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Description

E3 ubiquitin-protein ligase RNF31 (UniProt: Q96EP0, also known as EC: 2.3.2.27, HOIL-1-interacting protein, HOIP, RING finger protein 31, RING-type E3 ubiquitin transferase RNF31, Zinc in-between-RING-finger ubiquitin-associated domain protein) is encoded by the RNF31 (also known as ZIBRA) gene (Gene ID: 55072) in human. E3 ubiquitin-protein ligase RNF31 is a cytoplasmic protein that is a component of the linear ubiquitin chain assembly complex (LUBAC complex), which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG (NEMO) and receptor interacting serine/threonine Kinase 1 (RIPK1) and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. LUBAC-mediated polyubiquitination interferes with TNF-induced cell death and thereby prevents inflammation. Together with OUTLIN deubiquitinase, the LUBAC complex is also reported to regulate the canonical Wnt signaling pathway during angiogenesis. E3 ubiquitin-protein ligase RNF31 is expressed in both normal and transformed breast epithelial cell lines. It contains a polyubiquitin-binding (PUB) domain (aa 71-142) that mediates interaction with the PCNA-interacting motifs of C-terminus of the AAA+ ATPase p97 (VCP) and RNF31, with a strong preference for RNF3. It also has a ubiquitin-associated (UBA) domain (aa 564-615) that mediates association with RanBP-type and C3HC4-type zinc finger-containing protein 1 (RBCK1/HOIL1) via interaction with its ubiquitin-like (UBL) domain. (Ref.: Elliot, PR et al (2014). Mol. Cell 54(3), 335-48).