Relation Results

Summary

Name PKA
Primary ID SIGNOR-PF17
Type protein family
Formed by PRKACA, PRKACB, PRKACG
Relations 151
Pathways Axon guidance, Dopaminergic Synapse, FLT3-ITD signaling, GLP-1 and GIP receptor signaling in PDAC, Glycogenolysis, Glutamatergic synapse, GABAergic synapse , Macropinocytosis , Mitochondrial dynamics in T cell exhaustion, Nucleotide Biosynthesis, Neurotransmitters release, Oxytocin signaling, Thyroid Hormone Metabolism

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▶Modifications Tables

Relations
Regulator
Mechanism
target
score ℹ
+ PKA img/unknown.png phosphorylation GNMT 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263151 Ser10 DSVYRTRsLGVAAEG in vitro
pmid sentence
Activation of cAMP-dependent protein kinase by dibutyryl-cAMP, reported to cause GNMT phosphorylation under cell-free conditions, also had little effect on hepatocytic AdoMet and AdoHcy levels. Phosphorylation of GNMT would thus seem to play no role in regulation of the intracellular AdoMet/AdoHcy ratio, but could be involved in other GNMT functions, such as the binding of folates or aromatic hydrocarbons. The amino acid sequence surrounding Ser-10 (Val-Tyr-Arg-Thr-Arg-SerLeu-Gly-Val-Ala-Ala) could possibly qualify as a recognition site for AMPK as well as for PKA [32], the latter enzyme being capable of phosphorylating GNMT in intact hepatocytes (present study) as well as under cell-free conditions
Publications: 1 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation CAMKK2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277239 Ser100 HLSGRKLsLQERSQG Chlorocebus aethiops COS-7 Cell
pmid sentence
 Here we show that stimulation of cAMP-dependent protein kinase A (PKA) signaling in cells inactivates CaMKK2 by phosphorylation of three conserved serine residues. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-277238 Ser495 KTMIRKRsFGNPFEG Chlorocebus aethiops COS-7 Cell
pmid sentence
 Here we show that stimulation of cAMP-dependent protein kinase A (PKA) signaling in cells inactivates CaMKK2 by phosphorylation of three conserved serine residues. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-277240 Ser511 RREERSLsAPGNLLT Chlorocebus aethiops COS-7 Cell
pmid sentence
 Here we show that stimulation of cAMP-dependent protein kinase A (PKA) signaling in cells inactivates CaMKK2 by phosphorylation of three conserved serine residues. 
Publications: 3 Organism: Chlorocebus Aethiops
Pathways:Thyroid Hormone Metabolism
+ PKAdown-regulates img/direct_inhibition.png phosphorylation CAMKK2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-198146 Ser100 HLSGRKLsLQERSQG Homo sapiens
pmid sentence
Pka phosphorylates ser-100, ser-495, and ser-511the camp/pka pathway can inhibit camkk2 activity
Identifier Residue Sequence Organism Cell Line
SIGNOR-198150 Ser495 KTMIRKRsFGNPFEG Homo sapiens
pmid sentence
Pka phosphorylates ser-100, ser-495, and ser-511the camp/pka pathway can inhibit camkk2 activity
Identifier Residue Sequence Organism Cell Line
SIGNOR-198154 Ser511 RREERSLsAPGNLLT Homo sapiens
pmid sentence
Pka phosphorylates ser-100, ser-495, and ser-511the camp/pka pathway can inhibit camkk2 activity
Publications: 3 Organism: Homo Sapiens
Pathways:Thyroid Hormone Metabolism
+ PKAup-regulates activity img/direct-activation.png phosphorylation SLC4A4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263158 Ser1026 KKKKKKGsLDSDNDD Mus musculus
pmid sentence
Ser(982) in the C-terminus of kNBC1 is a target for PKA phosphorylation. Phosphorylation of Ser(982) in the sodium bicarbonate cotransporter kNBC1 shifts the HCO(3)(-) : Na(+) stoichiometry from 3 : 1 to 2 : 1 in murine proximal tubule cells Replacing Ser(982) at the C-terminus consensus PKA phosphorylation site with alanine resulted in a failure of PKA to phosphorylate the transporter and induce a stoichiometry shift.
Publications: 1 Organism: Mus Musculus
+ PKAup-regulates activity img/direct-activation.png phosphorylation PHF2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264513 Ser1056 FLTQRRPsASSPNNN Homo sapiens HEK-293 Cell
pmid sentence
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. We found that phosphorylated PHF2 then associates with ARID5B, a DNA-binding protein, and induce demethylation of methylated ARID5B. This modification leads to targeting of the PHF2-ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark. Replacement of all of four serine residues by alanines (4SA: Ser 757/Ser 899/Ser 954/Ser 1056) fully abrogated PKA phosphorylation of PHF2 (Fig. 2h).
Identifier Residue Sequence Organism Cell Line
SIGNOR-264510 Ser757 NARVKKEsGSSAAGI Homo sapiens HEK-293 Cell
pmid sentence
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. We found that phosphorylated PHF2 then associates with ARID5B, a DNA-binding protein, and induce demethylation of methylated ARID5B. This modification leads to targeting of the PHF2-ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark. Replacement of all of four serine residues by alanines (4SA: Ser 757/Ser 899/Ser 954/Ser 1056) fully abrogated PKA phosphorylation of PHF2 (Fig. 2h).
Identifier Residue Sequence Organism Cell Line
SIGNOR-264511 Ser899 RSKKRKGsDDAPYSP Homo sapiens HEK-293 Cell
pmid sentence
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. We found that phosphorylated PHF2 then associates with ARID5B, a DNA-binding protein, and induce demethylation of methylated ARID5B. This modification leads to targeting of the PHF2-ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark. Replacement of all of four serine residues by alanines (4SA: Ser 757/Ser 899/Ser 954/Ser 1056) fully abrogated PKA phosphorylation of PHF2 (Fig. 2h).
Identifier Residue Sequence Organism Cell Line
SIGNOR-264512 Ser954 QKSKKKKsAKRKLTP Homo sapiens HEK-293 Cell
pmid sentence
PHF2, a jmjC demethylase, is enzymatically inactive by itself, but becomes an active H3K9Me2 demethylase through PKA-mediated phosphorylation. We found that phosphorylated PHF2 then associates with ARID5B, a DNA-binding protein, and induce demethylation of methylated ARID5B. This modification leads to targeting of the PHF2-ARID5B complex to its target promoters, where it removes the repressive H3K9Me2 mark. Replacement of all of four serine residues by alanines (4SA: Ser 757/Ser 899/Ser 954/Ser 1056) fully abrogated PKA phosphorylation of PHF2 (Fig. 2h).
Publications: 4 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation GRIN2B 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276617 Ser1166 SDDFKRDsVSGGGPC Homo sapiens HEK-293 Cell
pmid sentence
Here we identify serine residue 1166 (Ser1166) in the carboxy-terminal tail of the NMDAR subunit GluN2B to be a direct molecular and functional target of PKA phosphorylation critical to NMDAR-dependent Ca(2+) permeation and Ca(2+) signaling in spines.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDE11A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276153 Ser117 GNLQRRAsQKELRKS in vitro
pmid sentence
The N-terminus has two phosphorylation sites for cyclic nucleotide monophosphate-dependent protein kinases (Ser117, Ser168). Phosphorylation of both by cAMP-dependent protein kinase decreased the EC50 value for cGMP from 72 to 23 μm. Effect of phosphorylations at Ser117 and Ser162. Here, serine phosphorylation by the catalytic subunit of cAK, albeit not known whether at position 117, 162 or both, increased cGMP affinity about threefold.
Identifier Residue Sequence Organism Cell Line
SIGNOR-276179 Ser162 RALLRKAsSLPPTTA in vitro
pmid sentence
The N-terminus has two phosphorylation sites for cyclic nucleotide monophosphate-dependent protein kinases (Ser117, Ser168). Phosphorylation of both by cAMP-dependent protein kinase decreased the EC50 value for cGMP from 72 to 23 μm. Effect of phosphorylations at Ser117 and Ser162. Here, serine phosphorylation by the catalytic subunit of cAK, albeit not known whether at position 117, 162 or both, increased cGMP affinity about threefold.
Publications: 2 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation CREB1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263653 Ser119 EILSRRPsYRKILND Homo sapiens
pmid sentence
CREB is phosphorylated on Ser133 by PKA (protein kinase A), promoting the recruitment of the co-activator proteins CBP (CREB-binding protein) and p300; this has been proposed to increase the transcription of CREB-dependent genes.
Publications: 1 Organism: Homo Sapiens
Pathways:Dopaminergic Synapse, FLT3-ITD signaling, GABAergic synapse , Oxytocin signaling, Thyroid Hormone Metabolism
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDE4D 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275988 Ser125 CRAMDRTsYAVETGH Chlorocebus aethiops
pmid sentence
Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.
Identifier Residue Sequence Organism Cell Line
SIGNOR-273939 Ser125 CRAMDRTsYAVETGH Chlorocebus aethiops
pmid sentence
Long PDE4 isoforms from all four sub-families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed.These were Ser89Ala-PDE4A8, Ser133Ala-PDE4B1, Ser13Ala-PDE4C2 and Ser126Ala-PDE4D5.
Publications: 2 Organism: Chlorocebus Aethiops
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDE4B 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273940 Ser133 GHSQRREsFLYRSDS Chlorocebus aethiops COS-1 Cell
pmid sentence
Long PDE4 isoforms from all four sub-families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed.These were Ser89Ala-PDE4A8, Ser133Ala-PDE4B1, Ser13Ala-PDE4C2 and Ser126Ala-PDE4D5.
Identifier Residue Sequence Organism Cell Line
SIGNOR-275986 Ser133 GHSQRREsFLYRSDS Chlorocebus aethiops COS-1 Cell
pmid sentence
Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.
Publications: 2 Organism: Chlorocebus Aethiops
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDE4C 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273938 Ser14 GEGAEACsRLSRSRG Chlorocebus aethiops
pmid sentence
Long PDE4 isoforms from all four sub-families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed.These were Ser89Ala-PDE4A8, Ser133Ala-PDE4B1, Ser13Ala-PDE4C2 and Ser126Ala-PDE4D5.
Identifier Residue Sequence Organism Cell Line
SIGNOR-275987 Ser14 GEGAEACsRLSRSRG Chlorocebus aethiops
pmid sentence
Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.
Publications: 2 Organism: Chlorocebus Aethiops
+ PKAup-regulates activity img/direct-activation.png phosphorylation CDK18 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264559 Ser14 KNFKRRFsLSVPRTE
pmid sentence
We previously revealed that PCTK3 is activated by two pathways: interaction with cytoplasmic cyclin A and phosphorylation at Ser-12 by protein kinase A (PKA)12. Activated PCTK3 phosphorylates retinoblastoma protein (Rb) in vitro. 
Publications: 1
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation CAD 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-267442 Ser1406 GAGGRRLsSFVTKGY in vitro
pmid sentence
The multifunctional protein CAD initiates de novo pyrimidine biosynthesis in mammalian cells. CAD is activated by MAP kinase (Erk1/2) just prior to the S phase of the cell cycle, when the demand for pyrimidine nucleotides is greatest, and down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. MAP kinase phosphorylates Thr456, while PKA phosphorylates Ser1406 and Ser1859, although only Ser1406 is involved in regulation. 
Publications: 1 Organism: In Vitro
Pathways:Nucleotide Biosynthesis
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDE4A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275985 Ser145 ATSQRREsFLYRSDS Chlorocebus aethiops COS-1 Cell
pmid sentence
Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.
Identifier Residue Sequence Organism Cell Line
SIGNOR-273937 Ser89 TRMSWPSsFHGTGTG Chlorocebus aethiops COS-1 Cell
pmid sentence
Long PDE4 isoforms from all four sub-families can be phosphorylated by protein kinase A (PKA). This leads to an increase in their activity and may thus contribute to cellular desensitization processes in cells where these isoforms are selectively expressed.These were Ser89Ala-PDE4A8, Ser133Ala-PDE4B1, Ser13Ala-PDE4C2 and Ser126Ala-PDE4D5.
Publications: 2 Organism: Chlorocebus Aethiops
+ PKAup-regulates activity img/direct-activation.png phosphorylation AQP5 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272087 Ser156 STDSRRTsPVGSPAL Homo sapiens HEK-293 Cell
pmid sentence
AQP5 can be directly phosphorylated by PKA at Ser 156 |Our data hint at a mechanism whereby phosphorylation of Ser 156 in AQP5 increases its membrane localization, thereby enhancing cancer cell proliferation.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation TRPV4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276232 Ser162 FDIVSRGsTADLDGL in vitro
pmid sentence
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-260885 Ser162 FDIVSRGsTADLDGL Homo sapiens
pmid sentence
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-260883 Ser189 DEEFREPsTGKTCLP Homo sapiens
pmid sentence
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-276233 Ser189 DEEFREPsTGKTCLP in vitro
pmid sentence
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-260881 Thr175 GLLPFLLtHKKRLTD Homo sapiens
pmid sentence
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-276231 Thr175 GLLPFLLtHKKRLTD in vitro
pmid sentence
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: 6 Organism: In Vitro, Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation NOXA1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264712 Ser172 DQVQRRGsLPPRQVP Homo sapiens Colonic Epithelium Cell Line
pmid sentence
On the other hand, our group has shown that protein kinase A (PKA) inhibits Nox1 activity in colon epithelial cells by phosphorylating NoxA1 at two distinct sites, Ser172 and Ser461
Identifier Residue Sequence Organism Cell Line
SIGNOR-264713 Ser461 VPAGPRMsGAPGRLP Homo sapiens Colonic Epithelium Cell Line
pmid sentence
On the other hand, our group has shown that protein kinase A (PKA) inhibits Nox1 activity in colon epithelial cells by phosphorylating NoxA1 at two distinct sites, Ser172 and Ser461
Publications: 2 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation RAP1A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-278057 Ser180 KKKPKKKsCLLL Homo sapiens Leukocyte
pmid sentence
Rap1 is phosphorylated and activated by PKA in neutrophils and platelets
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation FRAT1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276058 Ser188 RLQQRRGsQPETRTG Homo sapiens HEK-293T Cell
pmid sentence
Protein kinase A (PKA) was found to phosphorylate Ser188 in vitro as well as in intact cells. Importantly, activation of endogenous cAMP-coupled beta-adrenergic receptors with norepinephrine stimulated the phosphorylation of FRAT1 at Ser188. GSK-3 was also able to phosphorylate FRAT1 at Ser188 and other residues in vitro or when overexpressed in intact cells.  Phosphorylation of Ser188 by PKA inhibited the ability of FRAT1 to activate beta-catenin-dependent transcription.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation PTPN11 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276894 Ser189 GGGERFDsLTDLVEH Homo sapiens HEK-293T Cell
pmid sentence
 We identified two key amino acids in Shp2 that are phosphorylated by PKA. Thr-73 contributes a helix cap to helix αB within the N-terminal SH2 domain of Shp2, whereas Ser-189 occupies an equivalent position within the C-terminal SH2 domain. Utilizing double mutant PKA phosphodeficient (T73A/S189A) and phosphomimetic (T73D/S189D) constructs, in vitro binding assays, and phosphatase activity assays, we demonstrate that phosphorylation of these residues disrupts Shp2 interaction with tyrosine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-276893 Thr73 YGGEKFAtLAELVQY Homo sapiens HEK-293T Cell
pmid sentence
 We identified two key amino acids in Shp2 that are phosphorylated by PKA. Thr-73 contributes a helix cap to helix αB within the N-terminal SH2 domain of Shp2, whereas Ser-189 occupies an equivalent position within the C-terminal SH2 domain. Utilizing double mutant PKA phosphodeficient (T73A/S189A) and phosphomimetic (T73D/S189D) constructs, in vitro binding assays, and phosphatase activity assays, we demonstrate that phosphorylation of these residues disrupts Shp2 interaction with tyrosine-phosphorylated ligands and inhibits its protein-tyrosine phosphatase activity. 
Publications: 2 Organism: Homo Sapiens
Pathways:FLT3-ITD signaling
+ PKAup-regulates activity img/direct-activation.png phosphorylation GSTA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264796 Ser189 QEYTVKLsNIPTIKR 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
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation PPM1B 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277825 Ser195 MIQRVNGsLAVSRAL Homo sapiens HEK-293 Cell
pmid sentence
Collectively, these data suggest that PKA destabilizes PP2Cβ upon inflammatory stimuli via phosphorylation of Ser-195 in PP2Cβ.
Identifier Residue Sequence Organism Cell Line
SIGNOR-276494 Ser195 MIQRVNGsLAVSRAL Homo sapiens HEK-293 Cell
pmid sentence
Here, we show that protein kinase A (PKA) phosphorylates the PP2Cβ, which was inhibited by PKA-specific inhibitor, H89. Mutation analysis of serine residues in PP2Cβ revealed that Ser-195 in PP2Cβ is phosphorylated by PKA. Importantly, PKA inhibition by H89 abrogated the Forskolin-induced destabilization of PP2Cβ against ubiquitin-dependent proteosomal degradation pathway.
Publications: 2 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation GRK1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-274079 Ser21 AFIAARGsFDGSSSQ in vitro
pmid sentence
PKA Phosphorylates GRK1 on Ser21. Phosphorylation by PKA inhibits GRK1 activity.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260841 Ser21 AFIAARGsFDGSSSQ Homo sapiens
pmid sentence
Phosphorylation of GRK1 and GRK7 by cAMP-dependent Protein Kinase Attenuates Their Enzymatic Activities | We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.
Identifier Residue Sequence Organism Cell Line
SIGNOR-276034 Ser21 AFIAARGsFDGSSSQ in vitro
pmid sentence
 We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.Phosphorylation of GRK1 and GRK7 by PKA reduces the ability of GRK1 and GRK7 to phosphorylate rhodopsin in vitro.
Publications: 3 Organism: In Vitro, Homo Sapiens
+ PKAup-regulates quantity by stabilization img/direct-activation.png phosphorylation NKD2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273782 Ser223 SAHVRRPsTDPQPCS Homo sapiens HEK-293 Cell
pmid sentence
VIP and PGE2 rapidly activate protein kinase A (PKA) that then phosphorylates NKD2 at Ser-223, a process that is facilitated by the molecular scaffold A-kinase anchoring protein 12 (AKAP12). This phosphorylation stabilized NKD2, ensuring efficient cell-surface delivery of TGFα and increased EGFR activation.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation GRK7 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-274081 Ser23 YLQARKPsDCDSKEL in vitro
pmid sentence
PKA Phosphorylates GRK7 on Ser23 and Ser36. Phosphorylation by PKA inhibits GRK7 activity
Identifier Residue Sequence Organism Cell Line
SIGNOR-276036 Ser23 YLQARKPsDCDSKEL in vitro
pmid sentence
 We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.Phosphorylation of GRK1 and GRK7 by PKA reduces the ability of GRK1 and GRK7 to phosphorylate rhodopsin in vitro.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260839 Ser23 YLQARKPsDCDSKEL Homo sapiens
pmid sentence
Phosphorylation of GRK1 and GRK7 by cAMP-dependent Protein Kinase Attenuates Their Enzymatic Activities | We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.
Identifier Residue Sequence Organism Cell Line
SIGNOR-260840 Ser36 ELQRRRRsLALPGLQ Homo sapiens
pmid sentence
Phosphorylation of GRK1 and GRK7 by cAMP-dependent Protein Kinase Attenuates Their Enzymatic Activities | We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.
Identifier Residue Sequence Organism Cell Line
SIGNOR-274080 Ser36 ELQRRRRsLALPGLQ in vitro
pmid sentence
PKA Phosphorylates GRK7 on Ser23 and Ser36. Phosphorylation by PKA inhibits GRK7 activity
Identifier Residue Sequence Organism Cell Line
SIGNOR-276035 Ser36 ELQRRRRsLALPGLQ in vitro
pmid sentence
 We also determined that cAMP-dependent protein kinase (PKA) phosphorylates GRK1 at Ser(21) and GRK7 at Ser(23) and Ser(36) in vitro. These sites are also phosphorylated when FLAG-tagged GRK1 and GRK7 are expressed in HEK-293 cells treated with forskolin to stimulate the endogenous production of cAMP and activation of PKA.Phosphorylation of GRK1 and GRK7 by PKA reduces the ability of GRK1 and GRK7 to phosphorylate rhodopsin in vitro.
Publications: 6 Organism: In Vitro, Homo Sapiens
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation HSPB8 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276152 Ser24 RRDPFRDsPLSSRLL in vitro
pmid sentence
Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 susceptibility to chymotrypsinolysis. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-276151 Ser57 DWALPRLsSAWPGTL in vitro
pmid sentence
Human small heat shock protein with molecular mass 22 kD (HSP22, HspB8) contains two Ser residues (Ser24 and Ser57) in consensus sequence RXS and is effectively phosphorylated by cAMP-dependent protein kinase in vitro. Mutation S24D did not affect, whereas mutations S57D or S24,57D prevented phosphorylation of HSP22 by cAMP-dependent protein kinase thus indicating that Ser57 is the primary site of phosphorylation. Phosphorylation (or mutation) of Ser57 (or Ser24 and Ser57) resulted in changes of the local environment of tryptophan residues and increased HSP22 susceptibility to chymotrypsinolysis. 
Publications: 2 Organism: In Vitro
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation SNAI2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277905 Ser247 KYQCKNCsKTFSRMS Homo sapiens HuH-7 Cell
pmid sentence
 PKA-dependent phosphorylation is pivotal for FBXO28-mediated SNAI2 degradation. 
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation KCNK18 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263154 Ser252 QAMERSNsCPELVLG in vitro
pmid sentence
Phosphorylation of serine 264 in mouse TRESK was required for the binding of 14-3-3η. PKA was used to phosphorylate serine 264 in our further in vitro experiments.
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation AQP2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264563 Ser256 REVRRRQsVELHSPQ Canis lupus familiaris MDCK Cell
pmid sentence
For Ser-256 in AQP2, this hypothesis is in line with data from Zeleninaet al. (35), who showed that in isolated rat inner medulla prostaglandin E2 induces internalization of AQP2 without decreasing the amount of PKA-phosphorylated AQP2.|Phosphorylation of Ser-256 Is Necessary and Sufficient for Localization of AQP2 in the Apical Plasma Membrane
Publications: 1 Organism: Canis Lupus Familiaris
+ PKAup-regulates activity img/direct-activation.png phosphorylation SLC8B1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275728 Ser258 YQRQRRGsLFCPMPV
pmid sentence
However, the PDE2-inhibitory effect is eliminated when the mitochondrial S258A NCLX mutant that mimics a non-PKA phosphorylated state of NCLX is expressed. Altogether, our findings indicate that NCLX is regulated by the mitochondrial PDE2A2 form.|We show that caffeine, by inhibiting PDE2, enhances PKA phosphorylation leading to mitochondrial NCLX activation, thereby reducing neuronal excitotoxicity and enhancing learning in mice. |Moreover, PDE2 acts by diminishing mitochondrial cAMP, thus promoting NCLX phosphorylation at its PKA site.
Publications: 1
+ PKAup-regulates activity img/direct-activation.png phosphorylation GATA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276043 Ser262 IKPQRRLsASRRVGL Homo sapiens MCF-7 Cell
pmid sentence
 PKA-mediated phosphorylation increases the interaction between GATA3 and LRH-1 and the requirement for PKA in aromatase PII promoter stimulation involves at least three specific amino acid residues: GATA3 Ser308, GATA4 Ser261, and LRH-1 Ser469. 
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation ATG16L1 (isoform 2) 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277489 Ser268 SRAATRRsVSSFPVP in vitro
pmid sentence
PKA phosphorylates ATG16L1α at Ser268 and ATG16L1β at Ser269, driving phosphorylation-dependent degradation of ATG16L1 protein. 
Publications: 1 Organism: In Vitro
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation ATG16L1 (isoform 1) 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277488 Ser269 RAATKRLsQPAGGLL in vitro
pmid sentence
PKA phosphorylates ATG16L1α at Ser268 and ATG16L1β at Ser269, driving phosphorylation-dependent degradation of ATG16L1 protein. 
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation SEC14L2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273788 Ser289 VQISRGSsHQVEYEI in vitro
pmid sentence
 Thus, phosphorylation of SPF at Ser-289 appears necessary for maximal stimulation of squalene monooxygenase activity in vitro and absolutely required for the stimulation of cholesterol synthesis in cell culture. the 2.3-fold activation of SPF by PKA was reduced by 60% in the S289A mutant, indicating that phosphorylation of this site contributes to the activation of SPF.
Identifier Residue Sequence Organism Cell Line
SIGNOR-276028 Ser289 VQISRGSsHQVEYEI in vitro
pmid sentence
These results suggest that phosphorylation of SPF by PKA is a dynamic process and that, in the absence of PKA activity, SPF is rapidly inactivated.Thus, phosphorylation of SPF at Ser-289 appears necessary for maximal stimulation of squalene monooxygenase activity in vitro and absolutely required for the stimulation of cholesterol synthesis in cell culture.
Publications: 2 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation NLRP3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277274 Ser295 HKIVRKPsRILFLMD in vitro
pmid sentence
PKA directly phosphorylated the cytoplasmic receptor NLRP3 and attenuated its ATPase function. We found that Ser295 in human NLRP3 was critical for rapid inhibition and PKA phosphorylation.
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation GATA3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276042 Ser308 IKPKRRLsAARRAGT Homo sapiens MCF-7 Cell
pmid sentence
 PKA-mediated phosphorylation increases the interaction between GATA3 and LRH-1 and the requirement for PKA in aromatase PII promoter stimulation involves at least three specific amino acid residues: GATA3 Ser308, GATA4 Ser261, and LRH-1 Ser469. 
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDE8A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276416 Ser359 HKDRRKGsLDVKAVA in vitro
pmid sentence
We show that under elevated cAMP conditions, PKA acts to phosphorylate PDE8A on serine 359 and this action serves to enhance the activity of the enzyme. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-273783 Ser359 HKDRRKGsLDVKAVA Homo sapiens HeLa Cell
pmid sentence
 We show that under elevated cAMP conditions, PKA acts to phosphorylate PDE8A on serine 359 and this action serves to enhance the activity of the enzyme. 
Publications: 2 Organism: In Vitro, Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation GRK7 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263152 Ser36 ELQRRRRsLALPGLQ Xenopus laevis
pmid sentence
Recently, we have defined sites of phosphorylation by cAMP-dependent protein kinase (PKA) in the amino termini of both GRK1 and GRK7 in vitro. To determine the conditions under which GRK7 is phosphorylated in vivo, we have generated an antibody that recognizes GRK7 phosphorylated on Ser36, the PKA phosphorylation site. Using this phospho-specific antibody, we have shown that GRK7 is phosphorylated in vivo and is located in the cone inner and outer segments of mammalian, amphibian and fish retinas. The conservation of phosphorylation at Ser36 in GRK7 in these different species (which span a 400 million-year evolutionary period), and its light-dependent regulation, indicates that phosphorylation plays an important role in the function of GRK7
Publications: 1 Organism: Xenopus Laevis
Tissue: Retina
+ PKAup-regulates activity img/direct-activation.png phosphorylation SCN5A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275765 Ser36 AEKQARGsTTLQESR Homo sapiens Neuron
pmid sentence
Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate–activated protein kinase (AMPK)–dependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. | Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5
Identifier Residue Sequence Organism Cell Line
SIGNOR-275991 Ser525 TSMKPRSsRGSIFTF in vitro
pmid sentence
These results demonstrate that the effect of PKA stimulation to increase cardiac INa requires at least 2 processes: phosphorylation of consensus sites in the I-II interdomain linker, and one or more additional molecular events mediated by the kinase, that could include phosphorylation of other substrates/proteins.
Identifier Residue Sequence Organism Cell Line
SIGNOR-275766 Ser525 TSMKPRSsRGSIFTF Homo sapiens Neuron
pmid sentence
Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate–activated protein kinase (AMPK)–dependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. | Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5
Identifier Residue Sequence Organism Cell Line
SIGNOR-275764 Ser528 KPRSSRGsIFTFRRR Homo sapiens Neuron
pmid sentence
Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate–activated protein kinase (AMPK)–dependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. | Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5
Identifier Residue Sequence Organism Cell Line
SIGNOR-275992 Ser528 KPRSSRGsIFTFRRR in vitro
pmid sentence
These results demonstrate that the effect of PKA stimulation to increase cardiac INa requires at least 2 processes: phosphorylation of consensus sites in the I-II interdomain linker, and one or more additional molecular events mediated by the kinase, that could include phosphorylation of other substrates/proteins.
Publications: 5 Organism: Homo Sapiens, In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation PSMD2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273898 Ser361 ENNRFGGsGSQVDSA in vitro
pmid sentence
Seven of these kinases (PIM1/2/3, MAP4K1/2, PKA, and NEK6) directly and robustly phosphorylated recombinant GST-Rpn1 at S361 in vitro (Fig. 3D and SI Appendix, Fig. S3 A and B). 
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation CHKB 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275632 Ser39 TPKRRRAsSLSRDAE
pmid sentence
Choline kinase beta (CKbeta) is one of the CK isozymes involved in the biosynthesis of phosphatidylcholine. | This study provides evidence for CKβ phosphorylation by protein kinase A (PKA).|Phosphorylation sites were located on CKβ residues serine-39 and serine-40 as determined by mass spectrometry and site-directed mutagenesis. Phosphorylation increased the catalytic efficiencies for the substrates choline and ATP about 2-fold, without affecting ethanolamine phosphorylation, and the S39D/S40D CKβ phosphorylation mimic behaved kinetically very similar.
Identifier Residue Sequence Organism Cell Line
SIGNOR-275631 Ser40 PKRRRASsLSRDAER
pmid sentence
Choline kinase beta (CKbeta) is one of the CK isozymes involved in the biosynthesis of phosphatidylcholine. | This study provides evidence for CKβ phosphorylation by protein kinase A (PKA).|Phosphorylation sites were located on CKβ residues serine-39 and serine-40 as determined by mass spectrometry and site-directed mutagenesis. Phosphorylation increased the catalytic efficiencies for the substrates choline and ATP about 2-fold, without affecting ethanolamine phosphorylation, and the S39D/S40D CKβ phosphorylation mimic behaved kinetically very similar.
Publications: 2
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation KCNJ2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273779 Ser425 PRPLRREsEI in vitro
pmid sentence
KCNJ2 encodes Kir2.1, a pore-forming subunit of the cardiac inward rectifier current, I(K1). This PKA-simulated catecholaminergic stimulation caused marked reduction of outward I(K1) compared with Kir2.1-WT. PKA-induced reduction in I(K1) was eliminated by mutating the phosphorylation site at serine 425 (S425N).
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation KLHL3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273824 Ser433 PMNTRRSsVGVGVVE in vitro
pmid sentence
Consistent with the fact that S433 is a component of Akt and PKA phosphorylation motifs, in vitro kinase assay demonstrated that Akt and PKA can phosphorylate KLHL3 at S433, that was previously reported to be phosphorylated by PKC. 
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation MFN2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-274137 Ser442 AEEIRRLSVLVDDYQ Mus musculus Vascular Smooth Muscle Cell
pmid sentence
Mitofusin 2 (Mfn2) is an important suppressor of vascular smooth muscle cell (VSMC) proliferation. It contains a protein kinase A (PKA) phosphorylation site at serine 442 (S442) and can be phosphorylated by PKA
Publications: 1 Organism: Mus Musculus
+ PKAup-regulates activity img/direct-activation.png phosphorylation KCNJ4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263153 Ser443 NISYRREsAI Homo sapiens HEK-293 Cell
pmid sentence
Kir2.3 can be phosphorylated by PKAin vitro. We further show that the phosphorylation/dephosphorylation of Ser443 within the C-terminal Kir2.3 PDZ-binding motif RRESAI dynamically regulates the Kir2.3/TIP-1 association in heterologous HEK293T cells. These data suggest that TIP-1 may act as an important regulator for the endocytic pathway of Kir2.3.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates quantity img/direct_inhibition.png phosphorylation KCNA1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273777 Ser446 SDLSRRSsSTMSKSE Homo sapiens HMEpC Cell
pmid sentence
Phosphorylation of KCNA1 at Ser446 by PKA is involved on its cytoplasmic retention
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation SLC2A2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-250049 Ser491 VPETKGKsFEEIAAE Chlorocebus aethiops
pmid sentence
GLUT2 is rapidly phosphorylated by protein kinase A following activation of adenylyl cyclase by forskolin. serines 489 and 501/503 and threonine 510 in the carboxyl-terminal tail of the transporter are the in vitro and in vivo sites of phosphorylation. Stimulation of GLUT2 phosphorylation in beta cells reduces the initial rate of 3-O-methyl glucose uptake by approximately 48% but does not change the Michaelis constant. a consequence of GLUT2 phosphorylation is a reduction of its catalytic activity.
Publications: 1 Organism: Chlorocebus Aethiops
+ PKAup-regulates activity img/direct-activation.png phosphorylation PDZK1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273784 Ser505 MAKERAHsTASHSSS Cricetulus griseus CHO-K1 Cell
pmid sentence
Metabolic labeling experiments and phosphoamino acid analysis revealed that PDZK1 is phosphorylated at Ser residues within this region. Point-mutation analysis demonstrated that PDZK1 is phosphorylated at Ser-509. Interestingly, a mutant PDZK1, in which Ser-509 was replaced with Ala, lost the ability to up-regulate SR-BI protein.
Publications: 1 Organism: Cricetulus Griseus
+ PKAup-regulates activity img/direct-activation.png phosphorylation NR5A2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276041 Ser510 LPEIRAIsMQAEEYL Homo sapiens MCF-7 Cell
pmid sentence
 PKA-mediated phosphorylation increases the interaction between GATA3 and LRH-1 and the requirement for PKA in aromatase PII promoter stimulation involves at least three specific amino acid residues: GATA3 Ser308, GATA4 Ser261, and LRH-1 Ser469. 
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation SLC9A3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277847 Ser555 AEGERRGsLAFIRSP Homo sapiens CACO-2 Cell
pmid sentence
AMPK activation by 5-aminoimidazole-4-carboxamide ribonucleoside (AICAR) phosphorylated NHE3 at S555. S555 is the primary site of phosphorylation by protein kinase A (PKA), but AMPK phosphorylated S555 independently of PKA. We conclude that AMPK activation inhibits NHE3 activity and NHE3 inhibition is associated with phosphorylation of NHE3 at S555 and S563.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation HDAC4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277423 Ser584 EPGQRQPsEQELLFR in vitro
pmid sentence
 In vitro kinase assays have established that Ser584 and Ser265/266 are phosphorylated by protein kinase A (PKA). Overexpression of site-specific HDAC4 mutants (S584A, S265/266A) in HEK 293T cells, followed by HDAC activity assays, revealed the mutants to be less active than the wild-type protein.
Identifier Residue Sequence Organism Cell Line
SIGNOR-277425 in vitro
pmid sentence
 In vitro kinase assays have established that Ser584 and Ser265/266 are phosphorylated by protein kinase A (PKA). Overexpression of site-specific HDAC4 mutants (S584A, S265/266A) in HEK 293T cells, followed by HDAC activity assays, revealed the mutants to be less active than the wild-type protein.
Identifier Residue Sequence Organism Cell Line
SIGNOR-277424 in vitro
pmid sentence
 In vitro kinase assays have established that Ser584 and Ser265/266 are phosphorylated by protein kinase A (PKA). Overexpression of site-specific HDAC4 mutants (S584A, S265/266A) in HEK 293T cells, followed by HDAC activity assays, revealed the mutants to be less active than the wild-type protein.
Publications: 3 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation MYOM1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263156 Ser618 ARLKSRPsAPWTGQI in vitro
pmid sentence
This interaction is regulated by phosphorylation of Ser482 in the linker between myomesin domains My4 and My5. Myomesin phosphorylation at this site by cAMP-dependent kinase and similar or identical activities in muscle extracts block the association with titin.
Publications: 1 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation DNM1L 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-262551 Ser637 VPVARKLsAREQRDC in vitro
pmid sentence
For example, protein kinase A (PKA) phosphorylation of Drp1S600 has been reported to decrease Drp1 GTPase activity in vitro (23, 24), whereas phosphorylation of the same conserved serine residue by Ca2+-calmodulin–dependent protein kinase Iα (CaMKIα) in Drp1 isoform 3 has been reported to cause a significant increase in mitochondrial fission
Publications: 1 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation ARHGEF6 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272163 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-272160 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
+ PKAup-regulates activity img/direct-activation.png dephosphorylation ABCB1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272508 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-272509 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
Identifier Residue Sequence Organism Cell Line
SIGNOR-272510 Ser683 QAQDRKLsTKEALDE 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
+ PKAup-regulates activity img/direct-activation.png phosphorylation SLITRK1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273634 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
+ PKA img/unknown.png phosphorylation SI 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-263157 Ser7 sGLEISLI in vitro
pmid sentence
This paper reports the phosphorylation of the intracellular N-terminal tail of sucrase-isomaltase by protein kinase A and shows that this phosphorylation is targeted to Ser6 within a sequence Arg/Lys/Lys-Phe-Ser, which is conserved in all sucrase-isomaltase sequences known so far.
Publications: 1 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation ARHGAP17 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-272156 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
+ PKAup-regulates activity img/direct-activation.png phosphorylation PRKD2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275952 Ser706 ARIIGEKsFRRSVVG
pmid sentence
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-275951 Ser710 GEKSFRRsVVGTPAY
pmid sentence
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-275950 Ser876 QGLAERIsVL
pmid sentence
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
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation MOS 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-260819 Ser73 LGAGGFGsVYKATYR Homo sapiens
pmid sentence
The purified PKA catalytic subunit was able to phosphorylate recombinant p37v-mos in vitro, suggesting that the mechanism of in vivo inhibition of v-Mos kinase involves direct phosphorylation by PKA.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation PRKD3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275924 Ser731 ARIIGEKsFRRSVVG
pmid sentence
The results presented in this study indicate that during mitosis, PKD3 and PKD are phosphorylated at Ser(731) and Ser(744) within their activation loop by a mechanism that requires protein kinase C. Mitosis-associated PKD3 Ser(731) and PKD Ser(744) phosphorylation is related to the catalytic activation of these kinases as evidenced by in vivo phosphorylation of histone deacetylase 5, a substrate of PKD and PKD3.
Publications: 1
+ PKAup-regulates activity img/direct-activation.png phosphorylation PRKD1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275925 Ser742 GEKSFRRsVVGTPAY
pmid sentence
The results presented in this study indicate that during mitosis, PKD3 and PKD are phosphorylated at Ser(731) and Ser(744) within their activation loop by a mechanism that requires protein kinase C. Mitosis-associated PKD3 Ser(731) and PKD Ser(744) phosphorylation is related to the catalytic activation of these kinases as evidenced by in vivo phosphorylation of histone deacetylase 5, a substrate of PKD and PKD3.
Publications: 1
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation TRPC5 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273790 Ser794 SGGARAKsKSVSFNL Homo sapiens HEK-293 Cell
pmid sentence
Together, these results suggest that TRPC5 is directly phosphorylated by G(s)/cAMP/PKA at positions S794 and S796. These inhibitory effects were blocked by the protein kinase A (PKA) inhibitors, KT-5720 and H-89, as well as by two point mutations at consensus PKA phosphorylation sites on TRPC5 (S794A and S796A).
Identifier Residue Sequence Organism Cell Line
SIGNOR-276340 Ser794 SGGARAKsKSVSFNL Homo sapiens HEK-293 Cell
pmid sentence
We show that TRPC5 channels may become directly phosphorylated by PKA at serine residues 794 and 796, and that this phosphorylation abolishes the receptor-operated nonselective cation current mediated by TRPC5 channels in HEK-293 cells.
Identifier Residue Sequence Organism Cell Line
SIGNOR-273789 Ser796 GARAKSKsVSFNLGC Homo sapiens HEK-293 Cell
pmid sentence
Together, these results suggest that TRPC5 is directly phosphorylated by G(s)/cAMP/PKA at positions S794 and S796. These inhibitory effects were blocked by the protein kinase A (PKA) inhibitors, KT-5720 and H-89, as well as by two point mutations at consensus PKA phosphorylation sites on TRPC5 (S794A and S796A).
Identifier Residue Sequence Organism Cell Line
SIGNOR-276339 Ser796 GARAKSKsVSFNLGC Homo sapiens HEK-293 Cell
pmid sentence
We show that TRPC5 channels may become directly phosphorylated by PKA at serine residues 794 and 796, and that this phosphorylation abolishes the receptor-operated nonselective cation current mediated by TRPC5 channels in HEK-293 cells.
Publications: 4 Organism: Homo Sapiens
+ PKAdown-regulates quantity img/direct_inhibition.png phosphorylation TRPC5 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-277824 Ser796 GARAKSKsVSFNLGC Homo sapiens HEK-293 Cell
pmid sentence
Together, these results suggest that TRPC5 is directly phosphorylated by G(s)/cAMP/PKA at positions S794 and S796. These inhibitory effects were blocked by the protein kinase A (PKA) inhibitors, KT-5720 and H-89, as well as by two point mutations at consensus PKA phosphorylation sites on TRPC5 (S794A and S796A).
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation PIK3R1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276343 Ser83 YIGRKKIsPPTPKPR in vitro
pmid sentence
in vitro kinase assays using purified protein kinase A (PKA) and either GST fused full length p85 (GST-p85) or GST fused p85 peptide spanning amino acids 50-109 (GST-p85Δ2) as substrate.  Serine 83 phosphorylation on p85 is necessary for PI3K activation and membrane translocation in 14-3-3ζ overexpressing cells 
Publications: 1 Organism: In Vitro
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation GSK3B 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264819 Ser9 SGRPRTTsFAESCKP
pmid sentence
Interestingly, GSK3beta can be released from the multienzyme complex in response to PKA phosphorylation on serine 9, which suppresses GSK3beta activity.
Publications: 1
Pathways:FLT3-ITD signaling
+ PKAup-regulates activity img/direct-activation.png phosphorylation LIPE 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276174 Ser950 EGFHPRRsSQGATQM
pmid sentence
 Our results demonstrate that PKA activates human HSL against lipid substrates in vitro primarily through phosphorylation of Ser649 and Ser650. 
Identifier Residue Sequence Organism Cell Line
SIGNOR-276175 Ser951 GFHPRRSsQGATQMP
pmid sentence
 Our results demonstrate that PKA activates human HSL against lipid substrates in vitro primarily through phosphorylation of Ser649 and Ser650. 
Publications: 2
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation PIK3CG 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276321 Thr1024 YLALRHHtNLLIILF Homo sapiens HEK-293T Cell
pmid sentence
Anchored PKA activates PDE3B to enhance cAMP degradation and phosphorylates p110γ to inhibit PIP(3) production. 
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation LRP6 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275416 Thr1548 YAPSRRMtSVATAKG in vitro
pmid sentence
PKA phosphorylated LRP6, which enhanced the binding of Gα(s) to LRP6, its localization to the plasma membrane, and the production of cAMP in response to PTH. Only alteration of Thr1548 abolished the phosphorylation of LRP6C by PKA (Fig. 6B), and mass spectrometry analysis confirmed that Thr1548 was the PKA phosphorylation site in LRP6C (fig. S1).
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation BRSK2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276056 Thr260 VDAARRLtLEHIQKH in vitro
pmid sentence
BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260
Publications: 1 Organism: In Vitro
+ PKAup-regulates activity img/direct-activation.png phosphorylation PPP1R1B 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264956 Thr34 MIRRRRPtPAMLFRL Homo sapiens Neuron
pmid sentence
DARPP-32 (dopamine and cyclic AMP-regulated phospho-protein, relative molecular mass 32,000) is converted into an inhibitor of protein phosphatase 1 when it is phosphorylated by protein kinase A (PKA) at threonine 34.‚ 
Publications: 1 Organism: Homo Sapiens
Pathways:Dopaminergic Synapse
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation GLI1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276044 Thr374 PGCTKRYtDPSSLRK Chlorocebus aethiops COS-7 Cell
pmid sentence
Here, we report that activation of PKA retains Gli1 in the cytoplasm.Mutation analysis identifies Thr374 as a major PKA site determining Gli1 protein localization. 
Publications: 1 Organism: Chlorocebus Aethiops
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation KCNA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273778 Thr601 LKKFRSStSSSLGDK Homo sapiens HEK-293 Cell
pmid sentence
 In GIP receptor-expressing HEK293 cells, GIP reduced A-type peak ionic current amplitude of K(V)1.4 via activation of protein kinase A (PKA). Using mutant forms of K(V)1.4 with Ala-Ser/Thr substitutions in a potential PKA phosphorylation site, C-terminal phosphorylation was shown to be linked to GIP-mediated current amplitude decreases.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates quantity by destabilization img/direct_inhibition.png phosphorylation KCNA4 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276037 Thr601 LKKFRSStSSSLGDK Homo sapiens HEK-293 Cell
pmid sentence
In parallel experiments, it was shown that recombinant PKA catalytic subunits (Fig. 3A) or cell extracts from GIP-stimulated GIPR-HEK293-KV cells (Fig. 3B) increased phosphorylation of KV1.4, and active PKA phosphorylated Thr-601 in the C terminus of KV1.4 (Fig. 3D). These results therefore provide compelling evidence for a role for GIP-induced down-regulation of KV1.4, via phosphorylation-dependent endocytosis of the channel protein, in the modulation of insulin secretion.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation IQGAP2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-273742 Thr716 EYMHRRQtFIDNTDS Homo sapiens
pmid sentence
We show that IQGAP2 is regulated by an interaction with the A-kinase anchoring protein AKAP220. Phosphorylation of IQGAP2 via AKAP220-anchored PKA leads to enhanced Rac binding. Since AKAPs function to direct PKA toward specific substrates, we proposed that the formation of an IQGAP2/AKAP220/PKA ternary complex sharpens the response to cAMP.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates quantity by stabilization img/direct-activation.png phosphorylation DIAPH1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276484 Thr768 PVLPFGLtPKKLYKP Homo sapiens NCI-H295R Cell
pmid sentence
 DIAPH1 is phosphorylated in response to dibutyryl cAMP (Bt2cAMP) at Thr-759 via a pathway that requires extracellular signal-related kinase (ERK).We also show that Bt2cAMP promotes the PKA- and ERK-dependent phosphorylation of DIAPH1 at T759 and that mutation of this site alters the stability of the protein and the rate of cAMP-stimulated mitochondrial movement.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation GAD1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-276009 Thr91 RDARFRRtETDFSNL 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. We have identified one specific phosphorylation site, threonine 91 (T91), in hGAD67 that can be phosphorylated by PKA using MALDI-TOF.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation ABCC8 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-278146 Homo sapiens Pancreatic Beta Cell
pmid sentence
Activated PKA and EPAC enhance insulin granular exocytosis by insulin granular priming and phosphorylates sulfonylurea receptor (SUR1) KATP channel subunit and thereby closes KATP-channels in the plasma membrane [13,43,82], leading to membrane depolarization, and opening of the voltage gated Ca2+-channels. This leads to an increased influx of extracellular Ca2+, which triggers fusion of intracellular insulin-containing granules with the plasma membrane and thereby insulin secretion.
Identifier Residue Sequence Organism Cell Line
SIGNOR-278147 Homo sapiens Pancreatic Beta Cell
pmid sentence
Activated PKA and EPAC enhance insulin granular exocytosis by insulin granular priming and phosphorylates sulfonylurea receptor (SUR1) KATP channel subunit and thereby closes KATP-channels in the plasma membrane [13,43,82], leading to membrane depolarization, and opening of the voltage gated Ca2+-channels. This leads to an increased influx of extracellular Ca2+, which triggers fusion of intracellular insulin-containing granules with the plasma membrane and thereby insulin secretion.
Publications: 2 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation SYN1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264108 Homo sapiens Neuron
pmid sentence
Synapsins are exclusively localized to synaptic vesicles, which they coat as peripheral membrane proteins; they probably constitute one of the most abundant neuronal PKA substrates. Our study reveals an unexpectedly dynamic state of synapsins in nerve terminals: any changes in PKA or CaM Kinase I activity will modulate the amount of synapsin on synaptic vesicles. PKA Activation Triggers Synapsin Dissociation
Publications: 1 Organism: Homo Sapiens
Pathways:Neurotransmitters release
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation PHKA2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-267408 Homo sapiens
pmid sentence
Phosphorylation of the alpha and beta subunits by the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) also relieves inhibition of the gamma subunit and thereby activates the enzyme.
Publications: 1 Organism: Homo Sapiens
Pathways:Glycogenolysis
+ PKAup-regulates activity img/direct-activation.png phosphorylation mTORC2 0.351
Identifier Residue Sequence Organism Cell Line
SIGNOR-278149 Homo sapiens Pancreatic Beta Cell
pmid sentence
Additionally, PKA activates transducer of regulated CREB (TORC2) and cAMP response element-binding protein (CREB), which leads to beta cell proliferation through CREB- and TORC2-mediated IRS2 gene expression
Publications: 1 Organism: Homo Sapiens
Pathways:FLT3-ITD signaling
+ PKAup-regulates quantity by stabilization img/direct-activation.png phosphorylation SMN1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-253114 Homo sapiens HEK-293 Cell
pmid sentence
PKA increases SMN complex formation and SMN stability.|As expected, SMN was phosphorylated by PKA (Fig. ​(Fig.6D).6D).
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation SYN2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264109 Homo sapiens Neuron
pmid sentence
Synapsins are exclusively localized to synaptic vesicles, which they coat as peripheral membrane proteins; they probably constitute one of the most abundant neuronal PKA substrates. Our study reveals an unexpectedly dynamic state of synapsins in nerve terminals: any changes in PKA or CaM Kinase I activity will modulate the amount of synapsin on synaptic vesicles. PKA Activation Triggers Synapsin Dissociation
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates img/direct-activation.png phosphorylation MYBPC3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270128 Homo sapiens
pmid sentence
Phosphorylation of cmybp-c by pka speeds actomyosin interactions and contributes to increased cardiac contractility following _-adrenergic stimulation.7, 8 phosphorylation by pka is essential for proper cardiac function /for the human isoform, three pka sites were previously identified (ser275, ser284, and ser304) /our results indicate that pka phosphorylates up to four sites in both the murine and human m-domains including a novel site not previously described for either protein (ser307 for mouse and ser311 for human).
Publications: 1 Organism: Homo Sapiens
Tissue: Muscle
+ PPP1R1Bdown-regulates activity img/direct_inhibition.png binding PKA 0.488
Identifier Residue Sequence Organism Cell Line
SIGNOR-265087 Homo sapiens Neuron
pmid sentence
We find that DARPP-32 is converted into an inhibitor of PKA when phosphorylated at threonine 75 by cyclin-dependent kinase 5 (Cdk5). Cdk5 phosphorylates DARPP-32 in vitro and in intact brain cells. Phospho-Thr 75 DARPP-32 inhibits PKA in vitro by a competitive mechanism.
Publications: 1 Organism: Homo Sapiens
Pathways:Dopaminergic Synapse
+ PKAup-regulates img/indirect-activation.png Synaptic_plasticity 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-264961 Homo sapiens Neuron
pmid sentence
PKA is activated by Group I mGluRs in ACC neurons. The cAMP signaling pathway contributes to the activity-dependent synaptic plasticity in the anterior cingulate cortex
Publications: 1 Organism: Homo Sapiens
Tissue: Anterior Cingulate Cortex
Pathways:Dopaminergic Synapse, Glutamatergic synapse, GABAergic synapse , Oxytocin signaling
+ 3',5'-cyclic AMPup-regulates activity img/direct-activation.png chemical activation PKA 0.8
Identifier Residue Sequence Organism Cell Line
SIGNOR-258763 Homo sapiens
pmid sentence
Inactive PKA exists as a holoenzyme, comprised of two regulatory (R) subunits and two catalytic subunits . In the presence of cAMP, the holoenzyme becomes active by binding two cAMP molecules cooperatively to each R subunit, resulting in a conformational change in the R subunits, thus releasing the two C subunits to phosphorylate downstream targets
Publications: 1 Organism: Homo Sapiens
Pathways:Dopaminergic Synapse, FLT3-ITD signaling, Glutamatergic synapse, GABAergic synapse , Nucleotide Biosynthesis, Neurotransmitters release, Oxytocin signaling, Thyroid Hormone Metabolism
+ PKAup-regulates activity img/direct-activation.png phosphorylation ENAH 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-268285 Homo sapiens
pmid sentence
 Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts
Publications: 1 Organism: Homo Sapiens
Pathways:Axon guidance
+ PKAup-regulates activity img/direct-activation.png phosphorylation EVL 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-268287 Homo sapiens
pmid sentence
 Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts
Publications: 1 Organism: Homo Sapiens
Pathways:Axon guidance
+ AKAP12up-regulates activity img/direct-activation.png relocalization PKA 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-271837
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
+ PKAup-regulates activity img/direct-activation.png relocalization V-ATPase 0.299
Identifier Residue Sequence Organism Cell Line
SIGNOR-277763 Homo sapiens HeLa Cell
pmid sentence
It is worth noting that CA-PKA failed to rescue macropinocytosis in KRAS-knockdown cells, indicating that whereas PKA activation is necessary for mutant KRAS-dependent plasma membrane translocation of V-ATPase and induction of macropinocytosis, it is not sufficient (Extended Data Fig. 6e).
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation PHKA1 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-267409 Homo sapiens
pmid sentence
Phosphorylation of the alpha and beta subunits by the 3',5'-cyclic adenosine monophosphate (cAMP)-dependent protein kinase (PKA) also relieves inhibition of the gamma subunit and thereby activates the enzyme.
Publications: 1 Organism: Homo Sapiens
Pathways:Glycogenolysis
+ ADCY3up-regulates activity img/direct-activation.png binding PKA 0.519
Identifier Residue Sequence Organism Cell Line
SIGNOR-278073 Homo sapiens HaCaT Cell
pmid sentence
Although the generated cAMP is primarily involved in transmitting odor information to the olfactory bulbs in the brain, it has been demonstrated that an increase in cellular cAMP by ADCY3 could stimulate protein kinase A (PKA) signaling, which is well-known to regulate diverse physiological and pathological processes
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation TENT2 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270130 Homo sapiens HEK-293 Cell
pmid sentence
We found that Gld2 activity is regulated by site-specific phosphorylation in its disordered N-terminal domain. We identified two phosphorylation sites (S62, S110) where phosphomimetic substitutions increased Gld2 activity and one site (S116) that markedly reduced activity. Using mass spectrometry, we confirmed that HEK 293 cells readily phosphorylate the N-terminus of Gld2. We identified protein kinase A (PKA) and protein kinase B (Akt1) as the kinases that site-specifically phosphorylate Gld2 at S116, abolishing Gld2-mediated nucleotide addition.
Publications: 1 Organism: Homo Sapiens
+ PKAdown-regulates img/direct_inhibition.png phosphorylation BAD 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-270129 Homo sapiens
pmid sentence
Ser-155 is the major phosphoacceptor site for pka on bad, but that pka also phosphorylates ser-112 and ser-136. Phosphorylated bad appears to be the inactive moiety. These results implicate pkac as the candidate kinase for s112 phosphorylation in vivo.
Publications: 1 Organism: Homo Sapiens
Pathways:FLT3-ITD signaling
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation SYN3 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264110 Homo sapiens
pmid sentence
Synapsins are exclusively localized to synaptic vesicles, which they coat as peripheral membrane proteins; they probably constitute one of the most abundant neuronal PKA substrates. Our study reveals an unexpectedly dynamic state of synapsins in nerve terminals: any changes in PKA or CaM Kinase I activity will modulate the amount of synapsin on synaptic vesicles. PKA Activation Triggers Synapsin Dissociation
Publications: 1 Organism: Homo Sapiens
+ PDE2Adown-regulates activity img/direct_inhibition.png binding PKA 0.391
Identifier Residue Sequence Organism Cell Line
SIGNOR-275731
pmid sentence
We show that caffeine, by inhibiting PDE2, enhances PKA phosphorylation leading to mitochondrial NCLX activation, thereby reducing neuronal excitotoxicity and enhancing learning in mice. 
Publications: 1
+ PKAup-regulates img/indirect-activation.png Postsynaptic density assembly 0.7
Identifier Residue Sequence Organism Cell Line
SIGNOR-264960 Homo sapiens Neuron
pmid sentence
PKA is activated by Group I mGluRs in ACC neurons. The cAMP signaling pathway contributes to the activity-dependent synaptic plasticity in the anterior cingulate cortex
Publications: 1 Organism: Homo Sapiens
Tissue: Anterior Cingulate Cortex
Pathways:Glutamatergic synapse, Oxytocin signaling
+ AKAP11up-regulates quantity img/direct-activation.png binding PKA 0.432
Identifier Residue Sequence Organism Cell Line
SIGNOR-273741 Homo sapiens
pmid sentence
We show that IQGAP2 is regulated by an interaction with the A-kinase anchoring protein AKAP220. Phosphorylation of IQGAP2 via AKAP220-anchored PKA leads to enhanced Rac binding. Since AKAPs function to direct PKA toward specific substrates, we proposed that the formation of an IQGAP2/AKAP220/PKA ternary complex sharpens the response to cAMP.
Publications: 1 Organism: Homo Sapiens
+ PKAup-regulates activity img/direct-activation.png phosphorylation VASP 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-268286 Homo sapiens
pmid sentence
 Vertebrate Ena/VASP proteins are phosphorylated by PKA, as well as PKG, and the phosphorylation is required for full function in a number of cellular contexts
Publications: 1 Organism: Homo Sapiens
Pathways:Axon guidance
+ PKAup-regulates quantity by stabilization img/direct-activation.png phosphorylation SMN complex 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-253122 Homo sapiens HEK-293 Cell
pmid sentence
PKA increases SMN complex formation and SMN stability.
Publications: 1 Organism: Homo Sapiens
+ AKAP11down-regulates activity img/direct_inhibition.png binding PKA 0.432
Identifier Residue Sequence Organism Cell Line
SIGNOR-264818
pmid sentence
A-kinase anchoring protein 220 (AKAP220) is a multivalent anchoring protein that can sequester a variety of signal transduction enzymes. These include protein kinase A (PKA) and glycogen synthase kinase 3beta (GSK3beta).
Publications: 1
+ PKAup-regulates quantity img/direct-activation.png phosphorylation GABA-A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-264991 Homo sapiens Neuron
pmid sentence
The endocytosis of GABAARs is regulated by the interaction of the AP2 complex with β and γ2 subunits. Phosphorylation of β3 (S408/S409) and γ2 (Y365/Y367) by PKA/PKC and Src/Fyn, respectively, prevents binding to AP2 and thus stabilizes these receptors at the cell surface.
Publications: 1 Organism: Homo Sapiens
Pathways:GABAergic synapse , Oxytocin signaling
+ PKAdown-regulates activity img/direct_inhibition.png phosphorylation SCN2A 0.2
Identifier Residue Sequence Organism Cell Line
SIGNOR-275749 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
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