Relation Results

Identifier	Residue	Sequence	Organism
SIGNOR-248877	Ser10	TRSVSSSsYRRMFGG	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248878	Ser22	FGGPGTAsRPSSSRS	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248882	Ser26	GTASRPSsSRSYVTT	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248879	Ser27	TASRPSSsRSYVTTS	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248880	Ser34	SRSYVTTsTRTYSLG	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248881	Ser42	TRTYSLGsALRPSTS	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248883	Ser51	LRPSTSRsLYASSPG	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248884	Ser66	GVYATRSsAVRLRSS	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248886	Ser7	sSSSYRRM	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Identifier	Residue	Sequence	Organism
SIGNOR-248876	Ser9	STRSVSSsSYRRMFG	in vitro
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Publications:

10

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248909	Ser101	AAPEAGAsPVEKEAP	in vitro
pmid	sentence
8034575	Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. \| The other phosphorylated peptides were subjected to the same analysis, and Ser45 (peptide K5), Sel-80(peptide K7), and Ser99 (peptide K8) were confirmed to be the phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-248907	Ser118	GEAAEPGsPTAAEGE	in vitro
pmid	sentence
8034575	Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. \| We conclude that the primary phosphorylation site is Ser116 \|

Identifier	Residue	Sequence	Organism
SIGNOR-248925	Ser159	KKKKKRFsFKKSFKL	in vitro
pmid	sentence
8422248	These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III.

Identifier	Residue	Sequence	Organism
SIGNOR-139906	Ser159	KKKKKRFsFKKSFKL	Homo sapiens
pmid	sentence
16116087	The present experiments demonstrate that ptn stimulates phosphorylation of serines 713 and 726 in the marcks domain of _-adducin (and serine 724 in _-adducin) and serines 152 and 156 in the marcks protein itself through the activation of either pkc _ or _ and perhaps other pkc(s) isoforms.

Identifier	Residue	Sequence	Organism
SIGNOR-139910	Ser163	KRFSFKKsFKLSGFS	Homo sapiens
pmid	sentence
16116087	The present experiments demonstrate that ptn stimulates phosphorylation of serines 713 and 726 in the marcks domain of _-adducin (and serine 724 in _-adducin) and serines 152 and 156 in the marcks protein itself through the activation of either pkc _ or _ and perhaps other pkc(s) isoforms.

Identifier	Residue	Sequence	Organism
SIGNOR-248928	Ser163	KRFSFKKsFKLSGFS	in vitro
pmid	sentence
8422248	These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III.

Identifier	Residue	Sequence	Organism
SIGNOR-248931	Ser170	SFKLSGFsFKKNKKE	in vitro
pmid	sentence
8422248	These results indicate that in vitro, PKC phosphorylates MARCKS only at three sites, but not at Ser160 as that reported previously, and there was no preferential phosphorylation of MARCKS by either PKC isozyme I, II or III.

Identifier	Residue	Sequence	Organism
SIGNOR-248908	Ser46	VKVNGDAsPAAAESG	in vitro
pmid	sentence
8034575	Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. \| The other phosphorylated peptides were subjected to the same analysis, and Ser45 (peptide K5), Sel-80(peptide K7), and Ser99 (peptide K8) were confirmed to be the phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-248910	Ser81	AAGSGAAsPSAAEKG	in vitro
pmid	sentence
8034575	Of the 7 phosphorylated serine residues identified by Edman degradation, only 1 was within the known phosphorylation domain by protein kinase C. All the other phosphorylated serine residues originated from the N-terminal half of the molecule and were immediately followed by proline. \| The other phosphorylated peptides were subjected to the same analysis, and Ser45 (peptide K5), Sel-80(peptide K7), and Ser99 (peptide K8) were confirmed to be the phosphorylation sites.

Publications:

9

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248852	Ser102	VQARVLEsYRSCYVV	in vitro
pmid	sentence
1553557	Inhibition of the current was not seen in channels in which Ser103 was replaced by Ala, although other properties of the current were unchanged. These results indicate that inhibition of the potassium current results from direct phosphorylation of the channel subunit protein at Ser103.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-137841	Ser104	TKLTRIPsAKKYKDI	Homo sapiens
pmid	sentence
15917297	Pea-15 is phosphorylated on two ser residues, ser104 and ser116. Protein kinase c (pkc) phosphorylates ser104 / we report that phosphorylation of pea-15 blocks its interaction with erk1/2 in vitro and in vivo and that phosphorylation of both ser104 and ser116 is required for this effect.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Breast

Identifier	Residue	Sequence	Organism
SIGNOR-248905	Ser1062	AVKTVNEsASLRERI	in vitro
pmid	sentence
7926007	Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase C alpha mediated phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-248906	Ser1064	KTVNESAsLRERIEF	in vitro
pmid	sentence
7926007	Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase C alpha mediated phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-248933	Thr1362	YEEHIPYtHMNGGKK	in vitro
pmid	sentence
8463287	Therefore, the present study directly identifies threonine 1336 in the HIR as a phosphorylation site for insulin and PMA.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276866	Ser1064	NRKVTIYsFTGNQRN	in vitro
pmid	sentence
36040231	PKCα unexpectedly does not activate LRRK1 by phosphorylating the kinase domain, but instead phosphorylates a cluster of conserved residues (Ser1064, Ser1074 and Thr1075) located within a region of the CORB domain of the GTPase domain. we postulate that phosphorylation of Ser1064, Ser1074 and Thr1075 activates LRRK1 by promoting interaction and stabilization of the αC-helix on the kinase domain.

Identifier	Residue	Sequence	Organism
SIGNOR-276867	Ser1074	GNQRNRCsTFRVKRN	in vitro
pmid	sentence
36040231	PKCα unexpectedly does not activate LRRK1 by phosphorylating the kinase domain, but instead phosphorylates a cluster of conserved residues (Ser1064, Ser1074 and Thr1075) located within a region of the CORB domain of the GTPase domain. we postulate that phosphorylation of Ser1064, Ser1074 and Thr1075 activates LRRK1 by promoting interaction and stabilization of the αC-helix on the kinase domain.

Identifier	Residue	Sequence	Organism
SIGNOR-276865	Thr1075	NQRNRCStFRVKRNQ	in vitro
pmid	sentence
36040231	PKCα unexpectedly does not activate LRRK1 by phosphorylating the kinase domain, but instead phosphorylates a cluster of conserved residues (Ser1064, Ser1074 and Thr1075) located within a region of the CORB domain of the GTPase domain. we postulate that phosphorylation of Ser1064, Ser1074 and Thr1075 activates LRRK1 by promoting interaction and stabilization of the αC-helix on the kinase domain.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-273796	Ser1072	ARTAKRGsRFFCEPV	in vitro
pmid	sentence
26256210	PKCα associates with and phosphorylates FMNL2 at S1072 within its Diaphanous autoregulatory region, leading to the release of formin autoinhibition.

Identifier	Residue	Organism
SIGNOR-279098		Homo sapiens
pmid	sentence
26256210	In contrast, endogenous FMNL2 or FMNL2-GFP remained membrane associated, arguing that PKCalpha activation triggers FMNL2 relocation into intracellular membranes.\|We demonstrate that PKCalpha phosphorylates the FMNL2 C terminus to control its localization and autoinhibition, thus uncovering a mode of formin activation by PKCs.

Publications:

2

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249082	Ser1084	QRQRLAVsSRGENLV	Homo sapiens	Macrophage
pmid	sentence
11298324	Furthermore, we demonstrated that the cytoplasmic domains of CD163 variants are phosphorylated by PKC-alpha in vitro. Inhibition studies using specific kinase inhibitors reveal that both CKII and PKC are involved in the CD163 signaling mechanism resulting in the secretion of proinflammatory cytokines.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249242	Ser109	KERRRTEsINSAFAE	Homo sapiens
pmid	sentence
14636580	In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. In addition, phosphopeptide mapping analysis of wild-type and mutant forms of HAND1 shows that three of these conserved residues, T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues.

Identifier	Residue	Sequence	Organism
SIGNOR-249243	Ser98	RLGRRKGsGPKKERR	Homo sapiens
pmid	sentence
14636580	In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. In addition, phosphopeptide mapping analysis of wild-type and mutant forms of HAND1 shows that three of these conserved residues, T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249244	Thr107	PKKERRRtESINSAF	Homo sapiens	HEK-293 Cell
pmid	sentence
14636580	In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. In addition, phosphopeptide mapping analysis of wild-type and mutant forms of HAND1 shows that three of these conserved residues, T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249128	Ser1101	NAQNLMQsVKETVRE	in vitro
pmid	sentence
11741957	PKC Phosphorylates Serines 1033 and 1045 in Helix H5

Identifier	Residue	Sequence	Organism
SIGNOR-249129	Ser1113	VREAEAAsIKIRTDA	in vitro
pmid	sentence
11741957	PKC Phosphorylates Serines 1033 and 1045 in Helix H5

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-58859	Ser1105	LDRKRHNsISEAKMR	Homo sapiens
pmid	sentence
9660757	These data establish that direct phosphorylation by pka of ser1105 in the putative g-box of plcbeta3 inhibits galphaq-stimulated plcbeta3 activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279425	Ser111	TPEGRRTsRRKRAKV	Homo sapiens
pmid	sentence
29395062	Together, these data indicate that LPS-induced LSD1 phosphorylation by PKC\u03b1 is required for its interaction with p65 in the nucleus.\|We have previously reported that LSD1 is phosphorylated by PKCalpha on serine 112 site, and knockin mice bearing phosphorylation defective Lsd1 SA/SA alleles show altered circadian rhythms and impaired phase resetting (Nam et al., 2014).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-28880	Ser113	GQKFARKsTRRSIRL	Homo sapiens
pmid	sentence
7559487	Pleckstrin is a substrate for protein kinase c / a combination of phosphopeptide analysis and site-directed mutagenesis shows that three residues in the intervening sequence between the two pleckstrin ph domains become phosphorylated: ser113, thr114, and ser117. /these results suggest that the phosphorylation of at least two of the sites is required for maximal pleckstrin activity

Identifier	Residue	Sequence	Organism
SIGNOR-40048	Ser117	ARKSTRRsIRLPETI	Homo sapiens
pmid	sentence
8615792	To determine the role of pkc-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in cos cells. Phosphorylation was found to occur almost exclusively on ser-113 and ser-117. Replacing all these sites with glycine decreased phosphorylation by > 90% and reduced pleckstrin's ability to inhibit phosphoinositide hydrolysis by as much as 80%.

Identifier	Residue	Sequence	Organism
SIGNOR-28884	Ser117	ARKSTRRsIRLPETI	Homo sapiens
pmid	sentence
7559487	To determine the role of pkc-dependent phosphorylation in pleckstrin function, we mapped the phosphorylation sites in vivo of wild-type and site-directed mutants of pleckstrin expressed in cos cells. Phosphorylation was found to occur almost exclusively on ser-113 and ser-117. Replacing all these sites with glycine decreased phosphorylation by > 90% and reduced pleckstrin's ability to inhibit phosphoinositide hydrolysis by as much as 80%.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-132243	Ser1145	RDKRESDsERLKRTS	Homo sapiens
pmid	sentence
15590641	Phorbol ester-induced activation of protein kinase c (pkc) increased the ca(2+) sensitivity of wild-type trpm4 but not of two mutants mutated at putative pkc phosphorylation sites.

Identifier	Residue	Sequence	Organism
SIGNOR-132247	Ser1152	SERLKRTsQKVDLAL	Homo sapiens
pmid	sentence
15590641	Phorbol ester-induced activation of protein kinase c (pkc) increased the ca(2+) sensitivity of wild-type trpm4 but not of two mutants mutated at putative pkc phosphorylation sites.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276327	Ser1185	RTPATKRsFSKEVEE	Homo sapiens	HEK-293 Cell
pmid	sentence
21576361	Phospho-proteomic and mutational analyses revealed that eIF4G1 is a substrate for PKCα at Ser1186.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248893	Ser12	KSKPKDAsQRRRSLE	in vitro
pmid	sentence
2996780	We propose that protein kinase C is responsible for this modification based on the following evidence. First, the tumor promoters, 12-O-tetradecanoylphorbol-13-acetate and teleocidin, and synthetic diacylglycerol, known activators of protein kinase C in vivo, cause nearly complete phosphorylation of pp60src at serine 12. Second, among five purified serine/threonine-specific protein kinases tested, only protein kinase C phosphorylates pp60c-src and pp60v-src in vitro at serine 12. Third, purified protein kinase C phosphorylates a synthetic peptide corresponding to the N-terminal 20 amino acids of pp60c-src at serine 12. The physiological significance of this novel phosphorylation is discussed.

Publications:

1

Organism:

In Vitro

Pathways:

Axon guidance

Identifier	Residue	Sequence	Organism
SIGNOR-186755	Ser1200	SHSSQSSsKKSSSVH	Homo sapiens
pmid	sentence
19592459	Results showed that mutating s1076 altered the effect of pkc activation on bk(ca) channels in hek-293 cells

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-17905	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

Pathways:

B-cell activation, T cell activation, VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-248860	Ser13	ITSAARRsYVSSGEM	in vitro
pmid	sentence
2155236	Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polymerize tend to depolymerize after phosphorylation. Dephosphorylation of phospho-GFAP by phosphatase led to a recovery of the polymerization competence of GFAP. Most of the phosphorylation sites for cAMP-dependent protein kinase and protein kinase C on GFAP are the same, Ser-8, Ser-13, and Ser-34. cAMP-dependent protein kinase has one additional phosphorylation site, Thr-7.

Identifier	Residue	Sequence	Organism
SIGNOR-248862	Ser38	LGPGTRLsLARMPPP	in vitro
pmid	sentence
2155236	Glial fibrillary acidic protein (GFAP), the intermediate filament component of astroglial cells, can serve as an excellent substrate for both cAMP-dependent protein kinase and protein kinase C, in vitro. GFAP phosphorylated by each protein kinase does not polymerize, and the filaments that do polymerize tend to depolymerize after phosphorylation. Dephosphorylation of phospho-GFAP by phosphatase led to a recovery of the polymerization competence of GFAP. Most of the phosphorylation sites for cAMP-dependent protein kinase and protein kinase C on GFAP are the same, Ser-8, Ser-13, and Ser-34. cAMP-dependent protein kinase has one additional phosphorylation site, Thr-7.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249083	Ser1303	NKLRRQHsYDTFVDL	in vitro
pmid	sentence
11306676	These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels.

Identifier	Residue	Sequence	Organism
SIGNOR-249086	Ser1323	ALAPRSVsLKDKGRF	in vitro
pmid	sentence
11306676	These results indicate that PKC can directly phosphorylate S1303 and S1323 in the NR2B C terminus, leading to enhanced currents through NMDA receptor channels.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-180199	Ser132	GGDAPSPsKRPWARQ	Homo sapiens
pmid	sentence
18710826	Thus, recombinant phd1 was examined for in vitro phosphorylation using protein kinase a, protein kinase calpha, casein kinase i and ii and erk2. The protein was most strongly phosphorylated by protein kinase calpha, and the phosphorylation sites were found to be ser-132, ser-226 and ser-234.Mutation Of ser-132 or ser-234 to asp or glu diminished the enzymatic activity to 25-60%, while mutation of ser-226 scarcely influenced the activity.

Identifier	Residue	Sequence	Organism
SIGNOR-180203	Ser234	QRAIPPRsIRGDQIA	Homo sapiens
pmid	sentence
18710826	Thus, recombinant phd1 was examined for in vitro phosphorylation using protein kinase a, protein kinase calpha, casein kinase i and ii and erk2. The protein was most strongly phosphorylated by protein kinase calpha, and the phosphorylation sites were found to be ser-132, ser-226 and ser-234.Mutation Of ser-132 or ser-234 to asp or glu diminished the enzymatic activity to 25-60%, while mutation of ser-226 scarcely influenced the activity.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-124494	Ser1360	VLRSPSGsQRPSVSD	Homo sapiens
pmid	sentence
15121854	Egf stimulates a pkc-?-Dependent pathway that results in the phosphorylation of the ?4 Integrin subunit on serine residues and its redistribution to actin-rich structures together, these results highlight the importance of serine phosphorylation in regulating type ii hemidesmosome disassembly, implicate a cluster of serine residues within the connecting segment of ?4, and argue for a key role for pkc-? In regulating these structures

Identifier	Residue	Sequence	Organism
SIGNOR-124498	Ser1494	TLTRDYNsLTRSEHS	Homo sapiens
pmid	sentence
15121854	Egf stimulates a pkc-?-Dependent pathway that results in the phosphorylation of the ?4 Integrin subunit on serine residues and its redistribution to actin-rich structures together, these results highlight the importance of serine phosphorylation in regulating type ii hemidesmosome disassembly, implicate a cluster of serine residues within the connecting segment of ?4, and argue for a key role for pkc-? In regulating these structures

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249096	Ser138	KPRTIYSsYQLAALQ	in vitro
pmid	sentence
11343707	Dlx3 is primarily phosphorylated by PKC alpha. By deletion and mutational analysis, we show that the serine residue S(138), located in the homeodomain of Dlx3 protein, was specifically phosphorylated by PKC. The phosphorylation of purified Dlx3 proteins by PKC partially inhibited formation of complexes between Dlx3 protein and DNA. These results suggest that Dlx3 protein can be directly phosphorylated by PKC and this affects the DNA binding activity of Dlx3.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249095	Ser138	KPRTIYSsYQLAALQ	Mus musculus
pmid	sentence
11343707	Dlx3 is primarily phosphorylated by PKCalpha. By deletion and mutational analysis, we show that the serine residue S138, located in the homeodomain of Dlx3 protein, was specifically phosphorylated by PKC. The phosphorylation of purified Dlx3 proteins by PKC partially inhibited formation of complexes between Dlx3 protein and DNA. These results suggest that Dlx3 protein can be directly phosphorylated by PKC and this affects the DNA binding activity of Dlx3. \| Since DNA binding may reveal only a part of Dlx3 protein function, we cannot rule out the influence of phosphorylation on other biological functions. Thus, the characterization of the full biological function of PKC phosphorylation of Dlx3 protein will require further studies.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-249150	Ser139	EEWTRHGsFVNKPTR	Mus musculus
pmid	sentence
12052829	Among them, Ser(29) in p52(Shc) (equivalent to Ser(138) in p66(Shc)) was phosphorylated only after TPA stimulation. Phosphorylation of this site together with the intact phosphotyrosine-binding domain was essential for ShcA binding to the protein-tyrosine phosphatase PTP-PEST. TPA-induced ShcA phosphorylation at this site (and hence, its association with PTP-PEST) was inhibited by a protein kinase C-specific inhibitor and was induced by overexpression of constitutively active mutants of protein kinase Calpha, -epsilon, and -delta isoforms.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263047	Ser139	EEWTRHGsFVNKPTR	Mus musculus	NIH-3T3 Cell
pmid	sentence
12052829	Among them, Ser(29) in p52(Shc) (equivalent to Ser(138) in p66(Shc)) was phosphorylated only after TPA stimulation. Phosphorylation of this site together with the intact phosphotyrosine-binding domain was essential for ShcA binding to the protein-tyrosine phosphatase PTP-PEST. TPA-induced ShcA phosphorylation at this site (and hence, its association with PTP-PEST) was inhibited by a protein kinase C-specific inhibitor and was induced by overexpression of constitutively active mutants of protein kinase Calpha, -epsilon, and -delta isoforms.

Publications:

2

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-107684	Ser14	PFSCHYPsRLRRDPF	Homo sapiens
pmid	sentence
11342557	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Identifier	Residue	Sequence	Organism
SIGNOR-107688	Thr63	LSSAWPGtLRSGMVP	Homo sapiens
pmid	sentence
11342557	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-197940	Ser14	PFSCHYPsRLRRDPF	Homo sapiens
pmid	sentence
22721717	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Identifier	Residue	Sequence	Organism
SIGNOR-197949	Thr63	LSSAWPGtLRSGMVP	Homo sapiens
pmid	sentence
22721717	Hsp22 is phosphorylated by protein kinase c (at residues ser(14) and thr(63)) and by p44 mitogen-activated protein kinase (at residues ser(27) and thr(87)). Concerning the possible function of hsp22, no definitive conclusions can be drawn with the available data, although its function might be to bind to and modulate the activity of hsp27.Some Studies claimed that phosphorylation is required for the translocation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248869	Ser141	MASQKRPsQRHGSKY	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Identifier	Residue	Sequence	Organism
SIGNOR-248870	Ser146	RPSQRHGsKYLATAS	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Identifier	Residue	Sequence	Organism
SIGNOR-248871	Ser190	RGAPKRGsGKDSHHP	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Identifier	Residue	Sequence	Organism
SIGNOR-248872	Ser249	GLSLSRFsWGAEGQR	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Identifier	Residue	Sequence	Organism
SIGNOR-248873	Ser266	FGYGGRAsDYKSAHK	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Identifier	Residue	Sequence	Organism
SIGNOR-248874	Ser285	VDAQGTLsKIFKLGG	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Identifier	Residue	Sequence	Organism
SIGNOR-248875	Ser295	FKLGGRDsRSGSPMA	in vitro
pmid	sentence
2413024	MBP was phosphorylated by either protein kinase A or C \| Subsequent amino acid analysis and/or sequential Edman degradation of the purified phosphopeptides, together with the known primary sequence of this protein, revealed that 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 at various reaction velocities.

Publications:

7

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249065	Ser1416	ASYCSRDsRGHNDVY	Rattus norvegicus
pmid	sentence
11104776	PKC-dependent phosphorylation of NR2A(Ser(1416)) as a key mechanism in inhibiting alphaCaMKII-binding and promoting dissociation of alphaCaMKII.NR2A complex.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277429	Ser144	TLPSDKLsKIQTLKL	Homo sapiens	HEK-293T Cell
pmid	sentence
30733340	Because most of these sites were predicted to be phosphorylated by protein kinase C (PKC), we overexpressed PKCα in several cell lines and found that it phosphorylates Twist1 on Ser-144. we observed that PKCα-mediated Twist1 phosphorylation at Ser-144 inhibits Twist1 ubiquitination and consequently stabilizes it.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-172235	Ser1443	DKMKKSKsVKEDSNL	Homo sapiens
pmid	sentence
21349850	Using a mass spectrometry-based assay, we show that egf induces phosphorylation of iqgap1 ser(1443), a residue known to be phosphorylated by pkcthe nonphosphorylatable iqgap1 s1441a/s1443a had no effect. In contrast, the s1441e/s1443d mutation markedly enhanced the ability of iqgap1 to induce neurite outgrowth.

Identifier	Residue	Sequence	Organism
SIGNOR-128714	Ser1443	DKMKKSKsVKEDSNL	Homo sapiens
pmid	sentence
15355962	Using a mass spectrometry-based assay, we show that egf induces phosphorylation of iqgap1 ser(1443), a residue known to be phosphorylated by pkcthe nonphosphorylatable iqgap1 s1441a/s1443a had no effect. In contrast, the s1441e/s1443d mutation markedly enhanced the ability of iqgap1 to induce neurite outgrowth.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-133861	Ser1443	DKMKKSKsVKEDSNL	Homo sapiens	Breast Cancer Cell, Neuron
pmid	sentence
15695813	Using a mass spectrometry-based assay, we show that egf induces phosphorylation of iqgap1 ser(1443), a residue known to be phosphorylated by pkcthe nonphosphorylatable iqgap1 s1441a/s1443a had no effect. In contrast, the s1441e/s1443d mutation markedly enhanced the ability of iqgap1 to induce neurite outgrowth.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-180537	Ser145	VVCGDRAsGYHYNAL	Homo sapiens
pmid	sentence
18755856	Phosphorylation of farnesoid x receptor by protein kinase c promotes its transcriptional activity. pkcalpha phosphorylates in vitro fxr in its dna-binding domain on s135 and s154.

Identifier	Residue	Sequence	Organism
SIGNOR-180541	Ser164	CKGFFRRsITKNAVY	Homo sapiens
pmid	sentence
18755856	Phosphorylation of farnesoid x receptor by protein kinase c promotes its transcriptional activity. pkcalpha phosphorylates in vitro fxr in its dna-binding domain on s135 and s154.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-274092	Ser145	FSRPAVAsQRRAWAT	Homo sapiens
pmid	sentence
16956790	These data suggest a model whereby agonist-induced PKC phosphorylation of Ser(145) partially impairs TPbeta signalling while GRK2/3 phosphorylation at both Ser(239) and Ser(357) within its IC(3) and C-tail domains, respectively, sterically inhibits G-protein coupling, profoundly desensitizing signalling, and promotes beta-arrestin association and, in turn, facilitates TPbeta internalization.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-139302	Ser153	SMTDFYHsKRRLIFS	Homo sapiens
pmid	sentence
16055744	Binding of calmodulin to the carboxy-terminal region of p21 induces nuclear accumulation via inhibition of protein kinase c-mediated phosphorylation of ser153\| When phosphorylated at Ser153, p21 is located at the cytoplasm and disrupts stress fibers.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-243192	Ser159	KKKKKRFsFKKSFKL	in vitro
pmid	sentence
1560845	Here we report that MARCKS is a filamentous (F) actin crosslinking protein, with activity that is inhibited by PKC-mediated phosphorylation and by binding to calcium-calmodulin

Identifier	Residue	Sequence	Organism
SIGNOR-249650	Ser163	KRFSFKKsFKLSGFS	in vitro
pmid	sentence
1560845	Here we report that MARCKS is a filamentous (F) actin crosslinking protein, with activity that is inhibited by PKC-mediated phosphorylation and by binding to calcium-calmodulin

Identifier	Residue	Sequence	Organism
SIGNOR-249670	Ser170	SFKLSGFsFKKNKKE	in vitro
pmid	sentence
1560845	Here we report that MARCKS is a filamentous (F) actin crosslinking protein, with activity that is inhibited by PKC-mediated phosphorylation and by binding to calcium-calmodulin

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262941	Ser16	KYEPAAVsEQGDKKG	Mycolicibacterium chitae	OK Cell
pmid	sentence
14976217	Parathyroid hormone (PTH) inhibits Na+,K+-ATPase activity through protein kinase C- (PKC) and extracellular signal-regulated kinase- (ERK) dependent pathways and increases serine phosphorylation of the α1-subunit. These results suggest that PTH regulates Na(+),K(+)-ATPase by PKC and ERK-dependent alpha(1)-subunit phosphorylation and that the phosphorylation requires the expression of a serine at the 11 position of the Na(+),K(+)-ATPase alpha(1)-subunit.

Publications:

1

Organism:

Mycolicibacterium Chitae

Identifier	Residue	Sequence	Organism
SIGNOR-48677	Ser16	EKEAARRsRRIDRHL	Homo sapiens
pmid	sentence
9166747	Functional role of amino-terminal serine16 and serine27 of g alphaz in receptor and effector coupling.

Identifier	Residue	Sequence	Organism
SIGNOR-48681	Ser27	DRHLRSEsQRQRREI	Homo sapiens
pmid	sentence
9166747	Functional role of amino-terminal serine16 and serine27 of g alphaz in receptor and effector coupling.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-249227	Ser161	ENLTQVGsILGNLKD	Homo sapiens
pmid	sentence
12930825	Ion trap mass spectrometry revealed that platelet SNAP-23 was phosphorylated at Ser23/Thr24 and Ser161, after cell activation by thrombin; these sites were also identified in PKC-phosphorylated r-SNAP-23. SNAP-23 mutants that mimic phosphorylation at Ser23/Thr24 inhibited syntaxin 4 interactions, whereas a phosphorylation mutant of Ser161 had only minor effects. \| Because mutants that mimic SNAP-23 phosphorylation affect syntaxin 4 interactions, we hypothesize that SNAP-23 phosphorylation may be important for modulating SNARE-complex interactions during membrane trafficking and fusion.

Identifier	Residue	Sequence	Organism
SIGNOR-249228	Ser23	ITDESLEsTRRILGL	Homo sapiens
pmid	sentence
12930825	Ion trap mass spectrometry revealed that platelet SNAP-23 was phosphorylated at Ser23/Thr24 and Ser161, after cell activation by thrombin; these sites were also identified in PKC-phosphorylated r-SNAP-23. SNAP-23 mutants that mimic phosphorylation at Ser23/Thr24 inhibited syntaxin 4 interactions, whereas a phosphorylation mutant of Ser161 had only minor effects. \| Because mutants that mimic SNAP-23 phosphorylation affect syntaxin 4 interactions, we hypothesize that SNAP-23 phosphorylation may be important for modulating SNARE-complex interactions during membrane trafficking and fusion.

Identifier	Residue	Sequence	Organism
SIGNOR-249229	Thr24	TDESLEStRRILGLA	Homo sapiens
pmid	sentence
12930825	Ion trap mass spectrometry revealed that platelet SNAP-23 was phosphorylated at Ser23/Thr24 and Ser161, after cell activation by thrombin; these sites were also identified in PKC-phosphorylated r-SNAP-23. SNAP-23 mutants that mimic phosphorylation at Ser23/Thr24 inhibited syntaxin 4 interactions, whereas a phosphorylation mutant of Ser161 had only minor effects. \| Because mutants that mimic SNAP-23 phosphorylation affect syntaxin 4 interactions, we hypothesize that SNAP-23 phosphorylation may be important for modulating SNARE-complex interactions during membrane trafficking and fusion.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-260886	Ser162	FDIVSRGsTADLDGL	Homo sapiens
pmid	sentence
19661060	We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4.

Identifier	Residue	Sequence	Organism
SIGNOR-260884	Ser189	DEEFREPsTGKTCLP	Homo sapiens
pmid	sentence
19661060	We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4.

Identifier	Residue	Sequence	Organism
SIGNOR-260882	Thr175	GLLPFLLtHKKRLTD	Homo sapiens
pmid	sentence
19661060	We conclude that the serine/threonine kinases PKC and PKA enhance activation of the TRPV4 ion channel by phosphorylation at specific sites and that phosphorylation depends on assembly of PKC and PKA by AKAP79 into a signaling complex with TRPV4.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-234461	Ser162	LRRYTTFsKRKTGIM	Mus musculus
pmid	sentence
16537394	Mimicking phosphorylation of serine-162, a target of protein kinase c-alpha, with an aspartic acid substitution (srf-s162d) completely inhibited srf-dna binding and blocked alpha-actin gene transcription pkc? Highly phosphorylated serine-162.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276619	Ser163	EKIHKRNsVRLVIRK	Homo sapiens	JURKAT Cell
pmid	sentence
24502978	We demonstrate that β-arrestin-1 recruitment to the TCR, and bystander TCR and CXCR4 downregulation, are mechanistically mediated by the TCR-triggered PKC-mediated phosphorylation of β-arrestin-1 at Ser163.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275673	Ser165	CSMAALTsHLQNQSN
pmid	sentence
23195996	Phosphorylation of MBD4 promotes 5-meC glycosylase activity Further evidence emerged to support the involvement of MBD4 in active demethylation. Protein-kinase C phosphorylation of MBD4 at two specific serine residues (165 and 262) following parathyroid hormone stimulation was shown to promote demethylation within the CYP27B1 gene promoter [12]

Identifier	Residue	Sequence
SIGNOR-275672	Ser262	SGFVQSDsKRESVCN
pmid	sentence
23195996	Phosphorylation of MBD4 promotes 5-meC glycosylase activity Further evidence emerged to support the involvement of MBD4 in active demethylation. Protein-kinase C phosphorylation of MBD4 at two specific serine residues (165 and 262) following parathyroid hormone stimulation was shown to promote demethylation within the CYP27B1 gene promoter [12]

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-249069	Ser166	LGARAKEsLDLRAHL	in vitro
pmid	sentence
11121119	In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. \| Overphosphorylation of troponin I reduced its affinity for troponin C, as measured by isothermal titration microcalorimetry. Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-249068	Ser39	EPHAKKKsKISASRK	in vitro
pmid	sentence
11121119	In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. \| Overphosphorylation of troponin I reduced its affinity for troponin C, as measured by isothermal titration microcalorimetry. Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248958	Ser168	GRQKIHIsKKWGFTK	in vitro
pmid	sentence
9016777	Moreover, QM is phosphorylated by PKC and the extent of phosphorylation by PKC is correlated with the extent of inhibition of binding of QM to c-Jun.

Identifier	Residue	Organism
SIGNOR-248957		in vitro
pmid	sentence
9016777	QM is phosphorylated by PKC and the extent of phosphorylation by PKC is correlated with the extent of inhibition of binding of QM to c-Jun.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-163667	Ser172	DQVQRRGsLPPRQVP	Homo sapiens	HEK-293 Cell
pmid	sentence
20110267	Phosphorylation of nadph oxidase activator 1 (noxa1) on serine 282 by map kinases and on serine 172 by protein kinase c and protein kinase a prevents nox1 hyperactivation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277418	Ser174	VSISRSKsYRENGAP	Homo sapiens	HEK-293T Cell
pmid	sentence
30419043	We confirm that ARX is phosphorylated by PRKCA and demonstrate phosphorylation at serine 174. We demonstrate that phosphorylation is required for correct transcriptional activity of the ARX protein using transcriptome-wide analysis of gene expression of phospho-null mutants (alanines replacing serines) compared to ARX wild-type (ARX-WT) overexpressed in pancreatic alpha TC cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263168	Ser177	TEIYRIVsQKQMSDR	in vitro
pmid	sentence
22188018	This report shows for the first time that Rab11 is differentially phosphorylated by distinct PKC isoenzymes and that this post-translational modification might be a regulatory mechanism of intracellular trafficking.Our results demonstrate that classical PKC (PKCα and PKCβII but not PKCβI) directly phosphorylate Rab11 in vitro. In addition, novel PKCε and PKCη but not PKCδ isoenzymes also phosphorylate Rab11. Mass spectrometry analysis revealed that Ser 177 is the Rab11 residue to be phosphorylated in vitro by either PKCβII or PKCε.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249149	Ser179	MKKKDEGsYDLGKKP	Rattus norvegicus	Endothelial Cell
pmid	sentence
11916978	The phosphorylation state of Ser(183) in the cytoplasmic tail of syndecan-4 determines the binding affinity of the cytoplasmic tail to phosphatidylinositol 4,5-bisphosphate (PIP(2)), the capacity of the tail to multimerize, and its ability to activate protein kinase C (PKC) alpha. We sought to identify the kinase responsible for this phosphorylation and to determine its downstream effects on PKCalpha activity and on endothelial cell function. Among several PKC isoenzymes tested, only PKCalpha and -delta were able to specifically phosphorylate Ser(183) in vitro. However, studies in cultured endothelial cells showed that the phosphorylation level of syndecan-4 was significantly reduced in endothelial cells expressing a dominant negative (DN) PKCdelta but not a DN PKCalpha mutant.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277249	Ser18	KRRRTGGsLRGNPSS	Homo sapiens	HeLa Cell
pmid	sentence
28850619	Here, we report that Fbw7α, the only Fbw7 isoform detected in eggs, is phosphorylated by PKC (protein kinase C) at a key residue (S18) in a manner coincident with Fbw7α inactivation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263160	Ser18	SVHSKRRsRADLTAE	Homo sapiens	MCF-10A Cell
pmid	sentence
25086031	Cdc42 effector protein-4 (CEP4) was recently identified by our laboratory to be a substrate of multiple PKC isoforms in non-transformed MCF-10A human breast cells. MS/MS analysis verified that Ser(18) and Ser(80) were directly phosphorylated by PKCα in vitro. Phosphorylation of CEP4 severely diminished its affinity for Cdc42 while promoting Rac activation and formation of filopodia (microspikes).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263161	Ser80	SSKRSLLsRKFRGSK	Homo sapiens	MCF-10A Cell
pmid	sentence
25086031	Cdc42 effector protein-4 (CEP4) was recently identified by our laboratory to be a substrate of multiple PKC isoforms in non-transformed MCF-10A human breast cells. MS/MS analysis verified that Ser(18) and Ser(80) were directly phosphorylated by PKCα in vitro. Phosphorylation of CEP4 severely diminished its affinity for Cdc42 while promoting Rac activation and formation of filopodia (microspikes).

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277452	Ser181	TGTARYAsINTHLGI	in vitro
pmid	sentence
31096047	In the present study we analyzed the CK1δ kinase domain for phosphorylation sites targeted by PKCα. Several phosphorylation sites were identified in vitro by initially using GST-CK1δ wild type and phosphorylation-site mutant protein fragments originating from the CK1δ kinase domain. Residues S53, T176, and S181 could finally be confirmed as targets for PKCα. Determination of kinetic parameters of full-length wild type and mutant GST-CK1δ-mediated substrate phosphorylation revealed that integrity of residue T176 is crucial for maintaining CK1δ kinase activity.

Identifier	Residue	Sequence	Organism
SIGNOR-277451	Ser53	HPQLHIEsKIYKMMQ	in vitro
pmid	sentence
31096047	In the present study we analyzed the CK1δ kinase domain for phosphorylation sites targeted by PKCα. Several phosphorylation sites were identified in vitro by initially using GST-CK1δ wild type and phosphorylation-site mutant protein fragments originating from the CK1δ kinase domain. Residues S53, T176, and S181 could finally be confirmed as targets for PKCα. Determination of kinetic parameters of full-length wild type and mutant GST-CK1δ-mediated substrate phosphorylation revealed that integrity of residue T176 is crucial for maintaining CK1δ kinase activity.

Identifier	Residue	Sequence	Organism
SIGNOR-277450	Thr176	ENKNLTGtARYASIN	in vitro
pmid	sentence
31096047	In the present study we analyzed the CK1δ kinase domain for phosphorylation sites targeted by PKCα. Several phosphorylation sites were identified in vitro by initially using GST-CK1δ wild type and phosphorylation-site mutant protein fragments originating from the CK1δ kinase domain. Residues S53, T176, and S181 could finally be confirmed as targets for PKCα. Determination of kinetic parameters of full-length wild type and mutant GST-CK1δ-mediated substrate phosphorylation revealed that integrity of residue T176 is crucial for maintaining CK1δ kinase activity.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276025	Ser185	SAYVGRLsARPKLKA	in vitro
pmid	sentence
15604283	Peptide phosphorylation analyses and both phosphorylation and enzyme kinetic studies with GSTP1 proteins mutated at candidate amino acid residues established Ser-42 and Ser-184 as putative phospho-acceptor residues for both kinases in the GSTP1 protein. Together, these findings show PKA- and PKC-dependent phosphorylation as a significant post-translational mechanism of regulation of GSTP1 function. Together, these results further support S42 and S184 as major phosphor-acceptor residues for PKA and PKC and suggest that the increased activity of the phospho-GSTP1 was not simply a consequence of the negative charge introduced in the GSTP1 protein by the phosphate group.All eight PKC isoforms, PKC-α, PKC-βI, PKC-βII, PKC-ε, PKC-γ, PKC-η, and PKC-ζ phosphorylated the GSTP1 protein efficiently

Identifier	Residue	Sequence	Organism
SIGNOR-276024	Ser43	VETWQEGsLKASCLY	in vitro
pmid	sentence
15604283	Peptide phosphorylation analyses and both phosphorylation and enzyme kinetic studies with GSTP1 proteins mutated at candidate amino acid residues established Ser-42 and Ser-184 as putative phospho-acceptor residues for both kinases in the GSTP1 protein. Together, these findings show PKA- and PKC-dependent phosphorylation as a significant post-translational mechanism of regulation of GSTP1 function. Together, these results further support S42 and S184 as major phosphor-acceptor residues for PKA and PKC and suggest that the increased activity of the phospho-GSTP1 was not simply a consequence of the negative charge introduced in the GSTP1 protein by the phosphate group.All eight PKC isoforms, PKC-α, PKC-βI, PKC-βII, PKC-ε, PKC-γ, PKC-η, and PKC-ζ phosphorylated the GSTP1 protein efficiently

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249178	Ser187	RIMEKADsNKTRIDE	Homo sapiens
pmid	sentence
12459461	This study establishes that SNAP-25 is differentially phosphorylated by protein kinase C and protein kinase A in neuroendocrine PC12 cells. Using phosphopeptide mapping and site-directed mutagenesis we identified both Thr138 and Ser187 as the targets of SNAP-25 phosphorylation by protein kinase C

Identifier	Residue	Sequence	Organism
SIGNOR-249179	Thr138	GGFIRRVtNDARENE	Homo sapiens
pmid	sentence
12459461	This study establishes that SNAP-25 is differentially phosphorylated by protein kinase C and protein kinase A in neuroendocrine PC12 cells. Using phosphopeptide mapping and site-directed mutagenesis we identified both Thr138 and Ser187 as the targets of SNAP-25 phosphorylation by protein kinase C

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248973	Ser187	DLGERKPsSAAYQKA	in vitro
pmid	sentence
9244383	We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC \| Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198.

Identifier	Residue	Sequence	Organism
SIGNOR-248976	Ser188	LGERKPSsAAYQKAP	in vitro
pmid	sentence
9244383	We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC \| Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-160313	Ser187	RIMEKADsNKTRIDE	Homo sapiens	Neuron
pmid	sentence
18171919	Phosphorylation of snap-25 at ser187 mediates enhancement of exocytosis by a phorbol ester in ins-1 cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276147	Ser193	LQAAIQKsLKDPSNN	Homo sapiens	K-562 Cell
pmid	sentence
19343040	Here, we identify serine 193 as a novel in vivo phosphorylation site of all c-FLIP proteins. c-FLIP S193 phosphorylation is mediated by PKCa and PKCb.S193 phosphorylation increases the stability of the short c-FLIP proteins

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-168532	Ser198	KSSKNKKsFKERCCL	Homo sapiens
pmid	sentence
20940393	Here we test this hypothesis and show that ralb is phosphorylated at s198 by protein kinase c (pkc). this indicates phosphorylation of ralb is important for the development of lung metastasis in human bladder cancer cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-69930	Ser2	sLKNEPRV	Homo sapiens
pmid	sentence
10441128	Serine 2, threonine 147, and serine 561 were identified as phosphorylation sites of pld1 by pkcalpha in the cells.

Identifier	Residue	Sequence	Organism
SIGNOR-69934	Ser561	PRKFSKFsLYKQLHR	Homo sapiens
pmid	sentence
10441128	Serine 2, threonine 147, and serine 561 were identified as phosphorylation sites of pld1 by pkcalpha in the cells.

Identifier	Residue	Sequence	Organism
SIGNOR-69938	Thr147	PIPTRRHtFRRQNVR	Homo sapiens
pmid	sentence
10441128	Serine 2, threonine 147, and serine 561 were identified as phosphorylation sites of pld1 by pkcalpha in the cells.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-177940	Ser2	sSKRAKAK	Homo sapiens
pmid	sentence
22136066	Rlc can also be phosphorylated at ser1/ser2/thr9 by protein kinase c (pkc). Biophysical studies show that phosphorylation at these sites leads to an increase in the km of myosin light chain kinase (mlck) for rlc, thereby indirectly inhibiting myosin ii activity.

Identifier	Residue	Sequence	Organism
SIGNOR-192792	Ser3	sKRAKAKT	Homo sapiens
pmid	sentence
22136066	Rlc can also be phosphorylated at ser1/ser2/thr9 by protein kinase c (pkc). Biophysical studies show that phosphorylation at these sites leads to an increase in the km of myosin light chain kinase (mlck) for rlc, thereby indirectly inhibiting myosin ii activity

Identifier	Residue	Sequence	Organism
SIGNOR-191536	Thr10	SKRAKAKtTKKRPQR	Homo sapiens
pmid	sentence
22136066	Rlc can also be phosphorylated at ser1/ser2/thr9 by protein kinase c (pkc). Biophysical studies show that phosphorylation at these sites leads to an increase in the km of myosin light chain kinase (mlck) for rlc, thereby indirectly inhibiting myosin ii activity

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-138733	Ser2	sFRKVVRQ	Homo sapiens
pmid	sentence
16027158	We have identified serine 2 (ser-2) on coronin 1b as the major residue phosphorylated by pkc in vivo.In this work, we show that coronin 1b interacts in vivo with the arp2/3 complex and that this interaction is inhibited by pkc phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-181863	Ser201	TRPSPLTsVRVSAVL	Homo sapiens
pmid	sentence
18976636	After pharmacological pkc activation, kir7.1 currents were strongly inhibited. Co-application of pkc inhibitors attenuated this effect. Inactivation of pkc consensus sites also strongly attenuated the effect with a single site ((201)s) being essential for almost the total pkc sensitivity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249040	Ser205	AVGTRRGsPLLIGVR	in vitro
pmid	sentence
10806197	Phosphorylation of human glutamine:fructose-6-phosphate amidotransferase by cAMP-dependent protein kinase at serine 205 blocks the enzyme activity.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248945	Ser209	DTATKSGsTTKNRFV	Mus musculus
pmid	sentence
8662663	Phosphorylation of eIF-4E on serine 209 by protein kinase C is inhibited by the translational repressors, 4E-binding proteins.[..] This suggests a two-step model for the phosphorylation (and activation) of eIF4E by growth factors and hormones: first, dissociation of eIF4E .

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism
SIGNOR-115714	Ser21	SGRARTSsFAEPGGG	Homo sapiens
pmid	sentence
11884598	Convergence of multiple signaling cascades at glycogen synthase kinase 3: edg receptor-mediated phosphorylation and inactivation by lysophosphatidic acid through a protein kinase c-dependent intracellular pathway.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276154	Ser21	ADFRLNDsHKHKDKH	in vitro
pmid	sentence
18408216	In vitro kinase assays demonstrated that Ser(10) can be phosphorylated by casein kinase II, Ser(21) can be phosphorylated by protein kinase Calpha, and Ser(112) and Ser(394) can be phosphorylated by Cdk1.Collectively these results indicate that topo I is phosphorylated during mitosis at multiple sites, one of which enhances DNA relaxation activity in vitro and interaction with DNA in cells.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-76282	Ser21	KEEPKRRsARLSAKP	Homo sapiens
pmid	sentence
10739259	Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools.

Identifier	Residue	Sequence	Organism
SIGNOR-76286	Ser25	KRRSARLsAKPPAKV	Homo sapiens
pmid	sentence
10739259	Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249000	Ser214	LVRSREVsVDEGRAC	in vitro
pmid	sentence
9677319	Here we show that Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII) with stoichiometries in vitro of 0.2-1.3 mol of phosphate/mol of Rad. \| PKC and CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin. These findings suggest that the binding of Rad to calmodulin, as well as its ability to bind GTP, might be regulated by the activation of several serine kinases.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249002	Ser257	QIRLRRDsKEANARR	in vitro	Cardiac Muscle Fiber
pmid	sentence
9677319	Here we show that Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII) with stoichiometries in vitro of 0.2-1.3 mol of phosphate/mol of Rad. \| PKC and CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin. These findings suggest that the binding of Rad to calmodulin, as well as its ability to bind GTP, might be regulated by the activation of several serine kinases.

Identifier	Residue	Sequence	Organism
SIGNOR-249004	Ser273	AGTRRREsLGKKAKR	in vitro
pmid	sentence
9677319	Here we show that Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII) with stoichiometries in vitro of 0.2-1.3 mol of phosphate/mol of Rad. \| PKC and CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin. These findings suggest that the binding of Rad to calmodulin, as well as its ability to bind GTP, might be regulated by the activation of several serine kinases.

Identifier	Residue	Sequence	Organism
SIGNOR-249006	Ser290	GRIVARNsRKMAFRA	in vitro
pmid	sentence
9677319	Here we show that Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII) with stoichiometries in vitro of 0.2-1.3 mol of phosphate/mol of Rad. \| PKC and CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin. These findings suggest that the binding of Rad to calmodulin, as well as its ability to bind GTP, might be regulated by the activation of several serine kinases.

Identifier	Residue	Sequence	Organism
SIGNOR-249008	Ser299	KMAFRAKsKSCHDLS	in vitro
pmid	sentence
9677319	Here we show that Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII) with stoichiometries in vitro of 0.2-1.3 mol of phosphate/mol of Rad. \| PKC and CKII phosphorylate multiple C-terminal serine residues, including Ser214, Ser257, Ser273, Ser290 and Ser299. \| However, phosphorylation of Rad by PKC and CKII abolishes the interaction of Rad with calmodulin. These findings suggest that the binding of Rad to calmodulin, as well as its ability to bind GTP, might be regulated by the activation of several serine kinases.

Publications:

5

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-262617	Ser2236	ERLGSFGsITRQQEG	Mus musculus	C2C12 Cell
pmid	sentence
32444788	We identified the extended basophilic phosphosite motif RxRxxp[S/T]xxp[S/T] in various proteins including filamin-C (FLNc). Importantly, this extended motif, located in a unique insert in Ig-like domain 20 of FLNc, is doubly phosphorylated. The protein kinases responsible for this dual-site phosphorylation are Akt and PKCα. Proximity proteomics and interaction analysis identified filamin A-interacting protein 1 (FILIP1) as direct FLNc binding partner. FILIP1 binding induces filamin degradation, thereby negatively regulating its function. Here, dual-site phosphorylation of FLNc not only reduces FILIP1 binding, providing a mechanism to shield FLNc from FILIP1-mediated degradation, but also enables fast dynamics of FLNc necessary for its function as signaling adaptor in cross-striated muscle cells. In vitro kinase assays combined with LC-MS confirmed hFLNc-S2233 as a substrate of Akt, whereas PKCα preferentially targeted S2236.

Publications:

1

Organism:

Mus Musculus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277179	Ser226	LNPQWNEsFTFKLKP	Homo sapiens	HEK-293T Cell
pmid	sentence
26414765	Thus, the phosphorylation of PKCα at Ser226 and Thr228 by Mst1 and Mst2 is required for the optimal activation of PKCα.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277178	Thr228	PQWNESFtFKLKPSD	Homo sapiens	HEK-293T Cell
pmid	sentence
26414765	Thus, the phosphorylation of PKCα at Ser226 and Thr228 by Mst1 and Mst2 is required for the optimal activation of PKCα.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277177	Ser226	LNPQWNEsFTFKLKP	Homo sapiens	HEK-293T Cell
pmid	sentence
26414765	Thus, the phosphorylation of PKCα at Ser226 and Thr228 by Mst1 and Mst2 is required for the optimal activation of PKCα.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277176	Thr228	PQWNESFtFKLKPSD	Homo sapiens	HEK-293T Cell
pmid	sentence
26414765	Thus, the phosphorylation of PKCα at Ser226 and Thr228 by Mst1 and Mst2 is required for the optimal activation of PKCα.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-280146	Ser226	LNPQWNEsFTFKLKP	Homo sapiens
pmid	sentence
26414765	Mst1 and Mst2 activate PKC\u03b1 to disrupt the LyGDI-Rac complex.\|Thus, the phosphorylation of PKC\u03b1 at Ser226 and Thr228 by Mst1 and Mst2 is required for the optimal activation of PKC\u03b1.

Identifier	Residue	Sequence	Organism
SIGNOR-280147	Thr228	PQWNESFtFKLKPSD	Homo sapiens
pmid	sentence
26414765	Mst1 and Mst2 activate PKC\u03b1 to disrupt the LyGDI-Rac complex.\|Thus, the phosphorylation of PKC\u03b1 at Ser226 and Thr228 by Mst1 and Mst2 is required for the optimal activation of PKC\u03b1.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248919	Ser229	QRRSNPPsRKGSGFG	in vitro
pmid	sentence
8390988	Phosphorylation of connexin-32 by protein kinase C prevents its proteolysis by mu-calpain and m-calpain. \|In agreement with other authors (see Saez et al., 1990b), we have found that phosphorylation of connexin-32 by protein kinase A and protein kinase C occurs in serine residues, although we have detected trace amounts of phosphothreonine in connexin-32 phosphorylated by protein kinase C (results not shown). Indeed, Se233 has been shown to be the major phosphorylation site catalyzed by protein kinase A. However, Ser233, Ser239, and perhaps other serines are phosphorylated by protein kinase C (Saez et al., 1990b).

Identifier	Residue	Sequence
SIGNOR-248920	Ser233	NPPSRKGsGFGHRLS
pmid	sentence
8390988	Phosphorylation of connexin-32 by protein kinase C prevents its proteolysis by mu-calpain and m-calpain. \|In agreement with other authors (see Saez et al., 1990b), we have found that phosphorylation of connexin-32 by protein kinase A and protein kinase C occurs in serine residues, although we have detected trace amounts of phosphothreonine in connexin-32 phosphorylated by protein kinase C (results not shown). Indeed, Se233 has been shown to be the major phosphorylation site catalyzed by protein kinase A. However, Ser233, Ser239, and perhaps other serines are phosphorylated by protein kinase C (Saez et al., 1990b).

Publications:

2

Organism:

In Vitro,

Identifier	Residue	Sequence	Organism
SIGNOR-249066	Ser23	PAPIRRRsSNYRAYA	in vitro
pmid	sentence
11121119	In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. \| Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-249067	Ser24	APIRRRSsNYRAYAT	in vitro
pmid	sentence
11121119	In addition to the established phosphorylation sites (S22 and S23) we found that S38 and S165 were the other two main sites of phosphorylation. \| Phosphorylation of S22/23A also decreased its affinity for troponin C indicating that phosphorylation of S38 and/or S165 impedes binding of troponin I to troponin C. Formation of a troponin I/troponin C complex prior to cAMP-dependent protein kinase treatment did not prevent overphosphorylation.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-198478	Ser23	NDMKVRKsSTPEEVK	Homo sapiens	Leukemia Cell
pmid	sentence
22855535	Pkc_ phosphorylates cofilin at ser-23 and/or ser-24 during degranulationthese results indicate that a novel pkc_-mediated phosphorylation event regulates cofilin by inhibiting its ability to depolymerize f-actin and bind to 14-3-3_, thereby promoting f-actin polymerization

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-198482	Ser24	DMKVRKSsTPEEVKK	Homo sapiens	Leukemia Cell
pmid	sentence
22855535	Pkc_ phosphorylates cofilin at ser-23 and/or ser-24 during degranulationthese results indicate that a novel pkc_-mediated phosphorylation event regulates cofilin by inhibiting its ability to depolymerize f-actin and bind to 14-3-3_, thereby promoting f-actin polymerization

Publications:

2

Organism:

Homo Sapiens

Pathways:

Axon guidance

Identifier	Residue	Sequence	Organism
SIGNOR-37466	Ser233	VSSQHRYsTPHAFTF	Homo sapiens
pmid	sentence
12551925	For example, PKCα phosphorylates Raf-1 at serine 499 (13), but mutation of this residue did not impede activation of Raf-1 by the physiological stimulators Ras and Lck. Similarly, both v-Src and phorbol esters were able to activate Raf-1 even though the PKC phosphorylation sites at serine 497 and serine 499 were mutated to alanine (14). Thus, although some PKC phosphorylation sites on Raf-1 have been identified, these sites do not appear to be required for activation of Raf-1.

Identifier	Residue	Sequence	Organism
SIGNOR-37844	Ser497	ATVKSRWsGSQQVEQ	Homo sapiens
pmid	sentence
12551925	For example, PKCα phosphorylates Raf-1 at serine 499 (13), but mutation of this residue did not impede activation of Raf-1 by the physiological stimulators Ras and Lck. Similarly, both v-Src and phorbol esters were able to activate Raf-1 even though the PKC phosphorylation sites at serine 497 and serine 499 were mutated to alanine (14). Thus, although some PKC phosphorylation sites on Raf-1 have been identified, these sites do not appear to be required for activation of Raf-1.

Identifier	Residue	Sequence	Organism
SIGNOR-97644	Ser499	VKSRWSGsQQVEQPT	Homo sapiens
pmid	sentence
12551925	For example, PKCα phosphorylates Raf-1 at serine 499 (13), but mutation of this residue did not impede activation of Raf-1 by the physiological stimulators Ras and Lck. Similarly, both v-Src and phorbol esters were able to activate Raf-1 even though the PKC phosphorylation sites at serine 497 and serine 499 were mutated to alanine (14). Thus, although some PKC phosphorylation sites on Raf-1 have been identified, these sites do not appear to be required for activation of Raf-1.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-119600	Ser235	QPSTIATsMRDSLID	Homo sapiens
pmid	sentence
14654845	Pkc stimulation led to eif6 phosphorylation, and mutation of a serine residue in the carboxy terminus of eif6 impaired rack1/pkc-mediated translational rescue.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262918	Ser239	LIRGVKSsGKVVYFT	Sus scrofa
pmid	sentence
21864610	We demonstrated that the isoforms GlyT1a, GlyT1b, and GlyT1c were constitutively phosphorylated, and that phosphorylation was dramatically enhanced, in a time dependent fashion, after PKC activation by phorbol ester. The phosphorylation was PKC-dependent, since pre-incubation of the cells with bisindolylmaleimide I, a selective PKC inhibitor, abolished the phorbol ester-induced phosphorylation. Blotting with specific anti-phospho-tyrosine antibodies did not yield any signal that could correspond to GlyT1 tyrosine phosphorylation, suggesting that the phosphorylation occurs at serine and/or threonine residues. These results together suggest that conventional PKCα and/or β are responsible for the downregulation of glycine transport. We further analyzed the effect of more specific inhibitors to PKCα and PKCβ on the GlyT1 activity. As shown in Fig. 4, panels C-F, incubation of the cells with varying concentrations of the PKCβ inhibitors (referred as PKCβ inhibitor and LY333531) or the PKCα/γ (HDBBE) inhibitors did not prevent the reduction of glycine uptake triggered by PMA, suggesting that PKCα and PKCβ together regulate GlyT1 activity.

Identifier	Residue	Sequence	Organism
SIGNOR-262923	Ser625	PIVGSNGsSRLQDSR	Sus scrofa
pmid	sentence
21864610	We demonstrated that the isoforms GlyT1a, GlyT1b, and GlyT1c were constitutively phosphorylated, and that phosphorylation was dramatically enhanced, in a time dependent fashion, after PKC activation by phorbol ester. The phosphorylation was PKC-dependent, since pre-incubation of the cells with bisindolylmaleimide I, a selective PKC inhibitor, abolished the phorbol ester-induced phosphorylation. Blotting with specific anti-phospho-tyrosine antibodies did not yield any signal that could correspond to GlyT1 tyrosine phosphorylation, suggesting that the phosphorylation occurs at serine and/or threonine residues. These results together suggest that conventional PKCα and/or β are responsible for the downregulation of glycine transport. We further analyzed the effect of more specific inhibitors to PKCα and PKCβ on the GlyT1 activity. As shown in Fig. 4, panels C-F, incubation of the cells with varying concentrations of the PKCβ inhibitors (referred as PKCβ inhibitor and LY333531) or the PKCα/γ (HDBBE) inhibitors did not prevent the reduction of glycine uptake triggered by PMA, suggesting that PKCα and PKCβ together regulate GlyT1 activity.

Identifier	Residue	Sequence	Organism
SIGNOR-262919	Thr19	GAVPSEAtKRDQNLK	Sus scrofa
pmid	sentence
21864610	We demonstrated that the isoforms GlyT1a, GlyT1b, and GlyT1c were constitutively phosphorylated, and that phosphorylation was dramatically enhanced, in a time dependent fashion, after PKC activation by phorbol ester. The phosphorylation was PKC-dependent, since pre-incubation of the cells with bisindolylmaleimide I, a selective PKC inhibitor, abolished the phorbol ester-induced phosphorylation. Blotting with specific anti-phospho-tyrosine antibodies did not yield any signal that could correspond to GlyT1 tyrosine phosphorylation, suggesting that the phosphorylation occurs at serine and/or threonine residues. These results together suggest that conventional PKCα and/or β are responsible for the downregulation of glycine transport. We further analyzed the effect of more specific inhibitors to PKCα and PKCβ on the GlyT1 activity. As shown in Fig. 4, panels C-F, incubation of the cells with varying concentrations of the PKCβ inhibitors (referred as PKCβ inhibitor and LY333531) or the PKCα/γ (HDBBE) inhibitors did not prevent the reduction of glycine uptake triggered by PMA, suggesting that PKCα and PKCβ together regulate GlyT1 activity.

Identifier	Residue	Sequence	Organism
SIGNOR-262920	Thr276	DGIMYYLtPQWDKIL	Sus scrofa
pmid	sentence
21864610	We demonstrated that the isoforms GlyT1a, GlyT1b, and GlyT1c were constitutively phosphorylated, and that phosphorylation was dramatically enhanced, in a time dependent fashion, after PKC activation by phorbol ester. The phosphorylation was PKC-dependent, since pre-incubation of the cells with bisindolylmaleimide I, a selective PKC inhibitor, abolished the phorbol ester-induced phosphorylation. Blotting with specific anti-phospho-tyrosine antibodies did not yield any signal that could correspond to GlyT1 tyrosine phosphorylation, suggesting that the phosphorylation occurs at serine and/or threonine residues. These results together suggest that conventional PKCα and/or β are responsible for the downregulation of glycine transport. We further analyzed the effect of more specific inhibitors to PKCα and PKCβ on the GlyT1 activity. As shown in Fig. 4, panels C-F, incubation of the cells with varying concentrations of the PKCβ inhibitors (referred as PKCβ inhibitor and LY333531) or the PKCα/γ (HDBBE) inhibitors did not prevent the reduction of glycine uptake triggered by PMA, suggesting that PKCα and PKCβ together regulate GlyT1 activity.

Identifier	Residue	Sequence	Organism
SIGNOR-262921	Thr590	PALLEHRtGRYAPTI	Sus scrofa
pmid	sentence
21864610	We demonstrated that the isoforms GlyT1a, GlyT1b, and GlyT1c were constitutively phosphorylated, and that phosphorylation was dramatically enhanced, in a time dependent fashion, after PKC activation by phorbol ester. The phosphorylation was PKC-dependent, since pre-incubation of the cells with bisindolylmaleimide I, a selective PKC inhibitor, abolished the phorbol ester-induced phosphorylation. Blotting with specific anti-phospho-tyrosine antibodies did not yield any signal that could correspond to GlyT1 tyrosine phosphorylation, suggesting that the phosphorylation occurs at serine and/or threonine residues. These results together suggest that conventional PKCα and/or β are responsible for the downregulation of glycine transport. We further analyzed the effect of more specific inhibitors to PKCα and PKCβ on the GlyT1 activity. As shown in Fig. 4, panels C-F, incubation of the cells with varying concentrations of the PKCβ inhibitors (referred as PKCβ inhibitor and LY333531) or the PKCα/γ (HDBBE) inhibitors did not prevent the reduction of glycine uptake triggered by PMA, suggesting that PKCα and PKCβ together regulate GlyT1 activity.

Publications:

5

Organism:

Sus Scrofa

Identifier	Residue	Sequence	Organism
SIGNOR-145398	Ser24	GYLRKPKsMHKRFFV	Homo sapiens
pmid	sentence
16574739	We show that pkcalpha is likely to be directly involved in ser24 phosphorylation...These observations are entirely consistent with a recent independent study demonstrating that the IRS1-S24D mutant shows impaired insulin-stimulated IR-IRS-1 interactions, tyrosine phosphorylation of IRS-1, recruitment/activation of PI 3-Kinase, and insulin-stimulated Glut4 translocation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277530	Ser240	TKSGDKKsGRNFFRK	Homo sapiens
pmid	sentence
32881857	We showed that the first and second phase of RhoA activity are dependent on p63 and Ca2+/PKC, respectively, and further identified phosphorylation of serine 240 on p115 RhoGEF by PKC to be the mechanistic link between PKC and RhoA.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-138351	Ser243	RWLVVKDsFLLYMCL	Homo sapiens
pmid	sentence
15979581	The phosphorylation sites in phospholipase d2 (pld2) induced by activation of protein kinase calpha (pkcalpha) in cos 7 cells were analyzed by mass spectrometry. Ser134, 146, and 243, and thr72, 99/100, and 252 were identified. These sites were mutated to ala and the double mutation of ser243 and thr252 eliminated the phosphorylation. / the s243/t252a mutant showed a partial decrease in pld2 activity

Identifier	Residue	Sequence	Organism
SIGNOR-138355	Thr252	LLYMCLEtGAISFVQ	Homo sapiens
pmid	sentence
15979581	The phosphorylation sites in phospholipase d2 (pld2) induced by activation of protein kinase calpha (pkcalpha) in cos 7 cells were analyzed by mass spectrometry. Ser134, 146, and 243, and thr72, 99/100, and 252 were identified. These sites were mutated to ala and the double mutation of ser243 and thr252 eliminated the phosphorylation. / the s243/t252a mutant showed a partial decrease in pld2 activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-76320	Ser25	KDEPQRRsARLSAKP	Homo sapiens
pmid	sentence
10739259	Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools.

Identifier	Residue	Sequence	Organism
SIGNOR-76324	Ser29	QRRSARLsAKPAPPK	Homo sapiens
pmid	sentence
10739259	Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249268	Ser259	FPLRKTAsEPNLKVR	Rattus norvegicus	Cardiac Muscle Fiber
pmid	sentence
15367659	We also demonstrate that protein kinase D (PKD), a downstream effector of PKC, directly phosphorylates HDAC5 and stimulates its nuclear export. \| Finally, we assessed the ability of PKD to phosphorylate HDAC5 in cells by employing an antibody that specifically recognizes HDAC5 that has been phosphorylated at serine 259. HDAC5 was basally phosphorylated at serine 259, and phosphorylation at this site was dramatically increased by coexpression of constitutively active PKD S/E

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249269	Ser498	RPLSRTQsSPLPQSP	Rattus norvegicus	Cardiac Muscle Fiber
pmid	sentence
15367659	We also demonstrate that protein kinase D (PKD), a downstream effector of PKC, directly phosphorylates HDAC5 and stimulates its nuclear export. \| Finally, we assessed the ability of PKD to phosphorylate HDAC5 in cells by employing an antibody that specifically recognizes HDAC5 that has been phosphorylated at serine 259. HDAC5 was basally phosphorylated at serine 259, and phosphorylation at this site was dramatically increased by coexpression of constitutively active PKD S/E

Publications:

2

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248892	Ser26	TPPSAYGsVKAYTNF	Homo sapiens	Fibroblast
pmid	sentence
2946940	The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo. \| We present evidence suggesting that protein kinase C mediates phosphorylation of serine 25.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-120907	Ser262	SPAKDCGsQKYAYFN	Homo sapiens
pmid	sentence
14702389	Using immunoblotting and phosphospecific antibodies we were able to show that serine-262 (s262) on cx43 becomes phosphorylated in response to growth factor or pkc stimulation of cardiomyocytes.In cell-cell contact forming cultures, the s262d mutation reversed while the s262a mutation increased the inhibitory effect of cx43.Phosphorylation at s262, a pkc site that becomes phosphorylated in the cell environment in response to growth factor stimulation, cancels cx43 inhibition only in contact-forming myocytes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-249010	Ser265	SKKKKRAsFKRKSSK
pmid	sentence
9716136	Two isoforms of protein kinase C, but not others, regulate the localization of DGK-zeta. \|The PSD in MARCKS is phosphorylated by PKC, which suggested that DGK-zeta may also be a substrate for PKC, and that this couldregulate its intracellular location.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-52850	Ser266	SSYGQQSsFRQDHPS	Homo sapiens
pmid	sentence
9341188	Here we report thatews, a nuclearrna-bindingprooncoprotein, contains an iq domain, is phosphorylated byproteinkinase c, and interacts with calmodulin. Interestingly, pkc phosphorylation of ews inhibits its binding to rna homopolymers, and conversely,rna binding to ews interferes with pkc phosphorylation./ these data indicate that ews contains an iq domain with ser266 acting as the primary site for pkc phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-22984	Ser268	WQRRQRKsRRTI	Homo sapiens	T-lymphocyte
pmid	sentence
2303462	The interleukin-2 (il-2) receptor, the leukocyte-specific membrane glycoprotein, t200, and the class i major histocompatibility antigens (hla) have been identified as substrates for protein kinase c from these studies, it was concluded that ser-247 is the major site of phosphorylation in the il-2 receptor and that thr-250 is a minor site.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-22988	Thr271	RQRKSRRtI	Homo sapiens	T-lymphocyte
pmid	sentence
2303462	The interleukin-2 (il-2) receptor, the leukocyte-specific membrane glycoprotein, t200, and the class i major histocompatibility antigens (hla) have been identified as substrates for protein kinase c from these studies, it was concluded that ser-247 is the major site of phosphorylation in the il-2 receptor and that thr-250 is a minor site.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-202780	Ser27	EYVQTVKsSKGGPGS	Homo sapiens
pmid	sentence
24103589	The authors identified several phosphorylated residues by a combination of peptide mapping and sequence analysis and showed that recombinant pp60c-src phosphorylates annexin a1 near its amino terminus, at tyrosine 21 (tyr21). Also polyoma virus middle t/pp60c-src complex, recombinant pp50v-abl, and the egf receptor/kinase phosphorylated the same tyrosine residue. It was also shown that serine 27 residue of anxa1 is the primary site phosphorylated by protein kinase c (pkc). In the same study, the threonine 41 residue has been identified as a pkc substrate as well. The adenosine cyclic 3_,5_-phosphate dependent protein kinase a (pka) phosphorylates anxa1 in its carboxyl-terminal core at the threonine 216 residue (thr216) [2].The phosphorylation of serine 27 is essential for annexin a1 membrane localization.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273800	Ser274	SVRSAPSsAPSTPLS	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
21728994	Only BIM-I caused a reduction in 14-3-3 binding (Figure 3B), suggesting that PKC could be responsible for one or both of the serine phosphorylations, pSer274 and pSer299.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273801	Ser299	KDRPRKKsAPETLTL	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
21728994	Only BIM-I caused a reduction in 14-3-3 binding (Figure 3B), suggesting that PKC could be responsible for one or both of the serine phosphorylations, pSer274 and pSer299.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-83037	Ser284	KVIYSQPsARSEGEF	Homo sapiens	Neutrophil, Monocyte
pmid	sentence
11027562	We also demonstrated phosphorylation of ser 284, a putative pkc phosphorylation site, by immunoblotting with anti-phosphoserine-jam antibody in thrombin-stimulated platelets.

Identifier	Residue	Sequence	Organism
SIGNOR-248901	Thr92	DRVTFLPtGITFKSV	in vitro
pmid	sentence
7646439	Internal amino acid sequence analysis of the F11 antigen provided information concerning 68 amino acids and suggested two consensus phosphorylation sites for protein kinase C (PKC). The phosphorylation by PKC of the isolated F11 antigen was observed following stimulation by phorbol 12-myristate 13-acetate.

Publications:

2

Organism:

Homo Sapiens, In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-199872	Ser285	RKAGVGQsWKENSPL	Homo sapiens
pmid	sentence
23195225	We previously showed that the phosphorylation of ser253 within the cytoplasmic domain of human tissue factor (tf) initiates the incorporation and release of this protein into cell-derived microparticles. Furthermore, subsequent phosphorylation of ser258 terminates this process. The phosphorylation of ser253 is known to be mediated by protein kinase c_

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273798	Ser285	RDRCLQHsYAGAWAV	Homo sapiens	HeLa Cell
pmid	sentence
24837102	PKCα and PKCβ are required for phosphorylation of ICOSL and ICOSL-mediated cytokine induction. Therefore, S285 is required for PKC substrate (serine) phosphorylation of ICOSL, and each of the upstream arginines is similarly required for this phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249058	Ser29	ATPAARAsKKILLPE	Homo sapiens	HEK-293 Cell
pmid	sentence
11042191	Phosphorylation of GRK2 by protein kinase C abolishes its inhibition by calmodulin. In vitro, GRK2 was preferentially phosphorylated by PKC isoforms alpha, gamma, and delta. Two-dimensional peptide mapping of PKCalpha-phosphorylated GRK2 showed a single site of phosphorylation, which was identified as serine 29 by HPLC-MS. A S29A mutant of GRK2 was not phosphorylated by PKC in vitro and showed no phorbol ester-stimulated phosphorylation when transfected into human embryonic kidney (HEK)293 cells.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249175	Ser294	PHGSPRVsVTDDSWL	Homo sapiens
pmid	sentence
12351631	Protein kinase A negatively modulates the nuclear accumulation of NF-ATc1. \| 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 domain, and that mutation of these serines blocks the effect of PKA. Activation of endogenous PKA is similarly able to promote phosphorylation of these sites on NF-ATc1 in two lymphoid cell lines.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation

Identifier	Residue	Sequence
SIGNOR-275567	Ser297	GLRYNRLsAIPRSLA
pmid	sentence
29383184	PKCalpha/delta phosphorylate Sur8 at Thr-71 and Ser-297, respectively. This phosphorylation is essential for polyubiquitin-dependent degradation of Sur8.

Identifier	Residue	Sequence
SIGNOR-275568	Thr71	VAFSVDNtIKRPNPA
pmid	sentence
29383184	PKCalpha/delta phosphorylate Sur8 at Thr-71 and Ser-297, respectively. This phosphorylation is essential for polyubiquitin-dependent degradation of Sur8.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-149948	Ser299	FLELVVSsDKREARQ	Homo sapiens
pmid	sentence
17006539	A cell permeable analog of DAG increased TRPV5 activity within 30 min via protein kinase C activation of the channel since mutation of TRPV5 at the putative PKC phosphorylation sites S299 and S654 prevented the stimulatory effect of TK.

Identifier	Residue	Sequence	Organism
SIGNOR-149952	Ser654	YVEVFKNsDKEDDQE	Homo sapiens
pmid	sentence
17006539	A cell permeable analog of DAG increased TRPV5 activity within 30 min via protein kinase C activation of the channel since mutation of TRPV5 at the putative PKC phosphorylation sites S299 and S654 prevented the stimulatory effect of TK.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89150	Ser303	RGAPPRRsSIRNAHS	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89154	Ser304	GAPPRRSsIRNAHSI	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89158	Ser315	AHSIHQRsRKRLSQD	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89162	Ser320	QRSRKRLsQDAYRRN	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism
SIGNOR-89166	Ser328	QDAYRRNsVRFLQQR	Homo sapiens
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89170	Ser359	EERQTQRsKPQPAVP	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89174	Ser370	PAVPPRPsADLILNR	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-89178	Ser379	DLILNRCsESTKRKL	Homo sapiens	Neutrophil
pmid	sentence
12056906	Phosphopeptide mapping of p47(phox) showed that, as opposed to pkc zeta, pkc alpha, beta ii, and delta are able to phosphorylate all the major pkc sites. The use of p47(phox) mutants identified serines 303, 304, 315, 320, 328, 359, 370, and 379 as targets of pkc alpha, beta ii, and delta.Taken together, these results suggest that pkc alpha, beta ii, delta, and zeta expressed in human neutrophils can individually phosphorylate p47(phox) and induce both its translocation and nadph oxidase activation.

Publications:

8

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249182	Ser306	VSQEVTRsLKDFSSS	in vitro
pmid	sentence
12519779	Munc18a is essential for neurotransmitter release by exocytosis and can be phosphorylated by PKC in vitro on Ser-306 and Ser-313. We demonstrate that it is phosphorylated on Ser-313 in response to phorbol ester treatment in adrenal chromaffin cells. Mutation of both phosphorylation sites to glutamate reduces its affinity for syntaxin and so acts as a phosphomimetic mutation.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-196765	Ser31	YKPPPQKsLKELQEM	Homo sapiens
pmid	sentence
22469974	These results reveal a mechanism of downregulation of rhogdi2 activity through pkc-mediated phosphorylation of ser31.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-184448	Ser312	SKSHRRTsLPCIPRE	Homo sapiens
pmid	sentence
19261611	Phosphorylation and activation of pde3a required the activation of pkc

Identifier	Residue	Sequence	Organism
SIGNOR-184452	Ser428	IPKRLRRsLPPGLLR	Homo sapiens
pmid	sentence
19261611	Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-184456	Ser438	PGLLRRVsSTWTTTT	Homo sapiens
pmid	sentence
19261611	Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-184460	Ser465	VRRDRSTsIKLQEAP	Homo sapiens
pmid	sentence
19261611	Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding.

Identifier	Residue	Sequence	Organism
SIGNOR-184464	Ser492	MTLTKSRsFTSSYAI	Homo sapiens
pmid	sentence
19261611	Protein kinase c-mediated phosphorylation and activation of pde3a regulate camp levels in human platelets. together, these results demonstrate that platelet activation stimulates pkc-dependent phosphorylation of pde3a on ser(312), ser(428), ser(438), ser(465), and ser(492) leading to a subsequent increase in camp hydrolysis and 14-3-3 binding.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-165857	Ser312	ASLKRSPsASSLSSM	Homo sapiens
pmid	sentence
20519438	Furthermore, by using phosphoproteomic analysis, we determined that s309 and s311 of clip-170 are phosphorylated in cells and mapped s311 as a protein kinase a (pka) phosphorylation site.phosphorylation of s311 may be critical for establishing the ?folded Back? Conformation of clip-170clip-170 open and folded back conformations represent active and inactive modes of the protein, respectively

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273821	Ser322	GELRKEPsL	Homo sapiens	HCT-116 Cell
pmid	sentence
31177095	Analyses using HCT116 cells expressing WT Trop-2 (HCT116/WT) or Trop-2 alanine-substituted at Ser-303 (HCT116/S303A) or Ser-322 (HCT116/S322A) revealed that Trop-2 is phosphorylated at Ser-322. sing protein kinase C (PKC) inhibitors and PKC-specific siRNAs, we found that PKCα and PKCδ are responsible for Trop-2 phosphorylation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-275441	Ser324	RHLSNVSsTGSIDMV	in vitro
pmid	sentence
10090741	We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249109	Ser326	VERDLKNsEAASETQ	in vitro
pmid	sentence
11517287	In-vitro incubation with [_-32P]ATP showed that HSD-3.8 protein can be phosphorylated by PKC. The phosphate is probably linked to the serine residue presenting the sequence X LysXX SerX.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249011	Ser328	TPLSQLAsGRRDPRA	Homo sapiens	HEK-293 Cell
pmid	sentence
9722557	These results indicate that PKC-dependent phosphorylation is of critical importance to homologous regulation of hIP. Ser-328 is a primary site for PKC phosphorylation of hIP.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-278492	Ser33	QQQSYLDsGIHSGAT	Homo sapiens
pmid	sentence
25058461	As shown in Fig. 1 B, PKCalpha readily phosphorylated Ser33 and Ser37 / Thr41 on full-length beta-catenin (beta-catenin 1 - 781) and CTD deletion mutant (beta-catenin 1-682).\|To examine the effect of the armadillo repeats 1-5 on PKCalpha mediated beta-catenin degradation, DNA constructs expressing beta-catenin 1 - 781 and beta-catenin deletion mutants (beta-catenin 1-422 and beta-catenin 1-138) were transfected into HEK293 cells, followed by treatment with increasing concentrations of A23187 and CGK062, which are known activators of PKCalpha.

Identifier	Residue	Sequence	Organism
SIGNOR-278493	Ser37	YLDSGIHsGATTTAP	Homo sapiens
pmid	sentence
25058461	As shown in Fig. 1 B, PKCalpha readily phosphorylated Ser33 and Ser37 / Thr41 on full-length beta-catenin (beta-catenin 1 - 781) and CTD deletion mutant (beta-catenin 1-682).\|To examine the effect of the armadillo repeats 1-5 on PKCalpha mediated beta-catenin degradation, DNA constructs expressing beta-catenin 1 - 781 and beta-catenin deletion mutants (beta-catenin 1-422 and beta-catenin 1-138) were transfected into HEK293 cells, followed by treatment with increasing concentrations of A23187 and CGK062, which are known activators of PKCalpha.

Identifier	Residue	Sequence	Organism
SIGNOR-278494	Thr41	GIHSGATtTAPSLSG	Homo sapiens
pmid	sentence
25058461	As shown in Fig. 1 B, PKCalpha readily phosphorylated Ser33 and Ser37 / Thr41 on full-length beta-catenin (beta-catenin 1 - 781) and CTD deletion mutant (beta-catenin 1-682).\|To examine the effect of the armadillo repeats 1-5 on PKCalpha mediated beta-catenin degradation, DNA constructs expressing beta-catenin 1 - 781 and beta-catenin deletion mutants (beta-catenin 1-422 and beta-catenin 1-138) were transfected into HEK293 cells, followed by treatment with increasing concentrations of A23187 and CGK062, which are known activators of PKCalpha.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273802	Ser331	SQLRHKSsLSRRTSS	in vitro
pmid	sentence
27939168	PKCα phosphorylated the full length recombinant TIMAP in in vitro kinase assay and Ser331 of TIMAP was shown to be phosphorylated by PKC. Phosphorylation of TIMAP upon PKC activation in endothelial cells results in enrichment of TIMAP in the membrane, but no such change can be observed in PKC depleted cells. Phosphorylation state of TIMAP, through affecting PP1 activity, has a remarkable effect on endothelial barrier function.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248966	Ser334	PLGDDEAsATVSKTE	in vitro
pmid	sentence
9099669	Thus, the primary protein kinase C sites are Ser334 and Ser338, with minor phosphorylation of Thr335/336 and Ser343.

Identifier	Residue	Sequence	Organism
SIGNOR-248967	Ser338	DEASATVsKTETSQV	in vitro
pmid	sentence
9099669	Thus, the primary protein kinase C sites are Ser334 and Ser338, with minor phosphorylation of Thr335/336 and Ser343.

Identifier	Residue	Sequence	Organism
SIGNOR-249147	Ser338	DEASATVsKTETSQV	in vitro
pmid	sentence
11910029	Thus, the primary protein kinase C sites are Ser334 and Ser338, with minor phosphorylation of Thr335/336 and Ser343.

Identifier	Residue	Sequence	Organism
SIGNOR-248968	Ser343	TVSKTETsQVAPA	in vitro
pmid	sentence
9099669	Thus, the primary protein kinase C sites are Ser334 and Ser338, with minor phosphorylation of Thr335/336 and Ser343.

Identifier	Residue	Sequence	Organism
SIGNOR-249148	Ser343	TVSKTETsQVAPA	in vitro
pmid	sentence
11910029	Thus, the primary protein kinase C sites are Ser334 and Ser338, with minor phosphorylation of Thr335/336 and Ser343.

Identifier	Residue	Sequence	Organism
SIGNOR-248969	Thr336	GDDEASAtVSKTETS	in vitro
pmid	sentence
9099669	Thus, the primary protein kinase C sites are Ser334 and Ser338, with minor phosphorylation of Thr335/336 and Ser343.

Publications:

6

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-279097	Ser34	YKPPAQKsIQEIQEL	Homo sapiens
pmid	sentence
25924946	PKCalpha phosphorylates RhoGDIalpha at Ser34 to reduce its affinity for RhoA (but not for Rac1 or Cdc42) .

Publications:

1

Organism:

Homo Sapiens

Pathways:

Axon guidance

Identifier	Residue	Sequence	Organism
SIGNOR-249105	Ser340	DKRFYPEsSYKSTPV	Canis lupus familiaris
pmid	sentence
11502742	Protein kinase C regulates the phosphorylation and cellular localization of occludin. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. Both the phosphorylation of occludin and its incorporation into tight junctions induced by calcium switch were markedly inhibited by the PKC inhibitor GF-109203X.

Publications:

1

Organism:

Canis Lupus Familiaris

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249062	Ser344	CGRPDPSsFSRAREA	Homo sapiens	HEK-293 Cell
pmid	sentence
11085981	In the current study, we identified a PKC-mediated phosphorylation site in the delta-opioid receptor (DOR) and demonstrated that activation of PKC by stimulation of other types of GPCR or increase in intracellular Ca2+concentration in HEK 293 cells induces heterologous phosphorylation of DOR. Our results further established that DOR phosphorylation at Ser-344 by PKC results in internalization of DOR in HEK 293 cells through a beta-arrestin- and clathrin-mediated mechanism.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249236	Ser346	EWEAQRDsHLGPHRS	Homo sapiens
pmid	sentence
14576165	A phosphorylation site at serine residue 346 was identified that is selectively phosphorylated by PKC but not by PKA. This site is localized within a recognition motif for caspases, and phosphorylation strongly inhibits proteolytic processing of PS1 by caspase activity during apoptosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-163702	Ser35	ETPLNQEsARKSEPP	Homo sapiens
pmid	sentence
20122401	Wnt5a/pkcalpha-dependent phosphorylation on serine residue 35 of roralpha is crucial to link roralpha to wnt/beta-catenin signaling, which exerts inhibitory function of the expression of wnt/beta-catenin target genes.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268180	Ser352	TSGFQPVsIKPSKAD	Rattus norvegicus	Hippocampal Cell Line
pmid	sentence
16554470	We show that protein interacting with C-kinase 1 (PICK1) recruits activated protein kinase Cα (PKCα) to MycUNC5A at the plasma membrane, stimulating its endocytosis. We identify two PKCα phosphorylation sites at serines 408 and 587, as well as dileucine internalization motifs, which are required for this endocytosis.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-268179	Ser532	EPSPDSWsLRLKKQS	Rattus norvegicus	Hippocampal Cell Line
pmid	sentence
16554470	We show that protein interacting with C-kinase 1 (PICK1) recruits activated protein kinase Cα (PKCα) to MycUNC5A at the plasma membrane, stimulating its endocytosis. We identify two PKCα phosphorylation sites at serines 408 and 587, as well as dileucine internalization motifs, which are required for this endocytosis.

Publications:

2

Organism:

Rattus Norvegicus

Pathways:

Axon guidance

Identifier	Residue	Sequence
SIGNOR-248891	Ser359	SAQGSDVsLTACKV
pmid	sentence
2941417	As shown in Fig. 6A, the HLA heavy chain was phosphorylated by kinase C. \| The major site of in vivo phosphorylation of the HLA-B7 heavy chain was localized to Ser-335 which is conserved in all specificitie

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-248913	Ser36	AAAKIQAsFRGHMAR	in vitro
pmid	sentence
8080473	Phosphorylation of RC3 by PKC alpha, beta, or gamma was stimulated by Ca2+, phospholipid, and diacylglycerol. A single site, Ser36, which is adjacent to the predicted calmodulin (CaM)-binding domain, was phosphorylated by these enzymes. Phosphorylation of RC3 by PKC or PKM, a protease-degraded PKC, was inhibited by CaM. The effect of CaM apparently targets at RC3, as phosphorylation of protamine sulfate by PKM was not inhibited by CaM.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249089	Ser363	ALLQSSAsRKTQKKK	Homo sapiens
pmid	sentence
11325528	We found that Ebp1 was basally phosphorylated in AU565 breast cancer cells on serine/threonine residues and that this phosphorylation was enhanced by heregulin treatment. Both serine and threonine residues of a GST-Ebp1 fusion protein were phosphorylated by PKC in vitro. In vivo, we demonstrated that basal Ebp1 phosphorylation was dependent upon PKC.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249092	Thr366	QSSASRKtQKKKKKK	Homo sapiens	AU-565 Cell
pmid	sentence
11325528	We found that Ebp1 was basally phosphorylated in AU565 breast cancer cells on serine/threonine residues and that this phosphorylation was enhanced by heregulin treatment. Both serine and threonine residues of a GST-Ebp1 fusion protein were phosphorylated by PKC in vitro. In vivo, we demonstrated that basal Ebp1 phosphorylation was dependent upon PKC.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249048	Ser368	QRPSSRAsSRASSRP	Rattus norvegicus
pmid	sentence
10871288	Phosphorylation of connexin43 on serine368 by protein kinase C regulates gap junctional communication.\|These data strongly suggest that PKC directly phosphorylates Cx43 on S368 in vivo, which results in a change in single channel behavior that contributes to a decrease in intercellular communication.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism
SIGNOR-248992	Ser37	TASEHRKsSKPIMEK	in vitro
pmid	sentence
9389649	Endogenous HES-1 DNA-binding activity is post-translationally inhibited during NGF signaling in vivo, and phosphorylation of PKC consensus sites in the HES-1 DNA-binding domain inhibits DNA binding by purified HES-1 in vitro.

Identifier	Residue	Sequence	Organism
SIGNOR-248993	Ser38	ASEHRKSsKPIMEKR	in vitro
pmid	sentence
9389649	Endogenous HES-1 DNA-binding activity is post-translationally inhibited during NGF signaling in vivo, and phosphorylation of PKC consensus sites in the HES-1 DNA-binding domain inhibits DNA binding by purified HES-1 in vitro.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248999	Ser371	AHSSHLKsKKGQSTS	in vitro
pmid	sentence
9571186	Here, we demonstrate that cotransfection of p53 with either PKC alpha or PKC zeta increases p53's transcriptional activity. Mutagenesis of p53 indicates that serine 371 is the major site for phosphorylation by PKC alpha in vitro.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248962	Ser381	RNRKGYRsQRGHSRG	in vitro
pmid	sentence
9030777	Phosphorylation of vitronectin on Ser362 by protein kinase C attenuates its cleavage by plasmin.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276235	Ser388	VPQPLVDsYRQQQQL	Homo sapiens
pmid	sentence
19158275	Here, we report that p73 is able to induce cell cycle arrest independently of its amino-terminal transactivation domain, whereas this domain is crucial for p73 proapoptotic functions. its activity is regulated throughout the cell cycle and modified by protein kinase C-dependent phosphorylation at serine residue 388.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-279256	Ser39	VAYGVREsVFTVEGG	Homo sapiens
pmid	sentence
28555617	PKC\u03b1 phosphorylates PHB2-S39.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-248885	Ser39	TTSTRTYsLGSALRP
pmid	sentence
2500966	We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas 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.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-280082	Ser39	NLRRSNSsLFKSWRL	Homo sapiens
pmid	sentence
24337049	ROS production in endothelial cells or directly applying ROS induced PKC\u03b1 activation and phosphorylation of TRPM2 at Ser 39.\|ROS production in endothelial cells or directly applying ROS induced PKCalpha activation and phosphorylation of TRPM2 at Ser 39.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-27300	Ser39	FMRLRRLsTKYRTEK	Homo sapiens
pmid	sentence
7520867	Ptp-pest is phosphorylated in vitro by both cyclic amp-dependent protein kinase (pka) and protein kinase c (pkc) at two major sites, which we have identified as ser39 and ser435 / phosphorylation of ser39 in vitro decreases the activity of ptp-pest by reducing its affinity for substrate.

Identifier	Residue	Sequence	Organism
SIGNOR-27304	Ser435	KKLERNLsFEIKKVP	Homo sapiens
pmid	sentence
7520867	Ptp-pest is phosphorylated in vitro by both cyclic amp-dependent protein kinase (pka) and protein kinase c (pkc) at two major sites, which we have identified as ser39 and ser435. our results suggest that both pkc and pka are capable of phosphorylating, and therefore inhibiting, ptp-pest in vivo

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249023	Ser392	AARKKRIsVKKKQEQ	Homo sapiens
pmid	sentence
10531036	ARNO is phosphorylated in vivo by PKC on a single serine residue, S392, located within the carboxy-terminal polybasic domain. Mutation of S392 to alanine does not prevent ARNO-mediated actin rearrangements, suggesting that phosphorylation does not lead to ARNO activation [6]. Here, we report that phosphorylation negatively regulates ARNO exchange activity through a 'PH domain electrostatic switch'.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248985	Ser396	RPWTRGGsLERSQSR	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9353340	Phorbol ester-induced phosphorylation of the Ser394 and Ser400 as well as GRK2-mediated phosphorylation of the Ser404, Ser408, and Ser410, resulted in the desensitization of alpha1BAR-mediated inositol phosphate response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248986	Ser402	GSLERSQsRKDSLDD	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9353340	Phorbol ester-induced phosphorylation of the Ser394 and Ser400 as well as GRK2-mediated phosphorylation of the Ser404, Ser408, and Ser410, resulted in the desensitization of alpha1BAR-mediated inositol phosphate response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248987	Ser406	RSQSRKDsLDDSGSC	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9353340	Phorbol ester-induced phosphorylation of the Ser394 and Ser400 as well as GRK2-mediated phosphorylation of the Ser404, Ser408, and Ser410, resulted in the desensitization of alpha1BAR-mediated inositol phosphate response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248988	Ser410	RKDSLDDsGSCLSGS	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9353340	Phorbol ester-induced phosphorylation of the Ser394 and Ser400 as well as GRK2-mediated phosphorylation of the Ser404, Ser408, and Ser410, resulted in the desensitization of alpha1BAR-mediated inositol phosphate response.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248989	Ser412	DSLDDSGsCLSGSQR	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
9353340	Phorbol ester-induced phosphorylation of the Ser394 and Ser400 as well as GRK2-mediated phosphorylation of the Ser404, Ser408, and Ser410, resulted in the desensitization of alpha1BAR-mediated inositol phosphate response.

Publications:

5

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-124352	Ser398	WKRLRSHsRQYVSGL	Homo sapiens
pmid	sentence
15107581	The peptide p9-s396a/s398a (both ser396 and ser398 to alanines) was phosphorylated only slightly or not phosphorylated by these kinases. Thus both ser396 and ser398 can be phosphorylated by camk ii and pkc

Identifier	Residue	Sequence	Organism
SIGNOR-66015	Ser398	WKRLRSHsRQYVSGL	Homo sapiens
pmid	sentence
10101032	In this study, we demonstrated that ser396 and ser398 are phosphorylated by pkc and, that phosphorylation of ser398 is particularly involved in pmainduced desensitization of the h1r.

Identifier	Residue	Sequence	Organism
SIGNOR-124356	Thr478	CNENFKKtFKRILHI	Homo sapiens
pmid	sentence
15107581	The peptide p10-t478a (thr478 to alanine) was not phosphorylated by pkc, indicating that thr478 can be phosphorylated by pkc.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Ovary

Identifier	Residue	Sequence	Organism
SIGNOR-91826	Ser40	SREVFDFsQRRKEYE	Homo sapiens
pmid	sentence
12198130	Phosphorylation of nrf2 at ser-40 by protein kinase c regulates antioxidant response element-mediated transcription / recently we reported evidence for the involvement of protein kinase c (pkc) in phosphorylating nrf2 and triggering its nuclear translocation in response to oxidative stress

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248903	Ser403	QRSRGRAsSHSSQTQ	in vitro
pmid	sentence
7925482	Mutation of both Ser-403/Ser-404 within a PKC motif flanking the nuclear localization signal inhibits transport of mutant lamin A to the nucleus in 64% of the cells. It is proposed that phosphorylation of the motif in vivo positively regulates nuclear localization together with the nuclear localization sequence.

Identifier	Residue	Sequence	Organism
SIGNOR-248904	Ser404	RSRGRASsHSSQTQG	in vitro
pmid	sentence
7925482	Mutation of both Ser-403/Ser-404 within a PKC motif flanking the nuclear localization signal inhibits transport of mutant lamin A to the nucleus in 64% of the cells. It is proposed that phosphorylation of the motif in vivo positively regulates nuclear localization together with the nuclear localization sequence.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276603	Ser41	RQKRSQGsSQFRSQG	in vitro
pmid	sentence
24225947	In this study, we identified a novel phosphorylation site at Ser(41) of B56α. This phosphoamino acid residue was efficiently phosphorylated in vitro by PKCα.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-194820	Ser413	PSKKRCNsIAALKAT	Homo sapiens
pmid	sentence
23909401	Collaboration of ampk and pkc to induce phosphorylation of ser413 on pip5k1b resulting in decreased kinase activity and reduced ptdins(4,5)p2 synthesis in response to oxidative stress and energy restriction. we demonstrate that pkc can directly phosphorylate ser413 in vitro

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276080	Ser415	QRKITRPsQRPKTPP	in vitro
pmid	sentence
17911614	Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of Ser(394) by protein kinase C slightly suppresses KIR3DL1 inhibitory function, and reduces receptor internalization and turnover.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248936	Ser42	TLLIRNGsEVRDPLV	in vitro
pmid	sentence
8506364	In vitro kinase assays show that Ser-59 can be uniquely phosphorylated by mitogen-activated protein kinase and that Ser-42 can be phosphorylated by either protein kinase A or protein kinase C.

Publications:

1

Organism:

In Vitro

Pathways:

T cell activation

Identifier	Residue	Sequence	Organism
SIGNOR-134613	Ser42	AKKKSKIsASRKLQL	Homo sapiens
pmid	sentence
15769444	Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction.

Identifier	Residue	Sequence	Organism
SIGNOR-134617	Ser44	KKSKISAsRKLQLKT	Homo sapiens
pmid	sentence
15769444	Phosphorylation at ser 23/24 (e.g., by pka or pkg) results in reduction in myofilament ca2+ sensitivity and an increase in crossbridge cycling rate, leading to acceleration of relaxation and an increase in power output but a reduced economy of contraction. Conversely, phosphorylation at ser 43/45 (by pkc) is associated with reduced maximum ca2+-activated force and decreased crossbridge cycling rates, which are likely to reduce power output and delay relaxation, with an increased economy of contraction.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-277900	Ser423	GRAGPFSsSRCGASV	in vitro
pmid	sentence
35931119	Through mass spectrometry, we identified that ULK1 is O-GlcNAcylated at Ser409, which is distinct from the previously reported Thr635/Thr754 sites. It has been demonstrated that PKCα mediates phosphorylation of ULK1 at Ser423, which attenuates its stability by shunting ULK1 to the chaperone-mediated autophagy (CMA) pathway.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-279558	Ser423	GRAGPFSsSRCGASV	Homo sapiens
pmid	sentence
30154410	ULK1 is phosphorylated by PKCalpha at S423 in vivo and in vitro.\|PKC\u03b1 phosphorylation of ULK1 does not change its kinase activity

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-34761	Ser43	FGYQRRAsDDGKLTD	Homo sapiens
pmid	sentence
7935389	Pka can inhibit raf-1 function directly via phosphorylation of the raf-1 kinase domain

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-273823	Ser43	IDGSHWLsMREVLRE	in vitro
pmid	sentence
26094731	Curcumin and calphostin C suppressed the activity and phosphorylation of recombinant UGT1A3 expressed in Sf9 cells. These results indicate that UGT1A3 undergoes phosphorylation, which is required for its catalytic activity. Calphostin C is a highly specific protein kinase C (PKC) inhibitor, so three predicted PKC phosphorylation sites in UGT1A3 were examined. In conclusion, phosphorylation plays an important role in UGT1A3 activity, and the serine at site 43 in UGT1A3 is most likely a phosphorylation site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-262753	Ser440	RSSPQRKsQRSSYVS	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). The PKC family contains 12 identified mammalian isoenzymes that are universally expressed in all cells and tissues and generally have a cytosolic distributionExamination of two groups of serine and threonine mutations (Fig. 3A, lanes 2 and 3) enabled us to localize the phosphorylation to four specific residues at positions 419, 422, 423, and 426. Fig. 3B shows the levels of phosphorylation with different combinations of the four mutations. Elimination of all four serines completely eliminated phosphorylation (Fig. 3B, lane 1).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-262752	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). The PKC family contains 12 identified mammalian isoenzymes that are universally expressed in all cells and tissues and generally have a cytosolic distributionExamination of two groups of serine and threonine mutations (Fig. 3A, lanes 2 and 3) enabled us to localize the phosphorylation to four specific residues at positions 419, 422, 423, and 426. Fig. 3B shows the levels of phosphorylation with different combinations of the four mutations. Elimination of all four serines completely eliminated phosphorylation (Fig. 3B, lane 1).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-262755	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). The PKC family contains 12 identified mammalian isoenzymes that are universally expressed in all cells and tissues and generally have a cytosolic distributionExamination of two groups of serine and threonine mutations (Fig. 3A, lanes 2 and 3) enabled us to localize the phosphorylation to four specific residues at positions 419, 422, 423, and 426. Fig. 3B shows the levels of phosphorylation with different combinations of the four mutations. Elimination of all four serines completely eliminated phosphorylation (Fig. 3B, lane 1).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-262754	Ser447	SQRSSYVsMRIDTHA	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). The PKC family contains 12 identified mammalian isoenzymes that are universally expressed in all cells and tissues and generally have a cytosolic distributionExamination of two groups of serine and threonine mutations (Fig. 3A, lanes 2 and 3) enabled us to localize the phosphorylation to four specific residues at positions 419, 422, 423, and 426. Fig. 3B shows the levels of phosphorylation with different combinations of the four mutations. Elimination of all four serines completely eliminated phosphorylation (Fig. 3B, lane 1).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:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-126958	Ser4517	LYMGGHGsRHSLAST	Homo sapiens
pmid	sentence
15272003	Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase calpha regulates endocytosis and association with adaptor moleculesthese results indicate that elimination of serine and threonine phosphorylation sites in the lrp cytoplasmic domain reduces the extent of tyr63 phosphorylation and leads to impaired association with the adaptor protein shc.

Identifier	Residue	Sequence	Organism
SIGNOR-127207	Ser4520	GGHGSRHsLASTDEK	Homo sapiens
pmid	sentence
15272003	Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase calpha regulates endocytosis and association with adaptor moleculesthese results indicate that elimination of serine and threonine phosphorylation sites in the lrp cytoplasmic domain reduces the extent of tyr63 phosphorylation and leads to impaired association with the adaptor protein shc.

Identifier	Residue	Sequence	Organism
SIGNOR-127211	Ser4523	GSRHSLAsTDEKREL	Homo sapiens
pmid	sentence
15272003	Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase calpha regulates endocytosis and association with adaptor moleculesthese results indicate that elimination of serine and threonine phosphorylation sites in the lrp cytoplasmic domain reduces the extent of tyr63 phosphorylation and leads to impaired association with the adaptor protein shc.

Identifier	Residue	Sequence	Organism
SIGNOR-127215	Thr4460	GFQHQRMtNGAMNVE	Homo sapiens
pmid	sentence
15272003	Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase calpha regulates endocytosis and association with adaptor moleculesthese results indicate that elimination of serine and threonine phosphorylation sites in the lrp cytoplasmic domain reduces the extent of tyr63 phosphorylation and leads to impaired association with the adaptor protein shc.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154617	Ser462	TLFQTKNsVMRKLYG	Homo sapiens
pmid	sentence
17463002	These data indicated that protein kinase c phosphorylation at ser(462) stimulates human ctp synthetase 1 activity, whereas phosphorylation at thr(455) inhibits activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-129260	Ser464	LLKHVTQsSRKLIRA	Homo sapiens	Neuron
pmid	sentence
15381704	We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-129264	Ser465	LKHVTQSsRKLIRAD	Homo sapiens	Neuron
pmid	sentence
15381704	We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-129268	Ser558	VPTYESAsIRRFQEG	Homo sapiens	Neuron
pmid	sentence
15381704	We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-129272	Ser594	HKAAVPAsEKLLLLK	Homo sapiens	Neuron
pmid	sentence
15381704	We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-129276	Thr373	TVLVKDStNRDSLDM	Homo sapiens	Neuron
pmid	sentence
15381704	We show that chat is differentially phosphorylated by protein kinase c (pkc) isoforms on four serines (ser-440, ser-346, ser-347, and ser-476) and one threonine (thr-255). This phosphorylation is hierarchical, with phosphorylation at ser-476 required for phosphorylation at other serines. Phosphorylation at some, but not all, sites regulates basal catalysis and activation.

Publications:

5

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97279	Ser473	PPSGTKKsKRGRGRP	Homo sapiens
pmid	sentence
12529391	Pkc-mediated phosphorylation at s486 does not affect s6k activity but eliminates the function of its nuclear localization signal and causes retention of an activated form of the kinase in the cytoplasm.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-86723	Ser48	RQGGRTSsQRQRDPE	Homo sapiens	Prostate Gland Cancer Cell
pmid	sentence
11980664	Phosphorylation of wild-type nkx3.1 decreased the apparent binding affinity of the protein for the consensus sequence by 3-fold relative to the nonphosphorylated protein (fig. 3) _ .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266415	Ser484	LSLQRTGsGGPGNHP	Homo sapiens	HEL Cell
pmid	sentence
25609252	PKC-induced phosphorylation events, as we have shown kindlin-3 to be a PKC phosphorylation target (Fig. 6C), are often followed by rapid activation of phosphatases (38).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276459	Ser496	ATPQRSGsVSNYRSC	in vitro
pmid	sentence
27784766	Purified PKC and Akt both phosphorylated AMPKα1 Ser487 in vitro with similar efficiency. PKC activation was associated with reduced AMPK activity, as inhibition of PKC increased AMPK activity and phorbol esters inhibited AMPK, an effect lost in cells expressing mutant AMPKα1 Ser487Ala. Consistent with a pathophysiological role for this modification, AMPKα1 Ser487 phosphorylation was inversely correlated with insulin sensitivity in human muscle.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-37470	Ser497	ATVKSRWsGSQQVEQ	Homo sapiens
pmid	sentence
8288587	Pkc can effectively phosphorylate raf-1, this is a direct effect of activated pkc and not the result of raf-1 autophosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-97648	Ser619	SLPKINRsASEPSLH	Homo sapiens
pmid	sentence
12551925	Pkc can effectively phosphorylate raf-1, this is a direct effect of activated pkc and not the result of raf-1 autophosphorylation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-126568	Ser5	sSKKRKPK	Homo sapiens	Macrophage, Monocyte
pmid	sentence
15221008	We conclude m-csf-mediated activation of pkcalpha can potentiate fmip action to initiate survival/differentiation signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-126572	Ser6	sKKRKPKV	Homo sapiens	Macrophage, Monocyte
pmid	sentence
15221008	We conclude m-csf-mediated activation of pkcalpha can potentiate fmip action to initiate survival/differentiation signaling.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-277261	Ser518	VFRTNGVsDVPTSPT	in vitro
pmid	sentence
27368100	These results suggest that PKC activates JAK2 and thereby STAT3 by directly phosphorylating T174 and S518.

Identifier	Residue	Sequence	Organism
SIGNOR-277262	Thr174	KVPVTHEtQEECLGM	in vitro
pmid	sentence
27368100	These results suggest that PKC activates JAK2 and thereby STAT3 by directly phosphorylating T174 and S518.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248935	Ser525	NTWGCGNsLRTALIN	in vitro
pmid	sentence
8477740	An interphase-specific phosphorylation at Ser525 matching the PKC consensus sequence and of peptides phosphorylated by unknown kinases was determined.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248960	Ser53	DEELEGIsPDELKDE	in vitro
pmid	sentence
9030586	Using synthetic peptide fragments containing putative phosphorylation sites of GMF, we demonstrate that PKA is capable of phosphorylating threonine 26 and serine 82, whereas PKC, p90 ribosomal S6 kinase, and casein kinase II, can phosphorylate serine 71, threonine 26, and serine 52, respectively.

Identifier	Residue	Sequence	Organism
SIGNOR-248959	Ser72	QPRFIVYsYKYQHDD	in vitro
pmid	sentence
9030586	Using synthetic peptide fragments containing putative phosphorylation sites of GMF, we demonstrate that PKA is capable of phosphorylating threonine 26 and serine 82, whereas PKC, p90 ribosomal S6 kinase, and casein kinase II, can phosphorylate serine 71, threonine 26, and serine 52, respectively.

Identifier	Residue	Sequence	Organism
SIGNOR-248961	Thr27	KFRFRKEtNNAAIIM	in vitro
pmid	sentence
9030586	Using synthetic peptide fragments containing putative phosphorylation sites of GMF, we demonstrate that PKA is capable of phosphorylating threonine 26 and serine 82, whereas PKC, p90 ribosomal S6 kinase, and casein kinase II, can phosphorylate serine 71, threonine 26, and serine 52, respectively.

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248894	Ser53	ISVSRSTsFRGGMGS	in vitro
pmid	sentence
7523419	Ser-52 in K18 is not glycosylated and matches consensus sequences for phosphorylation by CAM kinase, S6 kinase and protein kinase C, and all these kinases can phosphorylate K18 in vitro predominantly at that site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-204546	Ser536	GRGSKRLsRSVTMRK	Homo sapiens
pmid	sentence
24505490	A constitutively active form of pkc? Robustly increased basal and pma-stimulated nox5 activity and promoted the phosphorylation of nox5 on ser490, thr494, and ser498.

Identifier	Residue	Sequence	Organism
SIGNOR-204550	Ser544	RSVTMRKsQRSSKGS	Homo sapiens
pmid	sentence
24505490	A constitutively active form of pkc? Robustly increased basal and pma-stimulated nox5 activity and promoted the phosphorylation of nox5 on ser490, thr494, and ser498.

Identifier	Residue	Sequence	Organism
SIGNOR-204554	Thr540	KRLSRSVtMRKSQRS	Homo sapiens
pmid	sentence
24505490	A constitutively active form of pkc? Robustly increased basal and pma-stimulated nox5 activity and promoted the phosphorylation of nox5 on ser490, thr494, and ser498.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249209	Ser551	CVMRFLVsKRKFKES	Cricetulus griseus	CHO Cell
pmid	sentence
12754513	Phosphorylation of KCNQ2 channels was increased by muscarinic stimulation; this was prevented either by coexpression with AKAP(DeltaA) or pretreatment with PKC inhibitors that compete with diacylglycerol. These inhibitors also reduced muscarinic inhibition of M-current. \| These results suggest that Ser534 and 541 are key sites for PKC phosphorylation, although we have not ruled out the possibility that other PKC sites are involved in this process.

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-248896	Ser557	VSAGIQTsFRTGNPT	in vitro
pmid	sentence
7525583	We report that p68 is phosphorylated by protein kinase C in vitro and binds calmodulin in a Ca(2+)-dependent manner. Both phosphorylation and calmodulin binding inhibited p68 ATPase activity \| In addition, a 20-amino acid peptide corresponding to residues 549-568 of p68 was phosphorylated in a Ca- and phospholipid-dependent manner hy PKC

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249210	Ser558	SKRKFKEsLRPYDVM	Cricetulus griseus	CHO Cell
pmid	sentence
12754513	Phosphorylation of KCNQ2 channels was increased by muscarinic stimulation; this was prevented either by coexpression with AKAP(DeltaA) or pretreatment with PKC inhibitors that compete with diacylglycerol. These inhibitors also reduced muscarinic inhibition of M-current. \| These results suggest that Ser534 and 541 are key sites for PKC phosphorylation, although we have not ruled out the possibility that other PKC sites are involved in this process.

Publications:

1

Organism:

Cricetulus Griseus

Identifier	Residue	Sequence	Organism
SIGNOR-126876	Ser591	DKEKSKGsLKRK	Homo sapiens
pmid	sentence
15269224	Protein kinase calpha therefore critically and negatively regulates shp-1 function, forming part of a mechanism to retain shp-1 in a basal active state through interaction with its sh2 domains, and phosphorylating its c-terminal ser591 upon cellular activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249138	Ser595	GLMQQQKsFR	Homo sapiens
pmid	sentence
11781100	In summary, SHP2 is phosphorylated on serine residues 576 and 591 by PKC isoforms alpha, beta 1, beta 2, and eta.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249054	Ser619	RELTNRHsLPFSLPS	Homo sapiens	T-lymphocyte
pmid	sentence
11024037	However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249055	Ser623	NRHSLPFsLPSQMEP	Homo sapiens	T-lymphocyte
pmid	sentence
11024037	However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249056	Ser639	PDVPRLGsTFSLDTS	Homo sapiens	T-lymphocyte
pmid	sentence
11024037	However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249057	Ser642	PRLGSTFsLDTSMSM	Homo sapiens	T-lymphocyte
pmid	sentence
11024037	However, under normal conditions, PKC activation resulting from CD43 engagement was required to activate the MAPK pathway, suggesting that phosphorylation of Cbl on serine residues by PKC and its association with 14-3-3 molecules may play a role in preventing the Cbl inhibitory effect on the Ras-MAPK pathway.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-36788	Ser643	CFTPKGSsLKIEERA	Homo sapiens
pmid	sentence
8182108	Phosphorylation of both intact caldesmon and of its c-terminal fragment (658c), containing residues 658-756, significantly decreased their ability to inhibit acto-heavy meromyosin atpase.

Identifier	Residue	Sequence	Organism
SIGNOR-36792	Ser656	RAEFLNKsVQKSSGV	Homo sapiens
pmid	sentence
8182108	Phosphorylation of both intact caldesmon and of its c-terminal fragment (658c), containing residues 658-756, significantly decreased their ability to inhibit acto-heavy meromyosin atpase.

Identifier	Residue	Sequence	Organism
SIGNOR-36796	Ser677	AIVSKIDsRLEQYTS	Homo sapiens
pmid	sentence
8182108	Phosphorylation of both intact caldesmon and of its c-terminal fragment (658c), containing residues 658-756, significantly decreased their ability to inhibit acto-heavy meromyosin atpase.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Muscle, Smooth Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-127253	Ser657	QSDFEGFsYVNPQFV	Homo sapiens
pmid	sentence
15277524	Pkc is frequently autophosphorylated on two c-terminal sites, the turn motif (thr- 638 in human pkc) and the hydrophobic site (ser-657 in human pkc). Thus, it is becoming clear that autophosphorylation of pkc can be a regulated event and that it has significant impact on pkc function

Identifier	Residue	Sequence	Organism
SIGNOR-127257	Thr638	TRGQPVLtPPDQLVI	Homo sapiens
pmid	sentence
15277524	Pkc is frequently autophosphorylated on two c-terminal sites, the turn motif (thr- 638 in human pkc) and the hydrophobic site (ser-657 in human pkc). Thus, it is becoming clear that autophosphorylation of pkc can be a regulated event and that it has significant impact on pkc function

Publications:

2

Organism:

Homo Sapiens

Pathways:

Axon guidance, B-cell activation, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-237043	Ser657	QSDFEGFsYVNPQFV	Homo sapiens	Kidney Cell Line
pmid	sentence
18162466	In addition, knockdown of PHLPP expression reduces the rate of phorbol ester-triggered dephosphorylation of the hydrophobic motif, but not turn motif, of PKC alpha

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-237051	Ser657	QSDFEGFsYVNPQFV	Homo sapiens	Kidney Cell Line
pmid	sentence
18162466	In addition, knockdown of PHLPP expression reduces the rate of phorbol ester-triggered dephosphorylation of the hydrophobic motif, but not turn motif, of PKC alpha

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249265	Ser66	MLTKQNNsFQRSKRR	Chlorocebus aethiops
pmid	sentence
15228384	The plasma membrane translocation of diacylglycerol kinase delta1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain.

Identifier	Residue	Sequence	Organism
SIGNOR-249266	Ser70	QNNSFQRsKRRYFKL	Chlorocebus aethiops
pmid	sentence
15228384	The plasma membrane translocation of diacylglycerol kinase delta1 is negatively regulated by conventional protein kinase C-dependent phosphorylation at Ser-22 and Ser-26 within the pleckstrin homology domain.

Publications:

2

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-248954	Ser683	TKEFFRRsKIAVFDK	in vitro
pmid	sentence
8848293	Only two peptides containing Ser-662 and Ser-696 were found to be efficiently phosphorylated by protein kinase C (PKC). The peptide including Ser-696 was also phosphorylated by protein kinase G (PKG).

Identifier	Residue	Sequence	Organism
SIGNOR-248955	Ser717	GVARVRKsKGKYAYL	in vitro
pmid	sentence
8848293	Only two peptides containing Ser-662 and Ser-696 were found to be efficiently phosphorylated by protein kinase C (PKC). The peptide including Ser-696 was also phosphorylated by protein kinase G (PKG).

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249022	Ser880	YNVYGIEsVKI	Homo sapiens	HEK-293 Cell
pmid	sentence
10501226	Here, we show that the C terminus of GluR2 of the alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptor is phosphorylated by protein kinase C and that serine-880 is the major phosphorylation site. This phosphorylation also occurs in human embryonic kidney (HEK) cells by addition of 12-O-tetradecanoylphorbol 13-acetate.

Publications:

3

Organism:

In Vitro, Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248849	Ser686	WTETKKQsFKQTGEF	in vitro
pmid	sentence
1377674	Direct amino acid sequencing and peptide mapping of CF-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by PKA and PKG, and serines 686 and 790 were phosphorylated by PKC.

Identifier	Residue	Sequence	Organism
SIGNOR-248851	Ser790	IHRKTTAsTRKVSLA	in vitro
pmid	sentence
1377674	Direct amino acid sequencing and peptide mapping of CF-2 revealed that serines 660, 700, 737, and 813 as well as serine 768, serine 795, or both were phosphorylated by PKA and PKG, and serines 686 and 790 were phosphorylated by PKC.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263172	Ser687	KKYRERMsSNRPNLT	Chlorocebus aethiops	COS-1 Cell
pmid	sentence
12941954	These findings suggest that activation of a protein kinase, presumably PKC, mediates PMA-induced hmeprinβ shedding. By labeling COS-1 cells transfected with mutant constructs lacking the potential phosphorylation sites, we identified Ser687 as the main 32P-acceptor. These data provide evidence that the cytoplasmic domain of hmeprinβ can function as a PKC substrate.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism
SIGNOR-249143	Ser693	KKKFRTPsFLKKNKK	in vitro
pmid	sentence
11895774	Results of in vitro experiments with recombinant alpha adducin demonstrated that PKC-phosphorylated adducin was proteolyzed by calpain more quickly than unphosphorylated adducin. \| Phosphorylation of adducin by PKC may be a common mechanism for regulating adducin proteolysis by several proteases. \| The antibody used in panel B is specific for the PKC-phosphorylated form of adducin. This antibody was raised against the phosphopeptide CKKFRTP[pS]FLKKNK, corresponding to amino acids 656-668 of human gamma adducin

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-60120	Ser70	RDPVARTsPLQTPAA	Homo sapiens	Leukemia Cell
pmid	sentence
9738012	Purified pkca can efficiently and directly phosphorylate bcl2 at serine 70

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-142945	Ser703	SLVPSPKsFVYFIMR	Homo sapiens
pmid	sentence
16331690	There are two known phosphorylation-mediated inactivation mechanisms for trpc3 channels. Protein kinase g (pkg) inactivates trpc3 by direct phosphorylation on thr-11 and ser-263 of the trpc3 proteins, and protein kinase c (pkc) inactivates trpc3 by phosphorylation on ser-712.

Identifier	Residue	Sequence	Organism
SIGNOR-130269	Ser703	SLVPSPKsFVYFIMR	Homo sapiens
pmid	sentence
15533987	There are two known phosphorylation-mediated inactivation mechanisms for trpc3 channels. Protein kinase g (pkg) inactivates trpc3 by direct phosphorylation on thr-11 and ser-263 of the trpc3 proteins, and protein kinase c (pkc) inactivates trpc3 by phosphorylation on ser-712.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence
SIGNOR-275955	Ser706	ARIIGEKsFRRSVVG
pmid	sentence
12058027	Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.\|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead.

Identifier	Residue	Sequence
SIGNOR-275954	Ser710	GEKSFRRsVVGTPAY
pmid	sentence
12058027	Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.\|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead.

Identifier	Residue	Sequence
SIGNOR-275953	Ser876	QGLAERIsVL
pmid	sentence
12058027	Our data demonstrate that gastrin-stimulated PKD2 activation involves a heterotrimeric G alpha(q) protein as well as the activation of phospholipase C. Furthermore, we show that PKD2 can be activated by classical and novel members of the protein kinase C (PKC) family such as PKC alpha, PKC epsilon, and PKC eta.\|The position of PKD2 phosphorylated at Ser876 and Ser706/Ser710 is indicated by anarrowhead.

Publications:

3

Identifier	Residue	Sequence	Organism
SIGNOR-133188	Ser711	REFNSYGsRRGNDAV	Homo sapiens
pmid	sentence
15636585	Irp1 ser-711 is a phosphorylation site, critical for regulation of rna-binding and aconitase activities.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-59299	Ser713	KKKFRTPsFLKKSKK	Homo sapiens
pmid	sentence
9679146	Pkc phosphorylation of native and recombinant adducin inhibited actin capping measured using pyrene-actin polymerization and abolished activity of adducin in recruiting spectrin to ends and sides of actin filaments

Identifier	Residue	Sequence	Organism
SIGNOR-139870	Ser713	KKKFRTPsFLKKSKK	Homo sapiens
pmid	sentence
16116087	We now demonstrate that ptn stimulates the phosphorylation of serines 713 and 726 in the myristoylated alanine-rich protein kinase (pk) c substrate domain of beta-adducin through activation of either pkc alpha or beta.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-43744	Ser726	KKKFRTPsFLKKSKK	Homo sapiens
pmid	sentence
8810272	These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. Ser-726 and ser-713 in the c-terminal marcks-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites common for pka and pkc.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59229	Ser726	KKKFRTPsFLKKSKK	Homo sapiens	Neuron
pmid	sentence
9679146	These data demonstrate that adducin is a significant in vivo substrate for pkc or other pma-activated kinases in a variety of cells, and that phosphorylation of adducin occurs in dendritic spines that are believed to respond to external signals by changes in morphology and reorganization of cytoskeletal structures. Ser-726 and ser-713 in the c-terminal marcks-related domains of alpha- and beta-adducin, respectively, were identified as the major phosphorylation sites common for pka and pkc.

Publications:

2

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-66666	Ser738	ARIIGEKsFRRSVVG	Homo sapiens
pmid	sentence
10197446	These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748.

Identifier	Residue	Sequence	Organism
SIGNOR-66670	Ser742	GEKSFRRsVVGTPAY	Homo sapiens
pmid	sentence
10197446	These results provide direct evidence that pkd becomes activated in vivo as a consequence of pkc-mediated phosphorylation of serines 744 and 748.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248898	Ser741	TKADKRRsVRIGSYI	Sus scrofa	Porcine Aortic Endothelial Cell
pmid	sentence
7539802	We present here the identification of the major phosphorylation sites for PKC in Kit/SCFR. Two serine residues in the kinase insert, Ser-741 and Ser-746, are PKC-dependent phosphorylation sites in vivo and account for all phosphorylation by PKC in vitro. \| Two additional serine residues, Ser-821 close to the major tyrosine autophosphorylation site in the kinase domain and Ser-959 in the carboxyl terminus are SCF-stimulated PKC-dependent phosphorylation sites. \| Furthermore, the kinase activity of Kit/SCFR(S741A/S746A) toward an exogenous substrate was increased, which was reflected as a decreased Km and an increased Vmax, in accordance with the negative regulatory role of PKC on Kit/SCFR signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-248899	Ser746	RRSVRIGsYIERDVT	Sus scrofa
pmid	sentence
7539802	We present here the identification of the major phosphorylation sites for PKC in Kit/SCFR. Two serine residues in the kinase insert, Ser-741 and Ser-746, are PKC-dependent phosphorylation sites in vivo and account for all phosphorylation by PKC in vitro. \| Two additional serine residues, Ser-821 close to the major tyrosine autophosphorylation site in the kinase domain and Ser-959 in the carboxyl terminus are SCF-stimulated PKC-dependent phosphorylation sites. \| Furthermore, the kinase activity of Kit/SCFR(S741A/S746A) toward an exogenous substrate was increased, which was reflected as a decreased Km and an increased Vmax, in accordance with the negative regulatory role of PKC on Kit/SCFR signaling.

Identifier	Residue	Sequence	Organism
SIGNOR-248897	Ser821	ARDIKNDsNYVVKGN	Sus scrofa
pmid	sentence
7539802	We present here the identification of the major phosphorylation sites for PKC in Kit/SCFR. Two serine residues in the kinase insert, Ser-741 and Ser-746, are PKC-dependent phosphorylation sites in vivo and account for all phosphorylation by PKC in vitro. \| Two additional serine residues, Ser-821 close to the major tyrosine autophosphorylation site in the kinase domain and Ser-959 in the carboxyl terminus are SCF-stimulated PKC-dependent phosphorylation sites. \| Furthermore, the kinase activity of Kit/SCFR(S741A/S746A) toward an exogenous substrate was increased, which was reflected as a decreased Km and an increased Vmax, in accordance with the negative regulatory role of PKC on Kit/SCFR signaling.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-248900	Ser959	DHSVRINsVGSTASS	Sus scrofa	Porcine Aortic Endothelial Cell
pmid	sentence
7539802	We present here the identification of the major phosphorylation sites for PKC in Kit/SCFR. Two serine residues in the kinase insert, Ser-741 and Ser-746, are PKC-dependent phosphorylation sites in vivo and account for all phosphorylation by PKC in vitro. \| Two additional serine residues, Ser-821 close to the major tyrosine autophosphorylation site in the kinase domain and Ser-959 in the carboxyl terminus are SCF-stimulated PKC-dependent phosphorylation sites. \| Furthermore, the kinase activity of Kit/SCFR(S741A/S746A) toward an exogenous substrate was increased, which was reflected as a decreased Km and an increased Vmax, in accordance with the negative regulatory role of PKC on Kit/SCFR signaling.

Publications:

4

Organism:

Sus Scrofa

Identifier	Residue	Sequence	Organism
SIGNOR-28601	Ser741	TKADKRRsVRIGSYI	Homo sapiens
pmid	sentence
7539802	Phosphorylation of kit/scfr by pkc-_ in vitro: identification of ser-741 and ser-746 as the major phosphorylation sites for pkc / pkc, which acts in an scf-stimulated feedback loop, that negatively controls kit/scfr kinase activity

Identifier	Residue	Sequence	Organism
SIGNOR-28605	Ser746	RRSVRIGsYIERDVT	Homo sapiens
pmid	sentence
7539802	Phosphorylation of kit/scfr by pkc-_ in vitro: identification of ser-741 and ser-746 as the major phosphorylation sites for pkc / pkc, which acts in an scf-stimulated feedback loop, that negatively controls kit/scfr kinase activity

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-280079	Ser75	EIRSRHSsYPAGTED	Homo sapiens
pmid	sentence
24909179	Phosphorylation of BAD at ser112 and ser136 in the setting of lapatinib treatment was fully restored by PRKACA expression in BT474, SKBr3, and ZR-75-30 cells (XREF_FIG).\|We found that neither PRKACA nor PIM1 restored MAPK or PI3K activation after lapatinib or trastuzumab treatment, but rather inactivated the pro apoptotic protein BAD, thereby permitting survival signaling through BCL-XL.

Identifier	Residue	Sequence	Organism
SIGNOR-280080	Ser99	PFRGRSRsAPPNLWA	Homo sapiens
pmid	sentence
24909179	Phosphorylation of BAD at ser112 and ser136 in the setting of lapatinib treatment was fully restored by PRKACA expression in BT474, SKBr3, and ZR-75-30 cells (XREF_FIG).\|We found that neither PRKACA nor PIM1 restored MAPK or PI3K activation after lapatinib or trastuzumab treatment, but rather inactivated the pro apoptotic protein BAD, thereby permitting survival signaling through BCL-XL.

Publications:

2

Organism:

Homo Sapiens

Pathways:

VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-197285	Ser76	VQDTSGTsPVHDAAR	Homo sapiens
pmid	sentence
22558186	Cdk2 and pka were found to participate in p19ink4d phosphorylation process and that they would mediate serine 76 and threonine 141 modifications respectively. Nuclear translocation of p19ink4d induced by dna damage was shown to be dependent on serine 76 phosphorylation.

Identifier	Residue	Sequence	Organism
SIGNOR-197289	Thr141	RRDARGLtPLELALQ	Homo sapiens
pmid	sentence
22558186	Cdk2 and pka were found to participate in p19ink4d phosphorylation process and that they would mediate serine 76 and threonine 141 modifications respectively.we propose a sequential phosphorylation model for p19 in which modification at s76 would enable a second phosphorylation event at t141. The phosphorylation-induced structural changes could have functional implicancies for p19 in the dna damage response

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248890	Ser77	GEKGRALsTRCQPLE	in vitro
pmid	sentence
2584239	We have now determined that PKC phosphorylated serine 43 (and/or serine 45), serine 78, and threonine 144 in the free Tn-I subunit

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-249039	Ser795	VPPARPGsRGPAPGP	in vitro
pmid	sentence
10766777	Phosphorylation of dynamin I on Ser-795 by protein kinase C blocks its association with phospholipids.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-248950	Ser832	LIEFCYKsRSESKRM	Homo sapiens
pmid	sentence
8663994	In addition, protein kinase C specifically phosphorylates Ser-831 of GluR1 in HEK-293 cells and in cultured neurons.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249278	Ser840	VRSAFTTsTVVRMHV	in vitro
pmid	sentence
15894802	Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839.

Identifier	Residue	Sequence	Organism
SIGNOR-249285	Thr841	RSAFTTStVVRMHVG	in vitro
pmid	sentence
15894802	Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839.

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-97554	Ser862	IRNKARLsITGSVGE	Homo sapiens
pmid	sentence
12536214	Receptor internalization, altered;intracellular localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249223	Ser87	AARARFEsKVPSFYY	in vitro
pmid	sentence
12893243	The sites of phosphorylation by PKCalpha on centaurin-alpha1 were identified as S87 (peptide ARFEK) and T276 (peptide WFMDDRR) ( Fig. 5).

Identifier	Residue	Sequence	Organism
SIGNOR-249225	Thr276	GFRKRWFtMDDRRLM	in vitro
pmid	sentence
12893243	The sites of phosphorylation by PKCalpha on centaurin-alpha1 were identified as S87 (peptide ARFEK) and T276 (peptide WFMDDRR) ( Fig. 5).

Publications:

2

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-278261	Ser879	LIDRNQKsDKKPDRE	Homo sapiens
pmid	sentence
22798526	PKC\u03b1 phosphorylation of p120 at S879 is a critical phospho-switch mediating disassociation of p120 from VE-cadherin that results in AJ disassembly.\|We surmised that PKCalpha may function to disrupt AJs by signaling dissociation of p120 from VE-cadherin.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249081	Ser887	HSQPAPGsVKAPAKT	Mus musculus	Swiss-3T3 Cell
pmid	sentence
11278470	. Two-dimensional phosphopeptide mapping and site-directed mutagenesis demonstrated that PKC promoted phosphorylation of PLC beta1 at serine 887 in the nucleus of IGF-I-treated cells. Overexpression of either a PLC beta1 mutant in which the PKC phosphorylation site Ser(887) was replaced by alanine, or a dominant-negative PKC alpha, resulted in a sustained activation of nuclear PLC following IGF-I stimulation.

Publications:

1

Organism:

Mus Musculus

Pathways:

Thyroid Hormone Metabolism

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263177	Ser896	SSFKRRRsSKDTSTG	Rattus norvegicus	Neuron
pmid	sentence
15936117	Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms. The results show that PKC alpha phosphorylates preferentially S896 and PKC gamma preferentially S890.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-188581	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 gsk3_ or ser9 in gsk3_. 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

Identifier	Residue	Sequence	Organism
SIGNOR-32291	Ser95	RAVSREDsQRPGAHL	Homo sapiens
pmid	sentence
7727389	A survey of seven protein kinases showed that a1 was heavily phosphorylated by protein kinase c (pkc) and also was phosphorylated by casein kinase iiamino acid sequencing revealed that these sites were ser95, ser192, and ser199;phosphorylation at ser192 was more abundant than at ser95 and ser199. Phosphorylation by pkc inhibited the strand annealing activity of a1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-37718	Ser985	PHLDRLVsARSVSPT	Homo sapiens
pmid	sentence
8294430	These data show that phosphorylation of ser985 is a key mechanism for the negative regulation of hgf/sf receptor.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263163	Thr10	ENMEEGQtQKGCFEC	Rattus norvegicus	PC-12 Cell
pmid	sentence
12359212	In summary, a CNS neuron-specific membrane glycoprotein, M6a, could act as a novel NGF-gated Ca2+ channel through the phosphorylation with PKC and augments [Ca2+]i in M6a-S cells.

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-178695	Thr1120	EYEESQWtGERDTQS	Homo sapiens	HEK-293 Cell
pmid	sentence
21321125	Binding of _-arrestin2 to the nephrin intracellular domain depended on phosphorylation of nephrin threonine residues 1120 and 1125 by pkc_.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-172056	Thr1125	QWTGERDtQSSTVST	Homo sapiens	HEK-293 Cell
pmid	sentence
21321125	Binding of _-arrestin2 to the nephrin intracellular domain depended on phosphorylation of nephrin threonine residues 1120 and 1125 by pkc_.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248845	Thr115	ADRRKAAtMRERRRL	Chlorocebus aethiops
pmid	sentence
1335366	FGF inactivates myogenic helix-loop-helix proteins through phosphorylation of a conserved protein kinase C site in their DNA-binding domains.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276283	Thr1172	ARPMKDEtFGEYRSL	Homo sapiens	PANC-1 Cell
pmid	sentence
20335502	CKII phosphorylates T1172 of the L1 CD and phosphorylation of T1172 is responsible for loss of 2C2 signal.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249097	Thr134	KKVRKPRtIYSSYQL	in vitro
pmid	sentence
11343707	Dlx3 is primarily phosphorylated by PKC alpha. By deletion and mutational analysis, we show that the serine residue S(138), located in the homeodomain of Dlx3 protein, was specifically phosphorylated by PKC. The phosphorylation of purified Dlx3 proteins by PKC partially inhibited formation of complexes between Dlx3 protein and DNA. These results suggest that Dlx3 protein can be directly phosphorylated by PKC and this affects the DNA binding activity of Dlx3.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-260891	Thr147	ERPQIGGtIKQPPSN	in vitro
pmid	sentence
19948736	Phosphorylation of p22phox on threonine 147 enhances NADPH oxidase activity by promoting p47phox binding. \| Threonine 147 of p22phox Is Phosphorylated by PKC-α and PKC-δ in Vitro

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277628	Thr154	LRRLRPRtRKVKSVS	Homo sapiens	B-lymphocyte
pmid	sentence
34264265	In murine and guinea pig neutrophils, PKCδ is required for the phosphorylation of p40phox, a subunit of the NADPH oxidase complex (Li et al., 2016; Someya et al., 1999). In particular, it mediates phosphorylation of the threonine 154 (T154) residue of p40phox, a key regulatory step in the activation of the NADPH oxidase complex in peripheral neutrophils and B cells, in both mice and humans. In conclusion, the EBV-B cells of patients with PKCδ deficiency have impaired ROS production, associated with lower levels of phosphorylation of the cytosolic NADPH oxidase subunit p40phox by PKCδ.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-155102	Thr157	VLCVLATtDRRRRDL	Homo sapiens
pmid	sentence
17522053	Activation of protein kinase c (pkc) by 1-oleoyl-2-acetyl-sn-glycerol (oag) induced a marked increase of aqp1-dependent water permeability. This regulation was abolished in mutated aqp1 channels lacking both consensus pkc phosphorylation sites thr(157) and thr(239) (termed aqp1 deltapkc).

Identifier	Residue	Sequence	Organism
SIGNOR-155106	Thr239	APRSSDLtDRVKVWT	Homo sapiens
pmid	sentence
17522053	Activation of protein kinase c (pkc) by 1-oleoyl-2-acetyl-sn-glycerol (oag) induced a marked increase of aqp1-dependent water permeability. This regulation was abolished in mutated aqp1 channels lacking both consensus pkc phosphorylation sites thr(157) and thr(239) (termed aqp1 deltapkc).

Publications:

2

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism
SIGNOR-188181	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
SIGNOR-278322	Thr172	YGVPFLEtSAKTGMN	Homo sapiens
pmid	sentence
29312551	PKCalpha phosphorylates Rab37 on threonine 172.\|These data therefore supported a mechanism by which PKCalpha blocks Rab37 mediated cargos secretion by facilitating the dissociation of phosphorylated Rab37 from its targeting vesicles.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-273803	Thr172	YGVPFLEtSAKTGMN	Homo sapiens	PC-14 Cell
pmid	sentence
29312551	We also show that Rab37 is phosphorylated by protein kinase Cα (PKCα) at threonine 172 (T172), leading to attenuation of its GTP-bound state, and impairment of the Rab37-mediated exocytosis of TIMP1, and thus reduces its suppression activity on lung cancer cell motility.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276389	Thr193	KKRAKTItFSKNAVI	in vitro
pmid	sentence
22139477	The giant patch clamp together with site direct mutagenesis revealed that Thr-193 is the phosphorylation site on PKC that regulates the pH(i) sensitivity of ROMK1 channels. Mutation of PKC-induced phosphorylation sites (T193A) decreases the pH(i) sensitivity and increases the interaction of channel-PIP(2).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-263162	Thr2252	YLRKRNKtGKHDVQV	Homo sapiens	U-251MG Cell
pmid	sentence
15504744	Protein kinase C (PKC)-alpha phosphorylation of recombinant NG2 cytoplasmic domain and phorbol ester-induced PKC-dependent phosphorylation of full-length NG2 expressed in U251 cells are both blocked by mutation of Thr(2256), identifying this residue as a primary phosphorylation site. PKC-alpha-mediated NG2 phosphorylation at Thr(2256) is therefore a key step for initiating cell polarization and motility.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263164	Thr297	ACGRTTEtEKVQEFQ	in vitro
pmid	sentence
16087181	In deletion mutant analyses of potential phosphorylation sites in RLIP76, we identified T297 and S509 as targets for phosphorylation by PKCalpha. Phosphorylation at T297 increased doxorubicin (DOX)-transport activity approximately 2-fold for RLIP76 purified from recombinant source

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-202482	Thr346	AIQSRCCtVTRRALE	Homo sapiens
pmid	sentence
23957209	Phosphorylation of thr341 allows noxo1 to sufficiently interact with noxa1, an interaction that participates in nox1 activation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249246	Thr354	RKPANDItSQLEINF	Homo sapiens	Hodgkin Lymphoma Cell
pmid	sentence
14699138	We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. \| This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. \| Ki-1/57 Exits the Nucleus upon PMA Activation

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249252	Thr375	GRGARGGtRGGRGRI	Homo sapiens	Hodgkin Lymphoma Cell
pmid	sentence
14699138	We found a strong phosphorylation of Ki-1/57 by PKCalphabeta, PKCdelta, PKClambda/zeta, and especially by PKCsigma, however not by PKCmi. These data show that Ki-1/57 can serve in principal as a substrate for a wide variety of different PKC isoforms but also that its phosphorylation is strongest with PKCsigma. \| This suggests that the two threonine residues present in this fragment (Thr354 and Thr375) might be the main target residues for phosphorylation by PKC in vitro. \| Ki-1/57 Exits the Nucleus upon PMA Activation

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249259	Thr38	QKRHARVtVKYDRRE	Homo sapiens
pmid	sentence
32471307	A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP.

Identifier	Residue	Sequence	Organism
SIGNOR-96692	Thr38	QKRHARVtVKYDRRE	Homo sapiens
pmid	sentence
32471307	A major kinase for GPCR‐induced CPI‐17 phosphorylation is PKC which is activated by the PLCbeta‐produced signaling messenger diacylglycerol (DAG). It phosphorylates CPI‐17 at Thr38 residue that directly docks at the active site of MLCP, thereby inhibiting its activity and promoting an increase of phosphorylation of myosin and of other MLCP.\| CPI-17 can be also directly phosphorylated at Thr38 residue by MYPT1-associated kinase [222], by PAK, which is downstream of Rac and/or Cdc42 cascade [223], by Rho-associated coiled-coil kinase (ROCK) [224] and by PKN [225].

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249070	Thr434	MSFHRNHtATVRSHA	Homo sapiens
pmid	sentence
11123317	Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249071	Thr436	FHRNHTAtVRSHAEN	Homo sapiens	JURKAT Cell
pmid	sentence
11123317	Here, we present a selective mutagenesis analysis of two conserved threonine residues (T410 and T412) located at the membrane-proximal cytoplasmic region of CD5. These residues are contained within consensus phosphorylation motifs for protein kinase C and are shown here to be critical for in vivo protein kinase C-mediated phosphorylation of CD5.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-85175	Thr434	MSFHRNHtATVRSHA	Homo sapiens
pmid	sentence
11123317	Cd5 is a good pkc substrate. Phosphorylation of cd5 is necessary for cd5-mediated lipid second messenger generation.

Identifier	Residue	Sequence	Organism
SIGNOR-85179	Thr436	FHRNHTAtVRSHAEN	Homo sapiens
pmid	sentence
11123317	Cd5 is a good pkc substrate. Phosphorylation of cd5 is necessary for cd5-mediated lipid second messenger generation.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-154621	Thr455	MRLGKRRtLFQTKNS	Homo sapiens
pmid	sentence
17463002	These data indicated that protein kinase c phosphorylation at ser(462) stimulates human ctp synthetase 1 activity, whereas phosphorylation at thr(455) inhibits activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248844	Thr475	TPLSSSNtIRRPRNY	in vitro
pmid	sentence
1322130	The phosphorylation sites for both cAMP-dependent protein kinase and protein kinase C were located in a single peptide whose sequence was Arg-Arg-Asn-Ser-(P)-Phe-Thr-Pro-Leu-Ser-Ser-Ser-Asn-Thr(P)-Ile-Arg-Arg-Pro. The seryl residue nearest the N terminus was the residue specifically phosphorylated by cAMP-dependent protein kinase, whereas the threonine residue nearest the C terminus was phosphorylated by protein kinase C. \| Phosphorylation of bovine heart Fru-6-P,B-kinase by either protein kinase C or CAMP-dependent protein kinase results in activation of the enzyme.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-251620	Thr495	TGITRKKtFKEVANA	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:

1

Organism:

Homo Sapiens

Pathways:

VEGF Signaling

Identifier	Residue	Sequence	Organism
SIGNOR-275965	Thr53	IFTTCVDtRWRYMLM	in vitro
pmid	sentence
10206975	These results therefore indicate that Kir2.3 is directly modulated by PKC phosphorylation of its channel protein and threonine 53 is the PKC phosphorylation site in Kir2.3.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-133223	Thr567	QGRDKYKtLRQIRQG	Homo sapiens	A-431 Cell
pmid	sentence
15647376	Phosphorylation of ezrin is required for both conformational activation and for signaling to downstream events. The activating c-terminal threonine phosphorylation on t567 was first described to be downstream of the rho pathway (matsui et al., 1998). Additional studies have implicated protein kinase c (pkc) in the phosphorylation of ezrin t567.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-98803	Thr59	THIGPRTtRAQGISA	Homo sapiens
pmid	sentence
12609995	Antibodies generated against phosphorylated threonine 58 were used to demonstrate phosphorylation in response to pma treatment of the cells with kinetics similar to vasodilator-stimulated phosphoprotein phosphorylation. A phospho-mimetic mutation at this site (t58e) generated a partially activated pkg that was more sensitive to cgmp levels. A phospho- mutation (t58a) revealed that this residue is important but not sufficient for pkg activation by pkc.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Axon guidance

Identifier	Residue	Sequence	Organism
SIGNOR-77421	Thr678	RHIVRKRtLRRLLQE	Homo sapiens
pmid	sentence
10816576	Biochemical and morphological analyses indicate that threonine-phosphorylated EGFR molecules undergo normal internalization, but instead of sorting to lysosomal degradation, they recycle back to the cell surfaceThe inhibitory effects of pkc are mediated by a single threonine residue (threonine 654) of egfr

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249043	Thr695	GSKKKICtRKPRFMS	Homo sapiens
pmid	sentence
10823959	Furthermore, we demonstrate that the selectivity of PKC action on receptor signaling rests on phosphorylation of a threonine residue located in the G protein-interacting domain of the receptor. Modification at Thr(695) selectively disrupts mGluR1alpha-G(q/11) interaction without affecting signaling through G(s).

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-248970	Thr723	LRKRQYGtISHGIVE	in vitro
pmid	sentence
9109675	We report here that a cytoplasmic domain peptide from APLP1 is phosphorylated in vitro by protein kinase C and that a cytoplasmic domain peptide from APLP2 is phosphorylated in vitro by protein kinase C and cdc2 kinase.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249121	Thr758	NPLFKSAtTTVMNPK	Homo sapiens	Leukocyte
pmid	sentence
11700305	Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. \|

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249125	Thr760	LFKSATTtVMNPKFA	Homo sapiens	Leukocyte
pmid	sentence
11700305	Here, we identify catalytic domain fragments of protein kinase C (PKC) delta and PKCbetaI/II as the major protein kinases in leukocyte extracts that phosphorylate a peptide corresponding to the cytoplasmic tail of the integrin CD18 chain. The sites phosphorylated in vitro were identified as Ser-745 and Thr-758. PKCalpha and PKCeta also phosphorylated these residues, and PKCalpha additionally phosphorylated Thr-760. Ser-745, a novel site, was shown to become phosphorylated in T cells in response to phorbol ester stimulation. \|

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-249017	Thr850	EAKRMKLtFSEAIRN	in vitro
pmid	sentence
10366608	In addition, we identified threonine 830 as a potential PKC phosphorylation site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-170334	Thr888	FKVAARAtLRRSNVS	Homo sapiens
pmid	sentence
21135065	Casr(t888) is a protein kinase c (pkc) phosphorylation site in the receptor's intracellular domain that has previously been identified as a critical negative regulator of casr downstream signaling in vitro, thus, casr(t888) represents a functionally important, inhibitory phosphorylation site that contributes to the control of pth secretion.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249041	Thr91	GRQSKGLtQKDLATK	Homo sapiens	HUVEC Cell
pmid	sentence
10816571	EDF-1 was phosphorylated in vitro by PKC in the presence of Ca2+ and phospholipids \| This results shows that introduction of a single negative charge by phosphorylation at Thr-91 inhibited CaM-EDF-1 interactions.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-246581	Tyr658	SDFEGFSyVNPQFVH	Homo sapiens	Mast Cell
pmid	sentence
12881490	We present evidence that Tyr-662 and Tyr-658 of PKCbetaI and PKCalpha, respectively, are phosphorylated by Syk in the membrane compartment of FcepsilonRI-stimulated mast cells. These phosphorylations require prior PKC autophosphorylation of the adjacent serine residues (Ser-661 and Ser-657, respectively) and generate a binding site for the SH2 domain of the adaptor protein Grb-2.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation

Identifier	Residue	Organism
SIGNOR-280078		Homo sapiens
pmid	sentence
21281821	PKC\u03b1 phosphorylates and activates ARPC5, which organizes the actin net dorsolateral of nucleus.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279384		Homo sapiens
pmid	sentence
28028151	In response to chemokine stimulation, PKC\u03b1 phosphorylates DOCK8 at its three serine sites, promoting DOCK8 separation from LRCH1 and translocation to the leading edge to guide T cell migration.\|Taken our data together, we suggest that PKC\u03b1 phosphorylates DOCK8 at the Ser2077/2082/2087 sites to promote T cell migration.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-199454		Homo sapiens
pmid	sentence
23151663	Our findings suggest a molecular interaction between pka, hdpr1, and dvl and a possible contribution of this interaction to tumorigenesis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279557		Homo sapiens
pmid	sentence
19723022	PKCalpha dependent Rnd3 phosphorylation downregulates Rnd3 inhibitory activity and leads to increased signaling through the Rho-ROCK pathway.\|We further show that PKC\u03b1 directly phosphorylates Rnd3 in an in vitro kinase assay.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-256267		Homo sapiens	Hep-G2 Cell
pmid	sentence
15730925	PKC-alpha asODN (antisense oligonucleotides) could inhibit the growth and proliferation of HepG2 and induce its apoptosis by blocking the cell signal transduction related to PKC-alpha in vitro, and may be potentially used in the prevention and management of recurrent and metastatic HCC.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-256337		Homo sapiens
pmid	sentence
26010542	The luciferase reporter assay results revealed that the presence of both MZF-1 and Elk-1 significantly contributed to the upregulation of PKCα gene transcription activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-278382		Homo sapiens
pmid	sentence
19679839	In summary, titin is a PKC substrate with PKCalpha phosphorylating predominately the full-length titin molecule.\|Mechanical experiments with skinned LV myocardium revealed that PKCalpha significantly increases titin based passive tension, an effect that is reversed by PP1.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-248990		in vitro
pmid	sentence
9374536	However, when assayed in the presence of calcium/calmodulin, the activity of the B isoform was decreased following phosphorylation by either protein kinase.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-149406		Homo sapiens
pmid	sentence
16963226	Pkcalfa, but not pkcbeta, is the predominant cpkc isoenzyme required for cpla2 protein phosphorylation and maximal induction of cpla2 enzymatic activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-99310		Homo sapiens
pmid	sentence
12645577	Tnf-alfa binds to tnfr1 and activates pc-plc to induce pkcalfa and c-src activation, leading to tyrosine phosphorylation of ikkbeta at tyr188 and tyr199.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-268502		Homo sapiens
pmid	sentence
19948174	Here we demonstrate that C1P induces translocation of protein kinase C-alpha (PKC-alpha) from the soluble to the membrane fraction of bone marrow-derived macrophages.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-202007		Homo sapiens
pmid	sentence
23630338	C1a domain is critical for the dag-induced activation of pkcalfa.Furthermore, calcium and diacylglycerol activate protein kinase c, resulting in the phosphorylation of a large variety of substrates.

Identifier	Residue	Organism
SIGNOR-179279		Homo sapiens
pmid	sentence
18593525	The increases in the membrane levels of nacholeate itself and of dag induce a translocation and overexpression of protein kinase c (pkc) and subsequent reductions of cyclin d, cyclin-dependent kinases 4 and 6 (cdks 4 and 6), hypophosphorylation of the retinoblastoma protein, inhibition of e2f1 and knockdown of dihydrofolate reductase (dhfr) impairing dna synthesis.

Identifier	Residue	Organism
SIGNOR-100254		Homo sapiens
pmid	sentence
12954613	C1a domain is critical for the dag-induced activation of pkcalfa.Furthermore, calcium and diacylglycerol activate protein kinase c, resulting in the phosphorylation of a large variety of substrates.

Identifier	Residue	Organism
SIGNOR-121956		Homo sapiens
pmid	sentence
14967450	The molecular requirements for diacylglycerol (dag) and calcium (ca2+) to promote pkc membrane translocation, the hallmark of pkc activation, have been clarified.

Publications:

4

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-166368		Homo sapiens
pmid	sentence
20577053	The action of metformin was shown to be mediated through activation of apkc?/?, Which phosphorylates cbp at ser436, and disrupts the transcriptionally active creb-cbp-crtc2 complex,

Publications:

1

Organism:

Homo Sapiens

Pathways:

Thyroid Hormone Metabolism

Identifier	Residue	Organism
SIGNOR-126066		Homo sapiens
pmid	sentence
15209375	One of the most studied events controlled by ptdins(3,4,5)p3, comprises the activation of a of agc family protein kinases, including isoforms of protein kinase b (pkb)/akt, p70 ribosomal s6 kinase (s6k), serum and glucocorticoid-induced protein kinase (sgk) and protein kinase c (pkc), which play crucial roles in regulating physiological processes relevant to metabolism, growth, proliferation and survival. Here, we review recent biochemical, genetic and structural studies on the 3-phosphoinositide-dependent protein kinase-1 (pdk1), which phosphorylates and activates the agc kinase members regulated by pi 3-kinase. We also discuss whether inhibitors of pdk1 might have chemotherapeutic potential in the treatment of cancers in which the pdk1-regulated agc kinases are constitutively activated.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-191490		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-190344		Homo sapiens
pmid	sentence
Other

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-269853		in vitro
pmid	sentence
10366608	In addition, we identified threonine 830 as a potential PKC phosphorylation site.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-179291		Homo sapiens
pmid	sentence
18593525	The hrh1 predominantly couples to g?q/11 proteins, leading to the activation of phospholipase c (plc) and subsequent release of the second messengers inositol trisphosphate (ip3) and diacylglycerol (dag) followed by the activation of pkc and the release of [ca2+]i.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, Thyroid Hormone Metabolism, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-256283		Homo sapiens
pmid	sentence
16297876	We demonstrated that both Elk-1 and MZF-1 were highly expressed in human poor differentiated HCC cells and involved in the up-regulation of PKCa, which was essential for cell migration and invasion. Over-expression assay confirmed that the PKCa expression may be modulated by these two factors at the transcriptional level.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-99307		Homo sapiens
pmid	sentence
12645577	TNF-alpha Binds to tnfr1 and activates pc-plc to induce pkc? And c-src activation

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-271836
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-256266		Homo sapiens	Hep-G2 Cell
pmid	sentence
15730925	PKC-alpha asODN (antisense oligonucleotides) could inhibit the growth and proliferation of HepG2 and induce its apoptosis by blocking the cell signal transduction related to PKC-alpha in vitro, and may be potentially used in the prevention and management of recurrent and metastatic HCC.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-248991		in vitro
pmid	sentence
9374536	In contrast, phosphorylation of the A isoform with PKC caused a significant decrease in activity whether assayed in the presence or absence of calcium/calmodulin (to _25% of the unphosphorylated enzyme activity).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-263165		in vitro
pmid	sentence
12077120	TNF-α rapidly increases the concentration of functionally active RGS7 protein through two mechanisms. TNF-induced dephosphorylation of serine 434 liberates RGS7 from 14-3-3 binding and inhibition. , PKC α catalyzes the incorporation of phosphate into a truncation of RGS7 fused to maltose-binding protein (MBP.RGS7315–469).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-256282		Homo sapiens
pmid	sentence
16297876	We demonstrated that both Elk-1 and MZF-1 were highly expressed in human poor differentiated HCC cells and involved in the up-regulation of PKCa, which was essential for cell migration and invasion. Over-expression assay confirmed that the PKCa expression may be modulated by these two factors at the transcriptional level.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270278		in vitro
pmid	sentence
15894802	Thus, we showed that it is phosphorylation of Ser-839, not Thr-840, that is absolutely required for the unique Ca2+ oscillations produced by mGluR5 activation. The Thr-840 residue is important only in that it is permissive for the PKC-dependent phosphorylation of Ser-839.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Organism
SIGNOR-256336		Homo sapiens
pmid	sentence
26010542	The luciferase reporter assay results revealed that the presence of both MZF-1 and Elk-1 significantly contributed to the upregulation of PKCα gene transcription activity.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-256660		Homo sapiens	Hep-G2 Cell
pmid	sentence
15730925	PKC-alpha asODN (antisense oligonucleotides) could inhibit the growth and proliferation of HepG2 and induce its apoptosis by blocking the cell signal transduction related to PKC-alpha in vitro, and may be potentially used in the prevention and management of recurrent and metastatic HCC.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-268178		Rattus norvegicus	Hippocampal Cell Line
pmid	sentence
16554470	We show that protein interacting with C-kinase 1 (PICK1) recruits activated protein kinase Cα (PKCα) to MycUNC5A at the plasma membrane, stimulating its endocytosis. We identify two PKCα phosphorylation sites at serines 408 and 587, as well as dileucine internalization motifs, which are required for this endocytosis.

Publications:

1

Organism:

Rattus Norvegicus

Pathways:

Axon guidance

Identifier	Residue	Organism
SIGNOR-17809		Homo sapiens
pmid	sentence
1357097	These results suggest that the activation of protein kinase c by both arachidonic acid and phorbol esters may play a role in the potentiation of glutamate exocytosis.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279099		Homo sapiens
pmid	sentence
26206583	PKCalpha directly promoted the basal phosphorylation of endogenous myocardin at serine and threonine residues.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-279257		Homo sapiens
pmid	sentence
22031842	PKC\u03b1 then phosphorylates and activates endothelial cell protein tyrosine phosphatase 1B (PTP1B) , .

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-251559		Homo sapiens
pmid	sentence
12629049	Activation of PKC depends on the availability of DAG,a signaling lipid that is tightly and dynamically regulated.

Publications:

1

Organism:

Homo Sapiens

Pathways:

B-cell activation, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-58506		Homo sapiens
pmid	sentence
9651347	Our results indicate that ca2+ ions not only anchor the protein to membrane surfaces but also induce conformational changes resulting in pkc activation.

Identifier	Residue	Organism
SIGNOR-198822		Homo sapiens
pmid	sentence
22944199	The wnt/ca2+ signaling pathway is defined by the activation of plc (phospholipase c) through wnt/fzd resulting in an increase in intracellular ca2+ levels, which activate pkcs (protein kinase c) and camkii (calcium-calmodulin-dependent kinase ii) or cn (calcineurin), a phosphatase that activates the transcription factor nfat (nuclear factor of activated t cell).

Publications:

2

Organism:

Homo Sapiens

Tissue:

Muscle, Skeletal Muscle

Pathways:

Axon guidance, B-cell activation, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling

Identifier	Residue	Organism
SIGNOR-280081		Homo sapiens
pmid	sentence
24481838	PKC\u03b1\nnormally phosphorylates and inactivates NF2.\|PKCalpha normally phosphorylates and inactivates NF2.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism	Cell Line
SIGNOR-227489		Homo sapiens	HEK-293 Cell
pmid	sentence
22544755	The Par complex member Par-6, previously thought to inhibit aPKC, is a potent activator of aPKC in our assays. Par-6 and aPKC interact via PB1 domain heterodimerization, and this interaction activates aPKC by displacing the pseudosubstrate, although full activity requires the Par-6 CRIB-PDZ domains.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-248848		in vitro
pmid	sentence
1375933	We now report that NOS is stoichiometrically phosphorylated by cAMP dependent protein kinase, protein kinase C, and calcium/calmodulin-dependent protein kinase, with each kinase phosphorylating a different serine site on NOS.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-261981
pmid	sentence
16969355	Midostaurin (PKC412A), N-benzoyl-staurosporine, potently inhibits protein kinase C alpha (PKCalpha), VEGFR2, KIT, PDGFR and FLT3 tyrosine kinases

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-271618		Homo sapiens	U2-OS Cell
pmid	sentence
17069764	In this report, we demonstrated that LUBAC, a ubiquitin ligase complex, is an E3 of activated cPKCs. LUBAC preferentially bound PMA-activated PKCa and PKCbII and their constitutively active mutants (Fig. 2). degradation of PMA-activated PKCa was delayed in HOIL-1L/-MEF (Fig. 3F). These results indicate that LUBAC is the ubiquitin ligase that induces ubiquitination and degradation of activated cPKCs.

Publications:

1

Organism:

Homo Sapiens

Name	PRKCA View Modifications
Full Name	Protein kinase C alpha type
Synonyms	PKC-A, PKC-alpha \| PKCA, PRKACA
Primary ID	P17252
Links	- -
Type	protein
Relations	436
Pathways	GPCR_Breast Cancer, Axon guidance, B-cell activation, GPCR_CRC, GPCR_HCC, Mitochondrial dynamics in T cell exhaustion, T cell activation, Thyroid Hormone Metabolism, VEGF Signaling
Inhibitors	3-(1-methyl-3-indolyl)-4-[1-[1-(2-pyridinylmethyl)-4-piperidinyl]-3-indolyl]pyrrole-2,5-dione; bisindolylmaleimide i; midostaurin
Function	Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42 (PubMed:28028151). Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA). Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription. Phosphorylates SOCS2 at 'Ser-52' facilitating its ubiquitination and proteosomal degradation (By similarity).

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