Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-159840	Ser10	GAIASRMsFSSLKRK	Homo sapiens
pmid	sentence
18071304	Merlin contains a c-terminal serine 518, which is phosphorylated both by p21-activated kinase (pak) and protein kinase a (pka) (shaw et al., 2001;kissil et al., 2002;xiao et al., 2002;alfthan et al., 2004). Phosphorylation at this site is predicted to result in a more open conformation incapable of inhibiting cell growth,

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276391	Ser10	MTGSTPCsSMSNHTK	in vitro
pmid	sentence
22142472	GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress.

Identifier	Residue	Sequence	Organism
SIGNOR-276390	Ser11	TGSTPCSsMSNHTKE	in vitro
pmid	sentence
22142472	GSK-3β phosphorylated STK38 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of STK38 on residues S10 and S11, respectively. Our results indicate that that GSK-3β inhibits STK38's full activation, and suggest that STK38 activation is required to prevent cell death in response to oxidative stress.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-181788	Ser10	DQRQRSLsTSGESLY	Homo sapiens	Neuron
pmid	sentence
18951872	Csp is phosphorylated in vivo on a single residue, ser10, and this phosphorylation regulates its cellular functions,[...]PKA Phosphorylation of full-length csp protein stimulated 14-3-3 binding, and this was abolished in a ser10-ala mutant csp, confirming the binding site as phospho-ser10

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250059	Ser10	NFLRRRLsDSSFIAN	in vitro
pmid	sentence
10571231	Synapsin phosphorylation in the A domain, at the only phosphorylation site shared by all synapsins, dissociates synapsins from synaptic vesicles.This site is located in the N-terminal A domain and is a substrate for both PKA and CaM Kinase I

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-75339	Ser1006	GHGVRRAsDPVRTGS	Homo sapiens
pmid	sentence
10693759	Ci/gli zinc finger proteins mediate the transcriptional effects of hedgehog protein signals. In drosophila, ci action as transcriptional repressor or activator is contingent upon hedgehog-regulated, pka-dependent proteolytic processingall six pka phosphorylation sites are required for processing of gli3.

Identifier	Residue	Sequence	Organism
SIGNOR-75343	Ser849	NMLNRRDsSASTISS	Homo sapiens
pmid	sentence
10693759	Ci/gli zinc finger proteins mediate the transcriptional effects of hedgehog protein signals. In drosophila, ci action as transcriptional repressor or activator is contingent upon hedgehog-regulated, pka-dependent proteolytic processingall six pka phosphorylation sites are required for processing of gli3.

Identifier	Residue	Sequence	Organism
SIGNOR-75347	Ser865	YLSSRRSsGISPCFS	Homo sapiens
pmid	sentence
10693759	Ci/gli zinc finger proteins mediate the transcriptional effects of hedgehog protein signals. In drosophila, ci action as transcriptional repressor or activator is contingent upon hedgehog-regulated, pka-dependent proteolytic processingall six pka phosphorylation sites are required for processing of gli3.

Identifier	Residue	Sequence	Organism
SIGNOR-75351	Ser877	CFSSRRSsEASQAEG	Homo sapiens
pmid	sentence
10693759	Ci/gli zinc finger proteins mediate the transcriptional effects of hedgehog protein signals. In drosophila, ci action as transcriptional repressor or activator is contingent upon hedgehog-regulated, pka-dependent proteolytic processingall six pka phosphorylation sites are required for processing of gli3.

Identifier	Residue	Sequence	Organism
SIGNOR-75355	Ser907	TDASRRSsEASQSDG	Homo sapiens
pmid	sentence
10693759	Ci/gli zinc finger proteins mediate the transcriptional effects of hedgehog protein signals. In drosophila, ci action as transcriptional repressor or activator is contingent upon hedgehog-regulated, pka-dependent proteolytic processingall six pka phosphorylation sites are required for processing of gli3.

Identifier	Residue	Sequence	Organism
SIGNOR-75359	Ser980	VHAPRRCsDGGAHGY	Homo sapiens
pmid	sentence
10693759	Ci/gli zinc finger proteins mediate the transcriptional effects of hedgehog protein signals. In drosophila, ci action as transcriptional repressor or activator is contingent upon hedgehog-regulated, pka-dependent proteolytic processingall six pka phosphorylation sites are required for processing of gli3.

Publications:

6

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Sequence
SIGNOR-250026	Ser1018	QVEFRRLsISAESQS
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. Ser1018 within this multiphosphorylation domain is phosphorylated by PKA and is a major site of regulatory phosphorylation in vivo

Identifier	Residue	Organism
SIGNOR-267411		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:

2

Organism:

, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-110119	Ser1021	QEENRRDsWSYINSK	Homo sapiens	T-lymphocyte
pmid	sentence
11533025	PKA phosphorylationin vitro blocks the binding of the alpha4 tail to paxillin. A mutation that mimics alpha4 phosphorylation disrupts paxillin binding and promotes cell spreading

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250326	Ser1042	GGMQRKLsVALAFVG	Mus musculus	Macrophage
pmid	sentence
12196520	Ser-1042 and Ser-2054, located in the nucleotide binding domains of ABCA1, are major phosphorylation sites for PKA. ABCA1 phosphorylation may affect ApoA-I-dependent phospholipid efflux by either altering the conformation of the protein to a more active state or by affecting the interaction between ABCA1 and its partner proteins.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250327	Ser2054	GGNKRKLsTAMALIG	Mus musculus	Macrophage
pmid	sentence
12196520	Ser-1042 and Ser-2054, located in the nucleotide binding domains of ABCA1, are major phosphorylation sites for PKA. ABCA1 phosphorylation may affect ApoA-I-dependent phospholipid efflux by either altering the conformation of the protein to a more active state or by affecting the interaction between ABCA1 and its partner proteins.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-108569	Ser1050	AASLLRLsLYNNCIC	Homo sapiens	P-388D1 Cell
pmid	sentence
11416140	Downregulation of ciita function by protein kinase a (pka)-mediated phosphorylation phosphorylation at ciita serines 834 and 1050 accounts for the inhibitory effects of pka on ciita-driven class ii mhc transcription.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-108573	Ser834	QELPGRLsFLGTRLT	Homo sapiens	P-388D1 Cell
pmid	sentence
11416140	Downregulation of ciita function by protein kinase a (pka)-mediated phosphorylationphosphorylation at ciita serines 834 and 1050 accounts for the inhibitory effects of pka on ciita-driven class ii mhc transcription.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249989	Ser109	KERRRTEsINSAFAE	Rattus norvegicus	Rcho-1 Cell
pmid	sentence
14636580	In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. We determined that modification of HAND1 at residues 107 and 109 affects dimerization affinities with E-proteins, thus changing the bHLH dimer equilibrium within the cell. These modifications also affect HAND1 function.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249991	Thr107	PKKERRRtESINSAF	Rattus norvegicus	Rcho-1 Cell
pmid	sentence
14636580	In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. We determined that modification of HAND1 at residues 107 and 109 affects dimerization affinities with E-proteins, thus changing the bHLH dimer equilibrium within the cell. These modifications also affect HAND1 function.

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-70424	Ser11	TKQTARKsTGGKAPR	Homo sapiens
pmid	sentence
10464286	Identification of a novel phosphorylation site on histone h3 coupled with mitotic chromosome condensation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-235675	Ser1100	QGCRRRHsSETFSST	Homo sapiens
pmid	sentence
17360977	Tyrosine phosphorylation of IRS-1 initiates insulin signaling, whereas serine/threonine phosphorylation alters the ability of IRS-1 to transduce the insulin signalInsulin increased the phosphorylation of Ser312, Ser616, Ser636, Ser892, Ser1101, and Ser1223

Identifier	Residue	Sequence	Organism
SIGNOR-236729	Ser1222	ESSSTRRsSEDLSAY	Homo sapiens
pmid	sentence
17360977	Tyrosine phosphorylation of IRS-1 initiates insulin signaling, whereas serine/threonine phosphorylation alters the ability of IRS-1 to transduce the insulin signalInsulin increased the phosphorylation of Ser312, Ser616, Ser636, Ser892, Ser1101, and Ser1223

Identifier	Residue	Sequence	Organism
SIGNOR-236603	Ser1223	SSSTRRSsEDLSAYA	Homo sapiens
pmid	sentence
17360977	Tyrosine phosphorylation of IRS-1 initiates insulin signaling, whereas serine/threonine phosphorylation alters the ability of IRS-1 to transduce the insulin signalInsulin increased the phosphorylation of Ser312, Ser616, Ser636, Ser892, Ser1101, and Ser1223

Publications:

3

Organism:

Homo Sapiens

Tissue:

Ovary

Identifier	Residue	Sequence	Organism
SIGNOR-79148	Ser1105	LDRKRHNsISEAKMR	Homo sapiens
pmid	sentence
10893237	These data indicate that pkc and pka act similarly in that they inhibit galpha(q)-stimulated plcbeta(3) as a result of phosphorylation of ser(1105).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263110	Ser1107	LPDSRRGsSSSGDPP	Homo sapiens
pmid	sentence
19131331	Here, we identify protein kinase A (PKA) as a molecular switch that allows Gbeta(2)gammax dimers to effect voltage-independent inhibition of Ca(v)3.2 channels. Inhibition requires phosphorylation of Ser(1107), a critical serine residue on the II-III loop of the channel pore protein. S1107A prevents inhibition of unitary currents by recombinant Gbeta(2)gamma(2) dimers but does not disrupt dimer binding nor change its specificity.

Identifier	Residue	Sequence	Organism
SIGNOR-263111	Ser1144	AWSSRRSsWSSLGRA	Homo sapiens
pmid	sentence
19131331	Here, we identify protein kinase A (PKA) as a molecular switch that allows Gbeta(2)gammax dimers to effect voltage-independent inhibition of Ca(v)3.2 channels. Inhibition requires phosphorylation of Ser(1107), a critical serine residue on the II-III loop of the channel pore protein. S1107A prevents inhibition of unitary currents by recombinant Gbeta(2)gamma(2) dimers but does not disrupt dimer binding nor change its specificity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-70718	Ser1137	EGPTRRLsLPGQLGA	Homo sapiens
pmid	sentence
10488078	Deletion of protein kinase a phosphorylation sites in the herg potassium channel inhibits activation shift by protein kinase afour consensus pka phosphorylation sites (s283a, s890a, t895a, s1137a)

Identifier	Residue	Sequence	Organism
SIGNOR-70722	Ser283	CASVRRAsSADDIEA	Homo sapiens
pmid	sentence
10488078	Deletion of protein kinase a phosphorylation sites in the herg potassium channel inhibits activation shift by protein kinase afour consensus pka phosphorylation sites (s283a, s890a, t895a, s1137a)

Identifier	Residue	Sequence	Organism
SIGNOR-70726	Ser890	RQRKRKLsFRRRTDK	Homo sapiens
pmid	sentence
10488078	Deletion of protein kinase a phosphorylation sites in the herg potassium channel inhibits activation shift by protein kinase afour consensus pka phosphorylation sites (s283a, s890a, t895a, s1137a)

Identifier	Residue	Sequence	Organism
SIGNOR-70730	Thr895	KLSFRRRtDKDTEQP	Homo sapiens
pmid	sentence
10488078	Deletion of protein kinase a phosphorylation sites in the herg potassium channel inhibits activation shift by protein kinase afour consensus pka phosphorylation sites (s283a, s890a, t895a, s1137a)

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-125545	Ser114	NRFTRRAsVCAEAYN	Homo sapiens
pmid	sentence
15187164	Serine 114 phosphorylation is required for both nuclear localization and down-regulation of il-2 production by riibeta.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-259402	Ser116	LSGERRYsMPPLFHT	Homo sapiens
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	Sequence	Organism	Cell Line
SIGNOR-276616	Ser1166	SDDFKRDsVSGGGPC	Homo sapiens	HEK-293 Cell
pmid	sentence
24431445	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

Identifier	Residue	Sequence	Organism
SIGNOR-112371	Ser1177	TSRIRTQsFSLQERQ	Homo sapiens
pmid	sentence
11729179	Recently many investigators have shown that protein phosphorylation of enos by several serine/threonine kinases is a critical control step for no production by endothelial cells. Phosphorylation by amp kinase, akt (or protein kinase b), or protein kinase aon serine 1179 (bovine) or serine 1177 (human) of enos leads to enhanced activity of the enzyme and, thus, augmented production of no.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262694	Ser1178	APTKRNSsPPPSPNK	in vitro
pmid	sentence
2548572	The ATPase is phosphorylated only at this site by the cAMP-dependent protein kinase, and the phosphorylation is inhibited by calmodulin. The effect of the phosphorylation is to decrease the Km for Ca2+ of the purified ATPase from about 10 microM to about 1.4 microM and to increase the Vmax of ATP hydrolysis about 2-fold.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-180902	Ser118	GRELRRMsDEFVDSF	Homo sapiens
pmid	sentence
18794113	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.

Identifier	Residue	Sequence	Organism
SIGNOR-67379	Ser118	GRELRRMsDEFVDSF	Homo sapiens
pmid	sentence
10230394	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.

Identifier	Residue	Sequence	Organism
SIGNOR-81129	Ser118	GRELRRMsDEFVDSF	Homo sapiens
pmid	sentence
10949026	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.

Identifier	Residue	Sequence	Organism
SIGNOR-180906	Ser75	EIRSRHSsYPAGTED	Homo sapiens
pmid	sentence
18794113	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.

Identifier	Residue	Sequence	Organism
SIGNOR-67387	Ser99	PFRGRSRsAPPNLWA	Homo sapiens
pmid	sentence
10230394	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.

Identifier	Residue	Sequence	Organism
SIGNOR-81137	Ser99	PFRGRSRsAPPNLWA	Homo sapiens
pmid	sentence
10949026	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:

6

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250338	Ser118	GRELRRMsDEFVDSF	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10880354	Ser(155) is phosphorylated preferentially by PKA in vitro and is the only residue in BAD that becomes phosphorylated when cells are exposed to cAMP-elevating agents. The phosphorylation of BAD at Ser(155) prevents it from binding to Bcl-X(L) and promotes its interaction with 14-3-3 proteins.

Identifier	Residue	Sequence	Organism
SIGNOR-67383	Ser75	EIRSRHSsYPAGTED	Homo sapiens
pmid	sentence
10230394	Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase A\|Collectively, these results implicate PKA as the principal mitochondria-based S112 kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-180780	Ser99	PFRGRSRsAPPNLWA	in vitro
pmid	sentence
10949026	Survival factors, acting through kinases such as Akt and PKA, induce endogenous BAD phosphorylation at two evolutionarily conserved sites, Ser-112 and Ser-136, which leads to the translocation of BAD from the mitochondria to the cytoplasm and the inhibition of BAD-dependent death

Publications:

3

Organism:

Chlorocebus Aethiops, Homo Sapiens, In Vitro

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-166342	Ser119	EILSRRPsYRKILND	Rattus norvegicus	PC-12 Cell
pmid	sentence
8336722	The degree of CREB phosphorylation, assessed with antiserum specific for CREB phosphorylated at Ser-133, correlated with the amount of PKA liberated. The time course of phosphorylation closely paralleled the nuclear entry of the catalytic subun

Identifier	Residue	Organism
SIGNOR-255799		Mus musculus
pmid	sentence
15568017	We demonstrate that adenylyl cyclase signalling via PKA and its target transcription factor CREB are required for Wnt-directed myogenic gene expression.

Identifier	Residue	Organism	Cell Line
SIGNOR-131307		Mus musculus	Embryonic Cell Line
pmid	sentence
15568017	Using a combination of in vitro explant assays, mutant analysis and gene delivery into mouse embryos cultured ex vivo, we demonstrate that adenylyl cyclase signalling via PKA and its target transcription factor CREB are required for WNT-directed myogenic gene expression.

Identifier	Residue	Organism
SIGNOR-176560		Homo sapiens
pmid	sentence
21902831	Phosphorylation of CREB by PKA allows it to initiate the transcription of genes that contain a CRE element, two of which are PAX3 and MYF5.

Publications:

4

Organism:

Rattus Norvegicus, Mus Musculus, Homo Sapiens

Tissue:

Myotome, Skeletal Muscle

Pathways:

COVID-19 Causal Network, WNT Signaling, WNT Signaling and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-196397	Ser119	YGPPSRRsENRVVVS	Homo sapiens
pmid	sentence
22393468	Here, we show that pka phosphorylates srsf1 on serine 119 in vitro. Phosphorylation of srsf1 on this site enhanced the rna binding capacity of srsf1 in vivo

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250357	Ser120	RAKEVRGsGSYEYPV	Homo sapiens	SK-HEP-1 Cell
pmid	sentence
10728420	Gap junction channels formed of Cx40 are modulated by protein-kinase-A-mediated phosphorylation. Macroscopic conductance and permeability of Cx40 gap junctions is strongly increased by cAMP. two serine residues that can be phosphorylated by PKA, S120 and S345

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249982	Ser345	HSDKRRLsKASSKAR	Homo sapiens	SK-HEP-1 Cell
pmid	sentence
10728420	Gap junction channels formed of Cx40 are modulated by protein-kinase-A-mediated phosphorylation. Macroscopic conductance and permeability of Cx40 gap junctions is strongly increased by cAMP. two serine residues that can be phosphorylated by PKA, S120 and S345

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-267714	Ser1201	IPTLNRMsFSSNLNH	in vitro
pmid	sentence
2900138	TC1 = Ser-2Ser(P)-Met-3Ser(P)-Gly-Leu; TC2 = Arg-Met-1Ser(P)-Phe- Cyclic-AMP-dependent protein kinase phosphorylates sites 1 and 2 exclusively, whereas the AMP-activated protein kinase phosphorylates sites 1 and 3, plus at least one other minor site.[…]The results suggest that phosphorylation of site 3 is primarily responsible for the large decrease in Vmax produced by the AMP-activated protein kinase, while phosphorylation of site 1 may be primarily responsible for the increase in A0.5 for citrate and more modest depression of Vmax produced by cyclic-AMP-dependent protein kinase and ACK2

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249994	Ser121	LQQPRRLsTSSVSST	in vitro
pmid	sentence
9374536	Two isoforms of the inositol 1,4,5-trisphosphate 3-kinase have been identified, the A form and the B form. phosphorylation of isoform A by the cyclic AMP-dependent protein kinase increased activity 1.5-fold, whereas phosphorylation of isoform B decreased activity by 45%. major phosphorylation sites in the protein are Ser119 for PKA. Ser119 in the A isoform is conserved in the B isoform as Ser328

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-183445	Ser1217	SHHFRRRsFRGFWLT	Homo sapiens
pmid	sentence
19144650	We analyzed the duox1 phosphorylation state with an anti-rxx(ps/pt) antibody that could potentially recognize phosphorylation on ser955 and ser1217 but not on thr1007. duox1 but not duox2 activity is stimulated by forskolin (ec50 = 0.1 _m) via protein kinase a-mediated duox1 phosphorylation on serine 955. duox1 is positively regulated by the camp-dependent protein kinase a (pka)6 cascade

Identifier	Residue	Sequence	Organism
SIGNOR-183449	Ser955	KDLCRRAsYISQDMI	Homo sapiens
pmid	sentence
19144650	We analyzed the duox1 phosphorylation state with an anti-rxx(ps/pt) antibody that could potentially recognize phosphorylation on ser955 and ser1217 but not on thr1007. duox1 but not duox2 activity is stimulated by forskolin (ec50 = 0.1 _m) via protein kinase a-mediated duox1 phosphorylation on serine 955. duox1 is positively regulated by the camp-dependent protein kinase a (pka)6 cascade

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-195987	Ser122	DGRMVQLsPPALAAP	Homo sapiens
pmid	sentence
22310283	Thus, our data revealed a novel interplay between pka phosphorylation and tal1-mediated epigenetic regulation that regulates hematopoietic transcription and differentiation programs during hematopoiesis and leukemogenesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-17901	Ser1248	HGRAREGsFESRYQQ	Homo sapiens	T-lymphocyte, JURKAT Cell
pmid	sentence
1370476	The observation that pka also phosphorylates plc-yl on serine 1248 suggests that phosphorylation of this residue may be a common mechanism by which pkc and pka inhibit plc-yl.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249711	Ser13	ITSAARRsYVSSGEM	in vitro
pmid	sentence
2155236	GFAP can serve as a substrate for phosphorylation by CAMP-dependent protein kinase. CAMP-dependent protein kinase or protein kinase C phosphorylated Ser-8, Ser-13, and Ser-34.each phosphorylation was shown to induce disassembly of the glial filaments.

Identifier	Residue	Sequence	Organism
SIGNOR-249713	Ser38	LGPGTRLsLARMPPP	in vitro
pmid	sentence
2155236	GFAP can serve as a substrate for phosphorylation by CAMP-dependent protein kinase. CAMP-dependent protein kinase or protein kinase C phosphorylated Ser-8, Ser-13, and Ser-34.each phosphorylation was shown to induce disassembly of the glial filaments.

Identifier	Residue	Sequence	Organism
SIGNOR-249712	Thr7	tSAARRSY	in vitro
pmid	sentence
2155236	GFAP can serve as a substrate for phosphorylation by CAMP-dependent protein kinase. CAMP-dependent protein kinase or protein kinase C phosphorylated Ser-8, Ser-13, and Ser-34.each phosphorylation was shown to induce disassembly of the glial filaments.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-156873	Ser1364	PSGSQRPsVSDDTGC	Homo sapiens
pmid	sentence
17615294	Additionally, we show that s1360 and s1364 of beta4 are the only residues phosphorylated by pkc and pka in cells, respectivelywe have defined three regions on beta4 that together harbor all the serine and threonine phosphorylation sites and show that three serines (s1356, s1360, and s1364), previously implicated in hd regulation, prevent the interaction of beta4 with the plectin actin-binding domain when phosphorylated

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-264560	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-151816	Ser1406	GAGGRRLsSFVTKGY	Homo sapiens
pmid	sentence
17206380	Protein kinase a phosphorylation at thr456 of the multifunctional protein cad antagonizes activation by the map kinase cascade.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-250344	Ser1406	GAGGRRLsSFVTKGY
pmid	sentence
11986331	CAD is down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. PKA phosphorylates Ser1406 and Ser1859, although only Ser1406 is involved in regulation.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-250010	Ser141	MASQKRPsQRHGSKY	in vitro
pmid	sentence
2413024	Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161

Identifier	Residue	Sequence	Organism
SIGNOR-250011	Ser146	RPSQRHGsKYLATAS	in vitro
pmid	sentence
2413024	Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-161

Identifier	Residue	Sequence	Organism
SIGNOR-250012	Ser190	RGAPKRGsGKDSHHP	in vitro
pmid	sentence
2413024	Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-162

Identifier	Residue	Sequence	Organism
SIGNOR-250013	Ser266	FGYGGRAsDYKSAHK	in vitro
pmid	sentence
2413024	Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-163

Identifier	Residue	Sequence	Organism
SIGNOR-250014	Ser295	FKLGGRDsRSGSPMA	in vitro
pmid	sentence
2413024	Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-164

Identifier	Residue	Sequence	Organism
SIGNOR-250015	Thr169	FLPRHRDtGILDSIG	in vitro
pmid	sentence
2413024	Ser-46 and Ser-151 were specifically phosphorylated by protein kinase C, whereas Thr-34 and Ser-115 were phosphorylated preferentially by protein kinase A. Both kinases reacted with Ser-8, Ser-11, Ser-55, Ser-110, Ser-132, and Ser-165

Publications:

6

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-237444	Ser1444	NIKARASsSPVILVG	in vitro
pmid	sentence
24351927	Furthermore, our work establishes S1444 as a PKA-regulated 14-3-3 docking site.Strikingly, 14-3-3 binding to phospho-S1444 decreased LRRK2 kinase activity in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263066	Ser1445	PSPTSRQsPASPPPL	Homo sapiens	HEK-293 Cell
pmid	sentence
20622900	HScrib is a substrate of ERK and PKA. Under normal growth conditions, hScrib is phosphorylated at S853, most likely by ERK, and at S1445 by PKA. Interestingly, stimulation of MAPK by osmotic stress results in a marked loss of phosphorylation at the PKA site S1445, but a concomitant increase in phosphorylation at S1448, presumably also by ERK. At present, we have no information as to what are the functional consequences of ERK or PKA phosphorylation of hScrib. However, we can speculate that this will most likely affect the ability of hScrib to interact with some of its cellular partners, and studies are currently in progress to investigate these aspects further.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97938	Ser146	MEPERRDsQDGSSYR	Homo sapiens
pmid	sentence
12571245	Actin binding of human lim and sh3 protein is regulated by cgmp- and camp-dependent protein kinase phosphorylation on serine 146. Phosphorylation of lasp at ser-146 leads to a redistribution of the actin-bound protein from the tips of the cell membrane to the cytosol, accompanied with a reduced cell migration

Identifier	Residue	Sequence	Organism
SIGNOR-197720	Ser146	MEPERRDsQDGSSYR	Homo sapiens
pmid	sentence
22665060	Phosphorylation of lasp-1 by pka at serine 146 induces translocation of the lasp-1/zo-2 complex from the cytoplasm to the nucleus. Interaction occurs within the carboxyterminal proline-rich motif of zo-2 and the sh3 domain in lasp-1.

Identifier	Residue	Sequence	Organism
SIGNOR-250074	Ser146	MEPERRDsQDGSSYR	in vitro
pmid	sentence
12432067	Lasp-1 binds to non-muscle filamentous (F) actin in vitro in a phosphorylation-dependent manner. Phosphorylation of recombinant lasp-1 with recombinant PKA increased the Kd and decreased the Bmax for lasp-1 binding to F-actin. PKA-dependent phosphorylation sites in rabbit lasp-1 to S99 and S146

Publications:

3

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-191623	Ser153	SRRLRRVsLSEIGFG	Homo sapiens
pmid	sentence
22184064	Here, we report that cdk16 is activated by membrane-associated cyclin y (ccny). Treatment of transfected human cells with the protein kinase a (pka) activator forskolin blocked, while kinase inhibition promoted, ccny-dependent targeting of cdk16-green fluorescent protein (gfp) to the cell membrane. Ccny binding to cdk16 required a region upstream of the kinase domain and was found to be inhibited by phosphorylation of serine 153, a potential pka phosphorylation site.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-186462	Ser153	RKQERAAsAKGAAGA	Homo sapiens
pmid	sentence
19564421	Phox2a becomes phosphorylated by protein kinase a (pka) on ser153, which prevents association of phox2a with dna and terminates p27(kip1) transcription.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272088	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-126723	Ser1565	LSPFRRHsWGPGKNA	Homo sapiens
pmid	sentence
15229649	Elevation of the cellular concentration of camp activates the pka holoenzyme anchored to akap-lbc, which phosphorylates the anchoring protein on the serine 1565. This phosphorylation event induces the recruitment of 14-3-3, which inhibits the rho-gef activity of akap-lbc.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-140841	Ser157	EHIERRVsNAGGPPA	Homo sapiens
pmid	sentence
16197368	We show that, in human platelets, vasp is phosphorylated by pkc on ser157, but not ser239, in response to phorbol ester stimulation, in a manner blocked by the pkc inhibitor bim i (bisindolylmaleimide i).

Identifier	Residue	Sequence	Organism
SIGNOR-250064	Ser157	EHIERRVsNAGGPPA	Homo sapiens
pmid	sentence
12576312	Three phosphorylation sites have been identified in VASP: Ser157, Ser239, and Thr278, all of which can be phosphorylated by either PKA or PKG in vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250063	Ser239	GAKLRKVsKQEEASG	Homo sapiens
pmid	sentence
12576312	Three phosphorylation sites have been identified in VASP: Ser157, Ser239, and Thr278, all of which can be phosphorylated by either PKA or PKG in vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250065	Thr278	LARRRKAtQVGEKTP	in vitro
pmid	sentence
8182057	The vasodilator-stimulated phosphoprotein (VASP) is a major substrate for cAMP-dependent- (cAK) and cGMP-dependent protein kinase (cGK) in human platelets and other cardiovascular cells.‚ three VASP phosphorylation sites are phosphorylated by cAK and cGK. Thr, Ser I, and Ser 2 correspond to Thr278, Ser157, Ser239 of the VASP protein, respectively

Publications:

4

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263112	Ser1575	PEICRTVsGDLAAEE	in vitro
pmid	sentence
20937870	To identify the regulatory sites of phosphorylation under physiologically relevant conditions, Ca(V)1.1 channels were purified from skeletal muscle and sites of phosphorylation on the α1 subunit were identified by mass spectrometry. Two phosphorylation sites were identified in the proximal C-terminal domain, serine 1575 (S1575) and threonine 1579 (T1579), which are conserved in cardiac Ca(V)1.2 channels (S1700 and T1704, respectively). In vitro phosphorylation revealed that Ca(V)1.1-S1575 is a substrate for both cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II, whereas Ca(V)1.1-T1579 is a substrate for casein kinase 2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249996	Ser1598	RNAARRDsVLAASRD	in vitro
pmid	sentence
12529267	IP(3)R-I was phosphorylated by PKA and PKG in vitro and exclusively by PKG in vivo. Sequential phosphorylation by PKA and by PKG-Ialpha in vitro showed that PKA phosphorylated the same site as PKG (presumably S(1755)) and an additional PKA-specific site (S(1589)). Phosphorylation of IP(3)R-I in microsomes by PKG, PKA, or a combination of PKG and PKA inhibited IP(3)-induced Ca(2+) release to the same extent, implying that inhibition was mediated by phosphorylation of the PKG-specific site.

Identifier	Residue	Sequence	Organism
SIGNOR-249997	Ser1764	RPSGRREsLTSFGNG	in vitro
pmid	sentence
12529267	IP(3)R-I was phosphorylated by PKA and PKG in vitro and exclusively by PKG in vivo. Sequential phosphorylation by PKA and by PKG-Ialpha in vitro showed that PKA phosphorylated the same site as PKG (presumably S(1755)) and an additional PKA-specific site (S(1589)). Phosphorylation of IP(3)R-I in microsomes by PKG, PKA, or a combination of PKG and PKA inhibited IP(3)-induced Ca(2+) release to the same extent, implying that inhibition was mediated by phosphorylation of the PKG-specific site.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-38318	Ser16	KELEKRAsGQAFELI	Homo sapiens
pmid	sentence
8376365	Phosphorylation at either ser(16) or ser(63) strongly reduced or abolished the ability of stathmin to bind to and sequester soluble tubulin and its ability to act as a catastrophe factor by directly binding to the microtubules. The known in vivo phosphorylation sites of stathmin are ser-16 and ser-63 for cyclic amp-dependent protein kinase (pka).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-36370	Ser16	KELEKRAsGQAFELI	Homo sapiens	T-lymphocyte, Leukemia Cell
pmid	sentence
8125092	Phosphorylation of either serine 16 or 63 is sufficient to inhibit stathmin in vitro. Phosphorylation at ser-63 reduces tubulin binding 10-fold and suppresses the mt polymerization inhibition activity.

Identifier	Residue	Sequence	Organism
SIGNOR-38322	Ser63	AAEERRKsHEAEVLK	Homo sapiens
pmid	sentence
8376365	Phosphorylation at either ser(16) or ser(63) strongly reduced or abolished the ability of stathmin to bind to and sequester soluble tubulin and its ability to act as a catastrophe factor by directly binding to the microtubules. The known in vivo phosphorylation sites of stathmin are ser-16 and ser-63 for cyclic amp-dependent protein kinase (pka).

Identifier	Residue	Sequence	Organism
SIGNOR-36374	Ser63	AAEERRKsHEAEVLK	Homo sapiens
pmid	sentence
8125092	Phosphorylation of either serine 16 or 63 is sufficient to inhibit stathmin in vitro. Phosphorylation at ser-63 reduces tubulin binding 10-fold and suppresses the mt polymerization inhibition activity.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-66493	Ser16	PSWLRRAsAPLPGLS	Homo sapiens
pmid	sentence
10196226	Hosphorylation of hsp20 at ser16 is not only associated with cyclic nucleotide-dependent vasorelaxation but also inhibits agonist-induced contractile responses.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250030	Ser16	RSAIRRAsTIEMPQQ	Mus musculus
pmid	sentence
10988285	Phospholamban (PLB) can be phosphorylated at Ser(16) by cyclic AMP-dependent protein kinase. phosphorylation of Ser(16) is sufficient for mediating the maximal cardiac responses to beta-adrenergic stimulation.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-112164	Ser16	PGWEKRMsRSSGRVY	Homo sapiens
pmid	sentence
11723108	Pka and pkc readily phosphorylated pin1 and its ww domain in summary, we have demonstrated that phosphorylation of the pin1 ww domain on ser16 regulates its ability to function as a pser/thr-binding module. \|To examine the importance of Ser16 of Pin1, it was mutated to Glu to mimic pSer, and the mutant Pin1S16E failed to bind mitotic phosphoproteins

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263149	Ser16	AVGTKRGsDELFSTC	Rattus norvegicus
pmid	sentence
12851456	PKA directly phosphorylates PTB on conserved Ser-16, and PKA activation in PC12 cells induces Ser-16 phosphorylation. PTB carrying a Ser-16 to alanine mutation accumulates normally in the nucleus. However, export of this mutant protein from the nucleus is greatly reduced in heterokaryon shuttling assays. Conversely, hyperphosphorylation of PTB by coexpression with the catalytic subunit of PKA results in the accumulation of PTB in the cytoplasm.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250001	Ser1679	NVKSKIGsTDNIKYQ	Homo sapiens	HeLa Cell
pmid	sentence
11029056	CAMP-dependent protein kinase activity disrupts the MAP2-microtubule interaction in living HeLa cells. S319, S350, and S382 were thus identified as preferred targets of PKA

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250002	Ser1710	HVTSKCGsLKNIRHR	Homo sapiens	HeLa Cell
pmid	sentence
11029056	CAMP-dependent protein kinase activity disrupts the MAP2-microtubule interaction in living HeLa cells. S319, S350, and S382 were thus identified as preferred targets of PKA

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250003	Ser1742	KAQAKVGsLDNAHHV	Homo sapiens	HeLa Cell
pmid	sentence
11029056	CAMP-dependent protein kinase activity disrupts the MAP2-microtubule interaction in living HeLa cells. S319, S350, and S382 were thus identified as preferred targets of PKA

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-114277	Ser17	DASQRRRsLEPAENV	Homo sapiens
pmid	sentence
11804588	Pka activated src both in vitro and in vivo by phosphorylating src on serine 17

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-247988	Ser17	DASQRRRsLEPAENV	Homo sapiens
pmid	sentence
11804588	PKA activated Src both in vitro and in vivo by phosphorylating Src on serine 17 within its amino terminus

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263108	Ser1700	VNSDRRDsLQQTNTT	in vitro
pmid	sentence
19074150	We recently demonstrated that PKA activation led to increased alpha(1D) Ca(2+) channel activity in tsA201 cells by phosphorylation of the channel protein. Western blotting showed that the N terminus and C terminus were phosphorylated. Serines 1743 and 1816, two PKA consensus sites, were phosphorylated by PKA and identified by mass spectrometry.

Identifier	Residue	Sequence	Organism
SIGNOR-263109	Ser1773	AAHGKRPsIGNLEHV	in vitro
pmid	sentence
19074150	We recently demonstrated that PKA activation led to increased alpha(1D) Ca(2+) channel activity in tsA201 cells by phosphorylation of the channel protein. Western blotting showed that the N terminus and C terminus were phosphorylated. Serines 1743 and 1816, two PKA consensus sites, were phosphorylated by PKA and identified by mass spectrometry.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-163663	Ser172	DQVQRRGsLPPRQVP	Homo sapiens
pmid	sentence
20110267	We identified ser-282 as target of mapk and ser-172 as target of pkc and pka in vitro and in a transfected human embryonic kidney 293 (hek293) cell model using site directed mutagenesis and phosphopeptide mapping analysis. In hek293 cells, phosphorylation of these sites occurred at a basal level and down-regulated constitutive nox1 activity. I

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-195983	Ser172	NRVKRRPsPYEMEIT	Homo sapiens
pmid	sentence
22310283	The phosphorylation of serine 172 of tal1 specifically destabilizes tal1 interaction with histone demethylase lsd1 and, therefore, leads to the activation of the certain tal1 target genes in differentiated erythroid cells or t-cell leukemia.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-161860	Ser173	DGEFLRTsCGSPNYA	Homo sapiens
pmid	sentence
19942859	Pka associates with and phosphorylates ampk?1 At ser-173 to impede threonine thr-172 phosphorylation and thus activation of ampk1 by lkb1 in response to lipolytic signals

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-180576	Ser174	KGMLARGsYSIKSRF	Homo sapiens
pmid	sentence
18768928	The results indicate that phosphorylation of gdi_ at ser174 by pka suppresses rhoa activity, providing a potential protective signaling mechanism for inflammatory injury.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-109173	Ser176	QTAAKRAsRIYNT	Homo sapiens
pmid	sentence
11443111	We report in this study the acute functional regulation of rgs10 thru the specific and inducible phosphorylation of rgs10 protein at serine 168 by camp-dependent kinase a. This phosphorylation nullifies the rgs10 activity at the plasma membrane, which controls the g protein-dependent activation of the inwardly rectifying potassium channel.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250032	Ser178	TAHNKRIsTLTIEEG	in vitro
pmid	sentence
9407077	NIPP-1 is the RNA-binding subunit of a major species of protein phosphatase-1 in the nucleus. The purified recombinant protein was a potent (Ki = 9.9 +/- 0.3 pM) and specific inhibitor of protein phosphatase-1 and was stoichiometrically phosphorylated by protein kinases A and CK2. At physiological ionic strength, phosphorylation by these protein kinases drastically decreased the inhibitory potency of free NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A

Identifier	Residue	Sequence	Organism
SIGNOR-250033	Ser199	PKRKRKNsRVTFSED	in vitro
pmid	sentence
9407077	NIPP-1 is the RNA-binding subunit of a major species of protein phosphatase-1 in the nucleus. The purified recombinant protein was a potent (Ki = 9.9 +/- 0.3 pM) and specific inhibitor of protein phosphatase-1 and was stoichiometrically phosphorylated by protein kinases A and CK2. At physiological ionic strength, phosphorylation by these protein kinases drastically decreased the inhibitory potency of free NIPP-1. Sequencing and phosphoamino acid analysis of tryptic phosphopeptides enabled us to identify Ser178 and Ser199 as the phosphorylation sites of protein kinase A

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-83100	Ser1782	GAEIITQsPGRSSVA	Homo sapiens	HeLa Cell, Neuron
pmid	sentence
11029056	Specific phosphorylation states may enhance the interaction of map2 with the actin cytoskeleton, thereby providing a regulated mechanism for map2 function within distinct cytoskeletal domains

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-187410	Ser179	PGKARKKsSCQLL	Homo sapiens
pmid	sentence
19651783	These results provide a mechanistic explanation for the differential effects of rap1 phosphorylation by pka on effector protein interaction. camp is one among several pathways leading to rap1 activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250042	Ser180	KKKPKKKsCLLL	Chlorocebus aethiops
pmid	sentence
9867809	Phosphorylation of Rap1A by PKA abolished its binding activity to CRR. a mutant Rap1A(S180E), whose sole PKA phosphorylation residue, Ser-180, was substituted by an acidic residue, Glu, to mimic its phosphorylated form, failed to suppress Ras-dependent Raf-1 activation in COS-7 cells.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-137085	Ser181	YQPRRRKsVKNGQAE	Homo sapiens
pmid	sentence
15889150	We find that activation of camp-dependent protein kinase a (pka) induces phosphorylation of sox9 on its two s64 and s181 pka sites, and its nuclear localization by enhancing sox9 binding to the nucleocytoplasmic transport protein importin beta.

Identifier	Residue	Sequence	Organism
SIGNOR-137089	Ser64	EPDLKKEsEEDKFPV	Homo sapiens
pmid	sentence
15889150	We find that activation of camp-dependent protein kinase a (pka) induces phosphorylation of sox9 on its two s64 and s181 pka sites, and its nuclear localization by enhancing sox9 binding to the nucleocytoplasmic transport protein importin beta.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-133880	Ser183	GLRTRTGsNIDCEKL	Homo sapiens
pmid	sentence
15703181	We show that protein kinase a inhibits activation of caspase-9 and caspase-3 downstream of cytochrome c in xenopus egg extracts and in a human cell-free system. Protein kinase a directly phosphorylates human caspase-9 at serines 99, 183, and 195.

Identifier	Residue	Sequence	Organism
SIGNOR-133884	Ser195	EKLRRRFsSLHFMVE	Homo sapiens
pmid	sentence
15703181	We show that protein kinase a inhibits activation of caspase-9 and caspase-3 downstream of cytochrome c in xenopus egg extracts and in a human cell-free system. Protein kinase a directly phosphorylates human caspase-9 at serines 99, 183, and 195.

Identifier	Residue	Sequence	Organism
SIGNOR-133888	Ser99	NRQAAKLsKPTLENL	Homo sapiens
pmid	sentence
15703181	We show that protein kinase a inhibits activation of caspase-9 and caspase-3 downstream of cytochrome c in xenopus egg extracts and in a human cell-free system. Protein kinase a directly phosphorylates human caspase-9 at serines 99, 183, and 195.

Publications:

3

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence
SIGNOR-250343	Ser1859	PPRIHRAsDPGLPAE
pmid	sentence
11986331	CAD is down-regulated as the cells emerge from S phase by protein kinase A (PKA) phosphorylation. PKA phosphorylates Ser1406 and Ser1859, although only Ser1406 is involved in regulation.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-149689	Ser188	RLQQRRGsQPETRTG	Homo sapiens
pmid	sentence
16982607	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-250047	Ser188	ARRGKKKsGCLVL	Mus musculus
pmid	sentence
12654918	PKA phosphorylates RhoA on Ser188. the addition of a negative charge to Ser188 is sufficient to diminish both RhoA activation and activity within the context of a cell.

Publications:

1

Organism:

Mus Musculus

Pathways:

WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276892	Ser189	GGGERFDsLTDLVEH	Homo sapiens	HEK-293T Cell
pmid	sentence
25802336	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-276891	Thr73	YGGEKFAtLAELVQY	Homo sapiens	HEK-293T Cell
pmid	sentence
25802336	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

Identifier	Residue	Sequence	Organism
SIGNOR-251709	Ser1897	LLRKANPsRCHSRES	Mus musculus
pmid	sentence
28119464	These findings reveal an essential role for _1C phosphorylation at Ser1928 in stimulating CaV1.2 channel activity and vasoconstriction by AKAP-targeted PKA upon exposure to increased glucose and in diabetes

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-178018	Ser19	YWARRGFsLDSAVPE	Homo sapiens
pmid	sentence
18339632	We also demonstrate that phosphorylation of serine 19, a protein kinase a consensus site located in this n-terminal domain, results in increased tph2 stability and consequent increases in enzyme output in cell culture systems

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-92447	Ser191	HRFRRQLsEPCNSFP	Homo sapiens
pmid	sentence
12213813	The camp-dependent protein kinase a (pka) phosphorylates er81 on ser(191)/ser(216)ser(191) and ser(216), were identified, whose mutation to alanine reduces er81 activity upon erk-mapk stimulation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249986	Ser191	ARAAARLsLTDPLVA	in vitro
pmid	sentence
2504723	Platelet glycoprotein Ib beta is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase. phosphorylation of this residue may contribute to the inhibitory actions of cyclic AMP by inhibiting collagen-induced polymerization of actin.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250324	Ser205	HPFLRRNsGC	in vitro
pmid	sentence
11336675	AANAT1–207 was phosphorylated in vitro at both PKA sites, Thr-31 and Ser-205. regulation is achieved by binding to 14-3-3, which structurally modulates the substrate binding sites, leading to measurable effects on the affinity of AANAT for its substrates with an accompanying increase in activity at low substrate concentrations.

Identifier	Residue	Sequence	Organism
SIGNOR-250325	Thr31	PSCQRRHtLPASEFR	in vitro
pmid	sentence
11336675	AANAT1201 is phosphorylated at Thr-31 by PKA, it binds to 14-3-3. regulation is achieved by binding to 14-3-3, which structurally modulates the substrate binding sites, leading to measurable effects on the affinity of AANAT for its substrates with an accompanying increase in activity at low substrate concentrations.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250335	Ser2054	MPKKKKPsRLKGDNE	Homo sapiens
pmid	sentence
11050185	Changing a serine residue (Ser(2054)) to aspartic acid mutated the potential protein kinase A site adjacent to NLS2(APC), resulting in both inhibition of the NLS2(APC)-mediated nuclear import of a chimeric beta-galactosidase fusion protein and a reduction of full-length APC nuclear localization.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-118257	Ser209	VLKGKKLsLPA	Homo sapiens
pmid	sentence
14517323	We conclude that pka phosphorylation of serine 209 is required for the retrograde transport of the kdel receptor from the golgi complex to the er from which the retrieval of proteins bearing the kdel signal depends.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-167147	Ser21	LTEERDGsLNQSSGY	Homo sapiens
pmid	sentence
20658524	The serine 21 (s21) residue of fyn is a protein kinase a (pka) recognition site within an rxxs motif of the amino terminal sh4 domain of fyn. In addition, s21 is critical for fyn kinase-linked cellular signaling. Mutation of s21a blocks pka phosphorylation of fyn and alters its tyrosine kinase activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-83221	Ser21	SGRARTSsFAEPGGG	Homo sapiens
pmid	sentence
11035810	Phosphorylation of ser21 and inactivation of glycogen synthase kinase 3 by protein kinase a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-126659	Ser2152	TRRRRAPsVANVGSH	Homo sapiens
pmid	sentence
15228085	Site-directed mutagenesis analysis indicated that serine 2152 is the unique substrate in the c-terminal region of abp for endogenously activated pka.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, SARS-CoV ATTACHMENT AND ENTRY

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273786	Ser216	PTNLRRRsRSFTCNE	Homo sapiens	Blood Platelet
pmid	sentence
24244663	Cyclic AMP- and cyclic GMP-dependent kinases (PKA, PKG) inhibit the interaction of RGS18 and 14-3-3 by phosphorylating S216.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276281	Ser219	NSSEQRVsLDIDLWD	Homo sapiens
pmid	sentence
20215566	Mutagenesis of serine 219 (S219) and S369 at the PKA sites on RARA to either double alanines or double glutamic acids showed that both PKA sites are important for RARA activity.

Identifier	Residue	Sequence	Organism
SIGNOR-276282	Ser369	YVRKRRPsRPHMFPK	Homo sapiens
pmid	sentence
20215566	Mutagenesis of serine 219 (S219) and S369 at the PKA sites on RARA to either double alanines or double glutamic acids showed that both PKA sites are important for RARA activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250028	Ser220	KAKPSLLsRVGALTN	Mus musculus
pmid	sentence
11751901	PKA increased lipolysis in cells expressing Peri A because it abrogated the inhibitory actions of Peri A on lipolysis.‚ amino-terminal PKA sites (Ser-81, Ser-222, and Ser-276)

Identifier	Residue	Sequence	Organism
SIGNOR-250029	Ser277	QAVSRRRsEVRVPWL	Mus musculus
pmid	sentence
11751901	PKA increased lipolysis in cells expressing Peri A because it abrogated the inhibitory actions of Peri A on lipolysis.‚ amino-terminal PKA sites (Ser-81, Ser-222, and Ser-276)

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250492	Ser81	EPVVRRLsTQFTAAN	Mus musculus	NIH-3T3 Cell
pmid	sentence
11751901	PKA increased lipolysis in cells expressing Peri A because it abrogated the inhibitory actions of Peri A on lipolysis. amino-terminal PKA sites (Ser-81, Ser-222, and Ser-276)

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-250018	Ser229	LLFPRLKsISERLSV	in vitro
pmid	sentence
2176601	Phosphorylation at one of these sites (serine 243) could be increased by A kinase in vitro. phosphorylation of MIP reconstituted into single bilayers increased the voltage dependence and long-term closures of the channels observed.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-134605	Ser23	PAPIRRRsSNYRAYA	Homo sapiens
pmid	sentence
15769444	Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction.

Identifier	Residue	Sequence	Organism
SIGNOR-134609	Ser24	APIRRRSsNYRAYAT	Homo sapiens
pmid	sentence
15769444	Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250040	Ser233	VSSQHRYsTPHAFTF	Chlorocebus aethiops
pmid	sentence
12801936	Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras. Cyclic AMP (cAMP) blocks Raf-1 activation by stimulating its phosphorylation on serine 43 (Ser43), serine 233 (Ser233), and serine 259 (Ser259).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250041	Ser259	SQRQRSTsTPNVHMV	Chlorocebus aethiops	COS Cell
pmid	sentence
12801936	Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras. Cyclic AMP (cAMP) blocks Raf-1 activation by stimulating its phosphorylation on serine 43 (Ser43), serine 233 (Ser233), and serine 259 (Ser259).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250039	Ser43	FGYQRRAsDDGKLTD	Chlorocebus aethiops	COS Cell
pmid	sentence
12801936	Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras. Cyclic AMP (cAMP) blocks Raf-1 activation by stimulating its phosphorylation on serine 43 (Ser43), serine 233 (Ser233), and serine 259 (Ser259).

Identifier	Residue	Sequence	Organism
SIGNOR-86137	Ser621	PKINRSAsEPSLHRA	Homo sapiens
pmid	sentence
11971957	We have mapped all camp-induced phosphorylation sites in raf-1, showing that serines 43, 259, and 621 are phosphorylated by pka in vitro and induced by camp in vivo

Publications:

4

Organism:

Chlorocebus Aethiops, Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism
SIGNOR-249715	Ser233	NPPSRKGsGFGHRLS	in vitro
pmid	sentence
8390988	connexin- 32 is proteolyzed by pcalpain and mcalpain. phosphorylation of connexin-32 by protein kinase C, but not by protein kinase A, efficiently prevents its proteolysis by both calpain isoforms. major phosphorylation sites: Ser233(for protein kinase A). Phosphorylation of connexin-32 by protein kinase C,but not by protein kinase A, prevents the proteolytic attack of p-calpain and m-calpain. Phosphorylation of connexin-32 by protein kinase A and protein kinase C does not prevent its proteolysis by papain, a-chymotrypsin, proteinase K, and trypsin

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250346	Ser234	YRLTRFLsRVIKCDP	in vitro
pmid	sentence
8058338	PKA phosphorylates three distinct serine residues in cyclin D1 at positions 90, 197 and 234.

Identifier	Residue	Sequence	Organism
SIGNOR-250347	Ser90	NYLDRFLsLEPVKKS	in vitro
pmid	sentence
8058338	PKA phosphorylates three distinct serine residues in cyclin D1 at positions 90, 197 and 234.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-37839	Ser2347	TTCCRRSsNVSYKYS	Homo sapiens
pmid	sentence
8318012	Pka phosphorylates the cytoplasmic mpr 300 domain at ser20 and at a non-identified site,

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277538	Ser235	TTQLRLLsEDTDSQR	Homo sapiens	HEK-293 Cell
pmid	sentence
33110360	We confirmed the phosphorylation of T130, S235, and S364 by developing monoclonal antibodies against phospho-specific forms of these sites and showed that their phosphorylation is cell cycle-dependent. According to our results, PKA-mediated phosphorylation of E2F1 by PKA inhibits proliferation and glucose uptake and induces caspase-3 activation and senescence.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277537	Ser364	PLLSRMGsLRAPVDE	Homo sapiens	HEK-293 Cell
pmid	sentence
33110360	We confirmed the phosphorylation of T130, S235, and S364 by developing monoclonal antibodies against phospho-specific forms of these sites and showed that their phosphorylation is cell cycle-dependent. According to our results, PKA-mediated phosphorylation of E2F1 by PKA inhibits proliferation and glucose uptake and induces caspase-3 activation and senescence.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277536	Thr130	GEKSRYEtSLNLTTK	Homo sapiens	HEK-293 Cell
pmid	sentence
33110360	We confirmed the phosphorylation of T130, S235, and S364 by developing monoclonal antibodies against phospho-specific forms of these sites and showed that their phosphorylation is cell cycle-dependent. According to our results, PKA-mediated phosphorylation of E2F1 by PKA inhibits proliferation and glucose uptake and induces caspase-3 activation and senescence.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-63984	Ser236	IDKNRRKsCQACRLR	Homo sapiens
pmid	sentence
9891036	Phosphorylation of human estrogen receptor alpha by protein kinase a regulates dimerizationeralpha is phosphorylated by protein kinase a (pka) on serine-236 within the dna binding domain. Mutation of serine-236 to glutamic acid prevents dna binding by inhibiting dimerization by eralpha

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-64955	Ser239	AEVQRRLsPPECLNA	Homo sapiens
pmid	sentence
10037142	Recombinant ap-2 was phosphorylated in vitro by protein kinase a (pka) at ser239. Mutation of ser239 to ala abolished in vitro phosphorylation of ap-2 by pka, but not the dna binding activity of ap-2. Cotransfection studies showed that pka stimulated the effect of ap-2 on the apoe promoter, but not that of the s239a mutant.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-93531	Ser245	PSTSPRAsVTEESWL	Homo sapiens
pmid	sentence
12351631	Here we show that overexpression of pka causes phosphorylation and cytoplasmic accumulation of nf-atc1 in direct opposition to calcineurin by phosphorylating ser-245, ser-269, and ser-294 in the conserved serine-proline repeat domainwe further show that a complete block of nf-atc1 nuclear localization by pka requires a second kinase activity that can be supplied by glycogen synthase kinase-3 (gsk-3)

Identifier	Residue	Sequence	Organism
SIGNOR-93535	Ser269	PCNKRKYsLNGRQPP	Homo sapiens
pmid	sentence
12351631	Here we show that overexpression of pka causes phosphorylation and cytoplasmic accumulation of nf-atc1 in direct opposition to calcineurin by phosphorylating ser-245, ser-269, and ser-294 in the conserved serine-proline repeat domainwe further show that a complete block of nf-atc1 nuclear localization by pka requires a second kinase activity that can be supplied by glycogen synthase kinase-3 (gsk-3)

Identifier	Residue	Sequence	Organism
SIGNOR-93539	Ser294	PHGSPRVsVTDDSWL	Homo sapiens
pmid	sentence
12351631	Here we show that overexpression of pka causes phosphorylation and cytoplasmic accumulation of nf-atc1 in direct opposition to calcineurin by phosphorylating ser-245, ser-269, and ser-294 in the conserved serine-proline repeat domainwe further show that a complete block of nf-atc1 nuclear localization by pka requires a second kinase activity that can be supplied by glycogen synthase kinase-3 (gsk-3)

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250066	Ser25	PGTASRPsSSRSYVT	in vitro
pmid	sentence
2500966	Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

Identifier	Residue	Sequence	Organism
SIGNOR-250067	Ser39	TTSTRTYsLGSALRP	in vitro
pmid	sentence
2500966	Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

Identifier	Residue	Sequence	Organism
SIGNOR-250070	Ser47	LGSALRPsTSRSLYA	in vitro
pmid	sentence
2500966	Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

Identifier	Residue	Sequence	Organism
SIGNOR-250069	Ser51	LRPSTSRsLYASSPG	in vitro
pmid	sentence
2500966	Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

Identifier	Residue	Sequence	Organism
SIGNOR-250068	Ser66	GVYATRSsAVRLRSS	in vitro
pmid	sentence
2500966	Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

Identifier	Residue	Sequence	Organism
SIGNOR-250071	Ser7	sSSSYRRM	in vitro
pmid	sentence
2500966	Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure.

Publications:

6

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277625	Ser2548	TRFGRKLsIIRGIVE	in vitro
pmid	sentence
35908190	Moreover, phosphorylation of C-HEAT Ser2550 by cAMP-dependent protein kinase (PKA), the top hit in kinase activity screens, was found to hasten huntingtin degradation, such that levels of the catalytic subunit (PRKACA) were inversely related to huntingtin levels.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence
SIGNOR-275727	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
SIGNOR-86141	Ser259	SQRQRSTsTPNVHMV	Homo sapiens
pmid	sentence
11971957	Serines 43, 259, and 621 are phosphorylated by PKA in vitro and induced by cAMP in vivo.cAMP increased Raf-1 serine 259 phosphorylation in a PKA-dependent manner with kinetics that correlated with ERK deactivation.

Identifier	Residue	Sequence	Organism
SIGNOR-86145	Ser43	FGYQRRAsDDGKLTD	Homo sapiens
pmid	sentence
11971957	Serine 43 phosphorylation decreased the binding to ras in serum-starved but not in mitogen-stimulated cells. However, the kinase activity of a rafs43a mutant was fully inhibited by pka.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism
SIGNOR-250045	Ser260	NAALRREsQGSLNSS	in vitro
pmid	sentence
12534294	RGS14 is phosphorylated in vitro at Ser258 and Thr494 by PKA. cAMP-induced phosphorylation as an important modulator of RGS14 function since phosphorylation could enhance RGS14 binding to Galpha(i)-GDP

Identifier	Residue	Sequence	Organism
SIGNOR-250046	Thr495	SATGKRQtCDIEGLV	in vitro
pmid	sentence
12534294	RGS14 is phosphorylated in vitro at Ser258 and Thr494 by PKA. cAMP-induced phosphorylation as an important modulator of RGS14 function since phosphorylation could enhance RGS14 binding to Galpha(i)-GDP

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-266309	Ser27	SFGFTRTsARRRLAD	in vitro
pmid	sentence
21880142	PKA phosphorylates GPKOW at S27 and T316 in vitro. GPKOWs ability to bind RNA is sensitive to mutations of its PKA phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-266308	Thr316	GTASSRKtLWNQELY	in vitro
pmid	sentence
21880142	PKA phosphorylates GPKOW at S27 and T316 in vitro. GPKOWs ability to bind RNA is sensitive to mutations of its PKA phosphorylation sites.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-104954	Ser27	TSPTGRGsMAAPSLH	Homo sapiens
pmid	sentence
11162439	Serine 27, a human retinoid x receptor alpha residue, phosphorylated by protein kinase a is essential for cyclicamp-mediated downregulation of rxralpha function.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250048	Ser273	AGTRRREsLGKKAKR	in vitro
pmid	sentence
9677319	Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII). Incubation of Rad with PKA decreases GTP binding by 60-70%, but this effect seems to be independent of phosphorylation, as it is observed with the Ser273-->Ala mutant of Rad containing a mutation at the site of PKA phosphorylation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-129345	Ser2733	SVSPKRNsISRTHKD	Homo sapiens
pmid	sentence
15383279	Using a combination of biochemical, enzymatic, and immunofluorescence techniques, we show that the anchoring protein contributes to pkd activation in two ways: it recruits an upstream kinase pkceta and coordinates pka phosphorylation events that release activated protein kinase d. Thus, akap-lbc synchronizes pka and pkc activities in a manner that leads to the activation of a third kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163752	Ser275	LSAFRRTsLAGGGRR	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).

Identifier	Residue	Sequence	Organism
SIGNOR-163756	Ser284	AGGGRRIsDSHEDTG	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).

Identifier	Residue	Sequence	Organism
SIGNOR-163760	Ser304	SLLKKRDsFRTPRDS	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).

Identifier	Residue	Sequence	Organism
SIGNOR-163764	Ser311	SFRTPRDsKLEAPAE	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:

4

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-58972	Ser276	SMQLRRPsDRELSEP	Homo sapiens
pmid	sentence
9660950	The transcriptional activity of nf-kappa b is stimulated upon phosphorylation of its p65 subunit on serine 276 by protein kinase a (pka).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-198658	Ser279	KVAERRSsPLLRRKD	Homo sapiens
pmid	sentence
22865920	PKA/Cdk5-mediated phosphorylation of HDAC5 at Ser279 within the NLS promotes nuclear localization of HDAC5 and interaction with the nuclear corepressor complex

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250079	Ser2808	YNRTRRIsQTSQVSV	in vitro
pmid	sentence
14532276	PKA-mediated hyperphosphorylation of a conserved serine, Ser-2843 in skeletal RyR and Ser-2809 in cardiac RyR, results in an aberrant SR function during heart failure. hyperphosphorylated RyRs are leaky and therefore lead to a reduced SR Ca2+ load and impaired contractile function in heart failure

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250078	Ser2843	KKKTRKIsQSAQTYD	in vitro
pmid	sentence
14532276	PKA-mediated hyperphosphorylation of a conserved serine, Ser-2843 in skeletal RyR and Ser-2809 in cardiac RyR, results in an aberrant SR function during heart failure. hyperphosphorylated RyRs are leaky and therefore lead to a reduced SR Ca2+ load and impaired contractile function in heart failure

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250353	Ser2849	RSGSRRGsFDATGNS	Homo sapiens	HeLa Cell
pmid	sentence
7525582	HeLa cells treated with forskolin indicated that stimulation of protein kinase A in transfected cells could decrease the interaction of DP.AN.SerC23 with keratin IF networks. phosphorylation of Ser-C23 could destabilize interactions that occur either directly through this 20 residue sequence or that are dependent on its correct conformation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181859	Ser287	EICQRRTsYLPSEIM	Homo sapiens
pmid	sentence
18976636	Pka activation induced an increase of kir7.1 currents. This effect was absent in mutant kir7.1 channels lacking pka consensus site (287)s

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276027	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:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-277454	Ser3	sFPETDFQ	in vitro
pmid	sentence
31160797	These observations suggested that LINK-A expression potentially inhibits PKA phosphorylation/activity and PKA-mediated phosphorylation of TRIM71 at Ser3.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-125779	Ser305	IKRSKKNsLALSLTA	Homo sapiens
pmid	sentence
15193262	We show that phosphorylation of serine-305 in the hinge region of er_ by protein kinase a (pka) induced resistance to tamoxifenactivation of pka prevents tamoxifen-mediated inhibition of er transactivation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250036	Ser310	PEAQRRVsKNSKYNA	in vitro
pmid	sentence
14576165	PKA-mediated phosphorylation of PS1 is completely inhibited by mutation of Ser310.phosphorylation of Ser310 does not inhibit the caspase-mediated cleavage of PS1, and the biological function of this phosphorylation event remains to be determined in further experiments.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-140289	Ser312	SKSHRRTsLPCIPRE	Homo sapiens
pmid	sentence
16153182	Ser312 of pde3a was phosphorylated in an h-89-sensitive response to forskolin, indicative of phosphorylation by pka (camp-dependent protein kinase), but phosphorylation at this site did not stimulate 14-3-3 binding.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273799	Ser313	ADLNRTLsRREKKKA	Homo sapiens	HEK-293 Cell
pmid	sentence
31801866	PKCα phosphorylates PACSIN2 at serine 313 in the linker region and decreases its membrane binding and tubulation activities. Phosphorylation of PACSIN2 at S313 negatively regulated protein interaction between NS5A and core, which affected viral assembly

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262930	Ser32	DRAAKRLsLESEGAG	in vitro
pmid	sentence
17693641	Here we show that TPPP induces tubulin self-assembly into intact frequently bundled microtubules, and that the phosphorylation of specific sites distinctly affects the function of TPPP. The phosphorylation sites Thr(14), Ser(18), Ser(160) for Cdk5; Ser(18), Ser(160) for ERK2, and Ser(32) for PKA were identified by mass spectrometry. The phosphorylation by ERK2 or Cdk5 resulted in the loss of microtubule-assembling activity of TPPP. Thus our data suggest that ERK2 or Cdk5 can perturb the interaction of TPPP with tubulin, in contrast to PKA that is ineffective in this respect.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-169853	Ser320	ASPGRPSsVDTLLSP	Homo sapiens
pmid	sentence
21085490	Protein kinase a binds and activates heat shock factor 1hsf1 binds avidly to the catalytic subunit of pka, (pkac_) and becomes phosphorylated on a novel serine phosphorylation site within its central regulatory domain (serine 320 or s320), both in vitro and in vivo. Intracellular pkac_ levels and phosphorylation of hsf1 at s320 were both required for hsf1 to be localized to the nucleus, bind to response elements in the promoter of an hsf1 target gene

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250016	Ser329	LGGLCDLsSRY	Homo sapiens
pmid	sentence
12639913	Activation of MC4R by agonist is associated with protein kinase A (PKA) and GRK phosphorylation of serine/threonine residues in the C-terminal tail of MC4R, followed by -arrestin and dynamin-dependent internalization of the receptor. Thr312 and Ser329/330 in the C-terminal tail of MC4R are potential sites for PKA

Identifier	Residue	Sequence	Organism
SIGNOR-250017	Thr312	RSQELRKtFKEIICC	Homo sapiens
pmid	sentence
12639913	Activation of MC4R by agonist is associated with protein kinase A (PKA) and GRK phosphorylation of serine/threonine residues in the C-terminal tail of MC4R, followed by -arrestin and dynamin-dependent internalization of the receptor. Thr312 and Ser329/330 in the C-terminal tail of MC4R are potential sites for PKA

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-90976	Ser331	STRPRSLsLQPQLTQ	Homo sapiens
pmid	sentence
12147288	Ser-331 was found to be involved in pka-mediated phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273795	Ser333	RMKDRKFsWGQQRTN	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
25666616	Upon β2AR activation, a specific isoform of the second messenger cAMP-dependent protein kinase A (PKAα) rapidly phosphorylates USP20 on serine 333 located in its unique insertion domain. This phosphorylation of USP20 correlates with a characteristic SDS-PAGE mobility shift of the protein, blocks its deubiquitinase activity, promotes its dissociation from the activated β2AR complex, and facilitates trafficking of the ubiquitinated β2AR to autophagosomes, which fuse with lysosomes to form autolysosomes where receptors are degraded.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-92455	Ser334	PTYQRRGsLQLWQFL	Homo sapiens
pmid	sentence
12213813	Pka targets er81 on ser(334) in vivo. Surprisingly, phosphorylation of ser(334) severely reduces the dna-binding ability of er81 but also enhances the transactivation potential of er81. These counteractive effects of pka phosphorylation on er81-dependent transcription may cause the selective up-regulation of promoters with high but not low affinity for er81.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276855	Ser334	KHTRRKEsHAARRHQ	Homo sapiens	HEK-293 Cell
pmid	sentence
25274816	Mutating the single PKA site (S334A) in human KCa3.1 abolished the PKA-dependent regulation. CaM-affinity chromatography showed that CaM binding to KCa3.1 was decreased by PKA-dependent phosphorylation of S334, and this regulation was absent in the S334A mutant.The results above indicate that PKA activation led to a phosphorylation event that inhibited KCa3.1 channel activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158595	Ser337	FVQLRRKsDLETSEP	Homo sapiens
pmid	sentence
17959673	In this study, we demonstrate that the phosphorylation of p50 and p65 by the catalytic subunit of protein kinase a (pkac) is essential for nf-kappab dna binding and transactivation activity. treatment with h89 and knockdown of pkac in cells led to the inhibition of phosphorylation at p50 ser(337) and p65 ser(276) and loss of dna binding by nf-kappab.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-143392	Ser338	IEKRYRSsINDKIIE	Homo sapiens
pmid	sentence
16381800	Sterol regulatory element-binding protein 1 is negatively modulated by pka phosphorylation. ser338 of srebp-1a and ser314 of srebp-1c are pka phosphorylation sites.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250038	Ser339	GLQERRGsNVSLTLD	Chlorocebus aethiops
pmid	sentence
10601328	The PKA phosphorylation site on PTP-SL was identified as the Ser(231) residue. treatment of COS-7 cells with PKA activators, or overexpression of the Calpha catalytic subunit of PKA, inhibited the cytoplasmic retention of ERK2 and p38alpha by wild-type PTP-SL, but not by a PTP-SL S231A mutant.‚

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-276316	Ser342	RHEAKQRsVQRWREA	in vitro
pmid	sentence
21423175	In vitro kinase assays demonstrated that purified PKAc directly phosphorylates wild-type Flag–praja2, but not the Flag–praja2S342A,T389A mutant, confirming these residues as the main PKA phosphorylation sites (Fig. 5h).

Identifier	Residue	Sequence	Organism
SIGNOR-276325	Thr389	RVITQREtENNQMTS	in vitro
pmid	sentence
21423175	In vitro kinase assays demonstrated that purified PKAc directly phosphorylates wild-type Flag–praja2, but not the Flag–praja2S342A,T389A mutant, confirming these residues as the main PKA phosphorylation sites (Fig. 5h).

Identifier	Residue	Sequence	Organism
SIGNOR-276323	Thr389	RVITQREtENNQMTS	in vitro
pmid	sentence
21423175	In vitro kinase assays demonstrated that purified PKAc directly phosphorylates wild-type Flag–praja2, but not the Flag–praja2S342A,T389A mutant, confirming these residues as the main PKA phosphorylation sites (Fig. 5h).

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-200492	Ser342	LAHDRAPsRKDSLES	Homo sapiens
pmid	sentence
23337587	Interestingly, sufu stability is regulated via dual phosphorylation at ser342/ser346 by pka and gsk3, and blocking sufu phosphorylation either by mutating ser346 to ala or by treating cultured cells with pka inhibitors attenuates sufu ciliary accumulation, whereas phospho-mimetic forms of sufu exhibits increased ciliary localization

Identifier	Residue	Sequence	Organism
SIGNOR-200496	Ser346	RAPSRKDsLESDSST	Homo sapiens
pmid	sentence
21317289	We report that Sufu is phosphorylated at Ser-342 and Ser-346 by GSK3? and cAMP-dependent protein kinase A (PKA), respectively, and phosphorylation at this dual site stabilizes Sufu against Shh signaling-induced degradation

Identifier	Residue	Sequence	Organism
SIGNOR-119099	Ser346	RAPSRKDsLESDSST	Homo sapiens
pmid	sentence
23337587	Interestingly, sufu stability is regulated via dual phosphorylation at ser342/ser346 by pka and gsk3, and blocking sufu phosphorylation either by mutating ser346 to ala or by treating cultured cells with pka inhibitors attenuates sufu ciliary accumulation, whereas phospho-mimetic forms of sufu exhibits increased ciliary localization

Publications:

3

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Sequence	Organism
SIGNOR-171999	Ser342	LAHDRAPsRKDSLES	Homo sapiens
pmid	sentence
21317289	We report that Sufu is phosphorylated at Ser-342 and Ser-346 by GSK3? and cAMP-dependent protein kinase A (PKA), respectively, and phosphorylation at this dual site stabilizes Sufu against Shh signaling-induced degradation.

Identifier	Residue	Sequence	Organism
SIGNOR-172003	Ser346	RAPSRKDsLESDSST	Homo sapiens
pmid	sentence
21317289	We report that Sufu is phosphorylated at Ser-342 and Ser-346 by GSK3? and cAMP-dependent protein kinase A (PKA), respectively, and phosphorylation at this dual site stabilizes Sufu against Shh signaling-induced degradation

Publications:

2

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Sequence	Organism
SIGNOR-250356	Ser362	AAAHRKGsSSNEPSS	Chlorocebus aethiops
pmid	sentence
1545828	Human c-Fos protein is phosphorylated in vitro by PKA. phosphorylation of Fos occurs at serine residue 362. Modification of the Fos protein by phosphorylation with PKA then allows it to act as a regulator of its own synthesis by downregulating fos gene expression at a transcriptional level

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-105229	Ser364	ALREKKFsTKSDVWS	Homo sapiens	T-lymphocyte
pmid	sentence
11181701	Activation of the cooh-terminal src kinase (csk) by camp-dependent protein kinase inhibits signaling through the t cell receptor.Pka phosphorylates csk at s364 in vitro and in vivo leading to a two- to fourfold increase in csk activity that is necessary for camp-mediated inhibition of tcr-induced interleukin 2 secretion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-53172	Ser365	KDCERRFsRSDQLKR	Homo sapiens
pmid	sentence
9366517	Pka phosphorylated wt1 at ser-365 and ser-393 in vitro, as well as at additional sites, and this phosphorylation abolished the dna-binding activity of wt1 in vitro. Using wt1 mutants in which ser-365 and ser-393 were mutated to ala individually and in combination, we showed that phosphorylation of these sites was critical for inhibition of dna binding in vivo.

Identifier	Residue	Sequence	Organism
SIGNOR-53176	Ser393	KTCQRKFsRSDHLKT	Homo sapiens
pmid	sentence
9366517	Pka phosphorylated wt1 at ser-365 and ser-393 in vitro, as well as at additional sites, and this phosphorylation abolished the dna-binding activity of wt1 in vitro. Using wt1 mutants in which ser-365 and ser-393 were mutated to ala individually and in combination, we showed that phosphorylation of these sites was critical for inhibition of dna binding in vivo.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250354	Ser366	SPQVRTLsGSRPPLL	in vitro
pmid	sentence
11171059	EEF-2K can be phosphorylated in vitro by cAMP-dependent protein kinase (PKA) and that this induces significant Ca(2+)/calmodulin (CaM)-independent eEF-2K activity. sites of phosphorylation were Ser-365 and Ser-499

Identifier	Residue	Sequence	Organism
SIGNOR-250444	Ser500	RLHLPRAsAVALEVQ	in vitro
pmid	sentence
11171059	EEF-2K can be phosphorylated in vitro by cAMP-dependent protein kinase (PKA) and that this induces significant Ca(2+)/calmodulin (CaM)-independent eEF-2K activity. sites of phosphorylation were Ser-365 and Ser-499

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-111239	Ser367	PPYQRRGsLQLWQFL	Homo sapiens	RK-13 Cell
pmid	sentence
11682477	We further show that the increase in erm transcriptional activity after pka phosphorylation is closely correlated with a drastic reduction in the dna binding of the transcription factor. These results indicate that the phosphorylation of erm by pka is involved in erm-mediated transcription and suggest that the activation of erm is probably related to conformational changes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-172466	Ser373	RLMKRRKsV	Homo sapiens	HEK-293 Cell
pmid	sentence
21357689	Patch clamp analysis, flow cytometry, and immunocytochemistry studies of hek293 transfected with wt hk2p3.1 and cultured in the presence of pka activators or inhibitors all confirm that activation of pka resulted in an increase in hk2p3.1 current expression (figs. 4_4?6) and demonstrate the dynamic regulatory effect of pka activity on k2p3.1 channel expression.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178244	Ser38	YVVKRRDsATSFSLD	Homo sapiens	B-lymphocyte
pmid	sentence
18417471	We have found using sf9 insect cells to overexpress human gst-aid that a small fraction of the enzyme is phosphorylated at ser38 and thr27 and at two residues not reported previously, ser41 and ser43

Identifier	Residue	Sequence	Organism
SIGNOR-178248	Thr27	WAKGRREtYLCYVVK	Homo sapiens
pmid	sentence
18417471	We have found using sf9 insect cells to overexpress human gst-aid that a small fraction of the enzyme is phosphorylated at ser38 and thr27 and at two residues not reported previously, ser41 and ser43

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183475	Ser385	NSKERHNsVECLDGL	Homo sapiens
pmid	sentence
19151997	Using this approach, we identified s385 as an in vitro phosphorylation site. Mutation of this residue to alanine resulted in a reduced sensitivity of kir3.1* currents to h89 and forskolin, confirming an in vivo role for this novel site of the kir3.1 channel subunit in its regulation by pka.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275630	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-275629	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-120643	Ser39	AKIPKRAsMVHSLIE	Homo sapiens
pmid	sentence
14701748	Negative regulation of histone deacetylase 8 activity by cyclic amp-dependent protein kinase athe pka phosphoacceptor site of hdac8 is ser(39)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-172430	Ser393	GLMKRRSsV	Homo sapiens
pmid	sentence
21357689	Mutation of the ser393 to alanine, which can neither be phosphorylated nor mimic a phosphorylated residue, resulted in the channel failing to pass current all of our findings support the conclusion that camp-dependent protein kinase is responsible for the phosphorylation of the terminal serine in both k2p3.1 and k2p9.1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-128411	Ser396	FTWKRLRsHSRQYVS	Homo sapiens
pmid	sentence
15328002	Two amino acid residues (ser396, ser398) on hr1 were determined to be pkc phosphorylation sites by in vitro phosphorylation studies.Site-directed mutagenesis studies suggests that the ser398 residue was primarily involved in pkc-mediated desensitization. Possibly, phosphorylation of the residues is required for receptor transport from endosomes to lysosomes.

Identifier	Residue	Sequence	Organism
SIGNOR-128415	Ser398	WKRLRSHsRQYVSGL	Homo sapiens
pmid	sentence
15328002	Two amino acid residues (ser396, ser398) on hr1 were determined to be pkc phosphorylation sites by in vitro phosphorylation studies.Site-directed mutagenesis studies suggests that the ser398 residue was primarily involved in pkc-mediated desensitization. Possibly, phosphorylation of the residues is required for receptor transport from endosomes to lysosomes.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250072	Ser397	NQNSRRPsRATWLSL	in vitro
pmid	sentence
1706595	Phosphorylation of vitronectin by protein kinase A is stoichiometric (approx. 1 mol/mol), that it is targeted to one site (Ser-378) at the C-terminal edge of the heparin-binding domain. gh the role of phosphorylation by PKA remains to be established, the identification of Ser-378 as the sole site for PKA action, and the proximity of the phosphorylation site to the point of cleavage that converts V75 into V65 10' focuses attention on a putative role for PKA in the modulation of this cleavage.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250061	Ser40	GQGAPGPsLTGSPWP	in vitro
pmid	sentence
11359875	HTH1 was phosphorylated at Ser40 by PKA. Tyrosine hydroxylase (TH) has been reported to require binding of 14-3-3 proteins for optimal activation by phosphorylation. phosphorylationof hTH1‚4 at Ser40, to a stoichiometry of up to 1.0 molphosphate per mol TH subunit, dramatically increases their binding to 14-3-3 proteins.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250329	Ser408	REKSKKYsDVEVPAS	in vitro
pmid	sentence
8810272	Protein kinase A phosphorylates -adducin at three sites in the neck domain (Ser-408, ’436, and ’481) in addition to the MARCKS-related domain of both subunits. Phosphorylation by PKA, in contrast to PKC, reduced affinity of erythrocyte adducin for spectrin-F-actin complexes as well as activity of adducin in promoting binding of spectrin to F-actin.

Identifier	Residue	Sequence	Organism
SIGNOR-250330	Ser436	TCSPLRHsFQKQQRE	in vitro
pmid	sentence
8810272	Protein kinase A phosphorylates -adducin at three sites in the neck domain (Ser-408, ’436, and ’481) in addition to the MARCKS-related domain of both subunits. Phosphorylation by PKA, in contrast to PKC, reduced affinity of erythrocyte adducin for spectrin-F-actin complexes as well as activity of adducin in promoting binding of spectrin to F-actin.

Identifier	Residue	Sequence	Organism
SIGNOR-250331	Ser481	KEDGHRTsTSAVPNL	in vitro
pmid	sentence
8810272	Protein kinase A phosphorylates -adducin at three sites in the neck domain (Ser-408, ’436, and ’481) in addition to the MARCKS-related domain of both subunits. Phosphorylation by PKA, in contrast to PKC, reduced affinity of erythrocyte adducin for spectrin-F-actin complexes as well as activity of adducin in promoting binding of spectrin to F-actin.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276870	Ser409	NPKQRRFsDQAAGPA	Homo sapiens	HEK-293 Cell
pmid	sentence
25512381	Here, we found the disruption of microtubule and neurite outgrowth induced by MARK2 overexpression was blocked by active PKA. The interaction between PKA and MARK2 was confirmed by coimmunoprecipitation and immunocytochemistry both in vitro and in vivo. PKA was found to inhibit MARK2 kinase activity by phosphorylating a novel site, serine 409.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249999	Ser42	TLLIRNGsEVRDPLV	in vitro
pmid	sentence
8506364	Ser-42 can be phosphorylated by either protein kinase A or protein kinase C

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276267	Ser425	PRPLRREsEI	in vitro
pmid	sentence
19843922	PKA consensus site S425 required for PKA-mediated effects on Kir2.1 channels. PKA activation reduced outward IK1 for heteromeric Kir2.1 WT+V227F channels after 2 hours of PKA activation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250055	Ser428	SSKIRRLsACKQQ	Rattus norvegicus
pmid	sentence
11297520	Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell growth.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-259922	Ser429	PQRERKSsSSSEDRN	Rattus norvegicus	PC-12 Cell
pmid	sentence
11510412	The in vitro phosphorylation of a site unique to B-Raf (Ser429) has been proposed to be responsible for the negative regulation of the isoenzyme by Akt. Using phosphopetide mapping and site-directed mutagenesis we showed that Ser429 is phosphorylated upon cAMP elevation in PC12 cells and proposed that PKA is a major kinase phosphorylating the B-Raf-specific site in vivo

Identifier	Residue	Sequence	Organism
SIGNOR-250339	Ser429	PQRERKSsSSSEDRN	in vitro
pmid	sentence
11510412	Direct phosphorylation of B-Raf by PKA exerts a negative effect on its kinase activity, essentially via phosphorylation of Ser429

Publications:

2

Organism:

Rattus Norvegicus, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249998	Ser431	QRPYRREsEI	Chlorocebus aethiops
pmid	sentence
11181181	Phosphorylation of the Kir2.2 C terminus by protein kinase A inhibited the association with SAP97.‚

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-72147	Ser44	RLQERRGsNVALMLD	Homo sapiens
pmid	sentence
10559944	Here we show that cyclic-amp-dependent protein kinase (pka) phosphorylates serine residue 23 in the kim of heptp in vitro and in intact cells. This modification reduces binding of map kinases to the kim, an effect that is prevented by mutation of serine 23 to alanine.

Identifier	Residue	Organism
SIGNOR-182522		Homo sapiens
pmid	sentence
19047375	B2 adrenergic receptor stimulation induces the pka dependent phosphorylation of heptp and releases bound p38 mapk

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250023	Ser442	TPQLRRSsGTSGLLP	in vitro
pmid	sentence
8163498	Serine 427 is the target for cAMP-PK phosphorylation of the rat adipocyte cGI-PDE in vitro

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-262751	Ser443	PQRKSQRsSYVSMRI	in vitro
pmid	sentence
12175859	Here, we have identified phosphorylation sites on the human ρ1 GABA receptor for six protein kinases widely expressed in the brain: protein kinase C (PKC); cAMP‐dependent protein kinase (PKA); calmodulin‐dependent kinase (CaMKII); casein kinase (CKII); mitogen‐activated protein kinase (MAPK); and cGMP‐dependent protein kinase (PKG). These data, indicate that S422 and/or S423 are the major sites of PKA-mediated phosphorylation of the 1 GABA receptor.An extensive functional analysis comparing wild type 1 receptors and receptors with select or multiple phosphorylation sites removed as well as pharmacological manipulation of five kinase pathways failed to reveal any functional effects of phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-262750	Ser444	QRKSQRSsYVSMRID	in vitro
pmid	sentence
12175859	Here, we have identified phosphorylation sites on the human ρ1 GABA receptor for six protein kinases widely expressed in the brain: protein kinase C (PKC); cAMP‐dependent protein kinase (PKA); calmodulin‐dependent kinase (CaMKII); casein kinase (CKII); mitogen‐activated protein kinase (MAPK); and cGMP‐dependent protein kinase (PKG). These data, indicate that S422 and/or S423 are the major sites of PKA-mediated phosphorylation of the 1 GABA receptor.An extensive functional analysis comparing wild type 1 receptors and receptors with select or multiple phosphorylation sites removed as well as pharmacological manipulation of five kinase pathways failed to reveal any functional effects of phosphorylation

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-128429	Ser448	IRRPRSLsSPTVTLS	Homo sapiens
pmid	sentence
15328345	Nedd4-2 was a substrate for phosphorylation by pka in vitro and in cells;three nedd4-2 residues were phosphorylated by pka and were required for camp to inhibit nedd4-2 (relative functional importance ser-327 > ser-221 > thr-246).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250000	Ser4520	GGHGSRHsLASTDEK	Cricetulus griseus
pmid	sentence
11158305	LRP phosphorylation is mediated by PKA at residue serine 76 of its cytoplasmic tail and that this phosphorylation contributes to receptor-mediated endocytosis.

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-250328	Ser455	PAPSRTAsFSESRAD	in vitro
pmid	sentence
10653665	Phosphorylation of Recombinant Human ATP:Citrate Lyase by cAMP-Dependent Protein Kinase Abolishes Homotropic Allosteric Regulation of the Enzyme by Citrate and Increases the Enzyme Activity. Ser 454, which is phosphorylated by the catalytic subunit of cAMP-dependent protein kinase (PKA)

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-195203	Ser458	GKANRQVsITGFFQR	Homo sapiens
pmid	sentence
22148433	In this study, we identified s458, located in the pcna-interacting protein (pip-box) motif of p68, as a phosphorylation site for pka. Phosphomimetic mutation of s458 resulted in a decrease in p68 affinity for pcna as well as the processivity of pol _.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-145028	Ser464	QAIHQLRsVKMEQRK	Homo sapiens
pmid	sentence
16513649	Mutagenesis and mass spectrometry studies identified four pka phosphorylation sites: ser465 (minor site) and three amino acid residues ser568, ser569, and ser570 (major sites) within the carboxyl-terminal region. pka activation decreased sk2 surface localization

Identifier	Residue	Sequence	Organism
SIGNOR-145032	Ser567	SSSRRRRsSSTAPPT	Homo sapiens
pmid	sentence
16513649	Mutagenesis and mass spectrometry studies identified four pka phosphorylation sites: ser465 (minor site) and three amino acid residues ser568, ser569, and ser570 (major sites) within the carboxyl-terminal region. pka activation decreased sk2 surface localization

Identifier	Residue	Sequence	Organism
SIGNOR-145040	Ser568	SSRRRRSsSTAPPTS	Homo sapiens
pmid	sentence
16513649	Mutagenesis and mass spectrometry studies identified four pka phosphorylation sites: ser465 (minor site) and three amino acid residues ser568, ser569, and ser570 (major sites) within the carboxyl-terminal region. pka activation decreased sk2 surface localization

Identifier	Residue	Sequence	Organism
SIGNOR-145044	Ser569	SRRRRSSsTAPPTSS	Homo sapiens
pmid	sentence
16513649	Mutagenesis and mass spectrometry studies identified four pka phosphorylation sites: ser465 (minor site) and three amino acid residues ser568, ser569, and ser570 (major sites) within the carboxyl-terminal region. pka activation decreased sk2 surface localization

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276651	Ser465	FLQDVSAsTKSLQEL	Homo sapiens	U-937 Cell
pmid	sentence
25069723	In the presence of cAMP, recombinant PKA directly phosphorylated recombinant PARP1 on serines 465 (in the automodification domain) and 782 and 785 (both in the catalytic domain).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276652	Ser782	YSLLRGGsDDSSKDP	Homo sapiens	U-937 Cell
pmid	sentence
25069723	In the presence of cAMP, recombinant PKA directly phosphorylated recombinant PARP1 on serines 465 (in the automodification domain) and 782 and 785 (both in the catalytic domain).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276653	Ser785	LRGGSDDsSKDPIDV	Homo sapiens	U-937 Cell
pmid	sentence
25069723	In the presence of cAMP, recombinant PKA directly phosphorylated recombinant PARP1 on serines 465 (in the automodification domain) and 782 and 785 (both in the catalytic domain).

Publications:

3

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Sequence	Organism
SIGNOR-250025	Ser466	PVRMRRNsFTPLSSS	in vitro
pmid	sentence
12853467	PFK-2 that was phosphorylated on Ser466, but not Ser483, by PKA did not bind to 14-3-3s‚

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-98196	Ser479	QKEAKRSsADKGVAL	Homo sapiens
pmid	sentence
12578970	We found that protein kinase a phosphorylation of ser-479 in the asic1 c terminus interfered with pick1 binding.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-256110	Ser486	DDEITEAKsGTATPQRS	Rattus norvegicus	INS-1 Cell
pmid	sentence
17023420	These agents also enhanced phosphorylation of alpha-Ser(485/491) by the cAMP-dependent protein kinase. AMPK alpha-Ser(485/491) phosphorylation was necessary but not sufficient for inhibition of AMPK activity in response to forskolin/isobutylmethylxanthine.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-256112	Ser491	SSTPQRSCsAAGLHRPR	Rattus norvegicus	INS-1 Cell
pmid	sentence
17023420	These agents also enhanced phosphorylation of alpha-Ser(485/491) by the cAMP-dependent protein kinase. AMPK alpha-Ser(485/491) phosphorylation was necessary but not sufficient for inhibition of AMPK activity in response to forskolin/isobutylmethylxanthine.

Identifier	Residue	Sequence	Organism
SIGNOR-259865	Ser496	ATPQRSGsVSNYRSC	Homo sapiens
pmid	sentence
27784766	These data indicate a novel regulatory role of PKC to inhibit AMPKα1 in human cells. As PKC activation is associated with insulin resistance and obesity, PKC may underlie the reduced Protein kinase C phosphorylates AMP-activated protein kinase α1 Ser487. \| AMPK activity reported in response to overnutrition in insulin-resistant metabolic and vascular tissues.

Publications:

3

Organism:

Rattus Norvegicus, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250043	Ser490	KSPTRKKsGPFGSRR	in vitro
pmid	sentence
1406653	We have localized two of the sites of phosphorylation in vitro by cAMP-dependent kinase to serine residues 490 and 499. raplGAP undergoes phosphorylation at specific sites in vivo, the effects of phosphorylation on raplGAP have remained elusive.

Identifier	Residue	Sequence	Organism
SIGNOR-250044	Ser499	PFGSRRSsAIGIENI	in vitro
pmid	sentence
1406653	We have localized two of the sites of phosphorylation in vitro by cAMP-dependent kinase to serine residues 490 and 499. raplGAP undergoes phosphorylation at specific sites in vivo, the effects of phosphorylation on raplGAP have remained elusive.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250049	Ser491	VPETKGKsFEEIAAE	Chlorocebus aethiops
pmid	sentence
8626492	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250050	Ser503	AAEFQKKsGSAHRPK	Chlorocebus aethiops	COS Cell
pmid	sentence
8626492	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.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250051	Ser505	EFQKKSGsAHRPKAA	Chlorocebus aethiops	COS Cell
pmid	sentence
8626492	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:

3

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-146287	Ser5	sVSDEEMM	Homo sapiens	HEK-293 Cell
pmid	sentence
16636079	Phosphorylation on ser5 increases the f-actin-binding activity of l-plastin and promotes its targeting to sites of actin assembly in cells. L-plastin phosphorylation require protein kinase a.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-250053	Ser50	HVHAVREsQVELREQ
pmid	sentence
11283605	PKA-phosphorylation of Snapin significantly increases its binding to synaptosomal-associated protein-25 (SNAP-25). Mutation of Snapin serine 50 to aspartic acid (S50D) mimics this effect of PKA phosphorylation

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250056	Ser50	KQINKRAsGQAFELI	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9525956	Using in vitro phosphorylated recombinant protein, four phosphorylation sites were identified in the SCG10 sequence. Ser-50 and Ser-97 were the target sites for protein kinase A. phosphorylation negatively regulates the microtubule-depolymerizing activity of SCG10 and that all four sites participate in this regulation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250057	Ser97	AAEERRKsQEAQVLK	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9525956	Using in vitro phosphorylated recombinant protein, four phosphorylation sites were identified in the SCG10 sequence. Ser-50 and Ser-97 were the target sites for protein kinase A. phosphorylation negatively regulates the microtubule-depolymerizing activity of SCG10 and that all four sites participate in this regulation

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence
SIGNOR-249714	Ser514	SAPIRSAsQAEEEPS
pmid	sentence
10441130	Voltage-dependent L-type calcium (Ca) channels are heteromultimeric proteins that are regulated through phosphorylation by cAMP-dependent protein kinase (PKA) Mutagenesis of a single residue at Ser459 resulted in the loss of one site of phosphorylation by PKA, and mutagenesis of two residues at Ser478/479 resulted in the loss of approximately two sites of PKA-mediated phosphorylation

Identifier	Residue	Sequence
SIGNOR-250340	Ser533	KKSQHRSsSSAPHHN
pmid	sentence
10441130	Voltage-dependent L-type calcium (Ca) channels are heteromultimeric proteins that are regulated through phosphorylation by cAMP-dependent protein kinase (PKA) Mutagenesis of a single residue at Ser459 resulted in the loss of one site of phosphorylation by PKA, and mutagenesis of two residues at Ser478/479 resulted in the loss of approximately two sites of PKA-mediated phosphorylation

Identifier	Residue	Sequence
SIGNOR-250341	Ser534	KSQHRSSsSAPHHNH
pmid	sentence
10441130	Voltage-dependent L-type calcium (Ca) channels are heteromultimeric proteins that are regulated through phosphorylation by cAMP-dependent protein kinase (PKA) Mutagenesis of a single residue at Ser459 resulted in the loss of one site of phosphorylation by PKA, and mutagenesis of two residues at Ser478/479 resulted in the loss of approximately two sites of PKA-mediated phosphorylation

Publications:

3

Identifier	Residue	Sequence	Organism
SIGNOR-159844	Ser518	DTDMKRLsMEIEKEK	Homo sapiens
pmid	sentence
18071304	Merlin localizes to the cell membrane where it links the actin cytoskeleton to membrane proteins.we identify a novel pka phosphorylation site, serine 10, in the n terminus of merlin. s10a reduces the amount of cellular f-actin and merlin s10d stabilizes f-actin filaments.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264410	Ser524	GMRGRKSsGFPKSVK	in vitro
pmid	sentence
15280375	These results indicate that PKA phosphorylates 5-LO on Ser-523, which inhibits the catalytic activity of 5-LO and reduces cellular LT generation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-266302	Ser528	ELQFRRLsQEQVDNF	in vitro
pmid	sentence
27153535	PKA directly phosphorylated the Ser528 residue of MIC60. Phosphorylation of MIC60 Interrupts Parkin Recruitment and Formation of the MICOS Complex

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250006	Ser531	GSRSRTPsLPTPPTR	in vitro
pmid	sentence
9614189	S214 can be rapidly and selectively phosphorylated in vitro by PKA, and this single site strongly affects tau's ability to bind and stabilize microtubules.

Identifier	Residue	Sequence	Organism
SIGNOR-250008	Ser579	NVKSKIGsTENLKHQ	in vitro
pmid	sentence
12435421	Ser214, Ser262, Ser356, and Ser409 of tau441‚ were phosphorylated by PKA. tau in PHF is abnormally hyperphosphorylated and lacks its normal activity to bind to microtubules and to stimulate their assembly

Identifier	Residue	Sequence	Organism
SIGNOR-250007	Ser673	RVQSKIGsLDNITHV	in vitro
pmid	sentence
12435421	Ser214, Ser262, Ser356, and Ser409 of tau441‚ were phosphorylated by PKA. tau in PHF is abnormally hyperphosphorylated and lacks its normal activity to bind to microtubules and to stimulate their assembly

Identifier	Residue	Sequence	Organism
SIGNOR-250009	Ser726	DTSPRHLsNVSSTGS	in vitro
pmid	sentence
12435421	Ser214, Ser262, Ser356, and Ser409 of tau441‚ were phosphorylated by PKA. tau in PHF is abnormally hyperphosphorylated and lacks its normal activity to bind to microtubules and to stimulate their assembly

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-199934	Ser55	SCPKKPVsSYLRFSK	Homo sapiens
pmid	sentence
23201127	Here, we demonstrate that tfam is phosphorylated within its hmg box 1 (hmg1) by camp-dependent protein kinase in mitochondria. Hmg1 phosphorylation impairs the ability of tfam to bind dna and to activate transcription.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-144478	Ser552	QDTQRRTsMGGTQQQ	Homo sapiens
pmid	sentence
16476742	In the present study, we have shown that (i) beta-catenin can be phosphorylated by protein kinase a (pka) in vitro and in intact cells at two novel sites, ser-552 and ser-675;(ii) phosphorylation by pka promotes the transcriptional activity (tcf/lef transactivation) of beta-catenin

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-144482	Ser675	QDYKKRLsVELTSSL	Homo sapiens	HEK-293 Cell
pmid	sentence
16476742	In the present study, we have shown that (i) beta-catenin can be phosphorylated by protein kinase a (pka) in vitro and in intact cells at two novel sites, ser-552 and ser-675;(ii) phosphorylation by pka promotes the transcriptional activity (tcf/lef transactivation) of beta-catenin

Identifier	Residue	Organism	Cell Line
SIGNOR-140902		Homo sapiens	HEK-293 Cell
pmid	sentence
16199882	Although pka did not affect the formation of a complex between glycogen synthase kinase 3beta (gsk-3beta), beta-catenin, and axin, phosphorylation of beta-catenin by pka inhibited ubiquitination of beta-catenin in intact cells and in vitro.

Publications:

3

Organism:

Homo Sapiens

Pathways:

WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Sequence	Organism
SIGNOR-158946	Ser557	SGKFRRGsGSACSLL	Homo sapiens
pmid	sentence
17988215	The stimulatory effect of h89 on mcoln1 function was not observed when ser(557) and ser(559) were mutated to alanine residues, indicating that these two residues are essential for pka-mediated negative regulation of mcoln1.

Identifier	Residue	Sequence	Organism
SIGNOR-158950	Ser559	KFRRGSGsACSLLCC	Homo sapiens
pmid	sentence
17988215	The stimulatory effect of h89 on mcoln1 function was not observed when ser(557) and ser(559) were mutated to alanine residues, indicating that these two residues are essential for pka-mediated negative regulation of mcoln1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250024	Ser56	NLQLPPLsQRQSERA	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12441002	PKA-mediated phosphorylation of Ser-56 in UCR1 of PDE4B4 leads to activation of this long isoform

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-153218	Ser573	KVLLRRKsELPQDVY	Homo sapiens
pmid	sentence
17301223	Protein kinase a activates protein phosphatase 2a by phosphorylation of the b56delta subunit.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-60659	Ser579	NVKSKIGsTENLKHQ	Homo sapiens	Neuron
pmid	sentence
9771888	Tau is phosphorylated by gsk-3 at several sites found in alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by a-kinase.

Identifier	Residue	Sequence	Organism
SIGNOR-171066	Thr548	KKVAVVRtPPKSPSS	Homo sapiens
pmid	sentence
21215781	However, other kinases, such as cdk5, p38 and pka, also phosphorylate tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250062	Ser58	RKSKRRNsEFEIFVD	in vitro
pmid	sentence
9109552	The activation of tryptophan hydroxylase by protein kinase A is mediated by the phosphorylation of serine-58 within the regulatory domain of the enzyme.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263107	Ser58	QERRKSKsGAGKGKL	in vitro
pmid	sentence
10854908	The specificity of antibody G534 was examined using recombinant full-length rat ARPP-21 phosphorylated by PKA. Radiolabeled ARPP-21 from a reaction containing [γ32P]ATP correlated with the detection of phospho-Ser55-ARPP-21 by immunoblotting (Fig. 1A, left and middle panels).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-143373	Ser58	VVGARRSsWRVVSSI	Homo sapiens
pmid	sentence
16376338	Phosphorylation by pka leads to modulation of 14-3-3zeta dimerization and affect its interaction with partner proteins. Substitution of ser58 to ala completely abolished phosphorylation of 14-3-3zeta by pka.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-264422	Ser586	VVVLSRAsRSLSEGH	in vitro
pmid	sentence
19889959	As shown in Fig. 2C, an in vitro kinase assay carried out using PKA and a GST fusion protein containing the COOH-terminal 258 amino acids showed the protein to be efficiently phosphorylated in a time-dependent manner. \|Furthermore, a phosphorylation-negative mutant (S586A) VLCAD shows reduced electron transfer activity and a strong dominant-negative effect on fatty acid beta-oxidation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251617	Ser615	SYKIRFNsISCSDPL	Homo sapiens	Vascular Endothelium
pmid	sentence
24379783	The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251616	Ser633	WRRKRKEsSNTDSAG	Homo sapiens	Vascular Endothelium
pmid	sentence
24379783	The phosphorylation of both S617 and S635 have also been shown to promote increased eNOS-derived NO release (Michell et al., 2002). The phosphorylaiton of S617 can be induced by PKA or Akt activity, and may serve to sensitize eNOS to calmodulin binding and modulate the phosphorylation of other eNOS sites

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250019	Ser622	KKGEKRAsSPFRRVR	in vitro
pmid	sentence
12167624	PKA-dependent Nopp140 phosphorylation is important for its role in agp gene activation. both Ser627 and Ser628 are phosphorylated by PKA.

Identifier	Residue	Sequence	Organism
SIGNOR-250020	Ser623	KGEKRASsPFRRVRE	in vitro
pmid	sentence
12167624	PKA-dependent Nopp140 phosphorylation is important for its role in agp gene activation. both Ser627 and Ser628 are phosphorylated by PKA.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-91186	Ser623	KGEKRASsPFRRVRE	Homo sapiens
pmid	sentence
12167624	Here we demonstrate that protein kinase a (pka)-dependent phosphorylation of nopp140 at ser 627, together with c/ebpbeta, induces agp gene expression synergistically.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-271841	Ser627	KKRVRRPsESDKEDE	in vitro
pmid	sentence
14657015	Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin.

Identifier	Residue	Sequence	Organism
SIGNOR-271843	Ser696	KKRARRGsSSDEEGG	in vitro
pmid	sentence
14657015	Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin.

Identifier	Residue	Sequence	Organism
SIGNOR-271844	Ser698	RARRGSSsDEEGGPK	in vitro
pmid	sentence
14657015	Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin.

Identifier	Residue	Sequence	Organism
SIGNOR-271842	Ser772	LVTPRKKsKSKLEEK	in vitro
pmid	sentence
14657015	Following receptor activation, gravin binding to the receptor increases, a process dependent upon PKA-catalyzed phosphorylation of two canonical PKA sites (Ser696–698 and Ser772) located within the AKAP domain of gravin.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250336	Ser63	GILARRPsYRKILKD	in vitro
pmid	sentence
9016641	PKA catalytic subunit phosphorylates ATF-1 at Ser63 and that phosphorylation is essential for efficient DNA binding by ATF-1.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272162	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-272159	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
SIGNOR-250060	Ser643	KVGMDYRsCILRPGG	in vitro
pmid	sentence
10969067	PKA phosphorylation is suggested to play a regulatory role in EP24.15 enzyme activity. Mutation analysis of each putative PKA site, in vitro phosphorylation, and phosphopeptide mapping indicated serine 644 as the phosphorylation site. The most dramatic change upon PKA phosphorylation was a substrate-specific, 7-fold increase in both K(m) and k(cat) for GnRH.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-256153	Ser65	HSHSPRHsLRHSPGS	Homo sapiens
pmid	sentence
30017192	In this study, we found that PKCα stabilized and activated PIM-1L by phosphorylation at Ser65. The PIM-1L phosphorylation suppressed sotrastaurin-induced apoptosis. These findings suggest that PKCα promotes cell survival and proliferation by upregulating PIM-1L in acute myeloid leukemia.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250349	Ser660	FSAERRNsILTETLH	in vitro
pmid	sentence
1377674	CFTR is phosphorylated directly by PKA and PKC in vivo. phosphorylation by PKA is necessary to allow ATP hydrolysis by CFTR and that ATP hydrolysis is necessary for channel opening. CF-2 was phosphorylated by PKA in vitro on serines 660,700, 737, 813 and most likely on both serines 768 and 795.

Identifier	Residue	Sequence	Organism
SIGNOR-250348	Ser700	FGEKRKNsILNPINS	in vitro
pmid	sentence
1377674	CFTR is phosphorylated directly by PKA and PKC in vivo. phosphorylation by PKA is necessary to allow ATP hydrolysis by CFTR and that ATP hydrolysis is necessary for channel opening. CF-2 was phosphorylated by PKA in vitro on serines 660,700, 737, 813 and most likely on both serines 768 and 795.

Identifier	Residue	Sequence	Organism
SIGNOR-250351	Ser813	DIYSRRLsQETGLEI	in vitro
pmid	sentence
1377674	CFTR is phosphorylated directly by PKA and PKC in vivo. phosphorylation by PKA is necessary to allow ATP hydrolysis by CFTR and that ATP hydrolysis is necessary for channel opening. CF-2 was phosphorylated by PKA in vitro on serines 660,700, 737, 813 and most likely on both serines 768 and 795.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-21312	Ser660	FSAERRNsILTETLH	Homo sapiens
pmid	sentence
1716180	Cftr, the protein associated with cystic fibrosis, is phosphorylated on serine residues in response to camp agonists. Serines 660, 737, 795, and 813 were identified as in vivo targets for phosphorylation by protein kinase a.mutagenesis of all four sites abolished the response.

Identifier	Residue	Sequence	Organism
SIGNOR-21320	Ser795	TASTRKVsLAPQANL	Homo sapiens
pmid	sentence
1716180	Cftr, the protein associated with cystic fibrosis, is phosphorylated on serine residues in response to camp agonists. Serines 660, 737, 795, and 813 were identified as in vivo targets for phosphorylation by protein kinase a.mutagenesis of all four sites abolished the response.

Identifier	Residue	Sequence	Organism
SIGNOR-21324	Ser813	DIYSRRLsQETGLEI	Homo sapiens
pmid	sentence
1716180	Cftr, the protein associated with cystic fibrosis, is phosphorylated on serine residues in response to camp agonists. Serines 660, 737, 795, and 813 were identified as in vivo targets for phosphorylation by protein kinase a.mutagenesis of all four sites abolished the response.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273563	Ser682	EIEKLGRsIVSSPQG	in vitro
pmid	sentence
29230552	PKD2L1 channel activation by PKA phosphorylation. In this study, we observed the activity of PKD2L1 channel increased by the downstream cascades of β2AR and found the clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 that are significant in the channel regulation by phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-273562	Ser685	KLGRSIVsSPQGKSG	in vitro
pmid	sentence
29230552	PKD2L1 channel activation by PKA phosphorylation. In this study, we observed the activity of PKD2L1 channel increased by the downstream cascades of β2AR and found the clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 that are significant in the channel regulation by phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-273561	Ser686	LGRSIVSsPQGKSGP	in vitro
pmid	sentence
29230552	PKD2L1 channel activation by PKA phosphorylation. In this study, we observed the activity of PKD2L1 channel increased by the downstream cascades of β2AR and found the clustered phosphorylation sites, Ser-682, Ser-685, and Ser-686 that are significant in the channel regulation by phosphorylation.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250334	Ser685	VPLVQRGsANGL	in vitro
pmid	sentence
11278469	PKA directly phosphorylates GRK2 on serine 685. This modification increases G subunit binding to GRK2 and thus enhances the ability of the kinase to translocate to the membrane and phosphorylate the receptor.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-167349	Ser696	SSGARRPsLDSMENQ	Homo sapiens	Neuron
pmid	sentence
20682772	Furthermore, we find that activation of protein kinase a (pka) by forskolin reduces the recruitment of shp2 to ret and negatively affects ligand-mediated neurite outgrowth. In agreement with this, mutation of ser(696), a known pka phosphorylation site in ret, enhances shp2 binding to the receptor and eliminates the effect of forskolin on ligand-induced outgrowth.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-147208	Ser697	AVEDRKPsGLNGEAS	Homo sapiens
pmid	sentence
16785995	Pka can phosphorylate ser316 directly cd44 s291a and s316a mutants may disrupt downstream signalling events by displacing endogenous cd44 from plasma membrane microdomains.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-253009	Ser698	PEWPRRAsCTSSTSG	in vitro
pmid	sentence
196939	The results presented in this paper show that the phosphorylation of glycogen synthetase a by cyclic AMP-dependent protein kinase results in the phosphorylation of two distinct serines termed site-l and site-2, which account for 90% of the total phosphorylation

Identifier	Residue	Sequence	Organism
SIGNOR-253008	Ser8	MPLNRTLsMSSLPGL	in vitro
pmid	sentence
6263629	A reinvestigation of the phosphorylation of Rabbit Skeletal-muscle glycogen synthase by cyclic AMP dependent Protein Kinase: identification of the third site of phosphorylation at Serine-7

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249993	Ser7	sSAEGAAK	Homo sapiens
pmid	sentence
11438671	PKA preferentially phosphorylates serine 6 in human HMGN1. specific phosphorylation of the NBD of HMGN proteins serves to prevent the interaction of these proteins with their chromatin targets during mitosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272155	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	Organism
SIGNOR-250332	Ser713	KKKFRTPsFLKKSKK	in vitro
pmid	sentence
8810272	Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of - and -adducin, respectively, were identified as the major phosphorylation sites common for PKA and PKC. Phosphorylation by PKA, but not PKC, reduced the affinity of adducin for spectrin-F-actin complexes as well as the activity of adducin in promoting binding of spectrin to F-actin.

Identifier	Residue	Sequence	Organism
SIGNOR-250333	Ser726	KKKEKVEs	in vitro
pmid	sentence
8810272	Ser-726 and Ser-713 in the C-terminal MARCKS-related domains of - and -adducin, respectively, were identified as the major phosphorylation sites common for PKA and PKC. Phosphorylation by PKA, but not PKC, reduced the affinity of adducin for spectrin-F-actin complexes as well as the activity of adducin in promoting binding of spectrin to F-actin.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250315	Ser715	FMSSRRQsVLVKSNE	Homo sapiens	HEK-293 Cell
pmid	sentence
8094892	GluR6 glutamate receptor, transiently expressed in mammalian cells, is directly phosphorylated by PKA, and that intracellularly applied PKA increases the amplitude of the glutamate response. Site-specific mutagenesis of the serine residue (Ser 684) representing a PKA consensus site completely eliminates PKA-mediated phosphorylation of this site as well as the potentiation of the glutamate response.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-200456	Ser73	LTFLRIRsKKNEIMV	Homo sapiens
pmid	sentence
23333499	Our results show that km23-1 is required for camp-responsive element (cre) transcriptional activation by tgf_, with s73-km23-1 being required for the cre-dependent tgf_ stimulation of fibronectin (fn) transcription.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250352	Ser730	MKMRKKIsNAQLQTE	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
10898738	Elimination of the S730 but not the T325 PKA phosphorylation site of VACM-1 resulted in a complete inhibition of the VACM-1 activity, thus suggesting a direct effect of PKA on the VACM-1 receptor.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-21316	Ser737	EPLERRLsLVPDSEQ	Homo sapiens
pmid	sentence
19095655	AMPK phosphorylates CFTR in vitro at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.

Identifier	Residue	Sequence	Organism
SIGNOR-18141	Ser768	EPLERRLsLVPDSEQ	Homo sapiens
pmid	sentence
19095655	AMPK phosphorylates CFTR in vitro at two essential serines (Ser737and Ser768) in the R domain, formerly identified as "inhibitory" PKA sites.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-56395	Ser76	RVCAKRVsTQEDEEQ	Homo sapiens
pmid	sentence
9529381	This binding is regulated in vitro by phosphorylation of a single serine residue (ser76) in the immediately adjacent amino-terminal domain mp1. M-protein phosphorylation by camp-dependent kinase a inhibits binding to myosin lmm.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-249988	Ser8	MPLNRTLsMSSLPGL	in vitro
pmid	sentence
2117608	Phosphorylation of rabbit muscle glycogen synthase by cyclic AMP-dependent protein kinase has been shown to enhance subsequent phosphorylation by casein kinase I . phosphorylation at Ser7 is required for modification of Ser10 by casein kinase I.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-263117	Ser83	EEGTFRSsIRRLSTR	in vitro
pmid	sentence
15621037	PKA-dependent, alpha 1-specific NKA activation may be mediated through phosphorylation of the accessory protein PLM, rather than direct alpha1 subunit phosphorylation. we propose that phosphorylation of the small accessory protein phospholemman (PLM) by PKA at serine 68 is responsible for the observed isoform-specific activation of NKA.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249983	Ser83	QHDDGRVsYPLCFIF	in vitro
pmid	sentence
9030586	Protein kinase A (PKA)-phosphorylated GMF is a potent inhibitor of extracellular signal-regulated kinase (ERK) and enhancer of p38; both are subfamilies of mitogen-activated protein (MAP) kinase, suggesting GMF as a bifunctional regulator of the MAP kinase cascades. PKA is capable of phosphorylating threonine 26 and serine 82.

Identifier	Residue	Sequence	Organism
SIGNOR-249984	Thr27	KFRFRKEtNNAAIIM	in vitro
pmid	sentence
9030586	Protein kinase A (PKA)-phosphorylated GMF is a potent inhibitor of extracellular signal-regulated kinase (ERK) and enhancer of p38; both are subfamilies of mitogen-activated protein (MAP) kinase, suggesting GMF as a bifunctional regulator of the MAP kinase cascades. PKA is capable of phosphorylating threonine 26 and serine 82.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-171184	Ser83	EEGTFRSsIRRLSTR	Homo sapiens
pmid	sentence
21220422	We conclude that phosphorylation of plm increases its oligomerization into tetramers, decreases its binding to nka, and alters the structures of both the tetramer and nka regulatory complex.

Identifier	Residue	Sequence	Organism
SIGNOR-171188	Ser88	RSSIRRLsTRRR	Homo sapiens
pmid	sentence
21220422	We conclude that phosphorylation of plm increases its oligomerization into tetramers, decreases its binding to nka, and alters the structures of both the tetramer and nka regulatory complex.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249202	Ser853	IAEPMRRsVSEAALA	Mus musculus	NIH-3T3 Cell
pmid	sentence
11581251	HSL activity is known to be regulated by phosphorylation (3). PKA increases HSL activity via phosphorylation at Ser563, Ser659, and Ser660 (14,15), although phosphorylation at Ser565 by glycogen synthase kinase, AMP-dependent protein kinase, or Ca2+/calmodulin-dependent protein kinase II has been reported to prevent activation of the enzyme

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249203	Ser950	EGFHPRRsSQGATQM	Mus musculus	NIH-3T3 Cell
pmid	sentence
11581251	HSL activity is known to be regulated by phosphorylation (3). PKA increases HSL activity via phosphorylation at Ser563, Ser659, and Ser660 (14,15), although phosphorylation at Ser565 by glycogen synthase kinase, AMP-dependent protein kinase, or Ca2+/calmodulin-dependent protein kinase II has been reported to prevent activation of the enzyme

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249204	Ser951	GFHPRRSsQGATQMP	Mus musculus	NIH-3T3 Cell
pmid	sentence
11581251	HSL activity is known to be regulated by phosphorylation (3). PKA increases HSL activity via phosphorylation at Ser563, Ser659, and Ser660 (14,15), although phosphorylation at Ser565 by glycogen synthase kinase, AMP-dependent protein kinase, or Ca2+/calmodulin-dependent protein kinase II has been reported to prevent activation of the enzyme

Publications:

3

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-58259	Ser855	EPMRRSVsEAALAQP	Homo sapiens
pmid	sentence
9636039	Phosphorylation of bovine hormone-sensitive lipase by the amp-activated protein kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-196961	Ser857	PPYNRAVsLDSPVSV	Homo sapiens
pmid	sentence
22505454	Herein, we report the successful identification of six functional in vivo src-3 phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-129349	Ser857	PPYNRAVsLDSPVSV	Homo sapiens
pmid	sentence
15383283	Herein, we report the successful identification of six functional in vivo src-3 phosphorylation sites.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97550	Ser862	IRNKARLsITGSVGE	Homo sapiens
pmid	sentence
12536214	We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249987	Ser863	TSTLPRNsGAGASSG	Homo sapiens
pmid	sentence
8663994	Phosphorylation of Ser-845 on GluR1 by PKA potentiates its response to glutamate.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-116144	Ser87	SNSSPRHsEAATAQR	Homo sapiens
pmid	sentence
11903055	Protein kinase a enhances, whereas glycogen synthase kinase-3 beta inhibits, the activity of the exon 2-encoded transactivator domain of heterogeneous nuclear ribonucleoprotein d in a hierarchical fashion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249992	Ser872	SHMIHNRsKINLQDL	Rattus norvegicus
pmid	sentence
2369897	The intact, 100 kd microsomal enzyme and the 53 kd catalytic fragment of rat HMG-CoA reductase are both phosphorylated and inactivated by the AMP-activated protein kinase. this site is highly phosphorylated in intact liver under these conditions (Ser872 in the human enzyme).

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-198288	Ser879	LIDRNQKsDKKPDRE	Homo sapiens
pmid	sentence
22798526	We showed that pkc_ phosphorylation of p120 at serine (s)879 in response to thrombin or lipopolysaccharide challenge reduced p120 binding affinity for ve-cadherin and mediated aj disassembly secondary to ve-cadherin internalization

Publications:

1

Organism:

Homo Sapiens

Tissue:

Lung

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-265980	Ser88	GKQGARMsLLGKPLS	Homo sapiens	Respiratory Smooth Muscle
pmid	sentence
30061510	We conclude that phosphorylation of S53 on the amino terminus of Kv7.5 is essential for PKA-dependent enhancement of channel activity in response to βAR activation in vascular and airway smooth muscle cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-272146	Ser883	EIAGKKIsMKETKEL	Homo sapiens	Hep-G2 Cell
pmid	sentence
16467138	Within 20 min after addition of 8-Br-cAMP, BIG1 accumulated in nuclei, and this effect was blocked by protein kinase A (PKA) inhibitors H-89 and PKI, suggesting a dependence on PKA-catalyzed phosphorylation. \|Mutant BIG1 (S883A) in which Ala replaced Ser-883, a putative PKA phosphorylation site, did not move to the nucleus with cAMP addition, whereas replacement with Asp (S883D) resulted in nuclear accumulation of BIG1 without or with cAMP exposure, consistent with the mechanistic importance of a negative charge at that site

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263150	Ser893	EHIQRRLsLQLPILH	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
11976702	Here we show that the functional coupling of GABA(B)R1/GABA(B)R2 receptors to inwardly rectifying K(+) channels rapidly desensitizes. This effect is alleviated after direct phosphorylation of a single serine residue (Ser892) in the cytoplasmic tail of GABA(B)R2 by cyclic AMP (cAMP)-dependent protein kinase (PKA).

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188577	Ser9	SGRPRTTsFAESCKP	Homo sapiens	T-lymphocyte
pmid	sentence
19836308	Gsk3 is different from most kinases in that it is constitutively partially active and the most common regulatory mechanism is inhibition by phosphorylation of ser21 in gsk3alpha or ser9 in gsk3beta. This inhibitory phosphorylation can be mediated by several kinases, such as akt/protein kinase b (pkb), protein kinase c (pkc) and protein kinase a (pka).

Publications:

1

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog, WNT/FLT3

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273792	Ser9	SFRAARLsMRNRRND	Homo sapiens	HEK-293 Cell
pmid	sentence
20110357	Using specific pharmacological and molecular tools combined with patch-clamp current recordings, we found that in heterologously expressed HEK-293 (human embryonic kidney) cells, TRPM8 channel is inhibited by the G(i) protein/adenylate cyclase (AC)/cAMP/protein kinase A (PKA) signaling cascade. We further identified the TRPM8 S9 and T17 as two key PKA phosphorylation sites regulating TRPM8 channel activity. the intracellular serine/threonine protein phosphatase 2A (PP2A) dephosphorylates TRPM8 Ser-9 and Thr-17 inhibiting the channel activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273791	Thr17	MRNRRNDtLDSTRTL	Homo sapiens	HEK-293 Cell
pmid	sentence
20110357	Using specific pharmacological and molecular tools combined with patch-clamp current recordings, we found that in heterologously expressed HEK-293 (human embryonic kidney) cells, TRPM8 channel is inhibited by the G(i) protein/adenylate cyclase (AC)/cAMP/protein kinase A (PKA) signaling cascade. We further identified the TRPM8 S9 and T17 as two key PKA phosphorylation sites regulating TRPM8 channel activity. the intracellular serine/threonine protein phosphatase 2A (PP2A) dephosphorylates TRPM8 Ser-9 and Thr-17 inhibiting the channel activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250058	Ser9	NYLRRRLsDSNFMAN	in vitro
pmid	sentence
10571231	Synapsin phosphorylation in the A domain, at the only phosphorylation site shared by all synapsins, dissociates synapsins from synaptic vesicles.This site is located in the N-terminal A domain and is a substrate for both PKA and CaM Kinase I

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-73202	Ser927	KEKYRRMsLASAGFP	Homo sapiens	Neuron
pmid	sentence
10601308	Phosphorylation of serine 916 of ras-grf1 contributes to the activation of exchange factor activity by muscarinic receptors.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-145109	Ser93	KDGTKRKsLSDSESD	Homo sapiens
pmid	sentence
16531993	We demonstrate that p-ser 83-hp1gamma has an exclusively euchromatic localization, interacts with ku70 (a regulatory protein involved in multiple nuclear procesess), has impaired silencing activity and serves as a marker for transcription elongation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-260327	Ser937	ETSFRKLsFTESLTS
pmid	sentence
19531803	Ser940 of p105 was phosphorylated by PKA to a similar extent, whereas no phosphorylation of the same sequence occurred when Ser940 was substituted by Ala\|Mechanistically, phosphorylation of p105 at Ser940 by PKA appeared to attenuate the extent of IKK-dependent phosphorylation of p105 at Ser935, which could in turn influence the rate of activation of NF-kappaB

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250035	Ser94	SERGVRLsLPRASSL	Homo sapiens	HEK-293 Cell
pmid	sentence
12417592	Spinophilin is phosphorylated in vitro by protein kinase A (PKA). two major sites of phosphorylation, Ser-94 and Ser-177, that are located within the actin-binding domain of spinophilin. Phosphorylation of spinophilin by PKA modulated the association between spinophilin and the actin cytoskeleton. phosphorylation of spinophilin reduced the stoichiometry of the spinophilin-actin interaction. In contrast, the ability of spinophilin to bind to PP1 remained unchanged.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249990	Ser98	RLGRRKGsGPKKERR	Rattus norvegicus	Rcho-1 Cell
pmid	sentence
14636580	In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. We determined that modification of HAND1 at residues 107 and 109 affects dimerization affinities with E-proteins, thus changing the bHLH dimer equilibrium within the cell. These modifications also affect HAND1 function.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-250075	Ser99	KNKGKGFsVVADTPE	in vitro
pmid	sentence
12432067	Lasp-1 binds to non-muscle filamentous (F) actin in vitro in a phosphorylation-dependent manner. Phosphorylation of recombinant lasp-1 with recombinant PKA increased the Kd and decreased the Bmax for lasp-1 binding to F-actin. PKA-dependent phosphorylation sites in rabbit lasp-1 to S99 and S146

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-256115	Thr108	SPRAWRRPtIESHHVAI	Rattus norvegicus
pmid	sentence
10187789	In vitro, CaMKK is phosphorylated by PKA and this is associated with inhibition of enzyme activity. The major site of phosphorylation is threonine 108, although additional sites are phosphorylated with lower efficiency.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-263116	Thr11	TTSTRRVtFEADENE	in vitro
pmid	sentence
17242405	Identification of ChChd3 as a novel substrate of the cAMP-dependent protein kinase (PKA) using an analog-sensitive catalytic subunit. we used the recombinant GST-ChChd3 for an in vitro kinase assays to determine whether in vitro phosphorylation by PKA was direct. Fig. 6 demonstrates that PKA directly phosphorylates recombinant Chchd3 with a stoichiometry of 0.3 mol of phosphate incorporated per mol of ChChd3. Although three potential PKA phosphorylation sites exist in ChChd3, Thr10 represents the most likely site to be phosphorylated.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-174410	Thr131	LERAKRAtIMSLEDF	Homo sapiens
pmid	sentence
21677187	Here, we demonstrate that disc1 and pde4 modulate nde1 phosphorylation by camp-dependent protein kinase a (pka) and identify a novel pka substrate site on nde1 at threonine-131 (t131).Since phosphorylated t131 is detectable at multiple subcellular locations (centrosome, nucleus, postsynaptic density, proximal axon), there is potential for disc1/pde4 to influence several important brain processes that critically depend on the nde1/ndel1/lis1 comple

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250052	Thr138	GGFIRRVtNDARENE	Rattus norvegicus	PC-12 Cell
pmid	sentence
12459461	Thr138 as the exclusive site of SNAP-25 phosphorylation by protein kinase A in vivo. PMA or forskolin treatment alone resulted in dramatic phosphorylation of SNAP-25 Ser187 and/or Thr138 without appreciable neurotransmitter release.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-166559	Thr15	SQHLTGLtDEKVKAY	Homo sapiens	HEK-293 Cell
pmid	sentence
20610737	When coexpressed with the catalytic subunit of pka in transfected hek293 cells, wild-type (wt) pde10a2 (pde10a2wt) was phosphorylated at thr-16 these data confirm the previously reported findings that pka phosphorylation of pde10a2 on thr-16 results in a cytosolic localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-188177	Thr159	DNKLRRYtTFSKRKT	Mus musculus
pmid	sentence
12809504	Myotonic dystrophy protein kinase (DMPK), a muscle- and neuron-restricted kinase, enhanced SRF-mediated promoter activity of the skeletal and cardiac alpha-actin genes in C2C12 myoblasts as well as in nonmyogenic cells. \| Threonine 159 in the MADS box alphaI coil was a specific phosphorylation target in vitro as well as in vivo of both DMPK and protein kinase C-alpha.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-74284	Thr18	ALNKRRAtLPHPGGS	Homo sapiens	HEK-293 Cell
pmid	sentence
10644707	Further experiments demonstrated that mst3b, but not mst3, was effectively phosphorylated by activation of cyclic amp-dependent protein kinase (pka) in both in vivo and in vitro assays. The mutation of thr-18 into ala in mst3b (t18a), a putative pka phosphorylation site that is absent in mst3, abolished its phosphorylation by pka.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain, Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-137291	Thr192	PPREKKYtATKVVYS	Homo sapiens
pmid	sentence
15905176	Our results suggest that claudin-3 phosphorylation by pka, a kinase frequently activated in ovarian cancer, may provide a mechanism for the disruption of tjs in this cancer.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249985	Thr203	ILLARRPtKGIHEYD	Chlorocebus aethiops
pmid	sentence
12399457	PKA directly phosphorylates Galpha(13). Galpha(13)-T203A mutant (in COS-7 cells) could not be phosphorylated by PKA. PKA blocks Rho activation by phosphorylation of Galpha(13) Thr(203).

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-277455	Thr214	LVLRRRQtYLCYEVE	in vitro
pmid	sentence
31165764	Here we show that protein kinase A (PKA) physically binds to A3B and phosphorylates Thr214.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250054	Thr2159	NGATEQRtSSKESSP	in vitro
pmid	sentence
17088250	Short C-terminal splice variant of betaII-spectrin (betaIISigma2) is a substrate for phosphorylation. protein kinase A phosphorylates Thr-2159. Mammalian alphaII- and betaII-spectrin subunits form dimers that associate head to head with high affinity to form tetramers In vitro, protein kinase A phosphorylation of an active fragment of betaIISigma2 greatly reduced its interaction with alphaII-spectrin at the tetramerization site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250337	Thr288	APSSRRTtLCGTLDY	in vitro
pmid	sentence
11039908	Aurora2 is regulated by phosphorylation. phosphorylation occurs on a conserved residue, Threonine 288, within the activation loop of the catalytic domain of the kinase and results in a significant increase in the enzymatic activity. Threonine 288 resides within a consensus motif for the cAMP dependent kinase and can be phosphorylated by PKA in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-181526	Thr32	PILSRRNtVWLCYEV	Homo sapiens
pmid	sentence
18836454	Here we show that pka binds and specifically phosphorylates a3g at thr32 in vitro and in vivo. This phosphorylation event reduces the binding of a3g to vif and its subsequent ubiquitination and degradation, and thus promotes a3g antiviral activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-250342	Thr321	NTANRRTtPV	Chlorocebus aethiops
pmid	sentence
11805122	phosphorylation of stargazin at T321 by PKA inhibits its interaction with PSD-95.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence
SIGNOR-250031	Thr34	MIRRRRPtPAMLFRL
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.‚

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-275972	Thr369	DLINKKItPPFNPNV	in vitro
pmid	sentence
11096081	In this publication, we demonstrate that cAMP can activate Sgk and that this effect is mediated by PKA, which directly phosphorylates Thr369 in Sgk.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-116248	Thr370	GNWRRGStAGGCRNY	Homo sapiens
pmid	sentence
11909964	Activation of m-calpain (calpain ii) by epidermal growth factor is limited by protein kinase a phosphorylation of m-calpain.These Data point to a novel mechanism of negative control of calpain activation, direct phosphorylation by pka.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-259835	Thr41	SFENLMAtKYGPVVY
pmid	sentence
20974683	Phosphorylation of RGS13 by the cyclic AMP-dependent protein kinase inhibits RGS13 degradation.we show that PKA activation also leads to increased steady-state RGS13 expression through RGS13 phosphorylation, which inhibits RGS13 protein degradation. RGS13 phosphorylation was diminished by mutation of an N-terminal Thr residue (T41) identified as a phosphorylation site by mass spectrometry.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-176973	Thr443	RRQHRRGtKGGVSYR	Homo sapiens
pmid	sentence
22037869	Here, we report that thr443 phosphorylation at the intracellular domain of ca ix by protein kinase a (pka) is critical for its activation in hypoxic cells, with the fullest activity of ca ix also requiring dephosphorylation of ser448.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-236899	Thr508	MYSERRItVLYSLVQ	Mus musculus
pmid	sentence
26255772	These data suggest that PKA phosphorylation at T485 inhibits UBE3A ubiquitin ligase activity in cells.

Publications:

1

Organism:

Mus Musculus

Tissue:

Brain

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273781	Thr582	LEALQKTtPIRSQAD	Homo sapiens	HEK-293 Cell
pmid	sentence
32401166	Mechanistically, GPER1 activates PRKACA (protein kinase cAMP-activated catalytic subunit alpha), which in turn phosphorylates MORC2 at threonine 582 (T582). Phosphorylated MORC2 decreases its interaction with HSPA8 (heat shock protein family A [Hsp70] member 8) and LAMP2A (lysosomal associated membrane protein 2A), two core components of the chaperone-mediated autophagy (CMA) machinery, thus protecting MORC2 from lysosomal degradation by CMA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181191	Thr686	QQKIRKYtMRRLLQE	Homo sapiens
pmid	sentence
18799465	Pka directly phosphorylated erbb2 on thr-686, a highly conserved intracellular regulatory site that was required for the pka-mediated synergistic enhancement of neuregulin-induced erbb2-erbb3 activation and proliferation in scs.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-176614	Thr90	NKQDRTLtIVDTGIG	Homo sapiens
pmid	sentence
21919888	Thr90 phosphorylation of hsp90_ by protein kinase a regulates its chaperone machinery

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277410	Tyr70	HKETGNHyAMKILDK	in vitro
pmid	sentence
30274258	We found that the Src family kinase Fyn phosphorylates the catalytic subunit of PKA (PKA-C) at Y69, thereby increasing PKA kinase activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-253539
pmid	sentence
16293631	We report that activation of PKA retains Gli1 in the cytoplasm. Conversely, inhibition of PKA activity promotes nuclear accumulation of Gli1.We provide direct evidence to support that the cAMP/PKA signaling axis regulates Gli1 protein localization primarily through a site at Thr374. .These data suggest that Thr374 is an important PKA site responsible for PKA phosphorylation and for the transcriptional activity of Gli1.

Publications:

1

Pathways:

Sonic Hedgehog

Identifier	Residue	Organism
SIGNOR-75362		Homo sapiens
pmid	sentence
10693759	In vertebrates,pka-mediated phosphorylation of gli2 and gli3 initiates a phosphorylation cascade that leads to processing into repressors of transcription or frank degradation

Identifier	Residue	Organism
SIGNOR-154276		Homo sapiens
pmid	sentence
17419683	In vertebrates,pka-mediated phosphorylation of gli2 and gli3 initiates a phosphorylation cascade that leads to processing into repressors of transcription or frank degradation

Publications:

2

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Organism
SIGNOR-217364		Homo sapiens
pmid	sentence
9660950	The transcriptional activity of nf-kappa b is stimulated upon phosphorylation of its p65 subunit on serine 276 by protein kinase a (pka).

Identifier	Residue	Organism
SIGNOR-217391		Homo sapiens
pmid	sentence
17959673	In this study, we demonstrate that the phosphorylation of p50 and p65 by the catalytic subunit of protein kinase a (pkac) is essential for nf-kappab dna binding and transactivation activity. treatment with h89 and knockdown of pkac in cells led to the inhibition of phosphorylation at p50 ser(337) and p65 ser(276) and loss of dna binding by nf-kappab.

Publications:

2

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network

Identifier	Residue	Organism
SIGNOR-267410		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

Identifier	Residue	Organism
SIGNOR-176575		Homo sapiens
pmid	sentence
21902831	Wnt1 and wnt7a stimulation of precursor cells activates protein kinase a (pka), which, through the phosphorylation of creb, induces the expression of the myogenic transcription factors myf5, myod and pax3, resulting in the myogenic commitment of embryonic precursors.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

WNT Signaling, WNT Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-148478		Homo sapiens
pmid	sentence
16885213	In the absence of hh ligands, cubitus interruptus (in drosophila) and gli2 and gli3 (in vertebrates) are phosphorylated by protein kinase a and glycogen synthase kinase-3beta and are proteolytically processed in vertebrates, pka-mediated phosphorylation of gli2 and gli3 initiates a phosphorylation cascade that leads to processing into repressors of transcription or frank degradation

Identifier	Residue	Organism
SIGNOR-154273		Homo sapiens
pmid	sentence
17419683	In the absence of hh ligands, cubitus interruptus (in drosophila) and gli2 and gli3 (in vertebrates) are phosphorylated by protein kinase a and glycogen synthase kinase-3beta and are proteolytically processed in vertebrates, pka-mediated phosphorylation of gli2 and gli3 initiates a phosphorylation cascade that leads to processing into repressors of transcription or frank degradation

Publications:

2

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275730
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-262528		Homo sapiens
pmid	sentence
27065076	Adenylate cyclases (AC) produce cAMP from adenosin-tri-phosphate (ATP). High levels of cytosolic cAMP lead to activation of protein kinase A (PKA)

Publications:

1

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog, WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism
SIGNOR-152594		Homo sapiens
pmid	sentence
17251915	As pka suppresses the activity of gli, smo might use the stimulation of pi3k by galfai and gbetagamma subu- nits to block pka in cells that have high levels of camp.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258753		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

Identifier	Residue	Organism	Cell Line
SIGNOR-145131		Homo sapiens	Neuron
pmid	sentence
16537363	Protein kinase a (pka) and glycogen synthase kinase 3beta sequentially phosphorylate gli2 at multiple sites, identified by mutagenesis, thus resulting in a reduction of its transcriptional activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-152615		Homo sapiens
pmid	sentence
17251915	As pka suppresses the activity of gli, smo might use the stimulation of pi3k by galfai and gbetagamma subu- nits to block pka in cells that have high levels of camp.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-236991		Mus musculus
pmid	sentence
23644383	Here, we show that cyclic amp (camp)-dependent protein kinase (pka) phosphorylates lats and thereby enhances its activity sufficiently to phosphorylate yap on ser381.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-256111		Rattus norvegicus
pmid	sentence
17023420	These agents also enhanced phosphorylation of alpha-Ser(485/491) by the cAMP-dependent protein kinase. AMPK alpha-Ser(485/491) phosphorylation was necessary but not sufficient for inhibition of AMPK activity in response to forskolin/isobutylmethylxanthine.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism	Cell Line
SIGNOR-269863		Mus musculus	NIH-3T3 Cell
pmid	sentence
23644383	Here, we show that cyclic amp (camp)-dependent protein kinase (pka) phosphorylates lats and thereby enhances its activity sufficiently to phosphorylate yap on ser381.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-182573		Homo sapiens
pmid	sentence
19056373	These results indicate that phosphorylation of Gli2 by PKA induces Gli2 processing and destabilization

Publications:

1

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog

Identifier	Residue	Organism
SIGNOR-261292		Rattus norvegicus
pmid	sentence
10939335	In this report, we demonstrate that glutamate receptors and PKA are recruited into a macromolecular signaling complex through direct interaction between the MAGUK proteins, PSD-95 and SAP97, and AKAP79/150

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism	Cell Line
SIGNOR-259413		Homo sapiens	HEK-293 Cell
pmid	sentence
30017192	In this study, we found that PKCÎ± stabilized and activated PIM-1L by phosphorylation at Ser65. The PIM-1L phosphorylation suppressed sotrastaurin-induced apoptosis. These findings suggest that PKCÎ± promotes cell survival and proliferation by upregulating PIM-1L in acute myeloid leukemia.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258752		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

Identifier	Residue	Organism
SIGNOR-250021		in vitro
pmid	sentence
1375933	NOS is stoichiometrically phosphorylated by PKA, PKC, and CaMK, with each enzyme predominantly phosphorylating a distinct serine. CPT-CAMP has no effect on NOS activity

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-261087		Rattus norvegicus
pmid	sentence
2156866	Kinetic analysis indicated that H-89 inhibits protein kinase A, in competitive fashion against ATP.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Organism
SIGNOR-258754		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

Identifier	Residue	Organism
SIGNOR-270232		Homo sapiens
pmid	sentence
12536214	We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-176572		Homo sapiens
pmid	sentence
21902831	Wnt1 and wnt7a stimulation of precursor cells activates protein kinase a (pka), which, through the phosphorylation of creb, induces the expression of the myogenic transcription factors myf5, myod and pax3, resulting in the myogenic commitment of embryonic precursors.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Skeletal Muscle

Pathways:

WNT Signaling, WNT Signaling and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-181979		Rattus norvegicus	Osteoblast
pmid	sentence
18981475	These results suggest that camppka activation is involved in activation of lrp6(...) our results demonstrate that lrp6 can be directly phosphorylated by pka catalytic subunit.

Publications:

1

Organism:

Rattus Norvegicus

Pathways:

WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-236994		Mus musculus	NIH-3T3 Cell
pmid	sentence
23644383	Here, we show that cyclic amp (camp)-dependent protein kinase (pka) phosphorylates lats and thereby enhances its activity sufficiently to phosphorylate yap on ser381.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271835
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	Organism	Cell Line
SIGNOR-198492		Homo sapiens	HEK-293 Cell
pmid	sentence
22863277	The cAMP signaling cascade can activate protein kinase a (PKA)

Identifier	Residue	Organism
SIGNOR-141786		Homo sapiens
pmid	sentence
16293724	Pge2 receptors are coupled to the G protein Gs, which causes accumulation of cyclic adenosine monophosphate (cAMP) and activates protein kinase a (PKA), we confirmed that PGE2 treatment or transfection of cells with the active catalytic subunit of PKA also stimulated the activity of a cAMP-responsive-element driven reporter gene (CRE-luc).

Publications:

2

Organism:

Homo Sapiens

Pathways:

Sonic Hedgehog, WNT Signaling, WNT Signaling and Myogenesis

Identifier	Residue	Organism	Cell Line
SIGNOR-252490		Homo sapiens	Neuron
pmid	sentence
16537363	Indicating that akt positively regulates shh signaling by controlling pka-mediated gli inactivation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-267784		YES	Homo sapiens
pmid	sentence
12536214	We found that pka phosphorylation of the ampa receptor subunits glur4 and glur1 directly controlled the synaptic incorporation of ampa receptors in organotypic slices from rat hippocampus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-252401		Homo sapiens
pmid	sentence
8019002	Phosphorylation of neurofilament-L protein (NF-L) by the catalytic subunit of cAMP-dependent protein kinase (A-kinase) inhibits the reassembly of NF-L and disassembles filamentous NF-L.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-145113		Homo sapiens	Neuron
pmid	sentence
16537363	Indicating that akt positively regulates shh signaling by controlling pka-mediated gli inactivation.

Publications:

1

Organism:

Homo Sapiens

Pathways:

COVID-19 Causal Network, WNT/FLT3

Identifier	Residue	Organism
SIGNOR-144557		Homo sapiens
pmid	sentence
16481469	Mutation of either the three pka sites or pka-primed cki sites prevents phosphorylation of ci by cki in vitro and blocks ci cleavage in embryos

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-253019		Mus musculus	3T3-L1 Cell
pmid	sentence
20638365	Here we showed that cAMP-induced activation of protein kinase A (PKA) and Akt is essential for the transcriptional activation of PPAR-gamma

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Organism
SIGNOR-265344		Homo sapiens
pmid	sentence
10464286	Identification of a novel phosphorylation site on histone h3 coupled with mitotic chromosome condensation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-249995		in vitro
pmid	sentence
9374536	Two isoforms of the inositol 1,4,5-trisphosphate 3-kinase have been identified, the A form and the B form. phosphorylation of isoform A by the cyclic AMP-dependent protein kinase increased activity 1.5-fold, whereas phosphorylation of isoform B decreased activity by 45%. major phosphorylation sites in the protein are Ser119 for PKA. Ser119 in the A isoform is conserved in the B isoform as Ser328

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism	Cell Line
SIGNOR-260302		Homo sapiens	HEK-293 Cell
pmid	sentence
19531803	To determine whether AKAP95 and p105 were present in a complex in mammalian cells, FLAG-tagged AKAP95 wascoexpressed with Myc-tagged p105 in human embryonic kidney (HEK) 293 cells. Immunoprecipitation of either protein pulled down a complex containing AKAP95, p105, and PKA-Ca (Fig. 6D).\|The identification of a PKA phosphorylation site in the C-terminal region of p105 suggests that p105 is a candidate substrate for AKAP95-targeted PKA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-258751		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

Identifier	Residue	Organism
SIGNOR-42515		Homo sapiens
pmid	sentence
8663227	Phosphorylation and activation of a camp-specific phosphodiesterase by the camp-dependent protein kinase.

Publications:

1

Organism:

Homo Sapiens

Name	PRKACA View Modifications
Full Name	cAMP-dependent protein kinase catalytic subunit alpha
Synonyms	PKA C-alpha \| PKACA
Primary ID	P17612
Links	- -
Type	protein
Relations	428
Pathways	COVID-19 Causal Network, FAP: In vitro induction of adipogenesis, FAP: IBMX/rosiglitazone, FAP: GCR-cAMP crosstalk, Sonic Hedgehog, Myofiber: hypertrophy_cAMP, Pericyte: In vitro induction of adipogenesis, SARS-CoV ATTACHMENT AND ENTRY, WNT Signaling, WNT/FLT3, WNT Signaling and Myogenesis
Inhibitors	N-[2-(4-bromocinnamylamino)ethyl]isoquinoline-5-sulfonamide
Function	Phosphorylates a large number of substrates in the cytoplasm and the nucleus (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984). Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA, SOX9 and VASP (PubMed:15642694, PubMed:15905176, PubMed:16387847, PubMed:17333334, PubMed:17565987, PubMed:17693412, PubMed:18836454, PubMed:19949837, PubMed:20356841, PubMed:21085490, PubMed:21514275, PubMed:21812984). Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis (PubMed:21423175). RORA is activated by phosphorylation (PubMed:21514275). Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts (PubMed:19949837). Involved in chondrogenesis by mediating phosphorylation of SOX9 (By similarity). Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP (PubMed:15642694, PubMed:20356841). Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated (PubMed:17333334). RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+) (PubMed:17693412). PSMC5/RPT6 activation by phosphorylation stimulates proteasome (PubMed:17565987). Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation (PubMed:15905176). NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding (PubMed:15642694). Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation (By similarity). May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates APOBEC3G and AICDA (PubMed:16387847, PubMed:18836454). Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock (PubMed:21085490).

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