EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.3.16 | carboxymethylation |
PP2AC undergoes at least three different posttranslational modifications: phosphorylation of Tyr-307, carboxymethylation of Leu-309, and phosphorylation of unidentified threonine residues |
693027 |
| 3.1.3.16 | methylation |
- |
729715 |
| 3.1.3.16 | phosphoprotein |
in T-cells and fibroblasts, in response to interleukin-1, insulin or tumor necrosis factor alpha |
654485 |
| 3.1.3.16 | phosphoprotein |
insertion of stoichiometric and site-specific phospho-Ser/Thr residues in the C-terminal tail of PTEN. No single phospho-modification of the Ser/Thr C-terminal cluster is dominant and each is partially additive in antagonizing catalysis. Conformational closure is influenced by the aggregate effect of multiple phospho-sites rather than dominated by a single phosphorylation site |
751061 |
| 3.1.3.16 | phosphoprotein |
PA3346 is phosphorylated in the active state by HptB |
693226 |
| 3.1.3.16 | phosphoprotein |
phosphorylation by cyclin-dependent kinases lower PP1 activity in vitro and vivo |
708999 |
| 3.1.3.16 | phosphoprotein |
phosphorylation of PTPN12 at Ser19 changes its substrate interface, and by doing so, selectively decreases its activity toward the human epidermal growth factor receptor 2 (HER2)-pY1196 site, but not other HER2 phosphorylation sites or other known PTPN12 substrates. Phosphorylation of Ser19 by CDK2 specifically increases EGF-induced HER2-pY1196 and PAK1-pT423 phosphorylation. Phosphorylation of PTPN12 byCDK2 impairs recruitment of the serine/threonine-protein kinase 1 (PAK1) to HER2, resulting in the blockade of the HER2-pY1196-PAK1-T423 signaling pathway, thus increases tumor cell motility |
750513 |
| 3.1.3.16 | phosphoprotein |
PKA is known to phosphorylate and activate PP2A in brain |
709072 |
| 3.1.3.16 | phosphoprotein |
PP2AC undergoes at least three different posttranslational modifications: phosphorylation of Tyr-307, carboxymethylation of Leu-309, and phosphorylation of unidentified threonine residues |
693027 |
| 3.1.3.16 | proteolytic modification |
- |
663946 |
