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
RXRA
Gene Ontology Biological Process
- cellular lipid metabolic process [TAS]
- cholesterol metabolic process [TAS]
- gene expression [TAS]
- modulation by virus of host morphology or physiology [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- peroxisome proliferator activated receptor signaling pathway [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein homotetramerization [IDA]
- response to retinoic acid [IMP]
- retinoic acid receptor signaling pathway [IMP]
- small molecule metabolic process [TAS]
- transcription initiation from RNA polymerase II promoter [TAS]
- vitamin metabolic process [TAS]
Gene Ontology Molecular Function- DNA binding [IDA]
- RNA polymerase II regulatory region sequence-specific DNA binding [IDA]
- enzyme binding [IPI]
- ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- retinoic acid receptor activity [TAS]
- retinoic acid-responsive element binding [IDA]
- sequence-specific DNA binding [IDA]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription coactivator activity [TAS]
- transcription regulatory region DNA binding [IDA]
- vitamin D receptor binding [IPI]
- vitamin D response element binding [IDA]
- DNA binding [IDA]
- RNA polymerase II regulatory region sequence-specific DNA binding [IDA]
- enzyme binding [IPI]
- ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- retinoic acid receptor activity [TAS]
- retinoic acid-responsive element binding [IDA]
- sequence-specific DNA binding [IDA]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription coactivator activity [TAS]
- transcription regulatory region DNA binding [IDA]
- vitamin D receptor binding [IPI]
- vitamin D response element binding [IDA]
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Regulation of ligand-induced heterodimerization and coactivator interaction by the activation function-2 domain of the vitamin D receptor.
Twenty-epi analogs of 1alpha,25-dihydroxyvitamin D3 (1,25D3) are 100-1000 times more potent transcriptionally than the natural hormone. To determine whether this enhanced activity is mediated through modulation of the dimerization process or through interaction with coactivators, we performed quantitative protein-protein interaction assays with in vitro translated vitamin D receptor (ivtVDR) and fusion proteins containing glutathione-S-transferase (GST) and either the ligand-binding domain ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
VDR RXRA | 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 | - | |
RXRA VDR | 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 | - | |
VDR RXRA | 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 | - | |
RXRA VDR | 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 | - | |
RXRA VDR | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 1054350 | |
VDR RXRA | 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 | 503284 | |
RXRA VDR | 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 | 504651 | |
VDR RXRA | 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 | 504652 | |
VDR RXRA | 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 | 885851 | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 1055996 | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 885850 | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 885729 | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
RXRA VDR | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
VDR RXRA | 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 | - | |
VDR RXRA | 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 | - | |
RXRA VDR | 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 | - | |
RXRA VDR | 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. | High | - | BioGRID | - | |
VDR RXRA | 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 | - | |
RXRA VDR | 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