| + |
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 |
| + |
ROCK2 | up-regulates
phosphorylation
|
IRF4 |
0.428 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167467 |
Ser447 |
YHRSIRHsSIQE |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 20697158 |
Carock2 phosphorylated irf4 at either of 2 distinct phosphorylation sites, s446 and s447 / rock2-mediated phosphorylation of irf4 regulated the synthesis of il-17 and il-21 and the differentiation of th17 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167471 |
Ser448 |
HRSIRHSsIQE |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 20697158 |
Carock2 phosphorylated irf4 at either of 2 distinct phosphorylation sites, s446 and s447 / rock2-mediated phosphorylation of irf4 regulated the synthesis of il-17 and il-21 and the differentiation of th17 cells. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK2 | down-regulates 
phosphorylation
|
SH3GL2 |
0.414 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-140466 |
Thr14 |
KKQFHKAtQKVSEKV |
Homo sapiens |
|
| pmid |
sentence |
| 16164598 |
We identified the phosphorylation site of endophilin a1 at thr-14 endophilin t14d inhibited egf receptor internalization. Furthermore, phosphorylation of endophilin by rho-kinase inhibited the binding to cin85. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK2 | up-regulates activity
phosphorylation
|
PPP1R14A |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90832 |
Thr38 |
QKRHARVtVKYDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 32471307 |
A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP.| CPI-17 can be also directly phosphorylated at Thr38 residue by MYPT1-associated kinase [222], by PAK, which is downstream of Rac and/or Cdc42 cascade [223], by Rho-associated coiled-coil kinase (ROCK) [224] and by PKN [225]. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96696 |
Thr38 |
QKRHARVtVKYDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 32471307 |
A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP.| CPI-17 can be also directly phosphorylated at Thr38 residue by MYPT1-associated kinase [222], by PAK, which is downstream of Rac and/or Cdc42 cascade [223], by Rho-associated coiled-coil kinase (ROCK) [224] and by PKN [225]. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK2 | up-regulates
phosphorylation
|
DPYSL2 |
0.393 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77543 |
Thr555 |
DNIPRRTtQRIVAPP |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 10818093 |
Rho-kinase phosphorylated crmp-2 at thr-555 in vitro.we demonstrated that crmp-2 is phosphorylated by rho-kinase in drg neurons during lpa-induced growth cone collapse. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK2 | down-regulates activity
phosphorylation
|
PPP1R12A |
0.778 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249164 |
Thr853 |
PREKRRStGVSFWTQ |
in vitro |
|
| pmid |
sentence |
| 12220642 |
Rho kinase is known to control smooth muscle contractility by phosphorylating the 110 kDa myosin-targetting subunit (MYPT1) of the myosin-associated form of protein phosphatase 1 (PP1M). Phosphorylation of MYPT1 at Thr695 has previously been reported to inhibit the catalytic activity of PP1. Here, we show that the phosphorylation of Thr850 by Rho kinase dissociates PP1M from myosin, providing a second mechanism by which myosin phosphatase activity is inhibited. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ROCK2 | up-regulates 
|
Actin_cytoskeleton_reorganization |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261722 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261712 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
GEM | down-regulates activity
binding
|
ROCK2 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261711 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261717 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 16757346 |
We have found that Gem binds specifically to ROKβ in the coiled‐coil domain adjacent to the Rho binding site. The interaction between Gem and ROKβ leads to inhibition of MLC and MBS phosphorylation but not phosphorylation of LIMK, indicating that Gem exerts its effect by altering the substrate specificity of ROKβ |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261721 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261707 |
|
|
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16757346 |
We have found that Gem binds specifically to ROKβ in the coiled‐coil domain adjacent to the Rho binding site. The interaction between Gem and ROKβ leads to inhibition of MLC and MBS phosphorylation but not phosphorylation of LIMK, indicating that Gem exerts its effect by altering the substrate specificity of ROKβ |
|
| Publications: |
4 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops |
| + |
ROCK2 | up-regulates quantity by expression
transcriptional regulation
|
LPP |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22886954 |
Inactivation of rho kinase (rok) with rok inhibitors significantly inhibited lpp mrna expression |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Y-27632 | down-regulates
chemical inhibition
|
ROCK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-207893 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
N-(6-fluoro-1H-indazol-5-yl)-6-methyl-2-oxo-4-[4-(trifluoromethyl)phenyl]-3,4-dihydro-1H-pyridine-5-carboxamide | down-regulates activity
chemical inhibition
|
ROCK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262230 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19740074 |
We also observed that several ROCK (Rho kinase) inhibitors such as Y-27632 and H-1152, suppressed LRRK2 with similar potency to which they inhibited ROCK2. In contrast, GSK429286A, a selective ROCK inhibitor, did not significantly inhibit LRRK2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ROCK2
- 
- 