p-Y348-SYK dissociates
收藏reactome.org2025-03-25 收录
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Structural and biophysical studies indicate that the adaptability of the Syk tandem SH2 domains is made possible by relatively weak interactions between the two SH2 domains and the flexibility of interdomain A (Zhang et al. 2008).
A large proportion of phosphorylated Syk is released into the cytosol. One factor that has been proposed for modulating the interactions of Syk with the receptor ITAM is the phosphorylation of Syk on Y130 (Keshvara et al. 1997).
结构生物学与生物物理学研究指出,Syk 连锁 SH2 结构域的适应性得以实现,得益于两个 SH2 结构域之间相对较弱的相互作用以及结构域间 A(Zhang 等人,2008 年)的柔韧性。
大量磷酸化的 Syk 被释放到细胞质中。Syk 与受体 ITAM 相互作用的调节因素之一,已被提出为 Syk 在 Y130 位点的磷酸化(Keshvara 等人,1997 年)。
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