Relation Results

Summary

Name PKC
Primary ID SIGNOR-PF53
Type protein family
Formed by PRKCA, PRKCB, PRKCD, PRKCE, PRKCG, PRKCH, PRKCI, PRKCQ, PRKCZ
Relations 27

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Type: Score: Layout: SPV 
0.20.20.20.20.20.20.20.20.20.20.20.20.20.20.20.470.20.20.20.2PKCSUN1NOXO1TRPV4MBD4AQP4KCNJ1KLHL3ARHGEF6ABCB1SLITRK1ARHGAP17GSTA4KCNK9PPP1R14BSCN2AAKAP12GAD2GNEGRM5NOS3

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation SUN1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263281 Ser113 HVSRQVTsSGVSHGG Homo sapiens HeLa Cell
pmid sentence
The SUN1-NXF1 association is at least partly regulated by a protein kinase C (PKC) which phosphorylates serine 113 (S113) in the N-terminal domain leading to reduced interaction.
Publications: 1 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png phosphorylation NOXO1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264728 Ser159 SRAAGRLsIHSLEAQ Homo sapiens
pmid sentence
Importantly, the constitutive activity of NoxO1 can be modulated. NoxO1 phosphorylation by PKC at Ser154 doubles its binding ability to NoxA1, which in turn acts as a molecular switch, allowing optimal interaction of NoxO1 with p22phox
Publications: 1 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png phosphorylation TRPV4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276229 Ser162 FDIVSRGsTADLDGL in vitro
pmid sentence
Activation of the TRPV4 ion channel is enhanced by phosphorylation. TRPV4 is phosphorylated in response to activation of PKC. We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4.
Identifier Residue Sequence Organism Cell Line
SIGNOR-276230 Ser189 DEEFREPsTGKTCLP in vitro
pmid sentence
Activation of the TRPV4 ion channel is enhanced by phosphorylation. TRPV4 is phosphorylated in response to activation of PKC. We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4.
Identifier Residue Sequence Organism Cell Line
SIGNOR-276228 Thr175 GLLPFLLtHKKRLTD in vitro
pmid sentence
Activation of the TRPV4 ion channel is enhanced by phosphorylation. TRPV4 is phosphorylated in response to activation of PKC. We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4.
Publications: 3 Organism: In Vitro
+ PKCup-regulates activity img/direct-activation.png phosphorylation MBD4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275675 Ser165 CSMAALTsHLQNQSN
pmid sentence
Phosphorylation of MBD4 promotes 5-meC glycosylase activity Further evidence emerged to support the involvement of MBD4 in active demethylation. Protein-kinase C phosphorylation of MBD4 at two specific serine residues (165 and 262) following parathyroid hormone stimulation was shown to promote demethylation within the CYP27B1 gene promoter [12]
Identifier Residue Sequence Organism Cell Line
SIGNOR-275674 Ser262 SGFVQSDsKRESVCN
pmid sentence
Phosphorylation of MBD4 promotes 5-meC glycosylase activity Further evidence emerged to support the involvement of MBD4 in active demethylation. Protein-kinase C phosphorylation of MBD4 at two specific serine residues (165 and 262) following parathyroid hormone stimulation was shown to promote demethylation within the CYP27B1 gene promoter [12]
Publications: 2
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation AQP4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276260 Ser180 TIFASCDsKRTDVTG in vitro
pmid sentence
Taken together this data shows that AQP4 in gliomas is the target of PKC phosphorylation, and albeit significantly phosphorylated at rest, phosphorylation can be further enhanced by PKC activation.This data suggests that in gliomas water permeability through AQP4 is under the regulation of PKC via phosphorylation of S180.
Publications: 1 Organism: In Vitro
+ PKCup-regulates activity img/direct-activation.png phosphorylation KCNJ1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275990 Ser201 FSKNAVIsKRGGKLC in vitro
pmid sentence
We conclude that ROMK1 is a substrate of PKC and that serine residues 4 and 201 are the two main PKC phosphorylation sites that are essential for the expression of ROMK1 in the cell surface.
Identifier Residue Sequence Organism Cell Line
SIGNOR-275989 Ser4 sSRNVFDT in vitro
pmid sentence
We conclude that ROMK1 is a substrate of PKC and that serine residues 4 and 201 are the two main PKC phosphorylation sites that are essential for the expression of ROMK1 in the cell surface.
Publications: 2 Organism: In Vitro
+ PKCup-regulates quantity by stabilization img/direct-activation.png phosphorylation KLHL3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273780 Ser433 PMNTRRSsVGVGVVE Chlorocebus aethiops COS-7 Cell
pmid sentence
We show that KLHL3 is phosphorylated at serine 433 in the Kelch domain (a site frequently mutated in hypertension with hyperkalemia) by protein kinase C in cultured cells and that this phosphorylation prevents WNK4 binding and degradation.
Publications: 1 Organism: Chlorocebus Aethiops
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation ARHGEF6 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272164 Ser640 RKTERKPsEEEYVIR Homo sapiens Blood Platelet
pmid sentence
ARHGEF6 is a Rho guanine nucleotide exchange factor for Rac1 and constitutively bound to GIT1. NO and PGI2 activate PKG and PKA, respectively and both kinases phosphorylate ARHGEF6 on Ser-684 and possibly on Ser-640. Phosphorylation of ARHGEF6 results in the assembly of a GIT1-ARHGEF6–14-3-3 complex. These changes might contribute to PGI2- and NO-mediated Rac1 inhibition.
Identifier Residue Sequence Organism Cell Line
SIGNOR-272161 Ser684 GSSTRKDsIPQVLLP Homo sapiens Blood Platelet
pmid sentence
Screening for potential mediators of this effect resulted in the identification of the Rac1-specific GTPase-activating protein ARHGAP17 and the guanine nucleotide exchange factor ARHGEF6 as new PKA and PKG substrates in platelets. We mapped the PKA/PKG phosphorylation sites to serine 702 on ARHGAP17 using Phos-tag gels and to serine 684 on ARHGEF6. |we show that ARHGEF6 is constitutively linked to GIT1, a GAP of Arf family small G proteins, and that ARHGEF6 phosphorylation enables binding of the 14-3-3 adaptor protein to the ARHGEF6/GIT1 complex.
Publications: 2 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png dephosphorylation ABCB1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272512 Ser661 SSNDSRSsLIRKRST Homo sapiens HEK-293 Cell
pmid sentence
Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function|P-gp is known to be phosphorylated at Ser667, Ser671, and Ser683 by PKA; at Ser661, Ser667, and Ser671 by PKC; and at Ser683 by Pim-1|simultaneous expression of PP5 and PPP2R3C reduced the phosphorylation detected by the antibodies that specifically recognize serine/threonine phosphorylated by PKA or serine phosphorylated by PKC. These results suggest that the PP5/PPP2R3C complex dephosphorylates PKA- and PKC-phosphorylated serine residues on P-gp
Identifier Residue Sequence Organism Cell Line
SIGNOR-272513 Ser667 SSLIRKRsTRRSVRG Homo sapiens HEK-293 Cell
pmid sentence
Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function|P-gp is known to be phosphorylated at Ser667, Ser671, and Ser683 by PKA; at Ser661, Ser667, and Ser671 by PKC; and at Ser683 by Pim-1|simultaneous expression of PP5 and PPP2R3C reduced the phosphorylation detected by the antibodies that specifically recognize serine/threonine phosphorylated by PKA or serine phosphorylated by PKC. These results suggest that the PP5/PPP2R3C complex dephosphorylates PKA- and PKC-phosphorylated serine residues on P-gp
Identifier Residue Sequence Organism Cell Line
SIGNOR-272514 Ser671 RKRSTRRsVRGSQAQ Homo sapiens HEK-293 Cell
pmid sentence
Protein phosphatase complex PP5/PPP2R3C dephosphorylates P-glycoprotein/ABCB1 and down-regulates the expression and function|P-gp is known to be phosphorylated at Ser667, Ser671, and Ser683 by PKA; at Ser661, Ser667, and Ser671 by PKC; and at Ser683 by Pim-1|simultaneous expression of PP5 and PPP2R3C reduced the phosphorylation detected by the antibodies that specifically recognize serine/threonine phosphorylated by PKA or serine phosphorylated by PKC. These results suggest that the PP5/PPP2R3C complex dephosphorylates PKA- and PKC-phosphorylated serine residues on P-gp
Publications: 3 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png phosphorylation SLITRK1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273635 Ser695 DCGSHSLsD in vitro
pmid sentence
In our studies, SICD was phosphorylated by PKA, PKC, and CK2, and association of SLITRK1 with 14-3-3 was regulated by phosphorylation at Ser695. Co-precipitation experiments demonstrated much greater recovery of 14-3-3 in SLITRK1 precipitates when wild-type or S695E was used, as compared with S695A, consistent with the results with purified peptides.
Publications: 1 Organism: In Vitro
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation ARHGAP17 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272157 Ser702 LSAPRRYsSSLSPIQ Homo sapiens Blood Platelet
pmid sentence
Screening for potential mediators of this effect resulted in the identification of the Rac1-specific GTPase-activating protein ARHGAP17 and the guanine nucleotide exchange factor ARHGEF6 as new PKA and PKG substrates in platelets. We mapped the PKA/PKG phosphorylation sites to serine 702 on ARHGAP17 using Phos-tag gels and to serine 684 on ARHGEF6. |ARHGAP17 is a Rho GTPase-activating protein of Rac1 and is bound to the SH3 domain of CIP4 via its SH3 binding region in resting platelets. Endothelial PGI2 stimulates the activation of PKA and leads to the phosphorylation of Ser-702 in ARHGAP17, which results in the dissociation of the ARHGAP17-CIP4 complex.
Publications: 1 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png phosphorylation GSTA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264795 Thr193 VKLSNIPtIKRFLEP Chlorocebus aethiops
pmid sentence
Mutational analysis show that the putative mitochondrial targeting signal resides within the C-terminal 20 amino acid residues of the protein and that the targeting signal requires activation by phosphorylation at the C-terminal-most protein kinase A (PKA) site at Ser-189 or protein kinase C (PKC) site at Thr-193.
Publications: 1 Organism: Chlorocebus Aethiops
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation KCNK9 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276059 Thr341 IEEISPStLKNSLFP Homo sapiens TsA-201 Cell
pmid sentence
PKC acts directly on hTASK3 channels to phosphorylate an identified amino acid in the C terminus region (Thr341), thereby reducing channel current. 
Publications: 1 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png phosphorylation PPP1R14B 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-265740 Thr57 VRRQGKVtVKYDRKE
pmid sentence
Recombinant tagged PHI-1 was phosphorylated by protein kinase C at two sites, one a Ser and one a Thr; phosphorylation enhanced inhibitory potency 50-fold.
Publications: 1
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation SCN2A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275750 Homo sapiens Neuron
pmid sentence
For example, protein kinase A (PKA) and protein kinase C (PKC) have been shown to phosphorylate multiple serine residues on the interdomain I-II and III-IV linkers of Nav1.2, significantly reducing current and increasing firing thresholds
Publications: 1 Organism: Homo Sapiens
+ AKAP12up-regulates activity img/direct-activation.png relocalization PKC 0.47
Identifier Residue Sequence Organism Cell Line
SIGNOR-271838
pmid sentence
A-kinase-anchoring protein 250 (AKAP250; gravin) acts as a scaffold that binds protein kinase A (PKA), protein kinase C and protein phosphatases, associating reversibly with the beta(2)-adrenergic receptor.
Publications: 1
+ PKCup-regulates activity img/direct-activation.png phosphorylation GAD2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276010 Homo sapiens Brain
pmid sentence
Here, we report the effect of phosphorylation on the two well-defined GAD isoforms, namely, GAD65 and GAD67, using highly purified preparations of recombinant human brain GAD65 and GAD67. GAD65 was activated by phosphorylation, while GAD67 was inhibited by phosphorylation.We further demonstrate that protein kinase A (PKA) and protein kinase C isoform epsilon are the protein kinases responsible for phosphorylation and regulation of GAD67 and GAD65, respectively.
Publications: 1 Organism: Homo Sapiens
+ PKCup-regulates activity img/direct-activation.png phosphorylation GNE 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-266072 Rattus norvegicus
pmid sentence
Protein kinase C phosphorylates and regulates UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase|Furthermore, PKC phosphorylates UDP-GlcNAc 2-epimerase and this phosphorylation results in an upregulation of the UDP-GlcNAc 2-epimerase enzyme activity.
Publications: 1 Organism: Rattus Norvegicus
Tissue: Liver
+ PKCup-regulates activity img/direct-activation.png phosphorylation GRM5 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269972 in vitro
pmid sentence
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
+ PKCdown-regulates activity img/direct_inhibition.png phosphorylation NOS3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-269971 Homo sapiens Vascular Endothelium
pmid sentence
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
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