RARA
Gene Ontology Biological Process
- apoptotic cell clearance [IMP]
- cellular response to estrogen stimulus [IDA]
- cellular response to retinoic acid [IDA]
- gene expression [TAS]
- intracellular estrogen receptor signaling pathway [IDA]
- negative regulation of granulocyte differentiation [IDA]
- negative regulation of interferon-gamma production [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of tumor necrosis factor production [IDA]
- positive regulation of T-helper 2 cell differentiation [IDA]
- positive regulation of binding [IMP]
- positive regulation of cell cycle [IMP]
- positive regulation of cell proliferation [IMP]
- positive regulation of interleukin-13 production [IDA]
- positive regulation of interleukin-4 production [IDA]
- positive regulation of interleukin-5 production [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA, IMP]
- positive regulation of transcription, DNA-templated [IDA, IMP]
- protein phosphorylation [IMP]
- response to estradiol [IDA]
- response to retinoic acid [IMP]
- retinoic acid receptor signaling pathway [IMP]
- signal transduction [IDA]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- chromatin DNA binding [IDA]
- enzyme binding [IPI]
- protein binding [IPI]
- protein domain specific binding [IPI]
- protein heterodimerization activity [IDA]
- protein kinase A binding [IDA]
- protein kinase B binding [IPI]
- receptor binding [IDA]
- retinoic acid binding [IDA]
- retinoic acid receptor activity [IDA]
- retinoic acid-responsive element binding [IDA]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription coactivator activity [IDA, IMP]
- transcription corepressor activity [IDA]
- transcription factor binding [IPI]
- chromatin DNA binding [IDA]
- enzyme binding [IPI]
- protein binding [IPI]
- protein domain specific binding [IPI]
- protein heterodimerization activity [IDA]
- protein kinase A binding [IDA]
- protein kinase B binding [IPI]
- receptor binding [IDA]
- retinoic acid binding [IDA]
- retinoic acid receptor activity [IDA]
- retinoic acid-responsive element binding [IDA]
- sequence-specific DNA binding transcription factor activity [IDA]
- transcription coactivator activity [IDA, IMP]
- transcription corepressor activity [IDA]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
LRIF1
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
RIF-1, a novel nuclear receptor corepressor that associates with the nuclear matrix.
The retinoic acid receptors (RARs) are ligand-dependent transcription factors that play critical roles in cell differentiation, embryonic development, and tumor suppression. RAR transcriptional activities are mediated by a growing family of nuclear receptor (NR) coregulators. Here we report the cloning and characterization of a novel protein RIF1 (receptor interacting factor) that interacts with RARalpha in vivo and in vitro. RIF1 ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RARA LRIF1 | Far Western Far Western An interaction is detected between a protein immobilized on a membrane and a purified protein probe. | Low | - | BioGRID | - | |
| LRIF1 RARA | 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