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AKT phosphorylates CDKN1B on T198. 26 / 26
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"Incomplete regulation of pS 10 p27 Kip1 by JNK activity might be possible presumably due to combinatory involvement of other molecules like Akt and/or KIS.In addition to phosphorylation of Ser10, phos[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Work by several laboratories convincingly showed that phosphorylation of p27 by AKT at T157 and also at T198 is required for nucleo cytoplasmic transport [XREF_BIBR - XREF_BIBR]."

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"Less common and not well understood is the phosphorylation of p27 Kip1 at Thr 157 and Thr 198 by Akt, p90-S6 kinases, AMPK, and PIM, that impairs its nuclear import resulting in cytoplasmic localization."

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"Incomplete regulation of pS 10 p27 Kip1 by JNK activity might be possible presumably due to combinatory involvement of other molecules like Akt and/or KIS.In addition to phosphorylation of Ser10, phos[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

sparser
"AKT phosphorylates the CDK inhibitor p27 on T198 and thereby inactivates p27 by preventing its localization to the nucleus ( xref ; xref )."

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"At least three PI3K effectors (AKT, SGK and RSK) contribute to T157 and T198 phosphorylation of p27, which impairs import of monomeric p27 and increases p27-cyclin D-CDK4 assembly."

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"Akt can also phosphorylate p27 on Thr198 and promote binding to 14-3-3 in the cytoplasm."

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"Akt acts downstream of PI3K to phosphorylate p27 at T157 and T198, leading to impaired nuclear p27 import, p27 accumulation in the cytoplasm, and loss of cyclin E-Cdk2 inhibition (Viglietto et al., 20[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Thus, mTOR mediated AKT and SGK activation promote p27 phosphorylation at T157 and T198, impairing p27 nuclear import and driving cellular proliferation and migration."

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"In conclusion, this study provides evidence that P4 induced RSK1 activation mediated by the cSrc and AKT signaling pathway, subsequently causing phosphorylation of p27 at T198, which in turn increased formation of the p27 and RhoA complex and RhoA activation, and finally enhanced migration in breast cancer cells."

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"Akt phosphorylates p27on Thr157, while both Akt and Rsk can phosphorylate p27 on Thr198."

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"For example, p27 phosphorylation at T157and T198 in the cytoplasm is mediated by AKT that also influences G1 progression [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"Depending on the cell type and stimulus condition, RSK, AKT, and/or SGK phosphorylate p27 on Thr198 [XREF_BIBR, XREF_BIBR, XREF_BIBR]."

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"Role of AKT in the P4 induced phosphorylation of p27 at T198 and migration enhancement in T47D cells."

sparser
"Akt can also phosphorylate p27 on Thr198 and promote binding to 14-3-3 in the cytoplasm ( xref ; xref ; xref )."

sparser
"Less common and not well understood is the phosphorylation of p27 Kip1 at Thr 157 and Thr 198 by Akt, p90-S6 kinases, AMPK, and PIM, that impairs its nuclear import resulting in cytoplasmic localization."

sparser
"Phosphorylation of p27 at T198 by Akt leads to p27 cytoplasmic mislocalization ( xref )."

rlimsp
"AKT phosphorylates p27 at multiple residues including S10, T157, and T198, which mediates p27 stability and/or localization depending on the cellular context (11)."

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"In the early G1 phase, Thr157 and Thr198 of p27 are phosphorylated by Akt, p90RSK1 (p90 ribosomal protein S6 kinases), SGK (serum and glucocorticoid‐inducible kinase), AMPK and PIM (although this phosphorylation is relatively rare), which will prevent the nuclear transfer of p27 .62 Moreover, Akt induces phosphorylation of Thr157 and Thr198 to form a recognition motif for 14‐3‐3 protein to prevent nuclear translocation of p27 .63 Thus, Akt might also implicate in the nuclear and cytoplasmic distribution of p27 ."

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"These results show that H. pylori infection induces AKT and PI3K mediated phosphorylation of p27 at T157 and T198 to cause cytoplasmic p27 mislocalization in gastric cancer, and that p27 mislocalization is an adverse prognostic feature in gastric cancer."

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"AKT phosphorylates the CDK inhibitor p27 on T198 and thereby inactivates p27 by preventing its localization to the nucleus."

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"Akt phosphorylates p27 KIP1 not only on Thr 198, but also on Thr 157 [78-80], which creates a binding site for 14-3-3beta, epsilon, gamma, tau and zeta (but not sigma) and leads to cytoplasmic relocal[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"Identification of p27kip1phosphorylation sites revealed that akt phosphorylated p27kip1at ser10(fig.4). Therefore, akt might participate in nuclear export of p27kip1as well as p27kip1degradation. Moreover, akt might be one of the unidentified ser10kinases."

sparser
"In the early G1 phase, Thr157 and Thr198 of p27 Kip1 are phosphorylated by Akt, p90RSK1 (p90 ribosomal protein S6 kinases), SGK (serum and glucocorticoid‐inducible kinase), AMPK and PIM (although this phosphorylation is relatively rare), which will prevent the nuclear transfer of p27 Kip1 . xref Moreover, Akt induces phosphorylation of Thr157 and Thr198 to form a recognition motif for 14‐3‐3 protein to prevent nuclear translocation of p27 Kip1 . xref Thus, Akt might also implicate in the nuclear and cytoplasmic distribution of p27 Kip1 ."

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"Akt directly binds to and phosphorylates p27 Kip1 at three residues, Ser10, Thr187, and Thr198 [XREF_BIBR - XREF_BIBR]."

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"Distribution of p27 Kip1 into cyclin and CDK complexes seems to be affected by phosphorylation of p27 Kip1 at T198, an event that can be mediated by AKT or p90 ribosomal protein S6 kinases (RSK) XREF_BIBR - XREF_BIBR (XREF_FIG)."