| + |
PKN1 | down-regulates 
phosphorylation
|
PGAM1 |
0.257 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91602 |
Ser118 |
QVKIWRRsYDVPPPP |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-91606 |
Ser23 |
WNLENRFsGWYDADL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates activity
phosphorylation
|
MARCKS |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-243199 |
Ser159 |
KKKKKRFsFKKSFKL |
in vitro |
|
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249651 |
Ser163 |
KRFSFKKsFKLSGFS |
in vitro |
|
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249671 |
Ser170 |
SFKLSGFsFKKNKKE |
in vitro |
|
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PKN1 |
phosphorylation
|
MARCKS |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248937 |
Ser159 |
KKKKKRFsFKKSFKL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248938 |
Ser163 |
KRFSFKKsFKLSGFS |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248939 |
Ser170 |
SFKLSGFsFKKNKKE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 8557118 |
PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |
|
| Publications: |
3 |
Organism: |
Chlorocebus Aethiops |
| + |
PKN1 | down-regulates activity
phosphorylation
|
MEFV |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275462 |
Ser208 |
VRLRRNAsSAGRLQG |
Mus musculus |
Bone Marrow-derived Macrophage |
| pmid |
sentence |
| 27270401 |
PKNs bind to human pyrin and phosphorylate S208 and S242. Pyrin forms an inflammasome when mutant or in response to bacterial modification of the GTPase RhoA. We found that RhoA activated the serine-threonine kinases PKN1 and PKN2 that bind and phosphorylate pyrin. Phosphorylated pyrin bound to 14-3-3 proteins, regulatory proteins that in turn blocked the pyrin inflammasome. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275461 |
Ser242 |
SGKMRPRsLEVTIST |
Mus musculus |
Bone Marrow-derived Macrophage |
| pmid |
sentence |
| 27270401 |
PKNs bind to human pyrin and phosphorylate S208 and S242. Pyrin forms an inflammasome when mutant or in response to bacterial modification of the GTPase RhoA. We found that RhoA activated the serine-threonine kinases PKN1 and PKN2 that bind and phosphorylate pyrin. Phosphorylated pyrin bound to 14-3-3 proteins, regulatory proteins that in turn blocked the pyrin inflammasome. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
PKN1 |
phosphorylation
|
CDC25C |
0.51 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249277 |
Ser216 |
SGLYRSPsMPENLNR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15791647 |
A role for PKN1 in mediating arsenite-induced G(2)/M delay was supported by the finding that expression of a constitutively active form of PKN1 (PKN1AF3) in HeLa cells delayed the mitotic entry of cell cycle. Further experiments indicate that PKN1 directly phosphorylated serine 216 (Ser216) in Cdc25C, which then facilitated association between Cdc25C and 14-3-3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates 
phosphorylation
|
SNAI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135609 |
Ser246 |
QACARTFsRMSLLHK |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 15833848 |
Pak1 phosphorylation of snail, a master regulator of epithelial-to-mesenchyme transition, modulates snail's subcellular localization and functionswe found for the first time that pak1 promotes transcription repression activity of snail from e-cadherin, occludin, and aromatase promoters. Pak1 regulates the repressor activity of snail by phosphorylating on ser(246). Pak1 phosphorylation of snail supports snail's accumulation in the nucleus as well as its repressor functions. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates
phosphorylation
|
FOXO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97882 |
Ser256 |
SPRRRAAsMDNNSKF |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12560069 |
Furthermore, estrogen induced phosphorylation and perinuclear localization of the cell survival forkhead transcription factor fkhr in the cytoplasm in a pak1-dependent manner. In addition, pak1 directly interacted with fkhr and phosphorylated it. The noticed phosphorylation-dependent exclusion of fkhr from the nucleus impaired the ability of fkhr to activate its target fas ligand promoter containing the fkhr binding motif (fre) in cells treated with estrogen or expressing catalytically active pak1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates
phosphorylation
|
FOXO |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252968 |
Ser256 |
SPRRRAAsMDNNSKF |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 12560069 |
Furthermore, estrogen induced phosphorylation and perinuclear localization of the cell survival forkhead transcription factor fkhr in the cytoplasm in a pak1-dependent manner. In addition, pak1 directly interacted with fkhr and phosphorylated it. The noticed phosphorylation-dependent exclusion of fkhr from the nucleus impaired the ability of fkhr to activate its target fas ligand promoter containing the fkhr binding motif (fre) in cells treated with estrogen or expressing catalytically active pak1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates
phosphorylation
|
RAF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-112549 |
Ser338 |
RPRGQRDsSYYWEIE |
Homo sapiens |
|
| pmid |
sentence |
| 11733498 |
Interaction between active pak1 and raf-1 is necessary for phosphorylation and activation of raf-1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135679 |
Ser339 |
PRGQRDSsYYWEIEA |
Homo sapiens |
|
| pmid |
sentence |
| 15849194 |
P21-activated kinase 1 (pak1)-dependent phosphorylation of raf-1 regulates its mitochondrial localization, phosphorylation of bad, and bcl-2 association. moreover, the mitochondrial translocation of raf-1 and the interaction between raf-1 and bcl-2 are regulated by raf-1 phosphorylation at ser-338/ser-339. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates activity
phosphorylation
|
PKN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249021 |
Ser374 |
GLYSRSGsLSGRSSL |
in vitro |
|
| pmid |
sentence |
| 10467162 |
Autophosphorylation of wild-type PKN increased the protein kinase activity, however, substitution of Thr64, Ser374, or Thr531 in the regulatory region of PKN with alanine, abolished this effect. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249020 |
Thr531 |
PNATGTGtFSPGASP |
in vitro |
|
| pmid |
sentence |
| 10467162 |
Autophosphorylation of wild-type PKN increased the protein kinase activity, however, substitution of Thr64, Ser374, or Thr531 in the regulatory region of PKN with alanine, abolished this effect. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249019 |
Thr64 |
ENLRRATtDLGRSLG |
in vitro |
|
| pmid |
sentence |
| 10467162 |
Autophosphorylation of wild-type PKN increased the protein kinase activity, however, substitution of Thr64, Ser374, or Thr531 in the regulatory region of PKN with alanine, abolished this effect. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CDK1 | up-regulates activity
phosphorylation
|
PKN1 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276834 |
Ser533 |
ATGTGTFsPGASPGS |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31981797 |
CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276833 |
Ser537 |
GTFSPGAsPGSEART |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31981797 |
CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276831 |
Ser562 |
LGTDSDSsPQKSSRD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31981797 |
CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276832 |
Ser916 |
TGEAPTLsPPRDARP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 31981797 |
CDK1 phosphorylates PKN1 at S533, S537, S562, and S916 in vitro and in cells during drug-induced mitotic arrest. Immunofluorescence staining further confirmed that PKN1 phosphorylation occurs during normal mitosis in a CDK1-dependent manner.Knockdown of PKN1 significantly inhibited anchorage-independent growth and migration without affecting proliferation in multiple cancer cell lines. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates
phosphorylation
|
MAPT |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84958 |
Ser637 |
VDLSKVTsKCGSLGN |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11104762 |
Phosphorylation of tau is regulated by pknthere is a pkn-specific phosphorylation site, ser-320, in mbdsthus pkn serves as a regulator of microtubules by specific phosphorylation of tau, which leads to disruption of tubulin assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
PKN1 | down-regulates
phosphorylation
|
ARHGEF2 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122191 |
Ser886 |
PVDPRRRsLPAGDAL |
Homo sapiens |
|
| pmid |
sentence |
| 14970201 |
Here we identify a region in the carboxyl terminus of gef-h1 that is important for suppression of its guanine nucleotide exchange activity by microtubules. This portion of the protein includes a coiled-coil motif, a proline-rich motif that may interact with src homology 3 domain-containing proteins, and a potential binding site for 14-3-3 proteins. We show that phosphorylation of gef-h1 at ser(885) by pak1 induces 14-3-3 binding to the exchange factor and relocation of 14-3-3 to microtubules. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates
phosphorylation
|
PGM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128722 |
Thr467 |
SANDKVYtVEKADNF |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 15378030 |
Pak1-mediated phosphorylation of pgm selectively on threonine 466 significantly increased pgm enzymatic activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates activity
phosphorylation
|
EGFR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174755 |
Thr678 |
RHIVRKRtLRRLLQE |
Homo sapiens |
|
| pmid |
sentence |
| 21749319 |
This identified thr654 in egfr as the pkn1 phosphorylation siteit has been shown that the phosphorylation of egfr at thr654 by pkc reduces the tyrosine kinase activity of the receptor |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates
phosphorylation
|
PKN1 |
0.547 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76640 |
Thr774 |
GYGDRTStFCGTPEF |
Homo sapiens |
|
| pmid |
sentence |
| 10753910 |
It is shown that activation in vitro and in vivo involves the activation loop phosphorylation of prk1/2 by 3-phosphoinositide-dependent protein kinase-1 (pdk1) /pdk1 phosphorylates the prks at their conserved activation loop threonines (thr-774 and thr-816 for prk1 and prk2, respectively) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates
phosphorylation
|
MAP3K20 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152768 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17251915 |
Phosphorylation of mltkalpha by pknalpha enhances its kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates
phosphorylation
|
MAPK14 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152765 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17251915 |
At the same time, rho signals to c-jun n-terminal kinase (jnk) and p38 through rock and protein kinase n (pkn), leading to the transcriptional regulation of jun |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | down-regulates
phosphorylation
|
PGAM |
0.331 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270282 |
|
|
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12189148 |
Activated pak1 inhibits glycolysis by association of its catalytic domain with pgam-b and subsequent phosphorylation of the enzyme on serine residues 23 and 118, thereby abolishing pgam activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PKN1 | up-regulates
phosphorylation
|
AR |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-152762 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17251915 |
Rho can sensitize the ar to low levels of circulating androgens by promoting the nuclear translocation of a transcriptional co-activator, fhl2 (four and a half lim domains 2), which binds ar, and by stimulating protein kinase n (pkn), which phosphorylates ar directly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IPA-3 | down-regulates activity
chemical inhibition
|
PKN1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262017 |
|
|
Homo sapiens |
Hepatobiliary Carcinoma Cell |
| pmid |
sentence |
| 23894351 |
In the current study, an allosteric small molecule PAK1 inhibitor, IPA-3, was evaluated for the potential in suppressing hepatocarcinogenesis. Consistent with other reports, inhibition of PAK1 activity was observed in several human HCC cell lines treated with various dosages of IPA-3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RHOA | up-regulates activity
binding
|
PKN1 |
0.847 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275465 |
|
|
Mus musculus |
Bone Marrow-derived Macrophage |
| pmid |
sentence |
| 27270401 |
PKNs bind to human pyrin and phosphorylate S208 and S242. Pyrin forms an inflammasome when mutant or in response to bacterial modification of the GTPase RhoA. We found that RhoA activated the serine-threonine kinases PKN1 and PKN2 that bind and phosphorylate pyrin. Phosphorylated pyrin bound to 14-3-3 proteins, regulatory proteins that in turn blocked the pyrin inflammasome. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
PKN1
- 
- 