+ |
LIMK1 | down-regulates
phosphorylation
|
CFL1 |
0.808 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-159885 |
Ser3 |
sGVAVSDG |
Homo sapiens |
|
pmid |
sentence |
18079118 |
Our results suggest that limk1-mediated cofilin phosphorylation is required for accurate spindle orientation by stabilizing cortical actin networks during mitosis |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LIMK1 | down-regulates activity
phosphorylation
|
CFL2 |
0.691 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-58596 |
Ser3 |
sGVTVNDE |
Homo sapiens |
|
pmid |
sentence |
9655398 |
Cofilin is known to be a potent regulator of actin filament dynamics, and its ability to bind and depolymerize actin is abolished by phosphorylation of serine residue at 3;. Here we show that lim-kinase 1 (limk-1), a serine/threonine kinase containing lim and pdz domains, phosphorylates cofilin at ser 3, both in vitro and in vivo |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AURKA | up-regulates activity
phosphorylation
|
LIMK1 |
0.265 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276399 |
Ser307 |
DRSPGAGsLGSPASQ |
in vitro |
|
pmid |
sentence |
22214762 |
Here, we report a novel functional cooperativity between Aur-A and LIMK1 through mutual phosphorylation. LIMK1 is recruited to the centrosomes during early prophase and then to the spindle poles, where it colocalizes with Aur-A. Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization. Aur-A also acts as a substrate of LIMK1, and the function of LIMK1 is important for its specific localization and regulation of spindle morphology. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
MAPKAPK2 | up-regulates
phosphorylation
|
LIMK1 |
0.366 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144333 |
Ser323 |
KDLGRSEsLRVVCRP |
Homo sapiens |
|
pmid |
sentence |
16456544 |
Mk2 activated limk1 by phosphorylation at ser-323. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC42BPA | up-regulates activity
phosphorylation
|
LIMK1 |
0.413 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250721 |
Thr508 |
PDRKKRYtVVGNPYW |
|
HeLa Cell |
pmid |
sentence |
11340065 |
Activation of LIM kinases by myotonic dystrophy kinase-related Cdc42-binding kinase alpha. \ In vitro, MRCKalpha phosphorylated the protein kinase domain of LIM kinases, and the site in LIMK2 phosphorylated by MRCKalpha proved to be threonine 505 within the activation segment. |
|
Publications: |
1 |
+ |
PAK1 | up-regulates activity
phosphorylation
|
LIMK1 |
0.597 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-72142 |
Thr508 |
PDRKKRYtVVGNPYW |
Homo sapiens |
|
pmid |
sentence |
10559936 |
Activation of lim-kinase by pak1 couplesp21-activated kinase (pak1) phosphorylates lim-kinase at threonine residue 508 within lim-kinase's activation loop |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ROCK1 | up-regulates activity
phosphorylation
|
LIMK1 |
0.6 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-74569 |
Thr508 |
PDRKKRYtVVGNPYW |
Homo sapiens |
|
pmid |
sentence |
10652353 |
Rho-associated kinase rock activates lim-kinase 1 by phosphorylation at threonine 508 within the activation loop. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPRG | down-regulates activity
dephosphorylation
|
LIMK1 |
0.263 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254711 |
Tyr507 |
KPDRKKRyTVVGNPY |
in vitro |
|
pmid |
sentence |
25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
LIMK1 | up-regulates activity
phosphorylation
|
AURKA |
0.265 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-276400 |
|
|
in vitro |
|
pmid |
sentence |
22214762 |
Here, we report a novel functional cooperativity between Aur-A and LIMK1 through mutual phosphorylation. LIMK1 is recruited to the centrosomes during early prophase and then to the spindle poles, where it colocalizes with Aur-A. Aur-A physically associates with LIMK1 and activates it through phosphorylation, which is important for its centrosomal and spindle pole localization. Aur-A also acts as a substrate of LIMK1, and the function of LIMK1 is important for its specific localization and regulation of spindle morphology. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
SSH1 | down-regulates activity
dephosphorylation
|
LIMK1 |
0.616 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277096 |
|
|
Homo sapiens |
|
pmid |
sentence |
23153585 |
In addition to its cofilin\u2013phosphatase activity, SSH1 can also dephosphorylate LIMK1 and LIMK2, although LIMK1 is a better substrate than LIMK2 [63] .|SSH1 suppresses the kinase activity of LIMK1 toward cofilin by dephosphorylation at Thr 508 in the kinase catalytic domain and other autophosphorylated residues [63]. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
dabrafenib | down-regulates activity
chemical inhibition
|
LIMK1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259216 |
|
|
in vitro |
|
pmid |
sentence |
24720932 |
Dabrafenib is known to inhibit V600E, V600K and V600D BRAF enzymes with in vitro IC50 values of 0.65, 0.5 and 1.84 nM, respectively. Dabrafenib can inhibit wild-type BRAF and CRAF kinases with IC50 values of 3.2 and 5.0 nM. Other kinases (SIK1, NEK111 and LIMK1) can be inhibited by dabrafenib when administered in high concentrations |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
RNF6 | down-regulates quantity by destabilization
polyubiquitination
|
LIMK1 |
0.444 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271481 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16204183 |
Consistent with a role in axonal growth, we found that Rnf6 binds to, polyubiquitinates, and targets LIMK1 for proteasomal degradation in growth cones of primary hippocampal neurons. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |