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
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
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
Novel DNA binding by a basic helix-loop-helix protein. The role of the dioxin receptor PAS domain.
Central issues surrounding the basic helix-loop-helix (bHLH) superfamily of dimeric transcription factors concern how specificity of partner selection and DNA binding are achieved. bHLH proteins bind DNA through the basic sequence that is contiguous with a helix-loop-helix dimerization domain. For the two subgroups within the family, dimerization is further regulated by an adjacent Per-Arnt-Sim homology (PAS) or leucine zipper (LZ) ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ARNT ARNT | 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 | 2446551 | |
| ARNT ARNT | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | - | |
| ARNT ARNT | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | High | - | BioGRID | 2640564 |
Curated By
- BioGRID