+ |
DAPK3 | up-regulates quantity by stabilization
phosphorylation
|
MDM2 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-123159 |
Ser166 |
SSRRRAIsETEENSD |
Homo sapiens |
|
pmid |
sentence |
15001356 |
Zip kinase was able to phosphorylate mdm2 at ser166, a site previously reported to be modified by akt kinase, thus demonstrating that zip kinase is a bona fide mdm2-binding protein. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DAPK3 | up-regulates
phosphorylation
|
TP53 |
0.415 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-153495 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
B-lymphocyte |
pmid |
sentence |
17339337 |
A cell-free ser(20) phosphorylation site assay was used to identify a broad range of calcium calmodulin kinase superfamily members, including chk2, chk1, dapk-1, dapk-3, drak-1, and ampk, as ser(20) kinases.Evaluation of these calcium calmodulin kinase superfamily members as candidate ser(20) kinases in vivo has shown that only chk1 or dapk-1 can stimulate p53 transactivation and induce ser(20) phosphorylation of p53. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DAPK3 | up-regulates
phosphorylation
|
MYL9 |
0.501 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-188789 |
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-188793 |
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 |
+ |
DAPK3 | up-regulates
phosphorylation
|
MYL12B |
0.526 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-16043 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
pmid |
sentence |
1178183 |
Hzipk phosphorylated the regulatory light chain of myosin ii (mrlc) at both ser19 and thr18 in vitro. Phosphorylation of mrlc is required to generate the driving force in the migration of the cells but not necessary for localization of myosin ii at the leading edge. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-95524 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
pmid |
sentence |
12429016 |
Hzipk phosphorylated the regulatory light chain of myosin ii (mrlc) at both ser19 and thr18 in vitro. Phosphorylation of mrlc is required to generate the driving force in the migration of the cells but not necessary for localization of myosin ii at the leading edge. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-16047 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
pmid |
sentence |
1178183 |
Hzipk phosphorylated the regulatory light chain of myosin ii (mrlc) at both ser19 and thr18 in vitro. Phosphorylation of mrlc is required to generate the driving force in the migration of the cells but not necessary for localization of myosin ii at the leading edge. |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
DAPK3 | up-regulates
phosphorylation
|
DAPK3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132455 |
Ser311 |
EYTIKSHsSLPPNNS |
Homo sapiens |
|
pmid |
sentence |
15611134 |
Zipk autophosphorylates in vitrowe have identified six phosphorylation sites in zipk that regulate both its enzyme activity and localization, including thr180, thr225, thr265, thr299, thr306, and ser311. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132459 |
Thr180 |
EFKNIFGtPEFVAPE |
Homo sapiens |
|
pmid |
sentence |
15611134 |
Mutational analysis showed that phosphorylation of thr180 in the kinase activation t-loop, thr225 in the substrate-binding groove, and thr265 in kinase subdomain x is essential for full zipk autophosphorylation and activity toward exogenous substrates. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132463 |
Thr225 |
LGETKQEtLTNISAV |
Homo sapiens |
|
pmid |
sentence |
15611134 |
Mutational analysis showed that phosphorylation of thr180 in the kinase activation t-loop, thr225 in the substrate-binding groove, and thr265 in kinase subdomain x is essential for full zipk autophosphorylation and activity toward exogenous substrates. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132467 |
Thr265 |
KDPKRRMtIAQSLEH |
Homo sapiens |
|
pmid |
sentence |
15611134 |
Mutational analysis showed that phosphorylation of thr180 in the kinase activation t-loop, thr225 in the substrate-binding groove, and thr265 in kinase subdomain x is essential for full zipk autophosphorylation and activity toward exogenous substrates. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132471 |
Thr299 |
PERRRLKtTRLKEYT |
Homo sapiens |
|
pmid |
sentence |
15611134 |
Zipk autophosphorylates in vitrowe have identified six phosphorylation sites in zipk that regulate both its enzyme activity and localization, including thr180, thr225, thr265, thr299, thr306, and ser311.Abrogation of phosphorylation of thr299, thr306, and ser311 had little effect on enzyme activity, but mutation of thr299 and thr300 to alanine resulted in redistribution of zipk from the cytosol to the nucleus |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-132475 |
Thr306 |
TTRLKEYtIKSHSSL |
Homo sapiens |
|
pmid |
sentence |
15611134 |
Zipk autophosphorylates in vitrowe have identified six phosphorylation sites in zipk that regulate both its enzyme activity and localization, including thr180, thr225, thr265, thr299, thr306, and ser311 |
|
Publications: |
6 |
Organism: |
Homo Sapiens |
+ |
DAPK3 | up-regulates
phosphorylation
|
RPL13A |
0.413 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182117 |
Ser77 |
PYHFRAPsRIFWRTV |
Homo sapiens |
Macrophage |
pmid |
sentence |
18995835 |
Zipk phosphorylates l13a in vitro / l13a is phosphorylated on ser77 in vitro |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DAPK3 | up-regulates quantity by stabilization
phosphorylation
|
CDKN1A |
0.321 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251085 |
Thr145 |
QGRKRRQtSMTDFYH |
in vitro |
|
pmid |
sentence |
15001356 |
ZIP kinase phosphorylates p21(WAF1) at Thr145 and alanine-substituted mutations in the p21(WAF1) phosphorylation site alter its ability to be phosphorylated by ZIP kinase. | Transfected ZIPK can promote the phosphorylation of p21(WAF1) at Thr145 in vivo and can increase the half-life of p21(WAF1) |
|
Publications: |
1 |
Organism: |
In Vitro |