E3 ubiquitin-protein ligase RNF114 (RNF114)

E3 ubiquitin-protein ligase RNF114 is a RING finger-type E3 ligase that catalyzes ubiquitin transfer to target proteins, promoting their degradation or functional modification[1][3][7]. It is characterized by a C3HC4-type RING-HC domain, a C2HC-, and two C2H2-type zinc fingers, and it contains a ubiquitin-interacting motif[1][4]. RNF114 plays essential roles in cellular processes such as cell cycle progression, apoptosis, and immune system regulation, notably by modulating NF-κB transcription, T-cell activation, and antiviral responses controlled by MAVS[2][3][6][7]. It is also implicated in developmental transitions, such as maternal-to-zygotic transition, where its activity ensures correct degradation of regulators like TAB1[4]. Malfunction or dysregulation of RNF114 has been associated with autoimmune diseases (e.g., psoriasis), cancer, inflammation, and viral infections[5][6].

Other names

RING finger protein 114ZNF228ZNF313PSORS12RING-type E3 ubiquitin transferase RNF114Zinc finger protein 228Zinc finger protein 313

Promotion of ubiquitination and proteasomal degradation of substrate proteins; Regulation of NF-κB pathway via substrate modification (e.g., A20, TAB1, MAVS); Modulation of immune response and interferon signaling by ubiquitin-dependent targeting of signaling intermediates