| + |
PRKCH | up-regulates activity 
phosphorylation
|
GSTP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276015 |
Ser185 |
SAYVGRLsARPKLKA |
in vitro |
|
| pmid |
sentence |
| 15604283 |
Peptide phosphorylation analyses and both phosphorylation and enzyme kinetic studies with GSTP1 proteins mutated at candidate amino acid residues established Ser-42 and Ser-184 as putative phospho-acceptor residues for both kinases in the GSTP1 protein. Together, these findings show PKA- and PKC-dependent phosphorylation as a significant post-translational mechanism of regulation of GSTP1 function. Together, these results further support S42 and S184 as major phosphor-acceptor residues for PKA and PKC and suggest that the increased activity of the phospho-GSTP1 was not simply a consequence of the negative charge introduced in the GSTP1 protein by the phosphate group.All eight PKC isoforms, PKC-α, PKC-βI, PKC-βII, PKC-ε, PKC-γ, PKC-η, and PKC-ζ phosphorylated the GSTP1 protein efficiently |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276014 |
Ser43 |
VETWQEGsLKASCLY |
in vitro |
|
| pmid |
sentence |
| 15604283 |
Peptide phosphorylation analyses and both phosphorylation and enzyme kinetic studies with GSTP1 proteins mutated at candidate amino acid residues established Ser-42 and Ser-184 as putative phospho-acceptor residues for both kinases in the GSTP1 protein. Together, these findings show PKA- and PKC-dependent phosphorylation as a significant post-translational mechanism of regulation of GSTP1 function. Together, these results further support S42 and S184 as major phosphor-acceptor residues for PKA and PKC and suggest that the increased activity of the phospho-GSTP1 was not simply a consequence of the negative charge introduced in the GSTP1 protein by the phosphate group.All eight PKC isoforms, PKC-α, PKC-βI, PKC-βII, PKC-ε, PKC-γ, PKC-η, and PKC-ζ phosphorylated the GSTP1 protein efficiently |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCH | down-regulates 
phosphorylation
|
GSK3A |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115730 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
| pmid |
sentence |
| 11884598 |
Furthermore, several pkc isotypes phosphorylate gsk-3 in vitro and in vivo. in the presence of atp, several isoforms (?, ___, _, ?, And of pkc phosphorylated both gsk-3? At ser 21 and gsk-3_ at ser 9 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCH | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276049 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCH | up-regulates
phosphorylation
|
ANXA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202792 |
Ser27 |
EYVQTVKsSKGGPGS |
Homo sapiens |
|
| pmid |
sentence |
| 24103589 |
The authors identified several phosphorylated residues by a combination of peptide mapping and sequence analysis and showed that recombinant pp60c-src phosphorylates annexin a1 near its amino terminus, at tyrosine 21 (tyr21). Also polyoma virus middle t/pp60c-src complex, recombinant pp50v-abl, and the egf receptor/kinase phosphorylated the same tyrosine residue. It was also shown that serine 27 residue of anxa1 is the primary site phosphorylated by protein kinase c (pkc). In the same study, the threonine 41 residue has been identified as a pkc substrate as well. The adenosine cyclic 3_,5_-phosphate dependent protein kinase a (pka) phosphorylates anxa1 in its carboxyl-terminal core at the threonine 216 residue (thr216) [2].The phosphorylation of serine 27 is essential for annexin a1 membrane localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCH |
phosphorylation
|
PTPN11 |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249137 |
Ser576 |
CAEMREDsARVYENV |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249140 |
Ser595 |
GLMQQQKsFR |
Homo sapiens |
|
| pmid |
sentence |
| 11781100 |
In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCH | up-regulates activity
phosphorylation
|
PRKD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275958 |
Ser706 |
ARIIGEKsFRRSVVG |
|
|
| pmid |
sentence |
| 12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275957 |
Ser710 |
GEKSFRRsVVGTPAY |
|
|
| pmid |
sentence |
| 12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275956 |
Ser876 |
QGLAERIsVL |
|
|
| pmid |
sentence |
| 12058027 |
Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead. |
|
| Publications: |
3 |
| + |
PRKCH | up-regulates
phosphorylation
|
PRKD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89423 |
Ser706 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
| pmid |
sentence |
| 12058027 |
Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. Our data suggest a two-step mechanism of activation of pkd2 via endogenously produced diacylglycerol and the activation of pkcs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89427 |
Ser710 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
| pmid |
sentence |
| 12058027 |
Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. Our data suggest a two-step mechanism of activation of pkd2 via endogenously produced diacylglycerol and the activation of pkcs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89431 |
Ser876 |
QGLAERIsVL |
Homo sapiens |
|
| pmid |
sentence |
| 12058027 |
Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. Our data suggest a two-step mechanism of activation of pkd2 via endogenously produced diacylglycerol and the activation of pkcs. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCH | up-regulates
phosphorylation
|
PRKD1 |
0.362 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66730 |
Ser738 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
| pmid |
sentence |
| 10197446 |
These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-66734 |
Ser742 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
| pmid |
sentence |
| 10197446 |
These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCH |
phosphorylation
|
ITGB2 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249118 |
Ser745 |
FEKEKLKsQWNNDNP |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249123 |
Thr758 |
NPLFKSAtTTVMNPK |
Homo sapiens |
Leukocyte |
| pmid |
sentence |
| 11700305 |
Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. | |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCH | down-regulates
phosphorylation
|
GSK3B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-188585 |
Ser9 |
SGRPRTTsFAESCKP |
Homo sapiens |
|
| pmid |
sentence |
| 19836308 |
Gsk3 is different from most kinases in that it is constitutively partially active and the most common regulatory mechanism is inhibition by phosphorylation of ser21 in gsk3_ or ser9 in gsk3_. This inhibitory phosphorylation can be mediated by several kinases, such as akt/protein kinase b (pkb), protein kinase c (pkc) and protein kinase a (pka). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCH | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251634 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
Vascular Endothelium |
| pmid |
sentence |
| 24379783 |
The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
staurosporine | down-regulates activity
chemical inhibition
|
PRKCH |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-258286 |
|
|
in vitro |
|
| pmid |
sentence |
| 22037378 |
Our data set represents the most detailed comprehensive assessment of the reactivity of known and clinical kinase inhibitors across the kinome published to date. | The data also show that for at least 15 of the 27 kinases that are the primary, intended targets for the compounds tested and that are represented in the assay panel, selective inhibitors, as assessed by both absolute selectivity across the kinome and selectivity relative to the primary target, are among the 72 tested here. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCH | up-regulates quantity by stabilization 
|
MCL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261908 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28939105 |
The results of our present study show that PKCη positively regulates the anti-apoptotic Bcl-2 family protein Mcl-1 by preventing its degradation via the proteasomal pathway involving Mcl-1 ubiquitin ligase Mule. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCH | up-regulates activity
phosphorylation
|
MAPK1 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261910 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 28939105 |
Protein kinase C-eta regulates Mcl-1 level via ERK1. knockdown of PKCη but not PKCα, -δ or -ε caused a significant decrease in ERK (extracellular signal-regulated kinase) phosphorylation. Knockdown of ERK1 but not ERK2 decreased Mcl-1 level, and the decrease in Mcl-1 caused by PKCη knockdown was restored by ERK1 overexpression. These results suggest that PKCη utilizes the ERK signaling pathway to protect against ubiquitin-mediated proteasomal degradation of Mcl-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1,2-diacyl-sn-glycerol | up-regulates activity
binding
|
PRKCH |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242593 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14967450 |
The molecular requirements for diacylglycerol (dag) and calcium (ca2+) to promote pkc membrane translocation, the hallmark of pkc activation, have been clarified. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKCH
- 
- 