| + |
MAPK1 | down-regulates activity 
phosphorylation
|
THRB |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102216 |
Ser142 |
IQKNLHPsYSCKYEG |
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 |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
THRB |
0.407 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102224 |
Ser142 |
IQKNLHPsYSCKYEG |
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 |
| + |
D-thyroxine | up-regulates activity 
chemical activation
|
THRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258401 |
|
|
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: |
1 |
Organism: |
Homo Sapiens |
| + |
3,3',5'-triiodothyronine | up-regulates activity
chemical activation, binding
|
THRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258384 |
|
|
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-267254 |
|
|
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: |
2 |
Organism: |
Rattus Norvegicus, Homo Sapiens |
| Tissue: |
Hypophysis |
| Pathways: | Thyroid Hormone Metabolism |
| + |
RXRB | up-regulates
binding
|
THRB |
0.623 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81455 |
|
|
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 |
| + |
ERK1/2 | down-regulates activity
phosphorylation
|
THRB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270143 |
|
|
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 |
| + |
ASXL3 | down-regulates activity
binding
|
THRB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266766 |
|
|
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 |
| + |
THRB | down-regulates activity
binding
|
GATA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267256 |
|
|
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 |
| + |
L-thyroxine | up-regulates activity
chemical activation
|
THRB |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258383 |
|
|
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: |
1 |
Organism: |
Rattus Norvegicus |
| Pathways: | Thyroid Hormone Metabolism |
| + |
TRIP11 | up-regulates
binding
|
THRB |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-50421 |
|
|
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 |
| + |
RXRA | up-regulates
binding
|
THRB |
0.712 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81449 |
|
|
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 |
| + |
Gbeta | down-regulates activity
phosphorylation
|
THRB |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270016 |
|
|
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 |
3.0
THRB
- 
- 