OTUD7B Protein, Human (sf9)

OTUD7B protein acts as a negative regulator of the non-canonical NF-kappa-B pathway by facilitating the deubiquitination of TRAF3, a suppressor of NF-kappa-B signaling, thereby dampening B-cell responses. In the context of non-canonical NF-kappa-B stimuli, OTUD7B targets 'Lys-48'-linked polyubiquitin chains on TRAF3, preventing its proteolysis and averting excessive activation of the non-canonical NF-kappa-B pathway. This negative regulatory role extends to mucosal immunity against infections. Additionally, OTUD7B modulates T cell receptor (TCR) signaling by deubiquitinating ZAP70, influencing NF-kappa-B activation in T cells. Furthermore, OTUD7B contributes to T cell homeostasis, playing a crucial role in normal T cell responses and the production of key cytokines such as IFNG and IL2. The protein also exhibits deubiquitinating activity towards EGFR and demonstrates versatility in hydrolyzing various polyubiquitin chain linkages, including 'Lys-11', 'Lys-48', and 'Lys-63'-linked polyubiquitin chains. While it exhibits a higher catalytic rate with 'Lys-11'-linked chains in vitro, the physiological significance of this preference remains uncertain.