regulates
binding
|
RARA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
3,3',5'-triiodothyronine | up-regulates activity
binding
|
THR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267276 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29407449 |
T3 binds its receptor (TR) in the nucleus. TRs are ligand-dependent transcription factors belonging to the type II group of NHRs. TRs are encoded by two genes, Thra and Thrb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid Hormone Metabolism |
| + |
NR0B2 | down-regulates quantity by repression 
transcriptional regulation
|
THR |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267806 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368516 |
Shp (short heterodimer partner) is an orphan nuclear receptor lacking a dna binding domain that interacts with nuclear receptors (nr) including thyroid receptor (tr), retinoic acid receptors (rar and rxr), and estrogen receptors alpha and beta (eralpha and erbeta). Shp acts as a negative regulator of these receptors by inhibiting dna binding and transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270298 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11368516 |
Shp (short heterodimer partner) is an orphan nuclear receptor lacking a dna binding domain that interacts with nuclear receptors (nr) including thyroid receptor (tr), retinoic acid receptors (rar and rxr), and estrogen receptors alpha and beta (eralpha and erbeta). Shp acts as a negative regulator of these receptors by inhibiting dna binding and transcriptional activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
THR |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270301 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12809513 |
We concluded that serine 142 of the tr dbd is the likely site of phosphorylation by t(4)-activated mapk and that the docking site on tr for activated mapk includes residues 128-133 (kgffrr), a basic amino acid-enriched motif novel for mapk substrates. Tr mutations in the proposed mapk docking domain and at residue 142 modulated t(4)-conditioned shedding of co-repressor and recruitment of co-activator proteins by the receptor, and they altered transcriptional activity of tr in a thyroid hormone response element-luciferase reporter assay. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
L-thyroxine | up-regulates activity
chemical activation
|
THR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270300 |
|
|
Rattus norvegicus |
Liver |
| pmid |
sentence |
| 2158622 |
We determined the affinity for T3 and analog binding characteristics of the translational products of c-erbA a- and /3-probes together with hepatic nuclear extracts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267808 |
|
|
Rattus norvegicus |
Liver |
| pmid |
sentence |
| 2158622 |
We determined the affinity for T3 and analog binding characteristics of the translational products of c-erbA a- and /3-probes together with hepatic nuclear extracts. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269881 |
|
|
Rattus norvegicus |
Liver |
| pmid |
sentence |
| 2158622 |
We determined the affinity for T3 and analog binding characteristics of the translational products of c-erbA a- and /3-probes together with hepatic nuclear extracts. |
|
| Publications: |
3 |
Organism: |
Rattus Norvegicus |
| Pathways: | Thyroid Hormone Metabolism |
| + |
RARG | up-regulates
binding
|
THR |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270296 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RARB | up-regulates
binding
|
THR |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270299 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
D-thyroxine | up-regulates activity
chemical activation
|
THR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270294 |
|
|
Homo sapiens |
Thyroid Epithelial Cell |
| pmid |
sentence |
| 6777394 |
The high levels of circulating D-T4 and presumably of circulating D-T3 originating from the peripheral conversion of D-T4 achieved after the chronic administration of D-T4 (Choloxin) may be responsible for a high degree of saturation of the human pituitary nuclear T3 receptors, thus resulting in the suppression of the TRH-induced TSH response. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269878 |
|
|
Homo sapiens |
Thyroid Epithelial Cell |
| pmid |
sentence |
| 6777394 |
The high levels of circulating D-T4 and presumably of circulating D-T3 originating from the peripheral conversion of D-T4 achieved after the chronic administration of D-T4 (Choloxin) may be responsible for a high degree of saturation of the human pituitary nuclear T3 receptors, thus resulting in the suppression of the TRH-induced TSH response. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267802 |
|
|
Homo sapiens |
Thyroid Epithelial Cell |
| pmid |
sentence |
| 6777394 |
The high levels of circulating D-T4 and presumably of circulating D-T3 originating from the peripheral conversion of D-T4 achieved after the chronic administration of D-T4 (Choloxin) may be responsible for a high degree of saturation of the human pituitary nuclear T3 receptors, thus resulting in the suppression of the TRH-induced TSH response. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
RARG | up-regulates activity
binding
|
THR |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267804 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RXRA | up-regulates
binding
|
THR |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270292 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10976919 |
Like many receptors belonging to the superfamily of steroid/thyroid nuclear receptors, thyroid hormone receptors (trs) bind to specific th-dna responsive elements (tre) upstream of target gene in heterodimeric complex with the 9-cis retinoid acid receptor (rxr). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269877 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10976919 |
Like many receptors belonging to the superfamily of steroid/thyroid nuclear receptors, thyroid hormone receptors (trs) bind to specific th-dna responsive elements (tre) upstream of target gene in heterodimeric complex with the 9-cis retinoid acid receptor (rxr). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ASXL3 | down-regulates activity
binding
|
THR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270302 |
|
|
Homo sapiens |
HEP-3B Cell |
| pmid |
sentence |
| 25450400 |
We determined that ASXL3 depletion augments the ligand-induced transcriptional activities of LXRα and TRβ, which were repressed by ASXL3 overexpression. The ligand-dependent interactions of ASXL3 with LXRα and TRβ were demonstrated by the GST pull-down and immunoprecipitation analyses. We confirmed that ASXL3 suppresses the expression of LXRα target genes through its recruitment to the LXR-response elements. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RARA | up-regulates activity
binding
|
THR |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267801 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
THR |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270303 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12809513 |
We concluded that serine 142 of the tr dbd is the likely site of phosphorylation by t(4)-activated mapk and that the docking site on tr for activated mapk includes residues 128-133 (kgffrr), a basic amino acid-enriched motif novel for mapk substrates. Tr mutations in the proposed mapk docking domain and at residue 142 modulated t(4)-conditioned shedding of co-repressor and recruitment of co-activator proteins by the receptor, and they altered transcriptional activity of tr in a thyroid hormone response element-luciferase reporter assay. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RXRB | up-regulates activity
binding
|
THR |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267805 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10976919 |
Like many receptors belonging to the superfamily of steroid/thyroid nuclear receptors, thyroid hormone receptors (trs) bind to specific th-dna responsive elements (tre) upstream of target gene in heterodimeric complex with the 9-cis retinoid acid receptor (rxr |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
THR | up-regulates activity
binding
|
RARG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267781 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIP11 | up-regulates
binding
|
THR |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270295 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9256431 |
Trip230 binds to rb independently of thyroid hormone while it forms a complex with tr in a thyroid hormone-dependent manner. Ectopic expression of the protein trip230 in cells, but not a mutant form that does not bind to tr, enhances specifically tr-dependent transcriptional activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269879 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9256431 |
Trip230 binds to rb independently of thyroid hormone while it forms a complex with tr in a thyroid hormone-dependent manner. Ectopic expression of the protein trip230 in cells, but not a mutant form that does not bind to tr, enhances specifically tr-dependent transcriptional activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
RXRA | up-regulates activity
binding
|
THR |
0.714 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267800 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10976919 |
Like many receptors belonging to the superfamily of steroid/thyroid nuclear receptors, thyroid hormone receptors (trs) bind to specific th-dna responsive elements (tre) upstream of target gene in heterodimeric complex with the 9-cis retinoid acid receptor (rxr). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
THR | up-regulates
binding
|
RARB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270314 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
Ee report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
THR | up-regulates
binding
|
RARG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270315 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIP11 | up-regulates activity
binding
|
THR |
0.432 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267803 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9256431 |
Trip230 binds to rb independently of thyroid hormone while it forms a complex with tr in a thyroid hormone-dependent manner. Ectopic expression of the protein trip230 in cells, but not a mutant form that does not bind to tr, enhances specifically tr-dependent transcriptional activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
THR | up-regulates activity
binding
|
RARB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267780 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15650024 |
We report that the retinoic acid receptors (rars), a distinct class of nuclear receptors, are also efficient heterodimer partners for trs |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
THR