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In the case of PKN2 the PK domain has all the catalytic residues and is also known to phosphorylate on Ser/Thr residues [ 62].
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Aurora-B is also known to phosphorylate Histone H3 (pHH3) at the serine 10 position during mitosis [ 12, 13].
On the other hand, MAPK and Akt are also known to phosphorylate the estrogen receptor (ER) at Ser-118 and Ser-167, respectively, thereby mimicking the effects of estrogenic activity in ER-positive cells in the absence of estrogen (E2) [6]–[8].
In addition, PKCs are also known to phosphorylate GRK2 enhancing its membrane recruitment and ability to desensitize GPCRs.
aPKCs are also known to phosphorylate Ser9/Ser21 of GSK-3 (Etienne-Manneville and Hall, 2003).
It is also known that AMPKα phosphorylates TSC2, thereby, constraining mTOR activity [43].
PKR, which is also known as EIF2αK2, is a serine/threonine kinase that phosphorylates eIF2α in response to virus infection.
Furthermore, it is also known that the downstream p38α target MK2 (MAPKAPK-2) (Stokoe et al, 1992) can phosphorylate p53 (switchingwitching on p53 transcriptional activity (She et al, 2002; Hsu et al, 2011).
Finally, VRK1 has also been known to phosphorylate several transcription factors, such as p53 [14], [14], ATF2 [15], and c-Jun [16], to increase transcription factor stability and activity.
By contrast, BAK1, which is already known to phosphorylate BIK1, hardly phosphorylated PBL27.
Because WNK1 and WNK3 are known to phosphorylate OSR1/SPAK, we also examined their expression.
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