人 RNF115 抗体对
01AB00586
Ring Finger Protein 115 (RNF115), also known as BCA2 or ZNF364, is an E3 ubiquitin ligase that plays critical roles in various cellular processes, including innate immunity and cellular trafficking. RNF115 is involved in regulating phagosomal maturation and immune responses by ubiquitinating specific proteins. For instance, it inhibits the post-endoplasmic reticulum (ER) trafficking of Toll-like receptors (TLRs) by catalyzing K11-linked ubiquitination of RAB1A and RAB13, which are essential for TLR-mediated immune responses. Additionally, RNF115 regulates phagosomal maturation by ubiquitinating vesicle trafficking proteins, impacting innate immune functions during bacterial infections. Its dysregulation has been implicated in diseases such as breast cancer, where it promotes cell proliferation by targeting p21Waf1/Cip1 for ubiquitin-mediated degradation.
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技术参数
- 靶点基因名
- RNF115
- 基因别名
- ZNF364
- 蛋白别名
- ring finger protein 115; RNF115
- UniProt
- Q9Y4L5
- 物种
- Human
产品详情
- 靶点名称
- RNF115
- 蛋白名称
- ring finger protein 115
- 蛋白别名
- E3 ubiquitin-protein ligase RNF115; RING finger protein 115; RING-type E3 ubiquitin transferase RNF115; Rab7-interacting RING finger protein; Rabring 7; Zinc finger protein 364
- 靶点基因名
- RNF115
- 基因别名
- ZNF364
- UniProt
- Q9Y4L5
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Ring Finger Protein 115 (RNF115), also known as BCA2 or ZNF364, is an E3 ubiquitin ligase that plays critical roles in various cellular processes, including innate immunity and cellular trafficking. RNF115 is involved in regulating phagosomal maturation and immune responses by ubiquitinating specific proteins. For instance, it inhibits the post-endoplasmic reticulum (ER) trafficking of Toll-like receptors (TLRs) by catalyzing K11-linked ubiquitination of RAB1A and RAB13, which are essential for TLR-mediated immune responses. Additionally, RNF115 regulates phagosomal maturation by ubiquitinating vesicle trafficking proteins, impacting innate immune functions during bacterial infections. Its dysregulation has been implicated in diseases such as breast cancer, where it promotes cell proliferation by targeting p21Waf1/Cip1 for ubiquitin-mediated degradation.