| + |
PRKCE | down-regulates 
phosphorylation
|
BAD |
0.346 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163908 |
Ser118 |
GRELRRMsDEFVDSF |
Homo sapiens |
|
| pmid |
sentence |
| 20179209 |
Pkcs phosphorylate bad under in vitro conditions, and the association of phosphorylated bad with pkc-mu or pkc-epsilon, as shown by immunoprecipitation, indicated direct involvement of pkcs in bad phosphorylation. To confirm these results, cells overexpressing pegfp-n1, wt-bad, or bad with a single site mutated (ser112ala;ser136ala;ser155ala), two sites mutated (ser(112/136)ala;ser(112/155)ala;ser(136/155)ala), or the triple mutant were tested. Igf-i protected completely against rapamycin-induced apoptosis in cells overexpressing wt-bad and mutants having either one or two sites of phosphorylation mutated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163912 |
Ser75 |
EIRSRHSsYPAGTED |
Homo sapiens |
|
| pmid |
sentence |
| 20179209 |
Pkcs phosphorylate bad under in vitro conditions, and the association of phosphorylated bad with pkc-mu or pkc-epsilon, as shown by immunoprecipitation, indicated direct involvement of pkcs in bad phosphorylation. To confirm these results, cells overexpressing pegfp-n1, wt-bad, or bad with a single site mutated (ser112ala;ser136ala;ser155ala), two sites mutated (ser(112/136)ala;ser(112/155)ala;ser(136/155)ala), or the triple mutant were tested. Igf-i protected completely against rapamycin-induced apoptosis in cells overexpressing wt-bad and mutants having either one or two sites of phosphorylation mutated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-163916 |
Ser99 |
PFRGRSRsAPPNLWA |
Homo sapiens |
|
| pmid |
sentence |
| 20179209 |
Pkcs phosphorylate bad under in vitro conditions, and the association of phosphorylated bad with pkc-mu or pkc-epsilon, as shown by immunoprecipitation, indicated direct involvement of pkcs in bad phosphorylation. To confirm these results, cells overexpressing pegfp-n1, wt-bad, or bad with a single site mutated (ser112ala;ser136ala;ser155ala), two sites mutated (ser(112/136)ala;ser(112/155)ala;ser(136/155)ala), or the triple mutant were tested. Igf-i protected completely against rapamycin-induced apoptosis in cells overexpressing wt-bad and mutants having either one or two sites of phosphorylation mutated |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity 
phosphorylation
|
SHC1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263048 |
Ser139 |
EEWTRHGsFVNKPTR |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 12052829 |
Among them, Ser(29) in p52(Shc) (equivalent to Ser(138) in p66(Shc)) was phosphorylated only after TPA stimulation. Phosphorylation of this site together with the intact phosphotyrosine-binding domain was essential for ShcA binding to the protein-tyrosine phosphatase PTP-PEST. TPA-induced ShcA phosphorylation at this site (and hence, its association with PTP-PEST) was inhibited by a protein kinase C-specific inhibitor and was induced by overexpression of constitutively active mutants of protein kinase Calpha, -epsilon, and -delta isoforms. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCE | up-regulates
phosphorylation
|
IQGAP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172239 |
Ser1443 |
DKMKKSKsVKEDSNL |
Homo sapiens |
|
| pmid |
sentence |
| 21349850 |
Using a mass spectrometry-based assay, we show that egf induces phosphorylation of iqgap1 ser(1443), a residue known to be phosphorylated by pkcthe nonphosphorylatable iqgap1 s1441a/s1443a had no effect. In contrast, the s1441e/s1443d mutation markedly enhanced the ability of iqgap1 to induce neurite outgrowth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128718 |
Ser1443 |
DKMKKSKsVKEDSNL |
Homo sapiens |
|
| pmid |
sentence |
| 15355962 |
Using a mass spectrometry-based assay, we show that egf induces phosphorylation of iqgap1 ser(1443), a residue known to be phosphorylated by pkcthe nonphosphorylatable iqgap1 s1441a/s1443a had no effect. In contrast, the s1441e/s1443d mutation markedly enhanced the ability of iqgap1 to induce neurite outgrowth. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-133865 |
Ser1443 |
DKMKKSKsVKEDSNL |
Homo sapiens |
|
| pmid |
sentence |
| 15695813 |
Using a mass spectrometry-based assay, we show that egf induces phosphorylation of iqgap1 ser(1443), a residue known to be phosphorylated by pkcthe nonphosphorylatable iqgap1 s1441a/s1443a had no effect. In contrast, the s1441e/s1443d mutation markedly enhanced the ability of iqgap1 to induce neurite outgrowth. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
TICAM2 |
0.592 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146991 |
Ser16 |
NSCPLSLsWGKRHSV |
Homo sapiens |
|
| pmid |
sentence |
| 16757566 |
Here we show that tram is transiently phosphorylated by pkcepsilon on serine-16 our study provides a possible target for these molecules in lps signaling. Dag may activate pkc?, Leading to the phosphorylation and activation of tram. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE |
phosphorylation
|
RAB11A |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263170 |
Ser177 |
TEIYRIVsQKQMSDR |
in vitro |
|
| pmid |
sentence |
| 22188018 |
This report shows for the first time that Rab11 is differentially phosphorylated by distinct PKC isoenzymes and that this post-translational modification might be a regulatory mechanism of intracellular trafficking.Our results demonstrate that classical PKC (PKCα and PKCβII but not PKCβI) directly phosphorylate Rab11 in vitro. In addition, novel PKCε and PKCη but not PKCδ isoenzymes also phosphorylate Rab11. Mass spectrometry analysis revealed that Ser 177 is the Rab11 residue to be phosphorylated in vitro by either PKCβII or PKCε. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | up-regulates activity
phosphorylation
|
GSTP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276021 |
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-276020 |
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 |
| + |
PRKCE | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276050 |
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 |
| + |
PRKCE | down-regulates
phosphorylation
|
CTNND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171712 |
Ser268 |
PQVRVGGsSVDLHRF |
Homo sapiens |
|
| pmid |
sentence |
| 21251911 |
We find that ctnnd1/p120ctn phosphorylation at serine 268 (p-s268) occurs in a strictly pkc_-dependent manner,serine/threonine phosphorylation of p120-ctn has been reported to affect the integrity of ajs [12], [24] and [25]. Xia et al. (2003) reported that several residues (ser122, ser252, ser268, ser288, thr310, ser312, ser873, and thr910) in p120ctn can be either phosphorylated or dephosphorylated upon pkc activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201600 |
Ser268 |
PQVRVGGsSVDLHRF |
Homo sapiens |
Breast Cancer Cell, Prostate Gland Cancer Cell, Lung Cancer Cell |
| pmid |
sentence |
| 23542175 |
We find that ctnnd1/p120ctn phosphorylation at serine 268 (p-s268) occurs in a strictly pkc_-dependent manner,serine/threonine phosphorylation of p120-ctn has been reported to affect the integrity of ajs [12], [24] and [25]. Xia et al. (2003) reported that several residues (ser122, ser252, ser268, ser288, thr310, ser312, ser873, and thr910) in p120ctn can be either phosphorylated or dephosphorylated upon pkc activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity
phosphorylation
|
ALDH2 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271864 |
Ser296 |
KSPNIIMsDADMDWA |
in vitro |
|
| pmid |
sentence |
| 28056995 |
Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (epsilonPKC). |e identified S279 as a critical εPKC phosphorylation site in the activation of ALDH2. The critical catalytic site, cysteine 302 (C302) of ALDH2 is susceptible to adduct formation by reactive aldehyde, 4HNE, which readily renders the enzyme inactive. We show that phosphomimetic mutations of T185E, S279E and T412E confer protection of ALDH2 against 4HNE-induced inactivation, indicating that phosphorylation on these three sites by εPKC likely also protects the enzyme against reactive aldehydes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271865 |
Thr202 |
KLGPALAtGNVVVMK |
in vitro |
|
| pmid |
sentence |
| 28056995 |
Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (epsilonPKC). |e identified S279 as a critical εPKC phosphorylation site in the activation of ALDH2. The critical catalytic site, cysteine 302 (C302) of ALDH2 is susceptible to adduct formation by reactive aldehyde, 4HNE, which readily renders the enzyme inactive. We show that phosphomimetic mutations of T185E, S279E and T412E confer protection of ALDH2 against 4HNE-induced inactivation, indicating that phosphorylation on these three sites by εPKC likely also protects the enzyme against reactive aldehydes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271866 |
Thr429 |
MQILKFKtIEEVVGR |
in vitro |
|
| pmid |
sentence |
| 28056995 |
Post-translational enhancement of ALDH2 activity can be achieved by serine/threonine phosphorylation by epsilon protein kinase C (epsilonPKC). |e identified S279 as a critical εPKC phosphorylation site in the activation of ALDH2. The critical catalytic site, cysteine 302 (C302) of ALDH2 is susceptible to adduct formation by reactive aldehyde, 4HNE, which readily renders the enzyme inactive. We show that phosphomimetic mutations of T185E, S279E and T412E confer protection of ALDH2 against 4HNE-induced inactivation, indicating that phosphorylation on these three sites by εPKC likely also protects the enzyme against reactive aldehydes. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
PRKCE | up-regulates activity
phosphorylation
|
MIIP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273828 |
Ser303 |
YHIHRRKsFDASDTL |
Homo sapiens |
HCT-116 Cell |
| pmid |
sentence |
| 29038521 |
Here, we show that EGF stimulation induces PKCε-dependent phosphorylation of migration and invasion inhibitory protein (MIIP) at Ser303; this phosphorylation promotes the interaction between MIIP and RelA in the nucleus, by which MIIP prevents histone deacetylase 6 (HDAC6)-mediated RelA deacetylation, and thus enhances transcriptional activity of RelA and facilitates tumor metastasis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity
phosphorylation
|
GLS |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277387 |
Ser314 |
RYVGKEPsGLRFNKL |
Homo sapiens |
NCI-H1299 Cell |
| pmid |
sentence |
| 29515166 |
PKCε is the kinase that phosphorylates GAC at Ser314. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275444 |
Ser324 |
RHLSNVSsTGSIDMV |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | up-regulates activity
phosphorylation
|
NLRP5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263175 |
Ser331 |
MQRKKESsVTEFISR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19542546 |
MATER protein as substrate of PKCepsilon in human cumulus cells. we performed coimmunoprecipitation experiments using HEK293T cells expressing human MATER; a similar approach was then followed in human cumulus/follicular cells. In MATER(+)HEK293T cells, we observed that this protein acts as a phosphorylation substrate of PKCepsilon. Since PKCepsilon is known to collaborate with antiapoptotic signalling pathways, this suggests a novel mechanism for the function of MATER in follicular maturation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE |
phosphorylation
|
OPRD1 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249064 |
Ser344 |
CGRPDPSsFSRAREA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11085981 |
In the current study, we identified a PKC-mediated phosphorylation site in the delta-opioid receptor (DOR) and demonstrated that activation of PKC by stimulation of other types of GPCR or increase in intracellular Ca2+concentration in HEK 293 cells induces heterologous phosphorylation of DOR. Our results further established that DOR phosphorylation at Ser-344 by PKC results in internalization of DOR in HEK 293 cells through a beta-arrestin- and clathrin-mediated mechanism. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | up-regulates
phosphorylation
|
PRKCE |
0.271 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179412 |
Ser346 |
SEEDRSKsAPTSPCD |
Homo sapiens |
|
| pmid |
sentence |
| 18604201 |
Specifically, we have identified three phosphorylation sites within pkcepsilon that control its association with 14-3-3.kinase (ser 350), gsk3 (ser 346) and pkc itself (ser 368) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
GJA1 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144461 |
Ser365 |
IVDQRPSsRASSRAS |
Homo sapiens |
|
| pmid |
sentence |
| 16474210 |
We previously showed that follicle-stimulating hormone (fsh) promoted phosphorylation of cx43 in rat primary granulosa cells. We further identified ser365, ser368, ser369, and ser373 in the carboxy-terminal tail as the major sites of phosphorylation by fsh, and found that the phosphorylation of these residues was essential for channel activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144469 |
Ser369 |
RPSSRASsRASSRPR |
Homo sapiens |
|
| pmid |
sentence |
| 16474210 |
We previously showed that follicle-stimulating hormone (fsh) promoted phosphorylation of cx43 in rat primary granulosa cells. We further identified ser365, ser368, ser369, and ser373 in the carboxy-terminal tail as the major sites of phosphorylation by fsh, and found that the phosphorylation of these residues was essential for channel activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144473 |
Ser373 |
RASSRASsRPRPDDL |
Homo sapiens |
|
| pmid |
sentence |
| 16474210 |
We previously showed that follicle-stimulating hormone (fsh) promoted phosphorylation of cx43 in rat primary granulosa cells. We further identified ser365, ser368, ser369, and ser373 in the carboxy-terminal tail as the major sites of phosphorylation by fsh, and found that the phosphorylation of these residues was essential for channel activity. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCE | down-regulates activity
phosphorylation
|
GABRG2 |
0.235 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263174 |
Ser366 |
FVSNRKPsKDKDKKK |
in vitro |
|
| pmid |
sentence |
| 17875639 |
Protein kinase C epsilon regulates gamma-aminobutyrate type A receptor sensitivity to ethanol and benzodiazepines through phosphorylation of gamma2 subunits. Our findings indicate that PKCepsilon phosphorylation of gamma2 regulates the response of GABA(A) receptors to specific allosteric modulators, and, in particular, PKCepsilon inhibition renders these receptors sensitive to low intoxicating concentrations of ethanol. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | down-regulates activity
phosphorylation
|
GJA1 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144465 |
Ser368 |
QRPSSRAsSRASSRP |
Rattus norvegicus |
|
| pmid |
sentence |
| 10871288 |
Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication.|These data strongly suggest that PKC directly phosphorylates Cx43 on S368 in vivo, which results in a change in single channel behavior that contributes to a decrease in intercellular communication. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCE | down-regulates
phosphorylation
|
KIR3DL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158129 |
Ser415 |
QRKITRPsQRPKTPP |
Homo sapiens |
|
| pmid |
sentence |
| 17911614 |
Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
CHAT |
0.316 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129300 |
Ser464 |
LLKHVTQsSRKLIRA |
Homo sapiens |
|
| pmid |
sentence |
| 15381704 |
We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129304 |
Ser465 |
LKHVTQSsRKLIRAD |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15381704 |
We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129308 |
Ser558 |
VPTYESAsIRRFQEG |
Homo sapiens |
|
| pmid |
sentence |
| 15381704 |
We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129312 |
Ser594 |
HKAAVPAsEKLLLLK |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15381704 |
We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
PRKCE |
phosphorylation
|
RPS6KB2 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97291 |
Ser473 |
PPSGTKKsKRGRGRP |
Homo sapiens |
|
| pmid |
sentence |
| 12529391 |
Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity
phosphorylation
|
TRPV1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249141 |
Ser502 |
YFLQRRPsMKTLFVD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11884385 |
Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues. | Patch clamp analysis of the point mutants where Ser or Thr residues were replaced with Ala in the total 16 putative phosphorylation sites showed that two Ser residues, Ser(502) and Ser(800) were involved in the potentiation of the capsaicin-evoked currents by either PMA or ATP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249230 |
Ser502 |
YFLQRRPsMKTLFVD |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14523239 |
We found that mutation of S800 to alanine significantly reduced the PMA-induced enhancement of capsaicin-evoked currents and the direct activation of TRPV1 by PMA. Mutation of S502 to alanine reduced PMA enhancement of capsaicin-evoked currents, but had no effect on direct activation of TRPV1 by PMA. Conversely, mutation of T704 to alanine had no effect on PMA enhancement of capsaicin-evoked currents but dramatically reduced direct activation of TRPV1 by PMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249231 |
Ser775 |
EGVKRTLsFSLRSSR |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14523239 |
We found that mutation of S800 to alanine significantly reduced the PMA-induced enhancement of capsaicin-evoked currents and the direct activation of TRPV1 by PMA. Mutation of S502 to alanine reduced PMA enhancement of capsaicin-evoked currents, but had no effect on direct activation of TRPV1 by PMA. Conversely, mutation of T704 to alanine had no effect on PMA enhancement of capsaicin-evoked currents but dramatically reduced direct activation of TRPV1 by PMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249142 |
Ser801 |
VPLLREAsARDRQSA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11884385 |
Direct phosphorylation of capsaicin receptor VR1 by protein kinase Cepsilon and identification of two target serine residues. | Patch clamp analysis of the point mutants where Ser or Thr residues were replaced with Ala in the total 16 putative phosphorylation sites showed that two Ser residues, Ser(502) and Ser(800) were involved in the potentiation of the capsaicin-evoked currents by either PMA or ATP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249232 |
Ser801 |
VPLLREAsARDRQSA |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 14523239 |
We found that mutation of S800 to alanine significantly reduced the PMA-induced enhancement of capsaicin-evoked currents and the direct activation of TRPV1 by PMA. Mutation of S502 to alanine reduced PMA enhancement of capsaicin-evoked currents, but had no effect on direct activation of TRPV1 by PMA. Conversely, mutation of T704 to alanine had no effect on PMA enhancement of capsaicin-evoked currents but dramatically reduced direct activation of TRPV1 by PMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249233 |
Ser821 |
YLRQFSGsLKPEDAE |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14523239 |
We found that mutation of S800 to alanine significantly reduced the PMA-induced enhancement of capsaicin-evoked currents and the direct activation of TRPV1 by PMA. Mutation of S502 to alanine reduced PMA enhancement of capsaicin-evoked currents, but had no effect on direct activation of TRPV1 by PMA. Conversely, mutation of T704 to alanine had no effect on PMA enhancement of capsaicin-evoked currents but dramatically reduced direct activation of TRPV1 by PMA. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249234 |
Thr145 |
QKSKKHLtDNEFKDP |
in vitro |
|
| pmid |
sentence |
| 14523239 |
We found that mutation of S800 to alanine significantly reduced the PMA-induced enhancement of capsaicin-evoked currents and the direct activation of TRPV1 by PMA. Mutation of S502 to alanine reduced PMA enhancement of capsaicin-evoked currents, but had no effect on direct activation of TRPV1 by PMA. Conversely, mutation of T704 to alanine had no effect on PMA enhancement of capsaicin-evoked currents but dramatically reduced direct activation of TRPV1 by PMA. | Edman sequencing and scintillation counting delineated T144 as the in vitro PKC phosphorylation site |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249235 |
Thr705 |
WKLQRAItILDTEKS |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14523239 |
We found that mutation of S800 to alanine significantly reduced the PMA-induced enhancement of capsaicin-evoked currents and the direct activation of TRPV1 by PMA. Mutation of S502 to alanine reduced PMA enhancement of capsaicin-evoked currents, but had no effect on direct activation of TRPV1 by PMA. Conversely, mutation of T704 to alanine had no effect on PMA enhancement of capsaicin-evoked currents but dramatically reduced direct activation of TRPV1 by PMA. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens, Chlorocebus Aethiops, In Vitro |
| + |
PRKCE |
phosphorylation
|
KRT18 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248847 |
Ser53 |
ISVSRSTsFRGGMGS |
in vitro |
|
| pmid |
sentence |
| 1374067 |
In conclusion, we have shown that the PKCe catalytic fragment physically associates with and phosphorylates CK8/18 HT29 cells. The nature of this association and its physiological significance remain to be determined. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | down-regulates quantity by destabilization
phosphorylation
|
NREP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273830 |
Ser59 |
LGSSELRsPRISYLH |
Homo sapiens |
U-118MG Cell |
| pmid |
sentence |
| 16229809 |
Site-directed mutagenesis of S59A retarded P311 degradation and induced glioma cell motility. In contrast, S59D mutation resulted in the rapid degradation of P311 and reduced glioma cell migration.Taken together, our results show that the serine phosphorylation of P311 is dependent on the function of both PKCε and PKCz. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity
phosphorylation
|
SLC4A3 |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249127 |
Ser67 |
EKPSRSYsERDFEFH |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11739292 |
We conclude that following Ang II stimulation of cells, PKCepsilon phosphorylates serine 67 of the AE3 cytoplasmic domain, inducing the Ang II-induced increase in anion transport observed in the hypertrophic myocardium. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
PRKD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89411 |
Ser706 |
ARIIGEKsFRRSVVG |
Homo sapiens |
|
| pmid |
sentence |
| 12058027 |
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. These pkcs are activated by gastrin in ags-b cells. Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89415 |
Ser710 |
GEKSFRRsVVGTPAY |
Homo sapiens |
|
| pmid |
sentence |
| 12058027 |
In cells transfected with pkc? Or pkc? The phosphorylation of ser876 was markedly more pronounced than the phosphorylation of ser706/ser710 / the phosphorylation of ser706/ser710 in pkd2 reflects the activation of the kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89419 |
Ser876 |
QGLAERIsVL |
Homo sapiens |
|
| pmid |
sentence |
| 12058027 |
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. These pkcs are activated by gastrin in ags-b cells. Thus, pkd2 is likely to be a novel downstream target of specific pkcs upon the stimulation of ags-b cells with gastrin. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity
phosphorylation
|
PRKD2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275961 |
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-275960 |
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-275959 |
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 |
| + |
PRKCE | up-regulates
phosphorylation
|
STAT3 |
0.409 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143832 |
Ser727 |
NTIDLPMsPRTLDSL |
Homo sapiens |
|
| pmid |
sentence |
| 16418226 |
Abrogation of pkcdelta activity inhibited insulin-induced stat3 phosphorylation, pkcdelta-stat3 association and nuclear translocation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Skin |
| + |
PRKCE | down-regulates
phosphorylation
|
PRKCE |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-117324 |
Ser729 |
QEEFKGFsYFGEDLM |
Homo sapiens |
|
| pmid |
sentence |
| 11964154 |
Protein kinase-inactive mutants of pkcepsilon were not phosphorylated at ser(729) in cells, and phosphorylation of this site leads to dephosphorylation of the activation-loop thr(566) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
FGFR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201671 |
Ser779 |
PLDQYSPsFPDTRSS |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 23564461 |
Phosphorylation of serine 779 in fibroblast growth factor receptor 1 and 2 by protein kinase c(epsilon) regulates ras/mitogen-activated protein kinase signaling and neuronal differentiationour findings show that in addition to fgfr tyrosine phosphorylation, the phosphorylation of a conserved serine residue, ser(779), can quantitatively control ras/mapk signaling to promote specific cellular responses. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates
phosphorylation
|
FGFR2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-201675 |
Ser782 |
PLEQYSPsYPDTRSS |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 23564461 |
Phosphorylation of serine 779 in fibroblast growth factor receptor 1 and 2 by protein kinase c(epsilon) regulates ras/mitogen-activated protein kinase signaling and neuronal differentiation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | up-regulates activity
phosphorylation
|
GRM5 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249281 |
Ser840 |
VRSAFTTsTVVRMHV |
in vitro |
|
| pmid |
sentence |
| 15894802 |
Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249288 |
Thr841 |
RSAFTTStVVRMHVG |
in vitro |
|
| pmid |
sentence |
| 15894802 |
Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCE |
phosphorylation
|
ADAP1 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249224 |
Ser87 |
AARARFEsKVPSFYY |
|
|
| pmid |
sentence |
| 12893243 |
The sites of phosphorylation by PKCalpha on centaurin-alpha1 were identified as S87 (peptide ARFEK) and T276 (peptide WFMDDRR) ( Fig. 5). | The phosphorylation site analysis was carried out twice after phosphorylation of centaurin-alpha1 with PKCalpha and once with PKC_. A similar pattern of phosphopeptides was obtained each time. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249226 |
Thr276 |
GFRKRWFtMDDRRLM |
in vitro |
|
| pmid |
sentence |
| 12893243 |
The sites of phosphorylation by PKCalpha on centaurin-alpha1 were identified as S87 (peptide ARFEK) and T276 (peptide WFMDDRR) ( Fig. 5). | The phosphorylation site analysis was carried out twice after phosphorylation of centaurin-alpha1 with PKCalpha and once with PKC_. A similar pattern of phosphopeptides was obtained each time. |
|
| Publications: |
2 |
Organism: |
, In Vitro |
| + |
PRKCE | up-regulates activity
phosphorylation
|
PPP1R14A |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249258 |
Thr38 |
QKRHARVtVKYDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 32471307 |
A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | down-regulates activity
phosphorylation
|
KCNK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276431 |
Thr383 |
TGLHSLStFRGLMKR |
in vitro |
|
| pmid |
sentence |
| 23229553 |
We have previously shown that carbamylated PAF-induced repolarization abnormalities result from the protein kinase C (PKC) ε-dependent phosphorylation of the two-pore domain potassium channel TASK-1. Further studies identified threonine 383 in the C terminus of human and canine TASK-1 as the phosphorylation site required for PAF-dependent inhibition of the channel. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | up-regulates
phosphorylation
|
OCLN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173635 |
Thr404 |
HYETDYTtGGESCDE |
Homo sapiens |
CACO-2 Cell |
| pmid |
sentence |
| 21545357 |
Thr403, thr404, thr424 and thr438 in the occludin c-terminal domain are the predominant sites of pkc_-dependent phosphorylation . The present study demonstrates that pkc_ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173639 |
Thr424 |
IREYPPItSDQQRQL |
Homo sapiens |
|
| pmid |
sentence |
| 21545357 |
Thr403, thr404, thr424 and thr438 in the occludin c-terminal domain are the predominant sites of pkc_-dependent phosphorylation . The present study demonstrates that pkc_ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-173643 |
Thr438 |
LYKRNFDtGLQEYKS |
Homo sapiens |
|
| pmid |
sentence |
| 21545357 |
Thr403, thr404, thr424 and thr438 in the occludin c-terminal domain are the predominant sites of pkc_-dependent phosphorylation . The present study demonstrates that pkc_ phosphorylates occludin on specific threonine residues and promotes assembly of epithelial tight junctions. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PRKCE | down-regulates activity
phosphorylation
|
NOS3 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251632 |
Thr495 |
TGITRKKtFKEVANA |
Homo sapiens |
|
| 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 |
| + |
PRKCE | up-regulates
phosphorylation
|
ATF2 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195761 |
Thr52 |
HKHKHEMtLKFGPAR |
Homo sapiens |
Melanoma Cell, Skin Cancer Cell |
| pmid |
sentence |
| 22304920 |
Pkc_ phosphorylation of atf2 on thr52. Pkc_ promotes oncogenic functions of atf2 in the nucleus while blocking its apoptotic function at mitochondria |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates
phosphorylation
|
PRKCE |
0.553 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-117320 |
Thr566 |
LNGVTTTtFCGTPDY |
Homo sapiens |
|
| pmid |
sentence |
| 11964154 |
In the present study, we analysed the contribution of the phosphoinositide-dependent kinase 1 (pdk-1) and pkcepsilon kinase activity in controlling the phosphorylation of thr(566) and ser(729). pdk-1 phosphorylation of the activation loop triggers autophosphorylation of the hydrophobic motif |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
mTORC2 | up-regulates activity
phosphorylation
|
PRKCE |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276347 |
Thr710 |
TREEPVLtLVDEAIV |
Homo sapiens |
|
| pmid |
sentence |
| 21806543 |
In the present study, we have identified the mTORC2 subunit Sin1 as a direct binding partner of the PKC (protein kinase C) ε kinase domain and map the interaction to the central highly conserved region of Sin1. Exploiting the conformational dependence for PKC phosphorylation, we demonstrate that mTORC2 is essential for acute priming of PKC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCE | down-regulates activity
phosphorylation
|
GAD1 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249264 |
Thr91 |
RDARFRRtETDFSNL |
in vitro |
|
| pmid |
sentence |
| 15147202 |
We have identified one specific phosphorylation site, threonine 91 (T91), in hGAD67 that can be phosphorylated by PKA using MALDI-TOF. Site-directed mutation of T91 to alanine abolished PKA-mediated phosphorylation and inhibition of GAD activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | up-regulates activity
phosphorylation
|
MGluR |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270280 |
|
|
in vitro |
|
| pmid |
sentence |
| 15894802 |
Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
bisindolylmaleimide i | down-regulates
chemical inhibition
|
PRKCE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190353 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1,2-diacyl-sn-glycerol | up-regulates activity
binding
|
PRKCE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242590 |
|
|
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-(1-methyl-3-indolyl)-4-[1-[1-(2-pyridinylmethyl)-4-piperidinyl]-3-indolyl]pyrrole-2,5-dione | down-regulates
chemical inhibition
|
PRKCE |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191496 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TRIM41 | down-regulates quantity by destabilization
polyubiquitination
|
PRKCE |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271668 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 17893151 |
RINCK induces the ubiquitination of PKC both in vitro and in cells. Overexpression of RINCK reduces the levels of PKC in cells, whereas genetic knockdown of endogenous RINCK increases the levels of PKC. The RINCK-mediated ubiquitination is likely to be polyubiquitination, because the ubiquitinated PKCβII was detected as a high molecular weight smear. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPKAP1 | up-regulates activity
binding
|
PRKCE |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276348 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21806543 |
In the present study, we have identified the mTORC2 subunit Sin1 as a direct binding partner of the PKC (protein kinase C) ε kinase domain and map the interaction to the central highly conserved region of Sin1. Exploiting the conformational dependence for PKC phosphorylation, we demonstrate that mTORC2 is essential for acute priming of PKC. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKCE
- 
- 