PIDD1
Gene Ontology Biological Process
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [IMP]
- cellular response to DNA damage stimulus [IDA]
- negative regulation of apoptotic process [IMP]
- positive regulation of NF-kappaB transcription factor activity [TAS]
- positive regulation of apoptotic process [TAS]
- signal transduction [TAS]
Gene Ontology Molecular Function
ATM
Gene Ontology Biological Process
- DNA damage induced protein phosphorylation [IDA]
- DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [TAS]
- DNA repair [TAS]
- cell cycle arrest [IMP]
- cellular response to DNA damage stimulus [IMP]
- cellular response to gamma radiation [IDA]
- double-strand break repair [TAS]
- double-strand break repair via homologous recombination [TAS]
- histone mRNA catabolic process [IDA]
- mitotic spindle assembly checkpoint [IMP]
- negative regulation of B cell proliferation [IMP]
- peptidyl-serine phosphorylation [IDA]
- phosphatidylinositol-3-phosphate biosynthetic process [IMP]
- positive regulation of DNA damage response, signal transduction by p53 class mediator [IMP]
- positive regulation of apoptotic process [IMP]
- pre-B cell allelic exclusion [ISS]
- protein autophosphorylation [IDA]
- protein phosphorylation [IDA]
- reciprocal meiotic recombination [TAS]
- replicative senescence [IMP]
- response to ionizing radiation [IDA]
- signal transduction [TAS]
- signal transduction involved in mitotic G2 DNA damage checkpoint [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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.
Publication
PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling.
Biochemical evidence implicates the death-domain (DD) protein PIDD as a molecular switch capable of signaling cell survival or death in response to genotoxic stress. PIDD activity is determined by binding-partner selection at its DD: whereas recruitment of RIP1 triggers prosurvival NF-?B signaling, recruitment of RAIDD activates proapoptotic caspase-2 via PIDDosome formation. However, it remains unclear how interactor selection, and thus ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATM PIDD1 | 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 | - | |
| ATM PIDD1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 3461655 |
Curated By
- BioGRID