人 MAST1 抗体对
01AB02853
Microtubule associated serine/threonine kinase 1 (MAST1) is a large, atypical member of the AGC kinase family, spanning approximately 1300–2400 amino acids and characterized by a conserved AGC catalytic domain with key motifs such as the activation segment (T-loop), RD-pocket, hydrophobic motif, and turn motif. Distinctively, MAST1 contains unique N-terminal DUF1908 and C-terminal PDZ domains, which are not found in other AGC kinases; the PDZ domain mediates protein-protein interactions, while the DUF domain is highly susceptible to post-translational modifications. All canonical domains are essential for MAST1 function, as demonstrated in knockout studies, and the kinase exhibits activities including protein serine/threonine kinase, ATP binding, and magnesium ion binding. Pathogenic mutations in MAST1 have been linked to neurological disorders in humans.
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技术参数
- 靶点基因名
- MAST1
- 基因别名
- KIAA0973; SAST
- 蛋白别名
- microtubule associated serine/threonine kinase 1; MAST1
- UniProt
- Q9Y2H9
- 物种
- Human
产品详情
- 靶点名称
- MAST1
- 蛋白名称
- microtubule associated serine/threonine kinase 1
- 蛋白别名
- Microtubule-associated serine/threonine-protein kinase 1; Syntrophin-associated serine/threonine-protein kinase
- 靶点基因名
- MAST1
- 基因别名
- KIAA0973; SAST
- UniProt
- Q9Y2H9
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Microtubule associated serine/threonine kinase 1 (MAST1) is a large, atypical member of the AGC kinase family, spanning approximately 1300–2400 amino acids and characterized by a conserved AGC catalytic domain with key motifs such as the activation segment (T-loop), RD-pocket, hydrophobic motif, and turn motif. Distinctively, MAST1 contains unique N-terminal DUF1908 and C-terminal PDZ domains, which are not found in other AGC kinases; the PDZ domain mediates protein-protein interactions, while the DUF domain is highly susceptible to post-translational modifications. All canonical domains are essential for MAST1 function, as demonstrated in knockout studies, and the kinase exhibits activities including protein serine/threonine kinase, ATP binding, and magnesium ion binding. Pathogenic mutations in MAST1 have been linked to neurological disorders in humans.