抗人 TRIM7 抗体对
01AB01391
Tripartite motif containing 7 (TRIM7) is an E3 ubiquitin ligase belonging to the TRIM protein family, characterized by a conserved RBCC motif comprising a RING finger, B-box domains, and a coiled-coil region, along with a variable C-terminal B30.2 domain that determines substrate specificity. TRIM7 localizes to both the nucleus and cytoplasm and mediates ubiquitination-dependent degradation of diverse protein substrates, thereby regulating multiple biological processes such as protein turnover, immune responses, and cellular signaling. Structurally, the crystal structure of its B30.2 domain has provided insights into its interaction with glycogenin-1, linking TRIM7 to glycogen biosynthesis. Functionally, TRIM7 plays paradoxical roles in infection by either promoting host defense or facilitating viral pathogenesis, and in cancer, it can act as both a tumor suppressor and promoter by influencing metastasis, apoptosis, and tumor immunity. Clinically, TRIM7 has been implicated as a potential biomarker and therapeutic target in diseases such as idiopathic pulmonary fibrosis and atherosclerosis.
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技术参数
- 靶点基因名
- TRIM7
- 基因别名
- GNIP; RNF90
- 蛋白别名
- tripartite motif containing 7; TRIM7
- UniProt
- Q9C029
- 物种
- Human
产品详情
- 靶点名称
- TRIM7
- 蛋白名称
- tripartite motif containing 7
- 蛋白别名
- E3 ubiquitin-protein ligase TRIM7; Glycogenin-interacting protein; RING finger protein 90; Tripartite motif-containing protein 7
- 靶点基因名
- TRIM7
- 基因别名
- GNIP; RNF90
- UniProt
- Q9C029
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Tripartite motif containing 7 (TRIM7) is an E3 ubiquitin ligase belonging to the TRIM protein family, characterized by a conserved RBCC motif comprising a RING finger, B-box domains, and a coiled-coil region, along with a variable C-terminal B30.2 domain that determines substrate specificity. TRIM7 localizes to both the nucleus and cytoplasm and mediates ubiquitination-dependent degradation of diverse protein substrates, thereby regulating multiple biological processes such as protein turnover, immune responses, and cellular signaling. Structurally, the crystal structure of its B30.2 domain has provided insights into its interaction with glycogenin-1, linking TRIM7 to glycogen biosynthesis. Functionally, TRIM7 plays paradoxical roles in infection by either promoting host defense or facilitating viral pathogenesis, and in cancer, it can act as both a tumor suppressor and promoter by influencing metastasis, apoptosis, and tumor immunity. Clinically, TRIM7 has been implicated as a potential biomarker and therapeutic target in diseases such as idiopathic pulmonary fibrosis and atherosclerosis.