53BP1 (Phospho-Ser6) Colorimetric Cell-Based ELISA Kit

Double-strand break (DSB) repair protein involved in response to DNA damage, telomere dynamics and class-switch recombination (CSR) during antibody genesis (PubMed:12364621, PubMed:22553214, PubMed:23333306, PubMed:17190600, PubMed:21144835, PubMed:28241136) . Plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage by promoting non-homologous end joining (NHEJ) -mediated repair of DSBs and specifically counteracting the function of the homologous recombination (HR) repair protein BRCA1 (PubMed:22553214, PubMed:23727112, PubMed:23333306) . In response to DSBs, phosphorylation by ATM promotes interaction with RIF1 and dissociation from NUDT16L1/TIRR, leading to recruitment to DSBs sites (PubMed:28241136) . Recruited to DSBs sites by recognizing and binding histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:23760478, PubMed:28241136, PubMed:17190600) . Required for immunoglobulin class-switch recombination (CSR) during antibody genesis, a process that involves the generation of DNA DSBs (PubMed:23345425) . Participates to the repair and the orientation of the broken DNA ends during CSR (By similarity) . In contrast, it is not required for classic NHEJ and V (D) J recombination (By similarity) . Promotes NHEJ of dysfunctional telomeres via interaction with PAXIP1 (PubMed:23727112) .

Nucleus. Chromosome. Chromosome, centromere, kinetochore. Localizes to the nucleus in absence of DNA damage (PubMed:28241136) . Following DNA damage, recruited to sites of DNA damage, such as double stand breaks (DSBs) : recognizes and binds histone H2A monoubiquitinated at 'Lys-15' (H2AK15Ub) and histone H4 dimethylated at 'Lys-20' (H4K20me2), two histone marks that are present at DSBs sites (PubMed:23333306, PubMed:23760478, PubMed:24703952, PubMed:28241136, PubMed:17190600) . Associated with kinetochores during mitosis (By similarity) .