TAF1B
Gene Ontology Biological Process
- RNA polymerase I transcriptional preinitiation complex assembly at the promoter for the nuclear large rRNA transcript [IDA]
- gene expression [TAS]
- termination of RNA polymerase I transcription [TAS]
- transcription elongation from RNA polymerase I promoter [TAS]
- transcription from RNA polymerase I promoter [TAS]
- transcription initiation from RNA polymerase I promoter [TAS]
- transcription, DNA-templated [NAS]
Gene Ontology Molecular Function- RNA polymerase I CORE element sequence-specific DNA binding [IDA]
- RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity [IDA]
- TBP-class protein binding [TAS]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [NAS]
- RNA polymerase I CORE element sequence-specific DNA binding [IDA]
- RNA polymerase I CORE element sequence-specific DNA binding transcription factor recruiting transcription factor activity [IDA]
- TBP-class protein binding [TAS]
- protein binding [IPI]
- sequence-specific DNA binding transcription factor activity [NAS]
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 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
A novel estrogen receptor alpha-associated protein, template-activating factor Ibeta, inhibits acetylation and transactivation.
Estrogen receptor-alpha (ERalpha) functions as a ligand-activated transcription factor that alters expression of estrogen-responsive genes in target cells. Numerous regulatory proteins interact with ERalpha to influence estrogen-mediated transactivation. We have identified a novel coregulatory protein, template-activating factor-Ibeta (TAF-Ibeta), which binds to ERalpha in vitro when the receptor is not complexed with an estrogen response element. The central region of TAF-Ibeta ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID