TRIM24
Gene Ontology Biological Process
Gene Ontology Molecular Function
ESR1
Gene Ontology Biological Process
- cellular response to estradiol stimulus [ISS]
- chromatin remodeling [NAS]
- gene expression [TAS]
- intracellular estrogen receptor signaling pathway [NAS]
- intracellular steroid hormone receptor signaling pathway [ISS]
- negative regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- negative regulation of gene expression [IDA]
- negative regulation of sequence-specific DNA binding transcription factor activity [IDA]
- phospholipase C-activating G-protein coupled receptor signaling pathway [ISS]
- positive regulation of cytosolic calcium ion concentration [ISS]
- positive regulation of nitric oxide biosynthetic process [IDA]
- positive regulation of nitric-oxide synthase activity [IDA]
- positive regulation of phospholipase C activity [ISS]
- positive regulation of retinoic acid receptor signaling pathway [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- regulation of transcription, DNA-templated [NAS]
- response to estradiol [IDA]
- response to estrogen [IDA]
- signal transduction [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- transcription, DNA-templated [TAS]
Gene Ontology Molecular Function- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- beta-catenin binding [IPI]
- chromatin binding [IDA]
- core promoter sequence-specific DNA binding [IDA]
- enzyme binding [IPI]
- estrogen receptor activity [NAS]
- estrogen response element binding [IDA]
- estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IGI]
- identical protein binding [IPI]
- nitric-oxide synthase regulator activity [NAS]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [NAS]
- steroid binding [ISS]
- steroid hormone receptor activity [TAS]
- transcription factor binding [IPI]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription [IDA]
- beta-catenin binding [IPI]
- chromatin binding [IDA]
- core promoter sequence-specific DNA binding [IDA]
- enzyme binding [IPI]
- estrogen receptor activity [NAS]
- estrogen response element binding [IDA]
- estrogen-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IGI]
- identical protein binding [IPI]
- nitric-oxide synthase regulator activity [NAS]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [NAS]
- steroid binding [ISS]
- steroid hormone receptor activity [TAS]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1alpha and estrogen receptors.
Hormonal regulation of gene activity is mediated by nuclear receptors acting as ligand-activated transcription factors. To achieve efficient regulation of gene expression, these receptors must interact with different type of molecules: 1) the steroid hormone, 2) the DNA response element, and 3) various proteins acting as transcriptional cofactors. In the present study, we have investigated how ligand and DNA binding ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ESR1 TRIM24 | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | - | BioGRID | - | |
| ESR1 TRIM24 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - | |
| ESR1 TRIM24 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| TRIM24 ESR1 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
| ESR1 TRIM24 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID