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
HIST2H3C
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
Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin.
Accurate read-out of chromatin modifications is essential for eukaryotic life. Mutations in the gene encoding X-linked ATRX protein cause a mental-retardation syndrome, whereas wild-type ATRX protein targets pericentric and telomeric heterochromatin for deposition of the histone variant H3.3 by means of a largely unknown mechanism. Here we show that the ADD domain of ATRX, in which most syndrome-causing mutations occur, ... [more]
Throughput
- Low Throughput
Additional Notes
- figure 2.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATRX HIST2H3C | 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 | 676563 | |
| ATRX HIST2H3C | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 676676 | |
| ATRX HIST2H3C | Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments. | Low | - | BioGRID | 676562 |
Curated By
- BioGRID