EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.7.11.18 | phosphoprotein |
- |
761603 |
| 2.7.11.18 | phosphoprotein |
diffential phosphorylation by Aurora B on serine residues during interphase and mitosis has regulatory function, phosphorylation sites for Aurora B on the enzyme, overview |
661665 |
| 2.7.11.18 | phosphoprotein |
diffential phosphorylation by Aurora B on serine residues, e.g. in the enzyme's IgG domain, during interphase and mitosis has regulatory function, phosphorylation sites for Aurora B on the enzyme, overview |
661665 |
| 2.7.11.18 | phosphoprotein |
eotaxin induces enzyme phosphorylation by serine/threonine protein kinases e.g. by MAP kinases ERK1/2 and p38 at Thr43, phosphorylation is required for activation of the enzyme |
661920 |
| 2.7.11.18 | phosphoprotein |
in vitro, the N-terminal actinbinding domain of MLCK210 is located within residues 27-157 and is phosphorylated by cAMP-dependent protein kinase (PKA) and Aurora B at serine residues 140/149 leading to a decrease in N27-157 binding to actin, leading role of the S149D mutation in attenuation of N27-157 binding to the cytoskeletal structures. In vitro phosphorylation and determination of phosphorylation sites, overview |
740026 |
| 2.7.11.18 | phosphoprotein |
PAK phosphorylation of MLCK by p21- activated kinase, a kinase activated by the Rho family of GTPases, can inhibit MLCK activity |
687922 |
| 2.7.11.18 | phosphoprotein |
protein kinase A phosphorylates MLCK in its regulatory domain at Ser1021 and Ser1034. The kinase activity of MLCK phosphorylated at Ser1021 is reduced, whereas that of MLCK phosphorylated at Ser1034 is not reduced |
684910 |
| 2.7.11.18 | phosphoprotein |
protein kinase A phosphorylates MLCK in its regulatory domain at Ser815 and Ser828. The kinase activity of MLCK phosphorylated at Ser815 is reduced, whereas that of MLCK phosphorylated at Ser828 is not reduced |
684910 |
| 2.7.11.18 | phosphoprotein |
reversible Ser/Thr and Tyr nmMLCK phosphorylation contributes to differential regulation of enzymatic activity and cellular spatial targeting of the kinase. cAMP-dependent protein kinase A (PKA)-mediated phosphorylation of nmMLCK exerts paradoxical effects on kinase activity depending on whether the Ser/Thr phosphorylation sites resides within the unique nmMLCK N-terminus, the putative Src homology (SH) 3-binding sequences, or the calcium/calmodulin binding region. Tyr phosphorylation of nmMLCK by pp60src or c-Abl occurs during barrier disruption, during recovery, as well as following exposure to barrier enhancing stimuli. pp60src- or c-Abl-mediated phosphorylation of nmMLCK at Y464 and Y471 increases MLC kinase activity. The two major nmMLCK splice variants, nmMLCK1 (about 211 kDa) and nmMLCK2 (about 203 kDa), differ by 69 amino acids within exon 11 (partially deleted in nmMLCK2), a stretch that contains the highly phosphorylated Y464 and Y471, suggesting that nmMLCK splice variants are differentially regulated by Tyr phosphorylation |
741240 |
| 2.7.11.18 | phosphoprotein |
the cardiac-specific isozyme probably performs also autophosphorylation |
686119 |
