EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.3.67 | acetylation |
inhibiton of PTEN |
694495 |
| 3.1.3.67 | more |
carbonylation of PTEN increases significantly in ethanol-fed mice compared to pair-fed control animals, corresponding to decreased PTEN3-phosphatase activity |
731861 |
| 3.1.3.67 | phosphoprotein |
C-terminal 51 amino acids contains a cluster of phosphorylation sites which regulates protein stability and function in cells, a phosphorylation-dependent intramolecular interaction regulates the membrane association and activity of the tumor suppressor PTEN, phosphorylation of the C-terminal cluster has an inhibitory effect on membrane association and activity |
694916 |
| 3.1.3.67 | phosphoprotein |
exposure of bovine aortic endothelial cells to cyclic strain results in a time-dependent PTEN phosphorylation. Maximal phosphorylation occurres at 10 min after the cyclic strain stimulation by 2.21fold relative to static condition |
681020 |
| 3.1.3.67 | 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 |
| 3.1.3.67 | phosphoprotein |
phosphorylation of several serine and threonine residues in the C-terminus of the protein inhibits PTEN, e.g., suppressing of membrane association, nuclear localization, PDZ-binding, ubiquitination, degradation and phosphatase activity. The phosphorylation sites form 2 separable groups comprising a close cluster of 4 residues, Ser380, Thr382, Thr383 and Ser385, and a pair of residues slightly more N-terminal, Thr366 and Ser370. The 380-385 cluster sites all appear to be phosphorylated by protein kinase CK2. |
694495 |
| 3.1.3.67 | phosphoprotein |
PTEN expression and PTEN phosphorylation are significantly increased in the livers of ethanol-fed mice |
731861 |
| 3.1.3.67 | phosphoprotein |
recombinant PTEN is phosphorylated in the infected insect cells at Ser-380, Thr-382, and Thr-383 at the C-terminal tail |
682679 |
| 3.1.3.67 | phosphoprotein |
the 50-amino-acid C-terminal domain, the tail, is necessary for maintaining protein stability and it also acts to inhibit PTEN function. The tail-dependent regulation of stability and activity is linked to the phosphorylation of three residues, S380, T382, and T383 within the tail. Therefor, the tail is likely to mediate the regulation of PTEN function through phosphorylation |
653215 |
| 3.1.3.67 | phosphoprotein |
the enzyme is activated by the phosphatidylinositol 3-kinase |
716688 |
