FIRRM

Forms a complex with FIGL1, which regulates DNA double-strand break (DSB) repair via homologous recombination (HR). The FIGNL1-FIRRM complex is essential for resolution of homologous recombination intermediates in response to DNA interstrand cross-links (ICLs). The complex regulates HR by promoting disassembly of RAD51 filaments from DNA and chromatin, thereby preventing DNA damage-independent RAD51 loading and persistent DNA accumulation of RAD51 recombinases. It also regulates HR during meiosis by promoting dissociation of DMC1 filaments from DNA (By similarity). Within the complex, provides the ATPase activity to disassemble DMC1 and RAD51 filaments, while FIRRM directly binds single-stranded DNA to facilitate this unloading. Independently of FIRRM, slso acts as a regulator of PLK1 kinase activity at kinetochores that promotes faithful chromosome segregation in prometaphase by bridging kinase and phosphatase activities. Phosphorylation of FIRRM by PLK1 negatively regulates its interaction with the phosphatase, PPP1CC, thus creating a negative feedback loop for maintaining proper PLK1 kinase activity during mitosis..

Function from UniProtKB (Q9NSG2), read 2026-09-23. CC BY 4.0.