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
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
The EBNA-3 gene family proteins disrupt the G2/M checkpoint.
The Epstein-Barr nuclear antigens (EBNA), EBNA-3, -4 and -6, have previously been shown to act as transcriptional regulators, however, this study identifies another function for these proteins, disruption of the G2/M checkpoint. Lymphoblastoid cell lines (LCLs) treated with a G2/M initiating drug azelaic bishydroxamine (ABHA) did not show a G2/M checkpoint response, but rather they display an increase in cell ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID