| + |
ROCK1 | up-regulates 
phosphorylation
|
RND3 |
0.686 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134703 |
Ser11 |
RRASQKLsSKSIMDP |
Homo sapiens |
|
| pmid |
sentence |
| 15775972 |
We show that rock phosphorylates endogenous rhoe at serine 11 upon cell stimulation with platelet-derived growth factor. Phosphorylation has no effect on rhoe binding to rock i, but instead increases rhoe protein stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
FHOD1 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160544 |
Ser1131 |
AARERKRsRGNRKSL |
Homo sapiens |
|
| pmid |
sentence |
| 18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160548 |
Ser1137 |
RSRGNRKsLRRTLKS |
Homo sapiens |
|
| pmid |
sentence |
| 18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160552 |
Thr1141 |
NRKSLRRtLKSGLGD |
Homo sapiens |
|
| pmid |
sentence |
| 18239683 |
Rock phosphorylates the c-terminal residues ser1131, ser1137, and thr1141 of formin homology domain protein 1 (fhod1). Phosphorylation of fhod1 at the three residues fully disrupts the autoinhibitory interaction, which culminates in formation of stress fibres. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates activity 
phosphorylation
|
ARHGAP35 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276177 |
Ser1150 |
LERGRKVsIVSKPVL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 19103606 |
these results indicate that Rho-kinase can phosphorylate p190A RhoGAP at Ser1150 in COS7 cells. Similarly, the immunoblot analysis, through the use of the anti-p190A RhoGAP-pT1226 and -pS1236 antibodies, revealed that Rho-kinase can phosphorylate p190A RhoGAP at Thr1226 and Ser1236 in COS7 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276176 |
Ser1236 |
PKPKPRPsITKATWE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 19103606 |
these results indicate that Rho-kinase can phosphorylate p190A RhoGAP at Ser1150 in COS7 cells. Similarly, the immunoblot analysis, through the use of the anti-p190A RhoGAP-pT1226 and -pS1236 antibodies, revealed that Rho-kinase can phosphorylate p190A RhoGAP at Thr1226 and Ser1236 in COS7 cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276178 |
Thr1226 |
LRSLRRNtKKPKPKP |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 19103606 |
these results indicate that Rho-kinase can phosphorylate p190A RhoGAP at Ser1150 in COS7 cells. Similarly, the immunoblot analysis, through the use of the anti-p190A RhoGAP-pT1226 and -pS1236 antibodies, revealed that Rho-kinase can phosphorylate p190A RhoGAP at Thr1226 and Ser1236 in COS7 cells |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 | down-regulates
phosphorylation
|
ARHGAP35 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182849 |
Ser1150 |
LERGRKVsIVSKPVL |
Homo sapiens |
|
| pmid |
sentence |
| 19103606 |
Rho-kinase, an effector of rhoa, phosphorylated p190a rhogap at ser(1150) and attenuated p190a rhogap activity in cos7 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182853 |
Ser1236 |
PKPKPRPsITKATWE |
Homo sapiens |
|
| pmid |
sentence |
| 19103606 |
Here we show that rho-kinase, an effector of rhoa, phosphorylated p190a rhogap at ser1150 and attenuated p190a rhogap activity in cos7 cells |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
GFAP |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100181 |
Ser13 |
ITSAARRsYVSSGEM |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100188 |
Ser38 |
LGPGTRLsLARMPPP |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100192 |
Thr7 |
tSAARRSY |
in vitro |
|
| pmid |
sentence |
| 12686604 |
We report here that aurora-b phosphorylates gfap and desmin in vitro, and this phosphorylation leads to a reduction in filament forming ability. The sites phosphorylated by aurora-b;thr-7/ser-13/ser-38 of gfap, and thr-16 of desmin are common with those related to rho-associated kinase (rho-kinase), which has been reported to phosphorylate gfap and desmin at cleavage furrow during cytokinesis. We identified ser-59 of desmin to be a specific site phosphorylated by aurora-b in vitro. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ROCK1 | down-regulates
phosphorylation
|
PFN1 |
0.27 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-196820 |
Ser138 |
MASHLRRsQY |
Homo sapiens |
|
| pmid |
sentence |
| 22479341 |
We previously identified pfn1 as a huntingtin aggregation inhibitor, and others have implicated it as a tumor-suppressor. Rho-associated kinase (rock) directly phosphorylates pfn1 at ser-137 to prevent its binding to polyproline sequences. This negatively regulates its anti-aggregation activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates quantity
phosphorylation
|
TP53 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280108 |
Ser15 |
PSVEPPLsQETFSDL |
Homo sapiens |
|
| pmid |
sentence |
| 33297931 |
Besides, ROCK1 phosphorylated p53 at ser15 to up-regulate its protein level. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
SOX9 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162643 |
Ser181 |
YQPRRRKsVKNGQAE |
Homo sapiens |
|
| pmid |
sentence |
| 20039424 |
Rho kinase-dependent activation of sox9 in chondrocytes. In vitro, rock directly phosphorylated sox9 at ser(181), and the overexpression of rock or the activation of the rhoa pathway in sw1353 chondrosarcoma cells increased sox9(ser181) phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
MYL12A |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263073 |
Ser19 |
KRPQRATsNVFAMFD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12185584 |
Phosphorylation of myosin II regulatory light chain (MRLC) is important for cell motility and cytokinesis in nonmuscle cells. Although the regulation of monophosphorylated MRLC at serine 19 throughout the cell cycle was examined in detail, MRLC diphosphorylation at both threonine 18 and serine 19 is still unclear. Here we found that Rho-kinase has an activity for MRLC diphosphorylation in nonmuscle cells using sequential column chromatographies. we showed that the inhibition of Rho-kinase reduced diphosphorylated MRLC in the center of cells even in the presence of phosphatase inhibitor, suggesting that Rho-kinase directly diphosphorylates MRLC (red arrow in Figure 6). Taken together, we propose a model of diphosphorylation of MRLC through dual pathways of both the direct phosphorylation and the inhibition of myosin phosphatase by Rho-kinase (Figure 6). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263074 |
Thr18 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 12185584 |
Phosphorylation of myosin II regulatory light chain (MRLC) is important for cell motility and cytokinesis in nonmuscle cells. Although the regulation of monophosphorylated MRLC at serine 19 throughout the cell cycle was examined in detail, MRLC diphosphorylation at both threonine 18 and serine 19 is still unclear. Here we found that Rho-kinase has an activity for MRLC diphosphorylation in nonmuscle cells using sequential column chromatographies. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
MYL9 |
0.664 |
| 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 |
| + |
ROCK1 | up-regulates
phosphorylation
|
MYL12B |
0.641 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91542 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 12185584 |
Here we found that rho-kinase has an activity for mrlc diphosphorylation at both threonine 18 and serine 19 in nonmuscle cells using sequential column chromatographies. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91546 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 12185584 |
Here we found that rho-kinase has an activity for mrlc diphosphorylation at both threonine 18 and serine 19 in nonmuscle cells using sequential column chromatographies. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates
phosphorylation
|
MYL9 |
0.664 |
| 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 |
| + |
ROCK1 | up-regulates
phosphorylation
|
PTEN |
0.674 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134851 |
Ser229 |
VKIYSSNsGPTRRED |
Homo sapiens |
|
| pmid |
sentence |
| 15793569 |
In addition, active rhoa is able to stimulate the phospholipid phosphatase activity of pten in human embryonic kidney cells and leukocytes, and this regulation seems to require rhoa's downstream effector, rhoa-associated kinase (rock). together with the observation that individual substitution of ser 229 and thr 223 restored some of the rescuing ability (fig. 4b), we conclude that effective regulation of pten by sdf-1 may require more than one of these residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134855 |
Thr232 |
YSSNSGPtRREDKFM |
Homo sapiens |
|
| pmid |
sentence |
| 15793569 |
In addition, active rhoa is able to stimulate the phospholipid phosphatase activity of pten in human embryonic kidney cells and leukocytes, and this regulation seems to require rhoa's downstream effector, rhoa-associated kinase (rock). together with the observation that individual substitution of ser 229 and thr 223 restored some of the rescuing ability (fig. 4b), we conclude that effective regulation of pten by sdf-1 may require more than one of these residues. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Hindbrain |
| + |
ROCK1 | up-regulates
phosphorylation
|
MAPK8IP3 |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134580 |
Ser314 |
RAREKRDsRNMEVQV |
Homo sapiens |
|
| pmid |
sentence |
| 15767678 |
Identification of rock1 as an upstream activator of the jip-3 to jnk signaling axis in response to uvb damage. phosphorylation of jip-3 by rock1 was crucial for the recruitment of jnk. Inhibition of the activity of rock1 in keratinocytes resulted in decreased activation of the jnk pathway and thus a reduction in apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134584 |
Ser364 |
TRLDRTGsSPTQGIV |
Homo sapiens |
|
| pmid |
sentence |
| 15767678 |
Identification of rock1 as an upstream activator of the jip-3 to jnk signaling axis in response to uvb damage. phosphorylation of jip-3 by rock1 was crucial for the recruitment of jnk. Inhibition of the activity of rock1 in keratinocytes resulted in decreased activation of the jnk pathway and thus a reduction in apoptosis. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134588 |
Ser365 |
RLDRTGSsPTQGIVN |
Homo sapiens |
|
| pmid |
sentence |
| 15767678 |
Identification of rock1 as an upstream activator of the jip-3 to jnk signaling axis in response to uvb damage. phosphorylation of jip-3 by rock1 was crucial for the recruitment of jnk. Inhibition of the activity of rock1 in keratinocytes resulted in decreased activation of the jnk pathway and thus a reduction in apoptosis. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates
phosphorylation
|
KCNK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176025 |
Ser336 |
IPRDLSTsDTCVEQS |
Homo sapiens |
|
| pmid |
sentence |
| 21838752 |
Task1 channels contain two putative rho kinase phosphorylation sites, ser(336) and ser(393) . Mutation of ser(393) rendered task1 channels insensitive to et(a) - or et(b)-mediated current inhibition. In contrast, removal of ser(336) selectively attenuated et(a) -dependent task1 regulation without affecting the et(b) pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
ARHGAP24 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249309 |
Ser391 |
RSSMNNGsPTALSGS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249304 |
Ser402 |
LSGSKTNsPKNSVHK |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249306 |
Ser413 |
SVHKLDVsRSPPLMV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249307 |
Ser415 |
HKLDVSRsPPLMVKK |
Homo sapiens |
|
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDS‚‚PAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573‚‚577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249305 |
Ser437 |
SGIVTNGsFSSSNAE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249302 |
Ser573 |
ENSNSCRsSTTTCPE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249303 |
Ser574 |
NSNSCRSsTTTCPEQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249310 |
Thr452 |
GLEKTQTtPNGSLQA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249299 |
Thr575 |
SNSCRSStTTCPEQD |
Homo sapiens |
|
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249300 |
Thr576 |
NSCRSSTtTCPEQDF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249301 |
Thr577 |
SCRSSTTtCPEQDFF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16862148 |
ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. | As shown in Fig. 5b, ROCK stimulated the incorporation of phosphate into FilGAP. We identified seven potential phosphorylation sites in FilGAP that was isolated by preparative SDSPAGE and subjected to trypsin digestion and mass spectrometry: Ser 391, Ser 402, Ser 413, Ser 415, Ser 437, Thr 452, and a cluster of serine and threonine residues (SSTTT) at position 573577 (see Supplementary Information, Table S2). |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176029 |
Ser393 |
GLMKRRSsV |
Homo sapiens |
|
| pmid |
sentence |
| 21838752 |
Task1 channels contain two putative rho kinase phosphorylation sites, ser(336) and ser(393) . Mutation of ser(393) rendered task1 channels insensitive to et(a) - or et(b)-mediated current inhibition. In contrast, removal of ser(336) selectively attenuated et(a) -dependent task1 regulation without affecting the et(b) pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
DNM1L |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262549 |
Ser637 |
VPVARKLsAREQRDC |
Mus musculus |
|
| pmid |
sentence |
| 31063459 |
We have also previously reported that ROCK1-mediated Drp1S600 phosphorylation resulted in enhanced mitochondrial fission in podocytes |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
VIM |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248998 |
Ser72 |
SSAVRLRsSVPGVRL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9565595 |
We found that vimentin, the most widely expressed intermediate filament protein, served as an excellent substrate for Rho-associated kinase (Rho-kinase) and that vimentin phosphorylated by Rho-kinase lost its ability to form filaments in vitro. Two amino-terminal sites on vimentin, Ser38 and Ser71, were identified as the major phosphorylation sites for Rho-kinase, and Ser71 was the most favored and unique phosphorylation site for Rho-kinase in vitro. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ROCK1 | up-regulates activity
phosphorylation
|
BECN1 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278198 |
Thr119 |
LSRRLKVtGDLFDIM |
Homo sapiens |
|
| pmid |
sentence |
| 23877263 |
Beclin1 is phosphorylated by ROCK1 at T119. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ROCK1 | down-regulates
phosphorylation
|
DES |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100177 |
Thr17 |
RVSSYRRtFGGAPGF |
in vitro |
|
| pmid |
sentence |
| 12686604 |
The sites phosphorylated by Aurora-B; Thr-7/Ser-13/Ser-38 of GFAP, and Thr-16 of desmin are common with those related to Rho-associated kinase (Rho-kinase), which has been reported to phosphorylate GFAP and desmin at cleavage furrow during cytokinesis. Rho-kinase was found to phosphorylate desmin at Thr-16, Thr-75, and Thr-76 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ROCK1 |
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4.0
ROCK1
- 
- 