| + |
PAK2 | down-regulates activity 
phosphorylation
|
MYLK |
0.512 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250222 |
Ser1208 |
MKSRRPKsSLPPVLG |
in vitro |
|
| pmid |
sentence |
| 10748018 |
PAK2 can directly phosphorylate MLCK, inhibiting its activity and limiting the development of isometric tension. PAK2 catalyzes MLCK phosphorylation on serine residues 439 and 991. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250223 |
Ser1760 |
RAIGRLSsMAMISGL |
in vitro |
|
| pmid |
sentence |
| 10748018 |
PAK2 can directly phosphorylate MLCK, inhibiting its activity and limiting the development of isometric tension. PAK2 catalyzes MLCK phosphorylation on serine residues 439 and 991. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
CAMK2G | down-regulates activity
phosphorylation
|
MYLK |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250700 |
Ser1760 |
RAIGRLSsMAMISGL |
|
|
| pmid |
sentence |
| 2160950 |
Phosphorylation of MLC kinase by CaM protein kinase II increased the dissociation constant of MLC kinase for calmodulin about 10 times without changing the Vmax. The location of the phosphorylation sites was identified by isolating and sequencing the tryptic phosphopeptides of MLC kinase. The preferred site was identified as serine 512 and the second site as serine 525. These sites are the same as the sites phosphorylated by cAMP-dependent protein kinase. |
|
| Publications: |
1 |
| + |
MYLK | up-regulates 
phosphorylation
|
MYL9 |
0.833 |
| 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 |
| + |
MYLK | down-regulates
phosphorylation
|
CALD1 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166049 |
Ser744 |
GLKVGVSsRINEWLT |
Homo sapiens |
|
| pmid |
sentence |
| 20536391 |
Phosphorylation of caldesmon by myosin light chain kinase increases its binding affinity for phosphorylated myosin filaments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ABL1 | up-regulates
phosphorylation
|
MYLK |
0.305 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167989 |
Tyr231 |
NQDDVGVyTCLVVNG |
Homo sapiens |
|
| pmid |
sentence |
| 20861316 |
Nonmuscle myosin light chain kinase (nmmlck), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167993 |
Tyr464 |
QEGSIEVyEDAGSHY |
Homo sapiens |
|
| pmid |
sentence |
| 20861316 |
We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167997 |
Tyr556 |
LNGQPIQyARSTCEA |
Homo sapiens |
|
| pmid |
sentence |
| 20861316 |
Nonmuscle myosin light chain kinase (nmmlck), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168001 |
Tyr846 |
DGGGSDRyGSLRPGW |
Homo sapiens |
|
| pmid |
sentence |
| 20861316 |
Nonmuscle myosin light chain kinase (nmmlck), a multi-functional cytoskeletal protein critical to vascular homeostasis, is highly regulated by tyrosine phosphorylation. We identified multiple novel c-abl-mediated nmmlck phosphorylation sites by mass spectroscopy analysis (including y231, y464, y556, y846) and examined their influence on nmmlck function and human lung endothelial cell (ec) barrier regulation. Tyrosine phosphorylation of nmmlck increased kinase activity |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Lung |
| + |
SRC | up-regulates
phosphorylation
|
MYLK |
0.427 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85005 |
Tyr464 |
QEGSIEVyEDAGSHY |
Homo sapiens |
|
| pmid |
sentence |
| 11113114 |
Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95238 |
Tyr464 |
QEGSIEVyEDAGSHY |
Homo sapiens |
|
| pmid |
sentence |
| 12408982 |
Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-95242 |
Tyr471 |
YEDAGSHyLCLLKAR |
Homo sapiens |
|
| pmid |
sentence |
| 12408982 |
Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85009 |
Tyr471 |
YEDAGSHyLCLLKAR |
Homo sapiens |
|
| pmid |
sentence |
| 11113114 |
Ec mlck-1 is phosphorylated by p60(src) on tyr(464) and tyr(471), resulting in a 2- to 3-fold increase in ec mlck-1 enzymatic activity. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
binding
|
MYLK |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106552 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11283607 |
Rock proteins are known to regulate mlc-phosphorylation, and apoptotic cells exhibit a gradual increase in levels of phosphorylated mlc concomitant with rock i cleavage. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HOXA10 | up-regulates quantity by expression
transcriptional regulation
|
MYLK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261643 |
|
|
Rattus norvegicus |
A10 Cell |
| pmid |
sentence |
| 15886193 |
Results from these experiments demonstrated that in 10T1/2 cells Hoxa10-1 increased the activity of the telokin promoter 3-fold without affecting the activity of the other promoters analyzed (Fig. 2A). Similar results were also observed in A10 SMC (data not shown). In contrast, Hoxb8 significantly repressed the activity of the telokin, smooth muscle α-actin, and SM22α promoters by 70, 50, and 70%, respectively |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
HOXB8 | down-regulates quantity by repression
transcriptional regulation
|
MYLK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261640 |
|
|
Rattus norvegicus |
A10 Cell |
| pmid |
sentence |
| 15886193 |
Results from these experiments demonstrated that in 10T1/2 cells Hoxa10-1 increased the activity of the telokin promoter 3-fold without affecting the activity of the other promoters analyzed (Fig. 2A). Similar results were also observed in A10 SMC (data not shown). In contrast, Hoxb8 significantly repressed the activity of the telokin, smooth muscle α-actin, and SM22α promoters by 70, 50, and 70%, respectively |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PAK | down-regulates activity
phosphorylation
|
MYLK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269973 |
|
|
in vitro |
|
| pmid |
sentence |
| 10748018 |
PAK2 can directly phosphorylate MLCK, inhibiting its activity and limiting the development of isometric tension. PAK2 catalyzes MLCK phosphorylation on serine residues 439 and 991. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MYLK | up-regulates
phosphorylation
|
MYL6B |
0.71 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65865 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10092231 |
Cytoskeletal dynamics are primarily modulated by interactions of actin and myosin ii that are regulated by myosin light chain kinase (mlck)-mediated phosphorylation of the regulatory myosin light chain (mlc). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PAK1 | down-regulates activity
phosphorylation
|
MYLK |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250317 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10092231 |
P21-activated kinase 1 (PAK1) phosphorylates MLCK, resulting in decreased MLCK activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
wortmannin | down-regulates
chemical inhibition
|
MYLK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207791 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FOXQ1 | down-regulates quantity by repression
transcriptional regulation
|
MYLK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261609 |
|
|
Rattus norvegicus |
A10 Cell |
| pmid |
sentence |
| 10896677 |
Results from this analysis revealed that the inhibitory activity of HFH-1 was contained within the forkhead DNA-binding domain. Truncated HFH-1 proteins that lack the entire forkhead domain were unable to repress telokin promoter activity, in contrast expression of the forkhead domain alone was able to repress promoter activity |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
MYLK
- 
- 