抗人 RNF123 抗体对
01AB00915
Ring finger protein 123 (RNF123) is an E3 ubiquitin-protein ligase encoded by the RNF123 gene and characterized by a RING finger motif, which facilitates protein-protein and protein-DNA interactions. RNF123 is primarily localized in the cytoplasm, cytosol, and nucleus, and plays a crucial role in protein degradation, including targeting chromatin-associated proteins such as HP1 for ubiquitination. Beyond its E3 ligase activity, RNF123 also acts as a negative regulator of innate antiviral signaling by inhibiting the production of type I interferons through direct interaction with RIG-I and MDA5, independent of its ubiquitin ligase function. This regulatory function involves its SPRY and coiled-coil domains, which compete with downstream adaptors in antiviral pathways. Clinically, increased expression of RNF123 has been linked to laminopathies and is associated with congenital muscular dystrophy, highlighting its relevance in both cellular regulation and disease.
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技术参数
- 靶点基因名
- RNF123
- 基因别名
- KPC1
- 蛋白别名
- ring finger protein 123; RNF123
- UniProt
- Q5XPI4
- 物种
- Human
产品详情
- 靶点名称
- RNF123
- 蛋白名称
- ring finger protein 123
- 蛋白别名
- E3 ubiquitin-protein ligase RNF123; Kip1 ubiquitination-promoting complex protein 1; RING finger protein 123
- 靶点基因名
- RNF123
- 基因别名
- KPC1
- UniProt
- Q5XPI4
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Ring finger protein 123 (RNF123) is an E3 ubiquitin-protein ligase encoded by the RNF123 gene and characterized by a RING finger motif, which facilitates protein-protein and protein-DNA interactions. RNF123 is primarily localized in the cytoplasm, cytosol, and nucleus, and plays a crucial role in protein degradation, including targeting chromatin-associated proteins such as HP1 for ubiquitination. Beyond its E3 ligase activity, RNF123 also acts as a negative regulator of innate antiviral signaling by inhibiting the production of type I interferons through direct interaction with RIG-I and MDA5, independent of its ubiquitin ligase function. This regulatory function involves its SPRY and coiled-coil domains, which compete with downstream adaptors in antiviral pathways. Clinically, increased expression of RNF123 has been linked to laminopathies and is associated with congenital muscular dystrophy, highlighting its relevance in both cellular regulation and disease.