+ |
LIMK2 | down-regulates activity
phosphorylation
|
SPOP |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278339 |
Ser171 |
VQDSVNIsGQNTMNM |
Homo sapiens |
|
pmid |
sentence |
33311589 |
LIMK2 phosphorylates SPOP at S59, S171 and S226.|Together, these results depict that LIMK2-mediated SPOP degradation is a key mechanism that regulates AR stability. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278338 |
Ser226 |
AARSPVFsAMFEHEM |
Homo sapiens |
|
pmid |
sentence |
33311589 |
LIMK2 phosphorylates SPOP at S59, S171 and S226.|Together, these results depict that LIMK2-mediated SPOP degradation is a key mechanism that regulates AR stability. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278337 |
Ser59 |
IKSSTFSsGANDKLK |
Homo sapiens |
|
pmid |
sentence |
33311589 |
LIMK2 phosphorylates SPOP at S59, S171 and S226.|Together, these results depict that LIMK2-mediated SPOP degradation is a key mechanism that regulates AR stability. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
LIMK2 | down-regulates activity
phosphorylation
|
NKX3-1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278951 |
Ser185 |
KTKRKQLsSELGDLE |
Homo sapiens |
|
pmid |
sentence |
34066036 |
LIMK2 also downregulates NKX3.1 mRNA levels.|While WT-NKX3.1 was efficiently phosphorylated, the S185A mutant showed no phosphorylation ( xref A), confirming that LIMK2 only phosphorylates the S185 site in NKX3.1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCD | down-regulates
phosphorylation
|
LIMK2 |
0.256 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-137927 |
Ser283 |
EGTLRRRsLRRSNSI |
Homo sapiens |
|
pmid |
sentence |
15923181 |
Activation of pkc by phorbol ester treatment of endothelial cells stimulated limk2 phosphorylation at ser-283 and inhibited nuclear import of limk2 |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-147716 |
Ser283 |
EGTLRRRsLRRSNSI |
Homo sapiens |
|
pmid |
sentence |
16820362 |
Recently we have shown that limk2 shuttles between cytoplasm and nucleus in endothelial cells and that nuclear import is inhibited by protein kinase c-mediated phosphorylation of ser-283. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
LIMK2 | down-regulates activity
phosphorylation
|
CFL1 |
0.765 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-105098 |
Ser3 |
sGVAVSDG |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
11171090 |
We report here that limk1 and limk2 phosphorylate both cofilin and actin-depolymerizing factor (adf) specifically at ser-3 and exhibit partially distinct substrate specificity when tested using site-directed cofilin mutants as substrates |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ROCK1 | up-regulates
phosphorylation
|
LIMK2 |
0.632 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-82755 |
Thr505 |
NDRKKRYtVVGNPYW |
Homo sapiens |
|
pmid |
sentence |
11018042 |
Specific activation of lim kinase 2 via phosphorylation of threonine 505 by rock, a rho-dependent protein kinase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDC42BPA | up-regulates activity
phosphorylation
|
LIMK2 |
0.396 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-107584 |
Thr505 |
NDRKKRYtVVGNPYW |
Chlorocebus aethiops |
COS Cell |
pmid |
sentence |
11340065 |
These results indicate that mrckalpha phosphorylates and activates lim kinases downstream of cdc42, which in turn regulates the actin cytoskeletal reorganization through the phosphorylation and inactivation of adf/cofilin. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
ROCK1 | up-regulates activity
phosphorylation
|
LIMK2 |
0.632 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249053 |
Thr526 |
NGKSYDEtVDIFSFG |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
11018042 |
Specific Activation of LIM kinase 2 via Phosphorylation of Threonine 505 by ROCK, a Rho-dependent Protein Kinase |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
LIMK2 | up-regulates activity
phosphorylation
|
SRPK1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-279625 |
|
|
Homo sapiens |
|
pmid |
sentence |
32859889 |
In vitro kinase assays revealed that LIMK2 phosphorylates SRPK1 (Fig. xref ).|LIMK2 promotes the metastatic progression of triple-negative breast cancer by activating SRPK1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LIMK2 | up-regulates quantity
phosphorylation
|
TWIST1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278952 |
|
|
Homo sapiens |
|
pmid |
sentence |
30716360 |
LIMK2 directly phosphorylated TWIST1, indicating that LIMK2 also regulates TWIST1 post-translationally (XREF_FIG).|LIMK2 positively regulates TWIST1 protein levels. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LIMK2 | down-regulates activity
phosphorylation
|
PTEN |
0.274 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-278363 |
|
|
Homo sapiens |
|
pmid |
sentence |
32931887 |
LIMK2 inhibits PTEN phosphatase activity in vitro and in cells.|PTEN phosphorylation and downregulation by LIMK2 promotes tumorigenesis and EMT in vivo. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |