3'-5' DNA helicase and substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response to stalled/damaged replication forks (PubMed:11956208, PubMed:23393192). Involved in genome maintenance by acting as an anti-recombinogenic helicase and preventing extensive strand exchange during homologous recombination: promotes RAD51 filament dissolution from stalled forks, thereby inhibiting homologous recombination and preventing excessive recombination (PubMed:17724085, PubMed:19736316). Also promotes cell death and DNA double-strand breakage in response to replication stress: together with MUS81, promotes the endonucleolytic DNA cleavage following prolonged replication stress via its helicase activity, possibly to eliminate cells with excessive replication stress (PubMed:23319600, PubMed:23361013). Plays a major role in remodeling of stalled DNA forks by catalyzing fork regression, in which the fork reverses and the two nascent DNA strands anneal (PubMed:25772361). In addition to the helicase activity, also acts as the substrate-recognition component of the SCF(FBH1) E3 ubiquitin ligase complex, a complex that mediates ubiquitination of RAD51, leading to regulate RAD51 subcellular location (PubMed:25585578). ATP + H2O = ADP + H(+) + phosphate Protein modification; protein ubiquitination. Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complex SCF(FBH1) composed of CUL1, SKP1, RBX1 and FBH1 (PubMed:11956208, PubMed:19736316, PubMed:23319600). Interacts with RAD51 (PubMed:23393192). Interacts with RPA2 (PubMed:23319600). Interacts (via PIP-box and RanBP2-type zinc finger) with PCNA (PubMed:23677613). Accumulates at sites of DNA damage or replication stress (PubMed:19736316, PubMed:23677613). PCNA is required for localization to DNA damage sites (PubMed:23677613). Localizes to the nucleoplasm in absence of DNA damage (PubMed:23677613). The PIP-box mediates the interaction with PCNA. Ubiquitinated (PubMed:23393192, PubMed:23677613). Ubiquitination by the DCX(DTL) complex, also named CRL4(CDT2), leading to its degradation: ubiquitination takes place after its localization to DNA damage sites, possibly to facilitate the translesion synthesis (TLS) pathway (PubMed:23677613). Defects in FBH1 are frequently observed in melanomas, resulting in increased survival in response to replicative stress. Its inactivation may play a role in oncogenic transformation. Belongs to the helicase family. UvrD subfamily. Truncated N-terminus. Truncated N-terminus. Truncated N-terminus.