| + |
PRKCA | down-regulates 
phosphorylation
|
MYL9 |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177940 |
Ser2 |
sSKRAKAK |
Homo sapiens |
|
| pmid |
sentence |
| 22136066 |
Rlc can also be phosphorylated at ser1/ser2/thr9 by protein kinase c (pkc). Biophysical studies show that phosphorylation at these sites leads to an increase in the km of myosin light chain kinase (mlck) for rlc, thereby indirectly inhibiting myosin ii activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192792 |
Ser3 |
sKRAKAKT |
Homo sapiens |
|
| pmid |
sentence |
| 22136066 |
Rlc can also be phosphorylated at ser1/ser2/thr9 by protein kinase c (pkc). Biophysical studies show that phosphorylation at these sites leads to an increase in the km of myosin light chain kinase (mlck) for rlc, thereby indirectly inhibiting myosin ii activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191536 |
Thr10 |
SKRAKAKtTKKRPQR |
Homo sapiens |
|
| pmid |
sentence |
| 22136066 |
Rlc can also be phosphorylated at ser1/ser2/thr9 by protein kinase c (pkc). Biophysical studies show that phosphorylation at these sites leads to an increase in the km of myosin light chain kinase (mlck) for rlc, thereby indirectly inhibiting myosin ii activity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity 
phosphorylation
|
MYL9 |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260307 |
Ser20 |
KRPQRATsNVFAMFD |
in vitro |
|
| pmid |
sentence |
| 21457715 |
Activation of the catalytic ATPase domain residing in the N‐terminus of the heavy chain relies on the reversible phosphorylation of the associated MLC on Ser19 (monophosphorylation), or in some cases on both Thr18 and Ser19 (diphosphorylation)|We detected Ser19 of MLC as the common phosphorylation site for the catalytic domains of MRCK_/_, ROK_, MLCK and PAK_, but only ROK_ and CRIK are able to phosphorylate both Thr18 and Ser19 residues causing diphosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260308 |
Thr19 |
KKRPQRAtSNVFAMF |
in vitro |
|
| pmid |
sentence |
| 21457715 |
Activation of the catalytic ATPase domain residing in the N‐terminus of the heavy chain relies on the reversible phosphorylation of the associated MLC on Ser19 (monophosphorylation), or in some cases on both Thr18 and Ser19 (diphosphorylation)|We detected Ser19 of MLC as the common phosphorylation site for the catalytic domains of MRCK_/_, ROK_, MLCK and PAK_, but only ROK_ and CRIK are able to phosphorylate both Thr18 and Ser19 residues causing diphosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ROCK2 | up-regulates activity
phosphorylation
|
MYL9 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261709 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 8702756 |
Here we found that Rho-kinase stoichiometrically phosphorylated myosin light chain (MLC). Peptide mapping and phosphoamino acid analyses revealed that the primary phosphorylation site of MLC by Rho-kinase was Ser-19, which is the site phosphorylated by MLC kinase. Rho-kinase phosphorylated recombinant MLC, whereas it failed to phosphorylate recombinant MLC, which contained Ala substituted for both Thr-18 and Ser-19. We also found that the phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261719 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 8702756 |
Here we found that Rho-kinase stoichiometrically phosphorylated myosin light chain (MLC). Peptide mapping and phosphoamino acid analyses revealed that the primary phosphorylation site of MLC by Rho-kinase was Ser-19, which is the site phosphorylated by MLC kinase. Rho-kinase phosphorylated recombinant MLC, whereas it failed to phosphorylate recombinant MLC, which contained Ala substituted for both Thr-18 and Ser-19. We also found that the phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261708 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 8702756 |
Here we found that Rho-kinase stoichiometrically phosphorylated myosin light chain (MLC). Peptide mapping and phosphoamino acid analyses revealed that the primary phosphorylation site of MLC by Rho-kinase was Ser-19, which is the site phosphorylated by MLC kinase. Rho-kinase phosphorylated recombinant MLC, whereas it failed to phosphorylate recombinant MLC, which contained Ala substituted for both Thr-18 and Ser-19. We also found that the phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261718 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 8702756 |
Here we found that Rho-kinase stoichiometrically phosphorylated myosin light chain (MLC). Peptide mapping and phosphoamino acid analyses revealed that the primary phosphorylation site of MLC by Rho-kinase was Ser-19, which is the site phosphorylated by MLC kinase. Rho-kinase phosphorylated recombinant MLC, whereas it failed to phosphorylate recombinant MLC, which contained Ala substituted for both Thr-18 and Ser-19. We also found that the phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CIT | up-regulates activity
phosphorylation
|
MYL9 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260305 |
Ser20 |
KRPQRATsNVFAMFD |
in vitro |
|
| pmid |
sentence |
| 21457715 |
Activation of the catalytic ATPase domain residing in the N‐terminus of the heavy chain relies on the reversible phosphorylation of the associated MLC on Ser19 (monophosphorylation), or in some cases on both Thr18 and Ser19 (diphosphorylation)|We detected Ser19 of MLC as the common phosphorylation site for the catalytic domains of MRCK_/_, ROK_, MLCK and PAK_, but only ROK_ and CRIK are able to phosphorylate both Thr18 and Ser19 residues causing diphosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260306 |
Thr19 |
KKRPQRAtSNVFAMF |
in vitro |
|
| pmid |
sentence |
| 21457715 |
Activation of the catalytic ATPase domain residing in the N‐terminus of the heavy chain relies on the reversible phosphorylation of the associated MLC on Ser19 (monophosphorylation), or in some cases on both Thr18 and Ser19 (diphosphorylation)|We detected Ser19 of MLC as the common phosphorylation site for the catalytic domains of MRCK_/_, ROK_, MLCK and PAK_, but only ROK_ and CRIK are able to phosphorylate both Thr18 and Ser19 residues causing diphosphorylation. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
ROCK1 | up-regulates
phosphorylation
|
MYL9 |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43031 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 8702756 |
Rho-kinase phosphorylates the mlc of intact myosin and activates its mgatpase activity in a gtp_?Rho-dependent manner. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
MYLK | up-regulates
phosphorylation
|
MYL9 |
0.832 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188797 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 19851336 |
More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related cdc42-binding kinase (mrck;also known as cdc42bp)6,34,45,46. These kinases phosphorylate rlcs on ser19, thr18 or both, to relieve the inhibition imposed on the myosin molecule by unphosphorylated rlcs and the head_head interaction outlined above. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188801 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 19851336 |
More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related cdc42-binding kinase (mrck;also known as cdc42bp)6,34,45,46. These kinases phosphorylate rlcs on ser19, thr18 or both, to relieve the inhibition imposed on the myosin molecule by unphosphorylated rlcs and the head_head interaction outlined above. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDC42BPA | up-regulates
phosphorylation
|
MYL9 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188781 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 19851336 |
More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related cdc42-binding kinase (mrck;also known as cdc42bp)6,34,45,46. These kinases phosphorylate rlcs on ser19, thr18 or both, to relieve the inhibition imposed on the myosin molecule by unphosphorylated rlcs and the head_head interaction outlined above. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188785 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 19851336 |
More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related cdc42-binding kinase (mrck;also known as cdc42bp)6,34,45,46. These kinases phosphorylate rlcs on ser19, thr18 or both, to relieve the inhibition imposed on the myosin molecule by unphosphorylated rlcs and the head_head interaction outlined above. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DAPK3 | up-regulates
phosphorylation
|
MYL9 |
0.501 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188789 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 19851336 |
More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related cdc42-binding kinase (mrck;also known as cdc42bp)6,34,45,46. These kinases phosphorylate rlcs on ser19, thr18 or both, to relieve the inhibition imposed on the myosin molecule by unphosphorylated rlcs and the head_head interaction outlined above. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188793 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 19851336 |
More than a dozen kinases have been reported to phosphorylate the rlcs of nm ii (fig. 2), including myosin light chain kinase (mlck;also known as mylk), rho-associated, coiled coil-containing kinase (rock), citron kinase, leucine zipper interacting kinase (zipk;also known as dapk3) and myotonic dystrophy kinase-related cdc42-binding kinase (mrck;also known as cdc42bp)6,34,45,46. These kinases phosphorylate rlcs on ser19, thr18 or both, to relieve the inhibition imposed on the myosin molecule by unphosphorylated rlcs and the head_head interaction outlined above. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
MYL9
- 
- 