Background：

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 acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex， thereby being required for the complex integrity and modulating the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer. Component of the BRISC complex， a multiprotein complex that specifically cleaves ’Lys-63’-linked ubiquitin in various substrates. Within the BRISC complex， acts as an adapter that bridges the interaction between BABAM1/NBA1 and the rest of the complex， thereby being required for the complex integrity. The BRISC complex is required for normal mitotic spindle