VDR
Gene Ontology Biological Process
- bile acid signaling pathway [IDA]
- cell morphogenesis [IMP]
- decidualization [IEP]
- gene expression [TAS]
- negative regulation of cell proliferation [IDA]
- negative regulation of keratinocyte proliferation [IMP]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- positive regulation of gene expression [IMP]
- positive regulation of keratinocyte differentiation [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of vitamin D 24-hydroxylase activity [IDA]
- regulation of calcidiol 1-monooxygenase activity [ISS]
- signal transduction [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- vitamin D receptor signaling pathway [IDA]
Gene Ontology Molecular Function- DNA binding [IDA]
- calcitriol binding [IDA]
- calcitriol receptor activity [IDA]
- lithocholic acid binding [IDA]
- lithocholic acid receptor activity [IDA]
- protein binding [IPI]
- retinoid X receptor binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- vitamin D response element binding [IDA]
- DNA binding [IDA]
- calcitriol binding [IDA]
- calcitriol receptor activity [IDA]
- lithocholic acid binding [IDA]
- lithocholic acid receptor activity [IDA]
- protein binding [IPI]
- retinoid X receptor binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- vitamin D response element binding [IDA]
Gene Ontology Cellular Component
MED14
Gene Ontology Biological Process
- androgen receptor signaling pathway [IDA]
- gene expression [TAS]
- intracellular steroid hormone receptor signaling pathway [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- regulation of transcription from RNA polymerase II promoter [TAS]
- transcription initiation from RNA polymerase II promoter [IDA, TAS]
Gene Ontology Molecular Function- RNA polymerase II transcription cofactor activity [IDA]
- ligand-dependent nuclear receptor transcription coactivator activity [NAS]
- protein binding [IPI]
- receptor activity [IDA]
- thyroid hormone receptor binding [IDA]
- transcription coactivator activity [IDA]
- transcription cofactor activity [IDA]
- vitamin D receptor binding [NAS]
- RNA polymerase II transcription cofactor activity [IDA]
- ligand-dependent nuclear receptor transcription coactivator activity [NAS]
- protein binding [IPI]
- receptor activity [IDA]
- thyroid hormone receptor binding [IDA]
- transcription coactivator activity [IDA]
- transcription cofactor activity [IDA]
- vitamin D receptor binding [NAS]
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
Binding of liganded vitamin D receptor to the vitamin D receptor interacting protein coactivator complex induces interaction with RNA polymerase II holoenzyme.
Because the vitamin D receptor interacting protein (DRIP) coactivator complex shares components with the RNA polymerase II (Pol II) holoenzyme complex, we tested whether the two protein complexes associate in cellular extracts. On initial purification steps, the DRIP complex copurified with the Pol II holoenzyme. Pol II was found to bind to the vitamin D receptor in a ligand-dependent fashion ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| VDR MED14 | 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. | Low | - | BioGRID | - | |
| VDR MED14 | 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. | Low | - | BioGRID | - | |
| VDR MED14 | 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