| + |
PRKCG | up-regulates activity 
phosphorylation
|
GRIN2B |
0.408 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249085 |
Ser1303 |
NKLRRQHsYDTFVDL |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249088 |
Ser1323 |
ALAPRSVsLKDKGRF |
in vitro |
|
| pmid |
sentence |
| 11306676 |
These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCG | up-regulates activity
phosphorylation
|
PEBP1 |
0.389 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249190 |
Ser153 |
RGKFKVAsFRKKYEL |
Rattus norvegicus |
Hippocampal Cell Line |
| pmid |
sentence |
| 12551925 |
Here we report that one mechanism involves dissociation of Raf kinase inhibitory protein (RKIP) from Raf-1. Classic and atypical but not novel PKC isoforms phosphorylate RKIP at serine 153 (Ser-153). RKIP Ser-153 phosphorylation by PKC either in vitro or in response to 12-O-tetradecanoylphorbol-13-acetate or epidermal growth factor causes release of RKIP from Raf-1, whereas mutant RKIP (S153V or S153E) remains bound. I |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCG | up-regulates activity
phosphorylation
|
GSTP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276019 |
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-276018 |
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 |
| + |
PRKCG |
phosphorylation
|
SDC2 |
0.359 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248975 |
Ser187 |
DLGERKPsSAAYQKA |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248978 |
Ser188 |
LGERKPSsAAYQKAP |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCG |
phosphorylation
|
EIF4E |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248947 |
Ser209 |
DTATKSGsTTKNRFV |
Mus musculus |
|
| pmid |
sentence |
| 8662663 |
Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCG | down-regulates 
phosphorylation
|
GSK3A |
0.329 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115726 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
|
| pmid |
sentence |
| 11884598 |
Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG |
phosphorylation
|
DAB2 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249027 |
Ser24 |
QAAPKAPsKKEKKKG |
Chlorocebus aethiops |
COS Cell |
| pmid |
sentence |
| 10542228 |
We have mapped the TPA-induced DOC-2/DAB2 protein phosphorylation site to Ser24, which appears to modulate the DOC-2/DAB2 inhibition of AP-1 transcription activity. Results indicate that phosphorylation of Ser24 is mediated by PKCbetaII, PKC_, and PKCdelta, but not CKII. This suggests that the PKC phosphorylation of Ser24 in DOC-2/DAB2 may be an underlying mechanisms for its tumor-suppressive function. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PRKCG | up-regulates
phosphorylation
|
ANXA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202788 |
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 |
| + |
PRKCG | up-regulates
phosphorylation
|
GRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83231 |
Ser29 |
ATPAARAsKKILLPE |
Homo sapiens |
|
| pmid |
sentence |
| 11042191 |
Phosphorylation of grk2 by protein kinase c abolishes its inhibition by calmodulinin vitro, grk2 was preferentially phosphorylated by pkc isoforms alpha, gamma, and delta |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates activity
phosphorylation
|
GRK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249060 |
Ser29 |
ATPAARAsKKILLPE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11042191 |
Phosphorylation of GRK2 by protein kinase C abolishes its inhibition by calmodulin. In vitro, GRK2 was preferentially phosphorylated by PKC isoforms alpha, gamma, and delta. Two-dimensional peptide mapping of PKCalpha-phosphorylated GRK2 showed a single site of phosphorylation, which was identified as serine 29 by HPLC-MS. A S29A mutant of GRK2 was not phosphorylated by PKC in vitro and showed no phorbol ester-stimulated phosphorylation when transfected into human embryonic kidney (HEK)293 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates activity
phosphorylation
|
TOP2A |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249196 |
Ser29 |
EDAKKRLsVERIYQK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12569090 |
Here, we have shown that the enzymatic activity of topoisomerase II alpha protein purified from HeLa cell nuclei was strongly enhanced following phosphorylation by protein kinase C. | Site-directed mutagenesis studies indicated that phosphorylation of serine 29 generated both of these phosphopeptides. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG |
phosphorylation
|
STXBP1 |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249184 |
Ser306 |
VSQEVTRsLKDFSSS |
in vitro |
|
| pmid |
sentence |
| 12519779 |
Munc18a is essential for neurotransmitter release by exocytosis and can be phosphorylated by PKC in vitro on Ser-306 and Ser-313. We demonstrate that it is phosphorylated on Ser-313 in response to phorbol ester treatment in adrenal chromaffin cells. Mutation of both phosphorylation sites to glutamate reduces its affinity for syntaxin and so acts as a phosphomimetic mutation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCG | down-regulates activity
phosphorylation
|
STXBP1 |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249187 |
Ser313 |
SLKDFSSsKRMNTGE |
Bos taurus |
Chromaffin Cell |
| pmid |
sentence |
| 12519779 |
Munc18a is essential for neurotransmitter release by exocytosis and can be phosphorylated by PKC in vitro on Ser-306 and Ser-313. We demonstrate that it is phosphorylated on Ser-313 in response to phorbol ester treatment in adrenal chromaffin cells. Mutation of both phosphorylation sites to glutamate reduces its affinity for syntaxin and so acts as a phosphomimetic mutation. |
|
| Publications: |
1 |
Organism: |
Bos Taurus |
| + |
PRKCG | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275445 |
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 |
| + |
PRKCG | up-regulates activity
phosphorylation
|
OCLN |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249107 |
Ser340 |
DKRFYPEsSYKSTPV |
Canis lupus familiaris |
|
| pmid |
sentence |
| 11502742 |
Protein kinase C regulates the phosphorylation and cellular localization of occludin. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. Both the phosphorylation of occludin and its incorporation into tight junctions induced by calcium switch were markedly inhibited by the PKC inhibitor GF-109203X. |
|
| Publications: |
1 |
Organism: |
Canis Lupus Familiaris |
| + |
PRKCG | up-regulates activity
phosphorylation
|
PSEN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249238 |
Ser346 |
EWEAQRDsHLGPHRS |
Homo sapiens |
HEK-293 Cell |
| 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 |
| + |
PRKCG | down-regulates activity
phosphorylation
|
STK17B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263178 |
Ser351 |
PEDSSMVsKRFRFDD |
Mus musculus |
NIH-3T3 Cell |
| pmid |
sentence |
| 18084041 |
These results suggest that phosphorylation of Ser350 plays an essential role in regulating translocation of DRAK2 to the nucleus from the cytoplasm, possibly by affecting the activity of the NLS. Ectopic expression of PKC-gamma induced cytoplasmic localization of DRAK2 and PKC-gamma phosphorylated Ser350 flanking the NLS. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
PRKCG | up-regulates activity
phosphorylation
|
NRGN |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248915 |
Ser36 |
AAAKIQAsFRGHMAR |
in vitro |
|
| pmid |
sentence |
| 8080473 |
Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. A single site, Ser36, which is adjacent to the predicted calmodulin (CaM)-binding domain, was phosphorylated by these enzymes. Phosphorylation of RC3 by PKC or PKM, a protease-degraded PKC, was inhibited by CaM. The effect of CaM apparently targets at RC3, as phosphorylation of protamine sulfate by PKM was not inhibited by CaM. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCG |
phosphorylation
|
PA2G4 |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249091 |
Ser363 |
ALLQSSAsRKTQKKK |
Homo sapiens |
|
| pmid |
sentence |
| 11325528 |
We found that Ebp1 was basally phosphorylated in AU565 breast cancer cells on serine/threonine residues and that this phosphorylation was enhanced by heregulin treatment. Both serine and threonine residues of a GST-Ebp1 fusion protein were phosphorylated by PKC in vitro. In vivo, we demonstrated that basal Ebp1 phosphorylation was dependent upon PKC. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249094 |
Thr366 |
QSSASRKtQKKKKKK |
Homo sapiens |
AU-565 Cell |
| pmid |
sentence |
| 11325528 |
We found that Ebp1 was basally phosphorylated in AU565 breast cancer cells on serine/threonine residues and that this phosphorylation was enhanced by heregulin treatment. Both serine and threonine residues of a GST-Ebp1 fusion protein were phosphorylated by PKC in vitro. In vivo, we demonstrated that basal Ebp1 phosphorylation was dependent upon PKC. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates activity
phosphorylation
|
GJA1 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249050 |
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 |
| + |
PRKCG | up-regulates quantity by stabilization
phosphorylation
|
VTN |
0.288 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248964 |
Ser381 |
RNRKGYRsQRGHSRG |
in vitro |
|
| pmid |
sentence |
| 9030777 |
Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCG | down-regulates activity
phosphorylation
|
CYTH2 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249025 |
Ser392 |
AARKKRIsVKKKQEQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 10531036 |
ARNO is phosphorylated in vivo by PKC on a single serine residue, S392, located within the carboxy-terminal polybasic domain. Mutation of S392 to alanine does not prevent ARNO-mediated actin rearrangements, suggesting that phosphorylation does not lead to ARNO activation [6]. Here, we report that phosphorylation negatively regulates ARNO exchange activity through a 'PH domain electrostatic switch'. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates
phosphorylation
|
KIR3DL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158133 |
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 |
| + |
PRKCG | down-regulates
phosphorylation
|
TNNI3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134632 |
Ser42 |
AKKKSKIsASRKLQL |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134636 |
Ser44 |
KKSKISAsRKLQLKT |
Homo sapiens |
|
| pmid |
sentence |
| 15769444 |
Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
PRKCG | up-regulates
phosphorylation
|
CHAT |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129316 |
Ser464 |
LLKHVTQsSRKLIRA |
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-129320 |
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-129324 |
Ser558 |
VPTYESAsIRRFQEG |
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-129328 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-129332 |
Thr373 |
TVLVKDStNRDSLDM |
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: |
5 |
Organism: |
Homo Sapiens |
| + |
PRKCG |
phosphorylation
|
RPS6KB2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97295 |
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 |
| + |
PRKCG | up-regulates
phosphorylation
|
RAF1 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37541 |
Ser497 |
ATVKSRWsGSQQVEQ |
Homo sapiens |
|
| pmid |
sentence |
| 8288587 |
Pkc can effectively phosphorylate raf-1, this is a direct effect of activated pkc and not the result of raf-1 autophosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37545 |
Ser619 |
SLPKINRsASEPSLH |
Homo sapiens |
|
| pmid |
sentence |
| 8288587 |
Pkc can effectively phosphorylate raf-1, this is a direct effect of activated pkc and not the result of raf-1 autophosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates
phosphorylation
|
ARHGEF7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205234 |
Ser518 |
LSASPRMsGFIYQGK |
Homo sapiens |
|
| pmid |
sentence |
| 25009260 |
Pkc_ directly phosphorylates _pix at ser583 and indirectly at ser340 in cells. herefore, we propose that pkc_ positively modulates dopamine release through _2pix phosphorylation. The pkc_-_pix-cdc42/rac1 phosphorylation axis may provide a new therapeutic target for the treatment of parkinsonian syndrome |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-205238 |
Ser761 |
DSLGRRSsLSRLEPS |
Homo sapiens |
|
| pmid |
sentence |
| 25009260 |
Pkc_ directly phosphorylates _pix at ser583 and indirectly at ser340 in cells. herefore, we propose that pkc_ positively modulates dopamine release through _2pix phosphorylation. The pkc_-_pix-cdc42/rac1 phosphorylation axis may provide a new therapeutic target for the treatment of parkinsonian syndrome |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates activity
phosphorylation
|
GRM5 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249282 |
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-249289 |
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 |
| + |
PRKCG | up-regulates
phosphorylation
|
GRIA4 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-97558 |
Ser862 |
IRNKARLsITGSVGE |
Homo sapiens |
|
| pmid |
sentence |
| 12536214 |
We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates activity
phosphorylation
|
GRIN1 |
0.358 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263176 |
Ser890 |
ITSTLASsFKRRRSS |
Rattus norvegicus |
Neuron |
| pmid |
sentence |
| 15936117 |
Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms. The results show that PKC alpha phosphorylates preferentially S896 and PKC gamma preferentially S890. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PRKCG | down-regulates
phosphorylation
|
HSP90AA1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202812 |
Thr115 |
GTIAKSGtKAFMEAL |
Homo sapiens |
|
| pmid |
sentence |
| 24117238 |
Threonine residue set, thr(115)/thr(425)/thr(603), of hsp90_ is specifically phosphorylated by pkc_phosphorylation of hsp90_ by pkc_ decreases the binding affinity of hsp90_ towards atp and co-chaperones such as cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202816 |
Thr425 |
KKCLELFtELAEDKE |
Homo sapiens |
|
| pmid |
sentence |
| 24117238 |
Threonine residue set, thr(115)/thr(425)/thr(603), of hsp90_ is specifically phosphorylated by pkc_, and, more interestingly, this threonine residue set serves as a 'phosphorylation switch' for hsp90_ binding or release of pkc_. Moreover, phosphorylation of hsp90_ by pkc_ decreases the binding affinity of hsp90_ towards atp and co-chaperones such as cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202820 |
Thr603 |
PCCIVTStYGWTANM |
Homo sapiens |
|
| pmid |
sentence |
| 24117238 |
Threonine residue set, thr(115)/thr(425)/thr(603), of hsp90_ is specifically phosphorylated by pkc_, and, more interestingly, this threonine residue set serves as a 'phosphorylation switch' for hsp90_ binding or release of pkc_. Moreover, phosphorylation of hsp90_ by pkc_ decreases the binding affinity of hsp90_ towards atp and co-chaperones such as cdc37 (cell-division cycle 37), thereby decreasing its chaperone activity. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates
phosphorylation
|
APTX |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-186409 |
Thr125 |
AKNPGLEtHRKRKRS |
Homo sapiens |
|
| pmid |
sentence |
| 19561170 |
We show the novel molecular consequences of increased kinase activities of mutants: aprataxin (aptx), a dna repair protein causative for autosomal recessive ataxia, was found to be a preferential substrate of mutant pkc gamma, and phosphorylation inhibited its nuclear entry. ollectively, phosphorylation occurred at thr111, reducing nuclear aptx. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates activity
phosphorylation
|
HABP4 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249249 |
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-249255 |
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 |
| + |
PRKCG |
phosphorylation
|
CD5 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249072 |
Thr434 |
MSFHRNHtATVRSHA |
Homo sapiens |
|
| pmid |
sentence |
| 11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249074 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
|
| pmid |
sentence |
| 11123317 |
Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates
phosphorylation
|
CD5 |
0.348 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85183 |
Thr436 |
FHRNHTAtVRSHAEN |
Homo sapiens |
|
| pmid |
sentence |
| 11123317 |
Cd5 is a good pkc substrate. Phosphorylation of cd5 is necessary for cd5-mediated lipid second messenger generation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | down-regulates activity
phosphorylation
|
NOS3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251633 |
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 |
| + |
PRKCG | up-regulates
phosphorylation
|
AMPA |
0.693 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270233 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12536214 |
We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PDPK1 | up-regulates
phosphorylation
|
PRKCG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126072 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15209375 |
One of the most studiedevents controlled by ptdins(3,4,5)p3, comprises the activation of aof agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum- and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
bisindolylmaleimide i | down-regulates
chemical inhibition
|
PRKCG |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190356 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| 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
|
PRKCG |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191499 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCG | up-regulates activity
phosphorylation
|
MGluR |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270279 |
|
|
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 |
3.0
PRKCG
- 
- 