IndraLab

Statements

AKT phosphorylates CDKN1B on threonine. 6 / 8
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trips
"Although Akt also phosphorylated p27(Kip1) at Ser(10) and Thr(187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
reach
"Although Akt also phosphorylated p27 (Kip1) at Ser (10) and Thr (187), these two sites were not involved in the binding to 14-3-3 proteins."
12042314
reach
"XREF_BIBR Akt directly phosphorylates p27 on multiple Threonine (T) residues, including T198, which have been shown to promote nuclear export and sequestration of p27 in the cytoplasm, resulting in the inactivation of the protein in human cells."
26997868
reach
"The nuclear localisation signal of p27 contains an AKT consensus site at threonine 157, and phosphorylation of this threonine residue on p27 by AKT inhibits p27 's import to the nucleus."
25965299
sparser
"The nuclear localisation signal of p27 contains an AKT consensus site at threonine 157, and phosphorylation of this threonine residue on p27 by AKT inhibits p27's import to the nucleus."
25965299
reach
"Less common and not well understood is the phosphorylation of p27 at Thr and Thr by Akt, p90‐S6 kinases, AMPK, and PIM, that impairs its nuclear import resulting in cytoplasmic localization.In UACC‐257 cells that stably overexpress NOX5, the observed decrease in p27 levels may, in part, be transcriptionally regulated since a modest decrease in p27 transcript levels was observed (Figure 4E)."
28762556