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
TOP2A
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- DNA ligation [IDA]
- DNA topological change [IDA]
- DNA unwinding involved in DNA replication [IBA]
- apoptotic chromosome condensation [IDA]
- cellular response to DNA damage stimulus [IDA]
- chromosome segregation [IMP]
- mitotic DNA integrity checkpoint [IBA]
- mitotic cell cycle [TAS]
- mitotic recombination [IBA]
- positive regulation of apoptotic process [IDA]
- positive regulation of single stranded viral RNA replication via double stranded DNA intermediate [IMP]
- positive regulation of viral genome replication [IMP]
- resolution of meiotic recombination intermediates [IBA]
- sister chromatid segregation [IBA]
Gene Ontology Molecular Function- DNA binding [IDA]
- DNA binding, bending [IDA]
- DNA topoisomerase type II (ATP-hydrolyzing) activity [IDA]
- DNA-dependent ATPase activity [IDA]
- chromatin binding [IDA]
- drug binding [IDA]
- enzyme binding [IPI]
- histone deacetylase binding [IPI]
- magnesium ion binding [IDA]
- poly(A) RNA binding [IDA]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [IPI]
- protein kinase C binding [IPI]
- ubiquitin binding [IMP]
- DNA binding [IDA]
- DNA binding, bending [IDA]
- DNA topoisomerase type II (ATP-hydrolyzing) activity [IDA]
- DNA-dependent ATPase activity [IDA]
- chromatin binding [IDA]
- drug binding [IDA]
- enzyme binding [IPI]
- histone deacetylase binding [IPI]
- magnesium ion binding [IDA]
- poly(A) RNA binding [IDA]
- protein C-terminus binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IPI]
- protein homodimerization activity [IPI]
- protein kinase C binding [IPI]
- ubiquitin binding [IMP]
Gene Ontology Cellular Component
Co-purification
An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.
Publication
Ataxia telangiectasia mutated-dependent regulation of topoisomerase II alpha expression and sensitivity to topoisomerase II inhibitor.
Topoisomerase II alpha (TOP2A) has a crucial role in proper chromosome condensation and segregation. Here we report the interaction of TOP2A with ataxia telangiectasia mutated (ATM) and its phosphorylation in an ATM-dependent manner after DNA damage. In vitro kinase assay and site-directed mutagenesis studies revealed that serine 1512 is the target of phosphorylation through ATM. Serine 1512 to Alanine mutation ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATM TOP2A | 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 | - | |
| TOP2A ATM | 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 TOP2A | 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 | 3675886 | |
| ATM TOP2A | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | Low | - | BioGRID | - |
Curated By
- BioGRID