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人 VTA1 抗体对
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人 VTA1 抗体对

01AB00445

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.

Human
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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.