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Updated: Jun 6, 2026

Functional Characterization of RING-Type E3 Ubiquitin Ligases In Vitro and In Planta
Published on: December 5, 2019
RNF13: an emerging RING finger ubiquitin ligase important in cell proliferation
Xianglan Jin1, He Cheng, Jie Chen
1National Laboratory of Medical Molecular Biology, Tsinghua University, Beijing, China.
Abstract:
Protein ubiquitination mediated by ubiquitin ligases plays a very important role in a wide spectrum of biological processes including development and disease pathogenesis. RING finger protein 13 (RNF13) is a recently identified ubiquitin ligase which contains an N-terminal protease-associated domain and a C-terminal RING finger domain separated by a transmembrane region. RNF13 is an evolutionarily conserved protein. Most interestingly, RNF13 expression is developmentally regulated during myogenesis and is upregulated in various human tumors. These data suggest that RNF13, acting as an ubiquitin ligase, might have profound biological functions during development and disease. This minireview summarizes recent work on RNF13 functions related to cell proliferation, differentiation and cancer development.
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