BAIT
RNF168
hRNF168
ring finger protein 168, E3 ubiquitin protein ligase
GO Process (14)
GO Function (7)
GO Component (5)
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
Homo sapiens
PREY
HNRNPM
CEAR, HNRNPM4, HNRPM, HNRPM4, HTGR1, NAGR1, hnRNP M
heterogeneous nuclear ribonucleoprotein M
GO Process (4)
GO Function (4)
GO Component (9)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Affinity Capture-MS
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 is identified by mass spectrometric methods.
Publication
RNF168 and USP10 regulate topoisomerase IIα function via opposing effects on its ubiquitylation.
Topoisomerase IIα (TOP2α) is essential for chromosomal condensation and segregation, as well as genomic integrity. Here we report that RNF168, an E3 ligase mutated in the human RIDDLE syndrome, interacts with TOP2α and mediates its ubiquitylation. RNF168 deficiency impairs decatenation activity of TOP2α and promotes mitotic abnormalities and defective chromosomal segregation. Our data also indicate that RNF168 deficiency, including in ... [more]
Nat Commun Aug. 25, 2016; 7();12638 [Pubmed: 27558965]
Throughput
- Low Throughput
Curated By
- BioGRID