| + |
PRKCZ | down-regulates quantity by destabilization 
phosphorylation
|
YAP1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276876 |
Ser109 |
KSHSRQAsTDAGTAG |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25660024 |
Yap and β-catenin are direct substrates of PKCζ.We show here that PKCζ suppresses intestinal stem cell function by promoting the downregulation of β-catenin and Yap through direct phosphorylation.Consistent with MS/MS analysis, mutation to alanine of these two sites completely abolished Yap phosphorylation by PKCζ. Interestingly, S109 and T110 sites were highly conserved among species (Figure S3B), which suggested an important role in Yap regulation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276877 |
Thr110 |
SHSRQAStDAGTAGA |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25660024 |
Yap and β-catenin are direct substrates of PKCζ.We show here that PKCζ suppresses intestinal stem cell function by promoting the downregulation of β-catenin and Yap through direct phosphorylation.Consistent with MS/MS analysis, mutation to alanine of these two sites completely abolished Yap phosphorylation by PKCζ. Interestingly, S109 and T110 sites were highly conserved among species (Figure S3B), which suggested an important role in Yap regulation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates 
phosphorylation
|
AQP9 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176278 |
Ser11 |
EGAEKGKsFKQRLVL |
Homo sapiens |
|
| pmid |
sentence |
| 21873454 |
Wt-pkc_-mediated phosphorylation of wt aqp9 in vitro. In the experiments, substitution of ser11 to ala markedly inhibited phosphorylation. the s11a mutation in fibroblasts caused a smoother cell periphery with fewer aqp9-induced filopodia |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates quantity by destabilization
phosphorylation
|
IRS1 |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236022 |
Ser1101 |
GCRRRHSsETFSSTP |
Homo sapiens |
|
| pmid |
sentence |
| 17360977 |
Tyrosine phosphorylation of IRS-1 initiates insulin signaling, whereas serine/threonine phosphorylation alters the ability of IRS-1 to transduce the insulin signalInsulin increased the phosphorylation of Ser312, Ser616, Ser636, Ser892, Ser1101, and Ser1223 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
PRKCZ | down-regulates
phosphorylation
|
CASP9 |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-141629 |
Ser144 |
GDVGALEsLRGNADL |
Homo sapiens |
|
| pmid |
sentence |
| 16287866 |
Inhibitor sensitivity and interactions with caspase 9 indicate that the predominant kinase that targets ser144 is the atypical protein kinase c isoform zeta (pkczeta). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
ATP1A1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263181 |
Ser16 |
KYEPAAVsEQGDKKG |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 12671055 |
Na,K-ATPase alpha(1) subunit was phosphorylated by PKC in hypoxia-treated AEC. In AEC treated with a PKC-zeta antagonist peptide or with the Na,K-ATPase alpha(1) subunit lacking the PKC phosphorylation site (Ser-18), hypoxia failed to decrease Na,K-ATPase abundance and function. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
IKBKB |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249015 |
Ser177 |
AKELDQGsLCTSFVG |
Homo sapiens |
|
| pmid |
sentence |
| 10022904 |
Activation of IkappaB kinase beta by protein kinase C isoforms. | Interestingly, recombinant active zetaPKC and alphaPKC are able to stimulate in vitro the activity of IKKbeta but not that of IKKalpha. In addition, evidence is presented here that recombinant zetaPKC directly phosphorylates IKKbeta in vitro, involving Ser177 and Ser181. Collectively, these results demonstrate a critical role for the PKC isoforms in the NF-kappaB pathway at the level of IKKbeta activation and IkappaB degradation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249016 |
Ser181 |
DQGSLCTsFVGTLQY |
Homo sapiens |
|
| pmid |
sentence |
| 10022904 |
Activation of IkappaB kinase beta by protein kinase C isoforms. | Interestingly, recombinant active zetaPKC and alphaPKC are able to stimulate in vitro the activity of IKKbeta but not that of IKKalpha. In addition, evidence is presented here that recombinant zetaPKC directly phosphorylates IKKbeta in vitro, involving Ser177 and Ser181. Collectively, these results demonstrate a critical role for the PKC isoforms in the NF-kappaB pathway at the level of IKKbeta activation and IkappaB degradation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates quantity by destabilization
phosphorylation
|
PIAS4 |
0.501 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275513 |
Ser18 |
MVMSFRVsDLQMLLG |
|
|
| pmid |
sentence |
| 27162139 |
In this study, we discovered a new protein isoform encoded by KIAA0317, termed fibrosis-inducing E3 ligase 1 (FIEL1), which potently stimulates the TGFbeta signaling pathway through the site-specific ubiquitination of PIAS4.FIEL1 targets PIAS4 using a double locking mechanism that is facilitated by the kinases PKCzeta and GSK3beta. Specifically, PKCzeta phosphorylation of PIAS4 and GSK3beta phosphorylation of FIEL1 are both essential for the degradation of PIAS4.|These experiments suggested that PKCzeta is an authentic regulator of PIAS4 protein stability; Q21 and phosphorylated S18 of PIAS4 are both required for FIEL1 interaction. |
|
| Publications: |
1 |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
BAX |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-155111 |
Ser184 |
VAGVLTAsLTIWKKM |
Homo sapiens |
|
| pmid |
sentence |
| 17525161 |
Protein kinase czeta abrogates the proapoptotic function of bax through phosphorylation. Overexpression of wild type or the constitutively active a119d but not the dominant negative k281w pkczeta mutant results in bax phosphorylation at serine 184. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
GSTP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276017 |
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-276016 |
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 |
| + |
PRKCZ | down-regulates
phosphorylation
|
MYH10 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146100 |
Ser1937 |
RGGPISFsSSRSGRR |
Homo sapiens |
|
| pmid |
sentence |
| 16611744 |
After egf stimulation, apkc_ translocates from the nucleus to the cytoplasm (figure 3) and is therefore able to interact with myosin ii-b. apkc_ phosphorylates nmhc ii-b on ser1937, which is located on the nonhelical tailpiece, leading to filament disassembly at certain sites of the cell |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
ADARB1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277392 |
Ser211 |
GDLSLSAsPVPASLA |
Homo sapiens |
Colorectal Cancer Cell |
| pmid |
sentence |
| 29694894 |
Here, we identified ADAR2 as a direct substrate of PKCζ in CRC cells. Phosphorylation of ADAR2 regulates its editing activity, which is required to maintain miR-200 steady-state levels, suggesting that the PKCζ/ADAR2 axis regulates miR-200 secretion through RNA editing. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277391 |
Ser216 |
SASPVPAsLAQPPLP |
Homo sapiens |
Colorectal Cancer Cell |
| pmid |
sentence |
| 29694894 |
Here, we identified ADAR2 as a direct substrate of PKCζ in CRC cells. Phosphorylation of ADAR2 regulates its editing activity, which is required to maintain miR-200 steady-state levels, suggesting that the PKCζ/ADAR2 axis regulates miR-200 secretion through RNA editing. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
PTPN7 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276047 |
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 |
| + |
PRKCZ | down-regulates quantity by destabilization
phosphorylation
|
SNAI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277437 |
Ser249 |
ARTFSRMsLLHKHQE |
Homo sapiens |
MCF-10A Cell |
| pmid |
sentence |
| 30804505 |
APKC kinases phosphorylate S249 of SNAI1, which leads to protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates
phosphorylation
|
NCF1 |
0.402 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89252 |
Ser303 |
RGAPPRRsSIRNAHS |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89260 |
Ser304 |
GAPPRRSsIRNAHSI |
Homo sapiens |
|
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89264 |
Ser315 |
AHSIHQRsRKRLSQD |
Homo sapiens |
|
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89268 |
Ser320 |
QRSRKRLsQDAYRRN |
Homo sapiens |
|
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89272 |
Ser328 |
QDAYRRNsVRFLQQR |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89280 |
Ser359 |
EERQTQRsKPQPAVP |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89284 |
Ser370 |
PAVPPRPsADLILNR |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-89288 |
Ser379 |
DLILNRCsESTKRKL |
Homo sapiens |
Neutrophil |
| pmid |
sentence |
| 12056906 |
Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation. |
|
| Publications: |
8 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates
phosphorylation
|
STK11 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185640 |
Ser307 |
IRQIRQHsWFRKKHP |
Homo sapiens |
|
| pmid |
sentence |
| 19414597 |
Here, we have identified s307 as a novel phosphorylation site in lkb1 and provide evidence that, in multiple cell types, phosphorylation of this site by protein kinase c ? (pkc-?) Induces nucleocytoplasmic transport of lkb1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle, Smooth Muscle |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
IRS1 |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236760 |
Ser307 |
TRRSRTEsITATSPA |
Cricetulus griseus |
|
| pmid |
sentence |
| 15069075 |
Extensive studies have provided evidence that phosphorylation of Ser307 in IRS-1 inhibits IR/IRS-1 complex formation and IRS-1 tyrosine phosphorylation after prolonged insulin-stimulation similar to our results. |
|
| Publications: |
1 |
Organism: |
Cricetulus Griseus |
| + |
PRKCZ | up-regulates
phosphorylation
|
RELA |
0.536 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151432 |
Ser311 |
RTYETFKsIMKKSPF |
Homo sapiens |
|
| pmid |
sentence |
| 17183360 |
Rela is phosphorylated at: ser276 by the catalytic subunit of protein kinase a (pkac), msk1 and msk2; at ser311 by the atypical pkczeta; at ser468 by ikkbeta, ikkepsilon and glycogen-synthase kinase-3beta (gsk3beta); at ser529 by ck2; and at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1)) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates
phosphorylation
|
IRS1 |
0.716 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123738 |
Ser323 |
MVGGKPGsFRVRASS |
Homo sapiens |
|
| pmid |
sentence |
| 15069075 |
Thus, pkc-zeta might promote feedback ir/irs-1 complex formation and irs-1 tyrosine phosphorylation through phosphorylation of ser318. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275447 |
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 |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277622 |
Ser34 |
SRSYVTTsTRTYSLG |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 33525953 |
Results suggest that aPKCs target multiple activation sites (Ser33/39/56) on Vimentin and therefore is essential for VIF dynamics regulation during the metastasis of prostate cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates quantity by stabilization
phosphorylation
|
PARD6A |
0.835 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276433 |
Ser345 |
RGDGSGFsL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 23249950 |
APKC associates and phosphorylates Par6 on S345. aPKC expression stabilizes Par6 protein levels. We show that the aPKC, PKCι, interacts with TGF-β receptors through Par6 and that these proteins localize to the leading edge of migrating cells. Furthermore, Par6 phosphorylation on serine 345 by TGF-β receptors is enhanced in the presence of aPKC. aPKC kinase activity, as well as an association with Par6, were found to be important for Par6 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
PSEN1 |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249239 |
Ser346 |
EWEAQRDsHLGPHRS |
Homo sapiens |
|
| pmid |
sentence |
| 14576165 |
A phosphorylation site at serine residue 346 was identified that is selectively phosphorylated by PKC but not by PKA. This site is localized within a recognition motif for caspases, and phosphorylation strongly inhibits proteolytic processing of PS1 by caspase activity during apoptosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
STK11 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160681 |
Ser428 |
SSKIRRLsACKQQ |
Homo sapiens |
|
| pmid |
sentence |
| 18250273 |
We conclude that pkc-zeta phosphorylates lkb1 at ser428, resulting in lkb1 nuclear export and hence ampk activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates quantity by destabilization
phosphorylation
|
CTNNB1 |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276878 |
Ser45 |
GATTTAPsLSGKGNP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25660024 |
Yap and β-catenin are direct substrates of PKCζ. Similar MS/MS analysis to map the sites phosphorylated in β-catenin by PKCζ identified S45 and several sites of low abundance that included S552 and S675 (Figure S3C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276879 |
Ser552 |
QDTQRRTsMGGTQQQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25660024 |
Yap and β-catenin are direct substrates of PKCζ. Similar MS/MS analysis to map the sites phosphorylated in β-catenin by PKCζ identified S45 and several sites of low abundance that included S552 and S675 (Figure S3C). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276880 |
Ser675 |
QDYKKRLsVELTSSL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 25660024 |
Yap and β-catenin are direct substrates of PKCζ. Similar MS/MS analysis to map the sites phosphorylated in β-catenin by PKCζ identified S45 and several sites of low abundance that included S552 and S675 (Figure S3C). |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
AKT3 |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249153 |
Ser472 |
RPHFPQFsYSASGRE |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 12162751 |
Full activation of the PKB enzyme requires phosphorylation of a threonine in the activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248996 |
Thr305 |
TDAATMKtFCGTPEY |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9512493 |
The activation of PKBbeta and PKBgamma by PDK1 was accompanied by the phosphorylation of the residues equivalent to Thr308 in PKBalpha, namely Thr309 (PKBbeta) and Thr305 (PKBgamma). PKBgamma which had been activated by PDK1 possessed a substrate specificity identical with that of PKBalpha and PKBbeta towards a range of peptides. The activation of PKBgamma and its phosphorylation at Thr305 was triggered by insulin-like growth factor-1 in 293 cells. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops, Homo Sapiens |
| + |
PRKCZ |
phosphorylation
|
TRAF2 |
0.41 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-184941 |
Ser55 |
QCGHRYCsFCLASIL |
Homo sapiens |
Lymphoma Cell |
| pmid |
sentence |
| 19336568 |
Here, we report that protein kinase czeta phosphorylates traf2 at ser(55), within the ring domain of the protein, after tnfalpha stimulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates
phosphorylation
|
CHAT |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129336 |
Ser558 |
VPTYESAsIRRFQEG |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15381704 |
Finally, basal chat phosphorylation in neurons is mediated predominantly by pkc at ser-476, with pkc activation increasing phosphorylation at ser-440 and enhancing chat activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129340 |
Ser594 |
HKAAVPAsEKLLLLK |
Homo sapiens |
|
| pmid |
sentence |
| 15381704 |
Finally, basal chat phosphorylation in neurons is mediated predominantly by pkc at ser-476, with pkc activation increasing phosphorylation at ser-440 and enhancing chat activity. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates quantity by destabilization
phosphorylation
|
NREP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273831 |
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 |
| + |
PRKCZ | up-regulates
phosphorylation
|
SP1 |
0.498 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149287 |
Ser641 |
GKVYGKTsHLRAHLR |
Homo sapiens |
|
| pmid |
sentence |
| 16943418 |
The hdac inhibitor tsa-induced cell-specific phosphatase release from the promoter, which serves as an 'on' mechanism for sp1 phosphorylation by phosphatidylinositol 3-kinase/protein kinase czeta (pi3k/pkczeta) at ser641, leading to p107 repressor derecruitment and lhr transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185741 |
Ser641 |
GKVYGKTsHLRAHLR |
Homo sapiens |
|
| pmid |
sentence |
| 19464346 |
The hdac inhibitor tsa-induced cell-specific phosphatase release from the promoter, which serves as an 'on' mechanism for sp1 phosphorylation by phosphatidylinositol 3-kinase/protein kinase czeta (pi3k/pkczeta) at ser641, leading to p107 repressor derecruitment and lhr transcriptional activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160766 |
Ser670 |
CGKRFTRsDELQRHK |
Homo sapiens |
|
| pmid |
sentence |
| 18258854 |
Here we have used a variety of approaches to identify 3 amino acids (thr668, ser670, and thr681) in the zinc finger domain of sp1 that are modified by pkc-zeta angiotensin ii, which activates pkc-? Phosphorylation (at thr410) via the angiotensin ii type 1 receptor, stimulates sp1 phosphorylation and increases sp1 binding to the platelet-derived growth factor-d promoter. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160770 |
Thr668 |
SYCGKRFtRSDELQR |
Homo sapiens |
|
| pmid |
sentence |
| 18258854 |
Here we have used a variety of approaches to identify 3 amino acids (thr668, ser670, and thr681) in the zinc finger domain of sp1 that are modified by pkc-zeta angiotensin ii, which activates pkc-? Phosphorylation (at thr410) via the angiotensin ii type 1 receptor, stimulates sp1 phosphorylation and increases sp1 binding to the platelet-derived growth factor-d promoter. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160774 |
Thr681 |
QRHKRTHtGEKKFAC |
Homo sapiens |
|
| pmid |
sentence |
| 18258854 |
Here we have used a variety of approaches to identify 3 amino acids (thr668, ser670, and thr681) in the zinc finger domain of sp1 that are modified by pkc-zeta angiotensin ii, which activates pkc-? Phosphorylation (at thr410) via the angiotensin ii type 1 receptor, stimulates sp1 phosphorylation and increases sp1 binding to the platelet-derived growth factor-d promoter. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
PRKCZ | down-regulates
phosphorylation
|
ADD2 |
0.279 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-139914 |
Ser713 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 16116087 |
We now demonstrate that ptn stimulates the phosphorylation of serines 713 and 726 in the myristoylated alanine-rich protein kinase (pk) c substrate domain of beta-adducin through activation of either pkc alpha or beta. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates
phosphorylation
|
ADD1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59303 |
Ser726 |
KKKFRTPsFLKKSKK |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9679146 |
These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. Ser-726 and ser-713 in the c-terminal marcks-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites common for pka and pkc. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43834 |
Ser726 |
KKKFRTPsFLKKSKK |
Homo sapiens |
|
| pmid |
sentence |
| 8810272 |
These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. Ser-726 and ser-713 in the c-terminal marcks-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites common for pka and pkc. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
PRKCZ | up-regulates
phosphorylation
|
PARD3 |
0.699 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94523 |
Ser827 |
REGFGRQsMSEKRTK |
Homo sapiens |
|
| pmid |
sentence |
| 12390250 |
These results imply that serine 827 in the apkc binding site of par-3 is a target of apkc and that the regulated interaction between a protein kinase, apkc, and its substrate, par-3, plays an essential role in the establishment of cell polarity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
GRM5 |
0.377 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249284 |
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-249291 |
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 |
| + |
PRKCZ | down-regulates
phosphorylation
|
GSK3B |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119889 |
Ser9 |
SGRPRTTsFAESCKP |
Homo sapiens |
|
| pmid |
sentence |
| 14657655 |
Phospho-gsk3b-specific antibodies also revolved that lkb1 regulates gsk3b phosphorylation at a known inhibitory site, serine-9. This localized phosphorylation is cdc42 and pkc-zeta-dependent. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ |
phosphorylation
|
WWC1 |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249262 |
Ser975 |
VRMKRPSsVKSLRSE |
in vitro |
|
| pmid |
sentence |
| 15081397 |
PKCzeta phosphorylates KIBRA at serine 975 and 978 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249263 |
Ser978 |
KRPSSVKsLRSERLI |
in vitro |
|
| pmid |
sentence |
| 15081397 |
PKCzeta phosphorylates KIBRA at serine 975 and 978 |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
YWHAB |
0.375 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249035 |
Thr143 |
SGDNKQTtVSNSQQA |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 10620507 |
Our results with the 14-3-3 mutants indirectly imply a new phosphorylation site, 130Ser (and to a lesser extent 141Thr), in 14-3-3b that regulates the association}dissociation of 14-3-3b and PKC-f. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
AKT2 |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248997 |
Thr309 |
SDGATMKtFCGTPEY |
in vitro |
|
| pmid |
sentence |
| 9512493 |
The activation of PKBbeta and PKBgamma by PDK1 was accompanied by the phosphorylation of the residues equivalent to Thr308 in PKBalpha, namely Thr309 (PKBbeta) and Thr305 (PKBgamma). PKBgamma which had been activated by PDK1 possessed a substrate specificity identical with that of PKBalpha and PKBbeta towards a range of peptides. The activation of PKBgamma and its phosphorylation at Thr305 was triggered by insulin-like growth factor-1 in 293 cells. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
HABP4 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249251 |
Thr354 |
RKPANDItSQLEINF |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249257 |
Thr375 |
GRGARGGtRGGRGRI |
Homo sapiens |
Hodgkin Lymphoma Cell |
| pmid |
sentence |
| 14699138 |
We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. | This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. | Ki-1/57 Exits the Nucleus upon PMA Activation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
PLA2G4A |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277518 |
Thr376 |
GSKFFMGtVVKKYEE |
Homo sapiens |
MCF-10-2A Cell |
| pmid |
sentence |
| 32559461 |
To further evaluate cPLA2 as a candidate substrate for PKCζ, we developed a custom antibody recognizing the cPLA2 T376 phosphorylation site. Specificity was validated in both serum starved/stimulated samples |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
PPP1R14A |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249261 |
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 |
| + |
PDPK1 | up-regulates
phosphorylation
|
PRKCZ |
0.558 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85501 |
Thr410 |
GPGDTTStFCGTPNY |
Homo sapiens |
|
| pmid |
sentence |
| 11141077 |
Our findings suggest that insulin, via pip(3), provokes increases in pkc-zeta enzyme activity through (a) pdk-1-dependent t410 loop phosphorylation, (b) t560 autophosphorylationcytoskeletal reorganization;tnni1(induces);desmin(induces);tpm1(induces);myo1c(induces);tnnt1(induces); |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates
phosphorylation
|
NR1H4 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179771 |
Thr456 |
GRLTELRtFNHHHAE |
Homo sapiens |
CACO-2 Cell |
| pmid |
sentence |
| 18668687 |
The effect of fic1 on fxr phosphorylation and nuclear localization and its effects on bsep promoter activity could be blocked with protein kinase c zeta (pkc zeta) inhibitors (pseudosubstrate or small interfering rna silencing). Recombinant pkc zeta directly phosphorylated immunoprecipitated fxr. The mutation of threonine 442 of fxr to alanine yielded a dominant negative protein, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
NOS3 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251637 |
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 |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
MAP1LC3B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273906 |
Thr50 |
QLPVLDKtKFLVPDH |
in vitro |
|
| pmid |
sentence |
| 31857374 |
LC3B is phosphorylated at Thr-50 within the LDS by serine/threonine kinase (STK) 3 and STK4. Here, we identified LIR motifs in STK3 and atypical protein kinase Cζ (PKCζ) and never in mitosis A (NIMA)-related kinase 9 (NEK9). All three kinases phosphorylated LC3B Thr-50 in vitro A phospho-mimicking substitution of Thr-50 impaired binding of several LIR-containing proteins, such as ATG4B, FYVE, and coiled-coil domain-containing 1 (FYCO1), and autophagy cargo receptors p62/sequestosome 1 (SQSTM1) and neighbor of BRCA1 gene (NBR1). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCZ | up-regulates
phosphorylation
|
PRKCZ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85505 |
Thr560 |
TSEPVQLtPDDEDAI |
Homo sapiens |
|
| pmid |
sentence |
| 11141077 |
Our findings suggest that insulin, via pip(3), provokes increases in pkc-zeta enzyme activity through (a) pdk-1-dependent t410 loop phosphorylation, (b) t560 autophosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates
phosphorylation
|
MARK3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124221 |
Thr564 |
RGTASRStFHGQPRE |
Homo sapiens |
|
| pmid |
sentence |
| 15084291 |
Hpar-1a, t564, is phosphorylated in vivo and by apkc in vitro.This study establishes a novel functional link between two central determinants of cellular polarity, apkc and par-1, and suggests a model by which apkc may regulate par-1 in polarized cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | down-regulates
phosphorylation
|
MARK2 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124217 |
Thr596 |
RGVSSRStFHAGQLR |
Homo sapiens |
|
| pmid |
sentence |
| 15084291 |
Hpar-1b is phosphorylated by apkc on threonine 595 importantly, phosphorylation of hpar-1b on t595 negatively regulates the kinase activity and plasma membrane localization of hpar-1b in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
phosphatidic acid | up-regulates
chemical activation
|
PRKCZ |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94867 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12401205 |
The pkc isoform pkc-zeta appear to be activated by direct interactions with pa |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
calcium(2+) | up-regulates
chemical activation
|
PRKCZ |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76991 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10777564 |
Wnt ligands working through frizzled receptors have a differential ability to stimulate release of intracellular calcium (ca(2+)) and activation of protein kinase c (pkc). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1,2-diacyl-sn-glycerol | up-regulates activity
binding
|
PRKCZ |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242599 |
|
|
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 |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
MGluR |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270274 |
|
|
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 |
| + |
PRKCZ | up-regulates
phosphorylation
|
NfKb-p65/p50 |
0.476 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217370 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17183360 |
Rela is phosphorylated at: ser276 by the catalytic subunit of protein kinase a (pkac), msk1 and msk2; at ser311 by the atypical pkczeta; at ser468 by ikkbeta, ikkepsilon and glycogen-synthase kinase-3beta (gsk3beta); at ser529 by ck2; and at ser536 by ikkbeta, ikkalfa, ikkepsilon, nf-kb activating kinase (nak, also known as tank-binding kinase-1 tbk1)) and rsk1 (also known as p90 ribosomal protein s6 kinase (p90s6k) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PRKCZ
- 
- 