Protein kinase B (PKB), also known as Akt (PKB/Akt), is a serine/threonine phosphoryl transferase and a downstream effector of the phosphoinositol3 kinase (PI3K) signaling. The AKT protein kinase (also referred to as protein kinase B or Rac-protein kinase) was initially identified as an acute transforming component of the AKT8 virus isolated from a murine T cell lymphoma1, 2.
PKB/Akt belongs to the AGC subfamily of the protein kinase superfamily, which consists of 518 members in humans and is conserved from primitive metazoans to humans3. The PKB subfamily comprises three mammalian isoforms, PKB , PKB and PKB (Akt1, Akt2 and Akt3, respectively), which are products of distinct genes and share a conserved structure that includes three functional domains: an N-terminal pleckstrin homology (PH) domain, a central kinase domain, and a C-terminal regulatory domain containing the hydrophobic motif (HM) phosphorylation site [FxxF(S/T)Y]4.
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