PRKDC
Gene Ontology Biological Process
- DNA repair [TAS]
- cellular protein modification process [TAS]
- cellular response to insulin stimulus [IMP]
- double-strand break repair [TAS]
- double-strand break repair via homologous recombination [IBA]
- double-strand break repair via nonhomologous end joining [TAS]
- innate immune response [TAS]
- negative regulation of protein phosphorylation [ISS]
- peptidyl-serine phosphorylation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of type I interferon production [TAS]
- regulation of circadian rhythm [ISS]
- signal transduction involved in mitotic G1 DNA damage checkpoint [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CHEK2
Gene Ontology Biological Process
- DNA damage checkpoint [TAS]
- DNA damage induced protein phosphorylation [IMP]
- G2/M transition of mitotic cell cycle [IMP]
- cellular protein catabolic process [IMP]
- cellular response to DNA damage stimulus [IMP, TAS]
- double-strand break repair [IMP]
- intrinsic apoptotic signaling pathway in response to DNA damage [IDA, IMP]
- positive regulation of transcription, DNA-templated [IDA]
- protein autophosphorylation [IDA]
- protein phosphorylation [IDA]
- protein stabilization [IDA]
- regulation of protein catabolic process [IMP]
- regulation of transcription, DNA-templated [IDA]
- replicative senescence [NAS]
- signal transduction in response to DNA damage [IDA]
- signal transduction involved in intra-S DNA damage checkpoint [IMP]
- spindle assembly involved in mitosis [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Biochemical Activity (Phosphorylation)
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.
Publication
Purification and characterization of ATM from human placenta. A manganese-dependent, wortmannin-sensitive serine/threonine protein kinase.
ATM is mutated in the human genetic disorder ataxia telangiectasia, which is characterized by ataxia, immune defects, and cancer predisposition. Cells that lack ATM exhibit delayed up-regulation of p53 in response to ionizing radiation. Serine 15 of p53 is phosphorylated in vivo in response to ionizing radiation, and antibodies to ATM immunoprecipitate a protein kinase activity that, in the presence ... [more]
Throughput
- Low Throughput
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
PRKDC CHEK2 | 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 | 3559811 | |
PRKDC CHEK2 | 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 | 2616465 |
Curated By
- BioGRID