RNF168
Gene Ontology Biological Process
- cellular response to DNA damage stimulus [IDA]
- double-strand break repair [IDA]
- histone H2A K63-linked ubiquitination [IDA, IMP]
- histone H2A monoubiquitination [IDA]
- histone H2A-K13 ubiquitination [IDA]
- histone H2A-K15 ubiquitination [IDA]
- interstrand cross-link repair [TAS]
- isotype switching [ISS]
- negative regulation of transcription elongation from RNA polymerase II promoter [IMP]
- positive regulation of DNA repair [IDA]
- protein K63-linked ubiquitination [IDA]
- protein ubiquitination [IDA]
- response to ionizing radiation [IDA]
- ubiquitin-dependent protein catabolic process [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TRIP12
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
TRIP12 and UBR5 suppress spreading of chromatin ubiquitylation at damaged chromosomes.
Histone ubiquitylation is a prominent response to DNA double-strand breaks (DSBs), but how these modifications are confined to DNA lesions is not understood. Here, we show that TRIP12 and UBR5, two HECT domain ubiquitin E3 ligases, control accumulation of RNF168, a rate-limiting component of a pathway that ubiquitylates histones after DNA breakage. We find that RNF168 can be saturated by ... [more]
Throughput
- Low Throughput
Additional Notes
- figure S5.
Curated By
- BioGRID