Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-263151	Ser10	DSVYRTRsLGVAAEG	in vitro
pmid	sentence
12697024	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

Identifier	Residue	Sequence	Organism
SIGNOR-198146	Ser100	HLSGRKLsLQERSQG	Homo sapiens
pmid	sentence
22778263	Pka phosphorylates ser-100, ser-495, and ser-511the camp/pka pathway can inhibit camkk2 activity

Identifier	Residue	Sequence	Organism
SIGNOR-198150	Ser495	KTMIRKRsFGNPFEG	Homo sapiens
pmid	sentence
22778263	Pka phosphorylates ser-100, ser-495, and ser-511the camp/pka pathway can inhibit camkk2 activity

Identifier	Residue	Sequence	Organism
SIGNOR-198154	Ser511	RREERSLsAPGNLLT	Homo sapiens
pmid	sentence
22778263	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

Identifier	Residue	Sequence	Organism
SIGNOR-263158	Ser1026	KKKKKKGsLDSDNDD	Mus musculus
pmid	sentence
11744745	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264513	Ser1056	FLTQRRPsASSPNNN	Homo sapiens	HEK-293 Cell
pmid	sentence
21532585	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
21532585	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
21532585	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
21532585	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

Identifier	Residue	Sequence	Organism
SIGNOR-276153	Ser117	GNLQRRAsQKELRKS	in vitro
pmid	sentence
18312413	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
SIGNOR-276179	Ser162	RALLRKAsSLPPTTA	in vitro
pmid	sentence
18312413	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

Identifier	Residue	Sequence	Organism
SIGNOR-263653	Ser119	EILSRRPsYRKILND	Homo sapiens
pmid	sentence
8386317	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

Identifier	Residue	Sequence	Organism
SIGNOR-273939	Ser125	CRAMDRTsYAVETGH	Chlorocebus aethiops
pmid	sentence
12023945	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
SIGNOR-275988	Ser125	CRAMDRTsYAVETGH	Chlorocebus aethiops
pmid	sentence
12023945	Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273940	Ser133	GHSQRREsFLYRSDS	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
12023945	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
12023945	Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence
SIGNOR-264559	Ser14	KNFKRRFsLSVPRTE
pmid	sentence
28361970	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

Identifier	Residue	Sequence	Organism
SIGNOR-275987	Ser14	GEGAEACsRLSRSRG	Chlorocebus aethiops
pmid	sentence
12023945	Phosphorylation of long PDE4 isoforms by PKA. COS1 cells were transfected to express various long PDE4 isoforms.

Identifier	Residue	Sequence	Organism
SIGNOR-273938	Ser14	GEGAEACsRLSRSRG	Chlorocebus aethiops
pmid	sentence
12023945	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

Identifier	Residue	Sequence	Organism
SIGNOR-267442	Ser1406	GAGGRRLsSFVTKGY	in vitro
pmid	sentence
17485345	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275985	Ser145	ATSQRREsFLYRSDS	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
12023945	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
12023945	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272087	Ser156	STDSRRTsPVGSPAL	Homo sapiens	HEK-293 Cell
pmid	sentence
26569106	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

Identifier	Residue	Sequence	Organism
SIGNOR-276232	Ser162	FDIVSRGsTADLDGL	in vitro
pmid	sentence
19661060	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
SIGNOR-260885	Ser162	FDIVSRGsTADLDGL	Homo sapiens
pmid	sentence
19661060	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
SIGNOR-260883	Ser189	DEEFREPsTGKTCLP	Homo sapiens
pmid	sentence
19661060	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
SIGNOR-276233	Ser189	DEEFREPsTGKTCLP	in vitro
pmid	sentence
19661060	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
SIGNOR-276231	Thr175	GLLPFLLtHKKRLTD	in vitro
pmid	sentence
19661060	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
SIGNOR-260881	Thr175	GLLPFLLtHKKRLTD	Homo sapiens
pmid	sentence
19661060	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264712	Ser172	DQVQRRGsLPPRQVP	Homo sapiens	Colonic Epithelium Cell Line
pmid	sentence
20943948	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
20943948	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276058	Ser188	RLQQRRGsQPETRTG	Homo sapiens	HEK-293T Cell
pmid	sentence
16982607	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

Identifier	Residue	Sequence	Organism
SIGNOR-264796	Ser189	QEYTVKLsNIPTIKR	Chlorocebus aethiops
pmid	sentence
12646569	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

Identifier	Residue	Sequence	Organism
SIGNOR-276034	Ser21	AFIAARGsFDGSSSQ	in vitro
pmid	sentence
15946941	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
SIGNOR-260841	Ser21	AFIAARGsFDGSSSQ	Homo sapiens
pmid	sentence
15946941	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
SIGNOR-274079	Ser21	AFIAARGsFDGSSSQ	in vitro
pmid	sentence
15946941	PKA Phosphorylates GRK1 on Ser21. Phosphorylation by PKA inhibits GRK1 activity.

Publications:

3

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273782	Ser223	SAHVRRPsTDPQPCS	Homo sapiens	HEK-293 Cell
pmid	sentence
30941853	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

Identifier	Residue	Sequence	Organism
SIGNOR-260839	Ser23	YLQARKPsDCDSKEL	Homo sapiens
pmid	sentence
15946941	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
SIGNOR-274081	Ser23	YLQARKPsDCDSKEL	in vitro
pmid	sentence
15946941	PKA Phosphorylates GRK7 on Ser23 and Ser36. Phosphorylation by PKA inhibits GRK7 activity

Identifier	Residue	Sequence	Organism
SIGNOR-276036	Ser23	YLQARKPsDCDSKEL	in vitro
pmid	sentence
15946941	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
SIGNOR-276035	Ser36	ELQRRRRsLALPGLQ	in vitro
pmid	sentence
15946941	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
SIGNOR-260840	Ser36	ELQRRRRsLALPGLQ	Homo sapiens
pmid	sentence
15946941	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
SIGNOR-274080	Ser36	ELQRRRRsLALPGLQ	in vitro
pmid	sentence
15946941	PKA Phosphorylates GRK7 on Ser23 and Ser36. Phosphorylation by PKA inhibits GRK7 activity

Publications:

6

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276152	Ser24	RRDPFRDsPLSSRLL	in vitro
pmid	sentence
18298377	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
SIGNOR-276151	Ser57	DWALPRLsSAWPGTL	in vitro
pmid	sentence
18298377	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

Identifier	Residue	Sequence	Organism
SIGNOR-263154	Ser252	QAMERSNsCPELVLG	in vitro
pmid	sentence
18397886	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264563	Ser256	REVRRRQsVELHSPQ	Canis lupus familiaris	MDCK Cell
pmid	sentence
12194985	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

Identifier	Residue	Sequence
SIGNOR-275728	Ser258	YQRQRRGsLFCPMPV
pmid	sentence
36476859	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276043	Ser262	IKPQRRLsASRRVGL	Homo sapiens	MCF-7 Cell
pmid	sentence
16109788	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

Identifier	Residue	Sequence	Organism
SIGNOR-273788	Ser289	VQISRGSsHQVEYEI	in vitro
pmid	sentence
15680919	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
SIGNOR-276028	Ser289	VQISRGSsHQVEYEI	in vitro
pmid	sentence
15680919	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276042	Ser308	IKPKRRLsAARRAGT	Homo sapiens	MCF-7 Cell
pmid	sentence
16109788	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273783	Ser359	HKDRRKGsLDVKAVA	Homo sapiens	HeLa Cell
pmid	sentence
22673573	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:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275765	Ser36	AEKQARGsTTLQESR	Homo sapiens	Neuron
pmid	sentence
33410863	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-275766	Ser525	TSMKPRSsRGSIFTF	Homo sapiens	Neuron
pmid	sentence
33410863	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
SIGNOR-275991	Ser525	TSMKPRSsRGSIFTF	in vitro
pmid	sentence
12242273	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-275764	Ser528	KPRSSRGsIFTFRRR	Homo sapiens	Neuron
pmid	sentence
33410863	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
SIGNOR-275992	Ser528	KPRSSRGsIFTFRRR	in vitro
pmid	sentence
12242273	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

Identifier	Residue	Sequence	Organism
SIGNOR-263152	Ser36	ELQRRRRsLALPGLQ	Xenopus laevis
pmid	sentence
18803695	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

Identifier	Residue	Sequence	Organism
SIGNOR-273898	Ser361	ENNRFGGsGSQVDSA	in vitro
pmid	sentence
31843888	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

Identifier	Residue	Sequence
SIGNOR-275632	Ser39	TPKRRRAsSLSRDAE
pmid	sentence
27149373	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
SIGNOR-275631	Ser40	PKRRRASsLSRDAER
pmid	sentence
27149373	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

Identifier	Residue	Sequence	Organism
SIGNOR-273779	Ser425	PRPLRREsEI	in vitro
pmid	sentence
19843922	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

Identifier	Residue	Sequence	Organism
SIGNOR-273824	Ser433	PMNTRRSsVGVGVVE	in vitro
pmid	sentence
26435498	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-274137	Ser442	AEEIRRLSVLVDDYQ	Mus musculus	Vascular Smooth Muscle Cell
pmid	sentence
20303493	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263153	Ser443	NISYRREsAI	Homo sapiens	HEK-293 Cell
pmid	sentence
19635485	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273777	Ser446	SDLSRRSsSTMSKSE	Homo sapiens	HMEpC Cell
pmid	sentence
23774215	Phosphorylation of KCNA1 at Ser446 by PKA is involved on its cytoplasmic retention

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273784	Ser505	MAKERAHsTASHSSS	Cricetulus griseus	CHO-K1 Cell
pmid	sentence
16174736	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276041	Ser510	LPEIRAIsMQAEEYL	Homo sapiens	MCF-7 Cell
pmid	sentence
16109788	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

Identifier	Residue	Sequence	Organism
SIGNOR-263156	Ser618	ARLKSRPsAPWTGQI	in vitro
pmid	sentence
9029142	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

Identifier	Residue	Sequence	Organism
SIGNOR-262551	Ser637	VPVARKLsAREQRDC	in vitro
pmid	sentence
31063459	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272163	Ser640	RKTERKPsEEEYVIR	Homo sapiens	Blood Platelet
pmid	sentence
26507661	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
26507661	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272508	Ser667	SSLIRKRsTRRSVRG	Homo sapiens	HEK-293 Cell
pmid	sentence
24333728	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
24333728	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
24333728	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

Identifier	Residue	Sequence	Organism
SIGNOR-273634	Ser695	DCGSHSLsD	in vitro
pmid	sentence
19640509	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

Identifier	Residue	Sequence	Organism
SIGNOR-263157	Ser7	sGLEISLI	in vitro
pmid	sentence
8521865	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272156	Ser702	LSAPRRYsSSLSPIQ	Homo sapiens	Blood Platelet
pmid	sentence
26507661	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

Identifier	Residue	Sequence
SIGNOR-275952	Ser706	ARIIGEKsFRRSVVG
pmid	sentence
12058027	Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.\|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead.

Identifier	Residue	Sequence
SIGNOR-275951	Ser710	GEKSFRRsVVGTPAY
pmid	sentence
12058027	Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.\|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead.

Identifier	Residue	Sequence
SIGNOR-275950	Ser876	QGLAERIsVL
pmid	sentence
12058027	Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.\|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead.

Publications:

3

Identifier	Residue	Sequence	Organism
SIGNOR-260819	Ser73	LGAGGFGsVYKATYR	Homo sapiens
pmid	sentence
8622681	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

Identifier	Residue	Sequence
SIGNOR-275924	Ser731	ARIIGEKsFRRSVVG
pmid	sentence
18692497	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

Identifier	Residue	Sequence
SIGNOR-275925	Ser742	GEKSFRRsVVGTPAY
pmid	sentence
18692497	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273790	Ser794	SGGARAKsKSVSFNL	Homo sapiens	HEK-293 Cell
pmid	sentence
21734191	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-273789	Ser796	GARAKSKsVSFNLGC	Homo sapiens	HEK-293 Cell
pmid	sentence
21734191	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:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-264819	Ser9	SGRPRTTsFAESCKP
pmid	sentence
26088133	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

Identifier	Residue	Sequence
SIGNOR-276174	Ser950	EGFHPRRsSQGATQM
pmid	sentence
19018281	Our results demonstrate that PKA activates human HSL against lipid substrates in vitro primarily through phosphorylation of Ser649 and Ser650.

Identifier	Residue	Sequence
SIGNOR-276175	Ser951	GFHPRRSsQGATQMP
pmid	sentence
19018281	Our results demonstrate that PKA activates human HSL against lipid substrates in vitro primarily through phosphorylation of Ser649 and Ser650.

Publications:

2

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276321	Thr1024	YLALRHHtNLLIILF	Homo sapiens	HEK-293T Cell
pmid	sentence
21474070	Anchored PKA activates PDE3B to enhance cAMP degradation and phosphorylates p110γ to inhibit PIP(3) production.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275416	Thr1548	YAPSRRMtSVATAKG	in vitro
pmid	sentence
21406690	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

Identifier	Residue	Sequence	Organism
SIGNOR-276056	Thr260	VDAARRLtLEHIQKH	in vitro
pmid	sentence
16870137	BRSK2 is activated by cyclic AMP-dependent protein kinase A through phosphorylation at Thr260

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264956	Thr34	MIRRRRPtPAMLFRL	Homo sapiens	Neuron
pmid	sentence
10604473	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.â€šÂ

Publications:

1

Organism:

Homo Sapiens

Pathways:

Dopaminergic Synapse

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276044	Thr374	PGCTKRYtDPSSLRK	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
16293631	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276037	Thr601	LKKFRSStSSSLGDK	Homo sapiens	HEK-293 Cell
pmid	sentence
15955806	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273778	Thr601	LKKFRSStSSSLGDK	Homo sapiens	HEK-293 Cell
pmid	sentence
15955806	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

Identifier	Residue	Sequence	Organism
SIGNOR-273742	Thr716	EYMHRRQtFIDNTDS	Homo sapiens
pmid	sentence
21776420	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276009	Thr91	RDARFRRtETDFSNL	Homo sapiens	Brain
pmid	sentence
15147202	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

Identifier	Residue	Organism	Cell Line
SIGNOR-264108		Homo sapiens	Neuron
pmid	sentence
10571231	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

Identifier	Residue	Organism	Cell Line
SIGNOR-264961		Homo sapiens	Neuron
pmid	sentence
23125836	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

Identifier	Residue	Organism
SIGNOR-270129		Homo sapiens
pmid	sentence
10230396	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

Identifier	Residue	Organism	Cell Line
SIGNOR-275749		Homo sapiens	Neuron
pmid	sentence
32599005	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

Identifier	Residue	Organism
SIGNOR-267409		Homo sapiens
pmid	sentence
10487978	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

Identifier	Residue	Organism
SIGNOR-268287		Homo sapiens
pmid	sentence
15066263	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

Identifier	Residue	Organism	Cell Line
SIGNOR-264960		Homo sapiens	Neuron
pmid	sentence
23125836	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

Identifier	Residue	Organism	Cell Line
SIGNOR-265087		Homo sapiens	Neuron
pmid	sentence
10604473	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

Identifier	Residue	Organism	Cell Line
SIGNOR-270130		Homo sapiens	HEK-293 Cell
pmid	sentence
31057087	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

Identifier	Residue	Organism	Cell Line
SIGNOR-253114		Homo sapiens	HEK-293 Cell
pmid	sentence
19103745	PKA increases SMN complex formation and SMN stability.\|As expected, SMN was phosphorylated by PKA (Fig. (Fig.6D).6D).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270128		Homo sapiens
pmid	sentence
20151718	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

Identifier	Residue	Organism
SIGNOR-264110		Homo sapiens
pmid	sentence
10571231	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

Identifier	Residue	Organism	Cell Line
SIGNOR-264991		Homo sapiens	Neuron
pmid	sentence
25600368	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

Identifier	Residue	Organism	Cell Line
SIGNOR-264109		Homo sapiens	Neuron
pmid	sentence
10571231	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

Identifier	Residue	Organism
SIGNOR-268285		Homo sapiens
pmid	sentence
15066263	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

Identifier	Residue	Organism
SIGNOR-268286		Homo sapiens
pmid	sentence
15066263	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

Identifier	Residue	Organism
SIGNOR-267408		Homo sapiens
pmid	sentence
10487978	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

Identifier	Residue	Organism
SIGNOR-258763		Homo sapiens
pmid	sentence
26687711	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275731
pmid	sentence
36476859	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

Identifier	Residue	Organism
SIGNOR-273741		Homo sapiens
pmid	sentence
21776420	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271837
pmid	sentence
14657015	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

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264818
pmid	sentence
26088133	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

Identifier	Residue	Organism	Cell Line
SIGNOR-253122		Homo sapiens	HEK-293 Cell
pmid	sentence
19103745	PKA increases SMN complex formation and SMN stability.

Publications:

1

Organism:

Homo Sapiens

Name	PKA View Modifications
Primary ID	SIGNOR-PF17
Type	protein family
Formed by	PRKACA, PRKACB, PRKACG
Relations	122
Pathways	Axon guidance, Dopaminergic Synapse, FLT3-ITD signaling, Glycogenolysis, Glutamatergic synapse, GABAergic synapse , Mitochondrial dynamics in T cell exhaustion, Nucleotide Biosynthesis, Neurotransmitters release, Oxytocin signaling, Thyroid Hormone Metabolism

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