DNA helicase which plays a role in chromatin-remodeling following DNA damage (PubMed:19661379, PubMed:29220653). Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair (PubMed:19661379). Able to catalyze nucleosome sliding in an ATP-dependent manner (PubMed:19661379). Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding (PubMed:19661379, PubMed:29220653). ATP + H2O = ADP + H(+) + phosphate Interacts (via macro domain) with PARP1; interacts only when PARP1 is poly-ADP-ribosylated (PARylated) (PubMed:19661379, PubMed:29220653). Interacts with CIAO1 (PubMed:23891004). Localizes at sites of DNA damage. Probably recruited to DNA damage sites by PARylated PARP1. Frequently overexpressed in hepatomacellular carcinomas. The macro domain mediates non-covalent poly(ADP-ribose)-binding and recruitment to DNA damage sites (PubMed:19661379, PubMed:29220653). Mediates auto-inhibition of ATPase activity by interacting with the N-terminal ATPase module, encompassing the helicase ATP-binding domain and helicase C-terminal domain (PubMed:29220653). PARP1 activation upon DNA damage and poly(ADP-ribose)-binding release the auto-inhibition by the macro domain and trigger ATPase activity (PubMed:29220653). Does not bind monomeric ADP-ribose and mono-ADP-ribose fails to release the auto-inhibition of the ATPase module by the macro domain (PubMed:29220653). Belongs to the SNF2/RAD54 helicase family.