Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. In these 2 complexes, it is probably required to maintain the stability of BABAM2 and help the 'Lys-63'-linked deubiquitinase activity mediated by brcc3/brcc36 component. The BRISC complex is required for normal mitotic spindle assembly and microtubule attachment to kinetochores via its role in deubiquitinating numa1. Plays a role in interferon signaling via its role in the deubiquitination of the interferon receptor ifnar1; deubiquitination increases ifnar1 activity by enhancing its stability and cell surface expression. Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in ifnar1 deubiquitination. Component of the ARISC complex, at least composed of uimc1/rap80, abraxas1, brcc3/brcc36, BABAM2 and babam1/nba1. Component of the BRCA1-A complex, at least composed of brca1, bard1, uimc1/rap80, abraxas1, brcc3/brcc36, BABAM2 and babam1/nba1. In the BRCA1-A complex, interacts directly with abraxas1 and BABAM2. Component of the BRISC complex, at least composed of abraxas2, brcc3/brcc36, babam2 and babam1/nba1. Localizes at sites of DNA damage at double-strand breaks (DSBs). The VWFA-like region is similar to the VWFA domain. Its presence reveals similarities between the structure of the 19S proteasome and the BRCA1-A complexes. Belongs to the BABAM1 family.