BAG6 is a member of the BAG protein family, which is implicated in diverse cellular processes including apoptosis, co-chaperone and DNA damage response. Recently, it has been shown that BAG6 forms a stable complex with UBL4A and GET4 and functions in membrane protein targeting and protein quality control. The BAG6 sequence contains a canonical nuclear localization signal (NLS) and is localized predominantly in the nucleus. However, GET4 and UBL4A are found mainly in cytoplasm. Whether GET4 and UBL4A are also involved in DNA damage response (DDR) in the context of the BAG6 complex remains unknown. Here, we provide evidence that the nuclear BAG6-UBL4A-GET4 complex mediates DDR signaling and damage-induced cell death. BAG6 appears to be the central component for the process, as depletion of BAG6 leads to the loss of both UBL4A and GET4 proteins and resistance to cell killing by DNA damage reagents. In addition, nuclear localization of BAG6 and phosphorylation of BAG6 by checkpoint kinase ATM are all required for cell killing and BAG6 appears to regulate UBL4A and GET4 to translocate to the nucleus upon DNA damage. GET4 and UBL4A play redundant roles in cell killing, as depletion of either one has no effect but co-depletion leads resistance. All 3 components of the BAG6 complex are required for optimal DDR signaling, as BAG6, and to a lesser extent, GET4 and UBL4A, regulate the recruitment of BRCA1 complex to sites of DNA damage. Together our results suggest that the nuclear BUG complex is an effector in DNA damage response pathway and its phosphorylation and nuclear localization are important determinants for its function.