ESR2
Gene Ontology Biological Process
- cell-cell signaling [TAS]
- extracellular negative regulation of signal transduction [NAS]
- gene expression [TAS]
- intracellular estrogen receptor signaling pathway [TAS]
- negative regulation of cell growth [NAS]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of sequence-specific DNA binding transcription factor activity [IDA]
- regulation of transcription, DNA-templated [TAS]
- signal transduction [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- DNA binding [TAS]
- core promoter sequence-specific DNA binding [IDA]
- enzyme binding [IPI]
- estrogen receptor activity [TAS]
- estrogen response element binding [IDA]
- ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IDA, NAS]
- protein binding [IPI]
- receptor antagonist activity [NAS]
- sequence-specific DNA binding transcription factor activity [TAS]
- steroid binding [ISS, TAS]
- steroid hormone receptor activity [TAS]
- transcription coactivator activity [TAS]
- DNA binding [TAS]
- core promoter sequence-specific DNA binding [IDA]
- enzyme binding [IPI]
- estrogen receptor activity [TAS]
- estrogen response element binding [IDA]
- ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IDA, NAS]
- protein binding [IPI]
- receptor antagonist activity [NAS]
- sequence-specific DNA binding transcription factor activity [TAS]
- steroid binding [ISS, TAS]
- steroid hormone receptor activity [TAS]
- transcription coactivator activity [TAS]
Gene Ontology Cellular Component
MED23
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro.
Target gene activation by nuclear hormone receptors, including estrogen receptors (ERs), is thought to be mediated by a variety of interacting cofactors. Here we identify a number of nuclear extract-derived proteins that interact with immobilized ER ligand binding domains in a 17beta-estradiol-dependent manner. The most prominent of these are components of the thyroid hormone receptor-associated protein (TRAP)/Mediator coactivator complex, which ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ESR2 MED23 | 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 | - |
Curated By
- BioGRID