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
MED1
Gene Ontology Biological Process
- ERK1 and ERK2 cascade [IDA]
- androgen biosynthetic process [IMP]
- androgen receptor signaling pathway [IDA]
- angiogenesis [ISS]
- cell morphogenesis [IMP]
- cellular lipid metabolic process [TAS]
- cellular response to epidermal growth factor stimulus [IDA]
- cellular response to steroid hormone stimulus [IDA]
- cellular response to thyroid hormone stimulus [IDA]
- erythrocyte development [ISS]
- fat cell differentiation [IDA]
- gene expression [TAS]
- intracellular steroid hormone receptor signaling pathway [IDA]
- keratinocyte differentiation [IMP]
- lens development in camera-type eye [ISS]
- mRNA transcription from RNA polymerase II promoter [ISS]
- megakaryocyte development [ISS]
- negative regulation of apoptotic process [ISS]
- negative regulation of keratinocyte proliferation [IMP]
- negative regulation of neuron differentiation [ISS]
- negative regulation of transcription from RNA polymerase II promoter [ISS]
- positive regulation of gene expression [IDA, IMP]
- positive regulation of keratinocyte differentiation [IMP]
- positive regulation of receptor activity [IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription, DNA-templated [IDA]
- regulation of RNA biosynthetic process [IMP]
- regulation of cell cycle [NAS]
- regulation of transcription from RNA polymerase I promoter [IDA]
- small molecule metabolic process [TAS]
- thyroid hormone mediated signaling pathway [IMP]
- transcription initiation from RNA polymerase II promoter [IDA, TAS]
Gene Ontology Molecular Function- LBD domain binding [IPI]
- RNA polymerase II transcription cofactor activity [IDA]
- chromatin binding [IMP]
- core promoter binding [IDA]
- estrogen receptor binding [IPI]
- ligand-dependent nuclear receptor binding [IDA, IPI]
- ligand-dependent nuclear receptor transcription coactivator activity [IMP, NAS]
- mediator complex binding [IDA]
- nuclear hormone receptor binding [IPI]
- peroxisome proliferator activated receptor binding [IPI]
- protein binding [IPI]
- receptor activity [IDA]
- retinoic acid receptor binding [IPI]
- sequence-specific DNA binding RNA polymerase II transcription factor activity [ISS]
- thyroid hormone receptor binding [IDA, IPI]
- thyroid hormone receptor coactivator activity [IMP]
- transcription coactivator activity [IDA, IMP]
- transcription cofactor activity [IDA]
- transcription factor binding [IPI]
- vitamin D receptor binding [IPI, NAS, TAS]
- LBD domain binding [IPI]
- RNA polymerase II transcription cofactor activity [IDA]
- chromatin binding [IMP]
- core promoter binding [IDA]
- estrogen receptor binding [IPI]
- ligand-dependent nuclear receptor binding [IDA, IPI]
- ligand-dependent nuclear receptor transcription coactivator activity [IMP, NAS]
- mediator complex binding [IDA]
- nuclear hormone receptor binding [IPI]
- peroxisome proliferator activated receptor binding [IPI]
- protein binding [IPI]
- receptor activity [IDA]
- retinoic acid receptor binding [IPI]
- sequence-specific DNA binding RNA polymerase II transcription factor activity [ISS]
- thyroid hormone receptor binding [IDA, IPI]
- thyroid hormone receptor coactivator activity [IMP]
- transcription coactivator activity [IDA, IMP]
- transcription cofactor activity [IDA]
- transcription factor binding [IPI]
- vitamin D receptor binding [IPI, NAS, TAS]
Co-localization
Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.
Publication
Regulation of the human p21(waf1/cip1) gene promoter via multiple binding sites for p53 and the vitamin D3 receptor.
The main regulator of the human tumor suppresser gene p21(waf1/cip1) is the transcription factor p53, but more recently it has been suggested to be a primary anti-proliferative target for the nuclear receptor VDR in the presence of its ligand 1alpha,25-dihydroxyvitamin D3 (1alpha,25(OH)2D3). To identify VDR responding regions, we analyzed 20 overlapping regions covering the first 7.1 kb of the p21(waf1/cip1) ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| VDR MED1 | 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 MED1 | 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 MED1 | Co-localization Co-localization Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments. | Low | - | BioGRID | 503233 | |
| VDR MED1 | 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 | - | |
| VDR MED1 | 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 | - | |
| VDR MED1 | 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 | - | |
| MED1 VDR | 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 | - | |
| MED1 VDR | 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 | - | |
| VDR MED1 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID