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Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Additionally we are shipping RNF169 Proteins (3) and many more products for this protein.
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The authors establish that RNF169 binds to ubiquitylated histone H2A-Lys13/Lys15 in a manner that involves its canonical ubiquitin-binding helix and a pair of arginine-rich motifs that interact with the nucleosome acidic patch.
Ubiquitin ligases RNF168 (show RNF168 Antibodies), RNF169, and RAD18 (show RAD18 Antibodies) specifically bind histone H2A Lys13/15-ubiquitylated nucleosomes. 53BP1 (show TP53BP1 Antibodies) chromatin recruitment may be activated by RNF168 (show RNF168 Antibodies) and blocked by RNF169 and RAD18 (show RAD18 Antibodies).
RNF169 as a component in DNA damage signal transduction and adds to the complexity of regulatory ubiquitylation in genome stability maintenance.
RNF168, its paralog RNF169, RAD18, and the BRCA1-interacting RAP80 protein accumulate at DNA double strand break sites through the use of bipartite modules composed of ubiquitin binding domains.
results show that RNF169 functions in a noncanonical fashion to harness RNF168 (show RNF168 Antibodies)-mediated protein recruitment to DSB-containing chromatin, thereby contributing to regulation of DSB repair pathway utilization.
Probable E3 ubiquitin-protein ligase that acts as a negative regulator of double-strand breaks (DSBs) repair following DNA damage. Recruited to DSB repair sites by recognizing and binding ubiquitin catalyzed by RNF168 and competes with TP53BP1 and BRCA1 for association with RNF168-modified chromatin, thereby acting as a negative regulator of DSBs repair. E3 ubiquitin- protein ligase activity is not required for regulation of DSBs repair (By similarity).
E3 ubiquitin-protein ligase RNF169