EGLN1
Gene Ontology Biological Process
- cellular response to hypoxia [TAS]
- negative regulation of cAMP catabolic process [ISS]
- negative regulation of cyclic-nucleotide phosphodiesterase activity [ISS]
- negative regulation of sequence-specific DNA binding transcription factor activity [IDA]
- oxygen homeostasis [IDA]
- peptidyl-proline hydroxylation to 4-hydroxy-L-proline [IDA]
- regulation of angiogenesis [ISS]
- regulation of transcription from RNA polymerase II promoter in response to hypoxia [TAS]
- response to hypoxia [IDA]
- response to nitric oxide [IDA]
Gene Ontology Molecular Function- enzyme binding [ISS]
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [IDA]
- peptidyl-proline 4-dioxygenase activity [IDA]
- peptidyl-proline dioxygenase activity [TAS]
- protein binding [IPI]
- enzyme binding [ISS]
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors [IDA]
- peptidyl-proline 4-dioxygenase activity [IDA]
- peptidyl-proline dioxygenase activity [TAS]
- protein binding [IPI]
HIST1H3A
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Binding of the CHD4 PHD2 finger to histone H3 is modulated by covalent modifications.
CHD4 (chromodomain helicase DNA-binding protein 4) ATPase is a major subunit of the repressive NuRD (nucleosome remodelling and deacetylase) complex, which is involved in transcriptional regulation and development. CHD4 contains two PHD (plant homeodomain) fingers of unknown function. Here we show that the second PHD finger (PHD2) of CHD4 recognizes the N-terminus of histone H3 and that this interaction is ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| EGLN1 HIST1H3A | 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 | 468190 |
Curated By
- BioGRID