ATRX
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- DNA damage response, signal transduction by p53 class mediator [ISS]
- DNA duplex unwinding [TAS]
- DNA methylation [TAS]
- DNA recombination [TAS]
- DNA replication-independent nucleosome assembly [IMP]
- cellular response to hydroxyurea [ISS]
- chromatin remodeling [IDA]
- negative regulation of telomeric RNA transcription from RNA pol II promoter [ISS]
- nucleosome assembly [IDA]
- positive regulation of nuclear cell cycle DNA replication [ISS]
- positive regulation of telomere maintenance [ISS]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- regulation of transcription, DNA-templated [TAS]
- replication fork processing [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
The ATRX-ADD domain binds to H3 tail peptides and reads the combined methylation state of K4 and K9.
Mutations in the ATRX protein are associated with the alpha-thalassemia and mental retardation X-linked syndrome (ATR-X). Almost half of the disease-causing mutations occur in its ATRX-Dnmt3-Dnmt3L (ADD) domain. By employing peptide arrays, chromatin pull-down and peptide binding assays, we show specific binding of the ADD domain to H3 histone tail peptides containing H3K9me3. Peptide binding was disrupted by the presence ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HIST1H3A ATRX | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | 4.68 | BioGRID | 2990308 | |
| HIST1H3A ATRX | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | - |
Curated By
- BioGRID