EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.3.48 | glycoprotein |
N-linked glycosylation |
95005 |
| 3.1.3.48 | glycoprotein |
receptor-type protein tyrosine phosphatase, isoforms RPTPgamma-A, RPTPgamma-B, RPTPgamma-C, RPTPgamma-S are glycoproteins |
94995 |
| 3.1.3.48 | more |
enzyme is farnesylated |
664802 |
| 3.1.3.48 | more |
subcellular localization of LmPRL-1 in Leishmania major promastigotes depends on its C-terminal farnesylation |
-, 750734 |
| 3.1.3.48 | no modification |
- |
94969 |
| 3.1.3.48 | phosphoprotein |
- |
730380 |
| 3.1.3.48 | phosphoprotein |
aggregation of the high-affinity IgE receptor FceRI induces the phosphorylation of PTP-PEST at Ser39, thus resulting in the suppression of enzyme activity |
729553 |
| 3.1.3.48 | phosphoprotein |
p52 isoform of shc undergoes tyrosine phosphorylation after growth factor stimulation, which results in Grb2 recruitment and subsequent Ras and MAPK activation |
709960 |
| 3.1.3.48 | phosphoprotein |
phosphorylation at Tyr128 and Tyr129 is catalyzed by the kinase PtkA |
729996 |
| 3.1.3.48 | 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 |
