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The Akt family of serine-threonine kinases consists of three members: Akt-1, Akt-2 and Akt-3. All Akt family members share a common structure with an N-terminal plekstrin domain, a central kinase domain and C-terminal hydrophobic domain. The Akt family members are not redundant and regulate a broad spectrum of cellular functions. To be fully activated, Akt requires phosphorylation at two specific sites: threonine 308 and serine 473. Upon activation, Akt moves from the membrane to the cytoplasm and nucleus where it phosphorylates its target.
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