ARNT
Gene Ontology Biological Process
- cellular response to hypoxia [TAS]
- mRNA transcription from RNA polymerase II promoter [IC]
- positive regulation of endothelial cell proliferation [IC]
- positive regulation of erythrocyte differentiation [IC]
- positive regulation of glycolytic process [IC]
- positive regulation of hormone biosynthetic process [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- positive regulation of vascular endothelial growth factor receptor signaling pathway [IC]
- positive regulation vascular endothelial growth factor production [IDA]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- regulation of transcription from RNA polymerase II promoter in response to oxidative stress [IDA]
- response to hypoxia [IDA]
- transcription, DNA-templated [TAS]
Gene Ontology Molecular Function- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [IDA]
- aryl hydrocarbon receptor binding [IPI]
- enhancer binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- sequence-specific DNA binding [IDA]
- sequence-specific DNA binding transcription factor activity [TAS]
- transcription factor binding [IPI]
- RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity [IDA]
- aryl hydrocarbon receptor binding [IPI]
- enhancer binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- sequence-specific DNA binding [IDA]
- sequence-specific DNA binding transcription factor activity [TAS]
- transcription factor binding [IPI]
Gene Ontology Cellular Component
TACC3
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
Coiled-coil coactivators play a structural role mediating interactions in hypoxia-inducible factor heterodimerization.
The hypoxia-inducible factor complex (HIF-α·aryl hydrocarbon receptor nuclear translocator (ARNT)) requires association with several transcription coactivators for a successful cellular response to hypoxic stress. In addition to the conventional global transcription coactivator CREB-binding protein/p300 (CBP/p300) that binds to the HIF-α transactivation domain, a new group of transcription coactivators called the coiled-coil coactivators (CCCs) interact directly with the second PER-ARNT-SIM (PAS) ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ARNT TACC3 | 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 | - | |
| ARNT TACC3 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | Low | - | BioGRID | - | |
| ARNT TACC3 | 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 | 2454997 | |
| ARNT TACC3 | 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 | 2495136 |
Curated By
- BioGRID