THRA
Gene Ontology Biological Process
- gene expression [TAS]
- hormone-mediated signaling pathway [IDA]
- negative regulation of DNA-templated transcription, initiation [IDA]
- negative regulation of RNA polymerase II transcriptional preinitiation complex assembly [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- regulation of transcription from RNA polymerase II promoter [IDA]
- transcription from RNA polymerase II promoter [IDA]
- transcription initiation from RNA polymerase II promoter [TAS]
Gene Ontology Molecular Function- TBP-class protein binding [IDA]
- protein binding [IPI]
- protein domain specific binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- thyroid hormone binding [IDA, IPI]
- thyroid hormone receptor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
- TBP-class protein binding [IDA]
- protein binding [IPI]
- protein domain specific binding [IPI]
- sequence-specific DNA binding transcription factor activity [IDA]
- thyroid hormone binding [IDA, IPI]
- thyroid hormone receptor activity [IDA]
- transcription factor binding [IPI]
- transcription regulatory region DNA binding [IDA]
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
TLS (translocated-in-liposarcoma) is a high-affinity interactor for steroid, thyroid hormone, and retinoid receptors.
Nuclear receptors for steroid hormones, thyroid hormone, retinoids, and vitamin D are thought to mediate their transcriptional effects in concert with coregulator proteins that modulate receptor interactions with components of the basal transcription complex. In an effort to identify potential coregulators, receptor fusions with glutathione-S-transferase were used to isolate proteins in nuclear extracts capable of binding nuclear hormone receptors. Glutathione-S-transferase ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID