EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.1.183 | glycoprotein |
murine POMK catalytic domain (residue 45-349) possesses three potential N-glycosylation sites, N66, N164 and N219, which are not conserved among species |
761207 |
| 2.7.1.183 | glycoprotein |
there are four potential N-linked glycosylation sites in the HsPOMK kinase domain: Asn67, Asn165, Asn220, and Asn235 |
760981 |
| 2.7.1.183 | no glycoprotein |
no glycosylation site is present in DrPOMK |
760981 |
| 2.7.1.183 | phosphoprotein |
SGK196 is primarily modified by N-glycosylation in breast cancer cells. N-glycosylation of SGK196 leads to suppression of cell migration, invasion, and metastasis in breast cancer cells, particularly in the basal-like breast cancer (BLBC) type. In addition, enzyme SGK196 N-glycosylation performs the regulatory function through the PI3K/AKT/GSK3beta signaling pathway. N-glycosylated SGK196 plays suppression roles in BLBC metastases. The phosphorylation of the enzyme can be abolished by RPN1 knockout |
762066 |
