Component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked polyubiquitin, leaving the last ubiquitin chain attached to its substrates ( , ). May act as a central scaffold protein that assembles the various components of the BRISC complex and retains them in the cytoplasm . Plays a role in regulating the onset of apoptosis via its role in modulating 'Lys-63'-linked ubiquitination of target proteins (By similarity). 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 activities by enhancing its stability and cell surface expression (, ). Down-regulates the response to bacterial lipopolysaccharide (LPS) via its role in IFNAR1 deubiquitination . Required for normal induction of p53/TP53 in response to DNA damage . Independent of the BRISC complex, promotes interaction between USP7 and p53/TP53, and thereby promotes deubiquitination of p53/TP53, preventing its degradation and resulting in increased p53/TP53-mediated transcription regulation and p53/TP53-dependent apoptosis in response to DNA damage .
Subcellular locations: Cytoplasm, Nucleus, Cytoplasm, Cytoskeleton, Spindle pole, Cytoplasm, Cytoskeleton
A minor proportion is detected in the nucleus (, ). Translocates into the nucleus in response to DNA damage . Directly binds to microtubules and is detected at the minus end of K-fibers . Co-localizes with NUMA1 at mitotic spindle poles .
Detected in heart muscle (at protein level). Detected in heart and muscle, and at much lower levels in brain .