
人 RABGGTB 抗体对
01AB02881
Rab geranylgeranyltransferase subunit beta (RABGGTB) encodes the beta subunit of Rab geranylgeranyltransferase, a cytosolic heterodimeric enzyme responsible for prenylating Rab GTPases. The beta subunit forms the catalytic core, containing the substrate-binding pocket, and associates with the alpha subunit to transfer geranylgeranyl groups to C-terminal cysteine motifs of Rab proteins. This post-translational modification is essential for the membrane association and function of Rabs in intracellular vesicle trafficking. While specific monogenic diseases directly attributed to RABGGTB mutations are not well-established, its dysfunction compromises Rab-mediated transport, potentially contributing to cellular pathologies involving defective vesicular dynamics.
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技术参数
- 靶点基因名
- RABGGTB
- 基因别名
- GGTB
- 蛋白别名
- Rab geranylgeranyltransferase subunit beta; RABGGTB
- UniProt
- P53611
- 物种
- Human
产品详情
- 靶点名称
- RABGGTB
- 蛋白名称
- Rab geranylgeranyltransferase subunit beta
- 蛋白别名
- Geranylgeranyl transferase type-2 subunit beta; Geranylgeranyl transferase type II subunit beta; GGTase-II-beta; Rab geranyl-geranyltransferase subunit beta; Rab GG transferase beta; Rab GGTase beta; Rab geranylgeranyltransferase subunit beta; Type II protein geranyl-geranyltransferase subunit beta
- 靶点基因名
- RABGGTB
- 基因别名
- GGTB
- UniProt
- P53611
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Rab geranylgeranyltransferase subunit beta (RABGGTB) encodes the beta subunit of Rab geranylgeranyltransferase, a cytosolic heterodimeric enzyme responsible for prenylating Rab GTPases. The beta subunit forms the catalytic core, containing the substrate-binding pocket, and associates with the alpha subunit to transfer geranylgeranyl groups to C-terminal cysteine motifs of Rab proteins. This post-translational modification is essential for the membrane association and function of Rabs in intracellular vesicle trafficking. While specific monogenic diseases directly attributed to RABGGTB mutations are not well-established, its dysfunction compromises Rab-mediated transport, potentially contributing to cellular pathologies involving defective vesicular dynamics.