
人 VTA1 抗体对
01AB00446
Vesicle trafficking 1 (VTA1) is a protein involved in the endosomal multivesicular bodies (MVB) pathway, which is crucial for sorting and degrading membrane proteins. VTA1 acts as a cofactor for VPS4A/B, catalyzing the disassembly of membrane-associated ESCRT-III complexes. It plays a role in the sorting and down-regulation of EGFR and is involved in HIV-1 budding. VTA1 is primarily localized to the nucleoplasm, vesicles, and cytosol. The protein contains an N-terminal C2H2 zinc finger domain and a C-terminal FYVE domain, which interacts with phosphatidylinositol-3-phosphate on endosomal membranes. Diseases associated with VTA1 include malignant choroid melanoma and frontotemporal dementia. Mutations in VTA1 may contribute to the pathogenesis of these conditions by disrupting normal vesicle trafficking and protein degradation processes.
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技术参数
- 靶点基因名
- VTA1
- 基因别名
- C6orf55
- 蛋白别名
- vesicle trafficking 1; VTA1
- UniProt
- Q9NP79
- 物种
- Human
产品详情
- 靶点名称
- VTA1
- 蛋白名称
- vesicle trafficking 1
- 蛋白别名
- Vacuolar protein sorting-associated protein VTA1 homolog; Dopamine-responsive gene 1 protein; DRG-1; LYST-interacting protein 5; LIP5; SKD1-binding protein 1; SBP1
- 靶点基因名
- VTA1
- 基因别名
- C6orf55
- UniProt
- Q9NP79
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Vesicle trafficking 1 (VTA1) is a protein involved in the endosomal multivesicular bodies (MVB) pathway, which is crucial for sorting and degrading membrane proteins. VTA1 acts as a cofactor for VPS4A/B, catalyzing the disassembly of membrane-associated ESCRT-III complexes. It plays a role in the sorting and down-regulation of EGFR and is involved in HIV-1 budding. VTA1 is primarily localized to the nucleoplasm, vesicles, and cytosol. The protein contains an N-terminal C2H2 zinc finger domain and a C-terminal FYVE domain, which interacts with phosphatidylinositol-3-phosphate on endosomal membranes. Diseases associated with VTA1 include malignant choroid melanoma and frontotemporal dementia. Mutations in VTA1 may contribute to the pathogenesis of these conditions by disrupting normal vesicle trafficking and protein degradation processes.