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- _4 value " Pim-1 and C-TAK1 underwent autophosphorylation, but only Pim-1 was able to phosphorylate C-TAK1 but not vice versa. The results show that the region between 81 and 165 of C-TAK1 is necessary for Pim1 to interact and it has at least two phosphorylation sites at threonine 90 or 95 or at 96. Phosphorylation by Pim-1 decreased C-TAK1 kinase activity significantly, in particular its ability to phosphorylate at serine 216 and inactivate Cdc25C, a protein that actively promotes cell cycle progression at the G(2)/M phase." provenance.
- _4 wasQuotedFrom 15319445 provenance.