NR3C1
Gene Ontology Biological Process
- cellular response to steroid hormone stimulus [IDA]
- gene expression [TAS]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- regulation of transcription, DNA-templated [IDA]
- signal transduction [TAS]
- transcription from RNA polymerase II promoter [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]
- glucocorticoid receptor activity [TAS]
- glucocorticoid-activated RNA polymerase II transcription factor binding transcription factor activity [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- steroid binding [IDA]
- steroid hormone binding [IDA]
- 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]
- glucocorticoid receptor activity [TAS]
- glucocorticoid-activated RNA polymerase II transcription factor binding transcription factor activity [IDA]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- steroid binding [IDA]
- steroid hormone binding [IDA]
Gene Ontology Cellular Component
SMARCC1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.
Nuclear hormone receptors are ligand-dependent transcriptional regulators that modulate chromatin structure. However, the precise molecular mechanisms by which receptors recruit chromatin-remodeling activity are not fully elucidated. We show that in the absence of its ligand-binding domain, the glucocorticoid receptor (GR) is able to interact with both nuclear receptor coactivators and the BRG1 chromatin-remodeling complex in vivo. Individually, the GR makes ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NR3C1 SMARCC1 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 3762967 | |
| NR3C1 SMARCC1 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | - | |
| NR3C1 SMARCC1 | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | Low | - | BioGRID | 2327385 |
Curated By
- BioGRID