EC Number   |
Posttranslational Modification |
Reference |
|---|
   4.4.1.14 | glycoprotein |
the enzyme harbors an N-glycosylation site |
729833 |
| 4.4.1.14 | more |
posttranslational regulation of ethylene biosynthesis |
34595 |
| 4.4.1.14 | more |
putative phosphorylation of the C-termini of ACS may promote interaction between ACS and 14-3-3 and may inhibit binding to ETO1 proteins, resulting in 1-aminocyclopropane-1-carboxylate and ethylene synthesis |
678358 |
| 4.4.1.14 | phosphoprotein |
cotton ACS2 interacts with Ca2+-dependent protein kinase CPK1. Bacterially expressed and purified recombinant ACS2 is phosphorylated by CPK1 in vitro and residue S460 is a possible phosphorylation site for CPK1. Phosphorylated ACS2 shows significantly increased ACS activity, leading to elevated ethylene production |
713608 |
| 4.4.1.14 | phosphoprotein |
in presence of oligogalacturonic acids, formation of phosphorylated isoform ACS2 is observed |
747428 |
| 4.4.1.14 | phosphoprotein |
phosphorylation/dephosphorylation of ACS2 regulates its turnover upstream of the ubiquitin-26S-proteasome degradation pathway. ACS2 is stabilized by phosphorylation and degraded after dephosphorylation. The amount of ACS2 affected by the protein kinase/phosphatase inhibitors significantly influences cellular ACS activity, 1-aminocyclopropane-1-carboxylic acid content, and ethylene production levels in tomato fruit tissue. Calcium-dependent protein kinase CDPK2, is one of the protein kinases that are able to phosphorylate ACS2 at residue S460. ACS2 is immediately phosphorylated after translation by CDPK and mitogen-activated protein kinase at different sites in response to wound signaling and almost all functional ACS2 molecules are phosphorylated in the cell. Phosphorylation at both sites is required for ACS2 stability |
716539 |
| 4.4.1.14 | phosphoprotein |
RCN1-containing protein phosphatase 2A complexes specifically dephosphorylate a C-terminal ACS6 phosphopeptide |
716667 |
