E3 ubiquitin-protein ligase RNF216 is an enzyme that in humans is encoded by the RNF216gene.
This gene encodes a cytoplasmic protein which specifically colocalizes and interacts with the serine/threonine protein kinase, receptor-interacting protein (RIP). Zinc finger domains of the encoded protein are required for its interaction with RIP and for inhibition of TNF- and IL1-induced NF-kappa B activation pathways. The encoded protein may also function as an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes and transfers it to substrates. Several alternatively spliced transcript variants have been described for this locus but the full-length natures of only some are known.
^Chen, Danying; Li Xiaoyan, Zhai Zhonghe, Shu Hong-Bing (May 2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation". J. Biol. Chem. (United States) 277 (18): 15985–91. doi:10.1074/jbc.M108675200. ISSN0021-9258. PMID11854271.Cite uses deprecated parameters (help)
Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID8076819.
Chen D, Li X, Zhai Z, Shu HB (2002). "A novel zinc finger protein interacts with receptor-interacting protein (RIP) and inhibits tumor necrosis factor (TNF)- and IL1-induced NF-kappa B activation". J. Biol. Chem.277 (18): 15985–91. doi:10.1074/jbc.M108675200. PMID11854271.
Fearns C, Pan Q, Mathison JC, Chuang TH (2006). "Triad3A regulates ubiquitination and proteasomal degradation of RIP1 following disruption of Hsp90 binding". J. Biol. Chem.281 (45): 34592–600. doi:10.1074/jbc.M604019200. PMID16968706.