Relation Results

Identifier	Residue	Sequence
SIGNOR-250638	Ser103	RGLKRSLsEMEIGMV
pmid	sentence
10753652	Skeletal muscle CaMKII enriches in nuclei and phosphorylates myogenic factor SRF at multiple sites. \| Microsequencing of these phosphorylated peptides identified that both Ser-103 and a novel residue, Thr-160 in the MADS box of SRF, were sites of phosphorylation. \| The location of Thr-160 in the 3-D structure of SRF suggests that its phosphorylation by nuclear CaMKII may directly influence DNA binding of SRF and other MADS box factors.

Identifier	Residue	Sequence
SIGNOR-250639	Thr160	NKLRRYTtFSKRKTG
pmid	sentence
10753652	Skeletal muscle CaMKII enriches in nuclei and phosphorylates myogenic factor SRF at multiple sites. \| Microsequencing of these phosphorylated peptides identified that both Ser-103 and a novel residue, Thr-160 in the MADS box of SRF, were sites of phosphorylation. \| The location of Thr-160 in the 3-D structure of SRF suggests that its phosphorylation by nuclear CaMKII may directly influence DNA binding of SRF and other MADS box factors.

Publications:

2

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250619	Ser1064	SCPIKEDsFLQRYSS	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250620	Ser1070	DSFLQRYsSDPTGAL	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250621	Ser1071	SFLQRYSsDPTGALT	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250622	Ser1081	TGALTEDsIDDTFLP	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250623	Ser1120	QPLNPAPsRDPHYQD	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250624	Ser1166	QKGSHQIsLDNPDYQ	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250625	Ser768	DEAYVMAsVDNPHVC	Homo sapiens	HEK-293 Cell
pmid	sentence
10347170	We show that serines 1046/1047 are sites for CaM kinase II phosphorylation, although there is a preference for serine 1047, which resides within the consensus -R-X-X-S-. In addition, we have identified major phosphorylation sites at serine 1142 and serine 1057, which lie within a novel -S-X-D- consensus. Mutation of serines 1046/1047 in full-length EGFR enhanced both fibroblast transformation and tyrosine autokinase activity that was significantly potentiated by additional mutation of serines 1057 and 1142. A single CaM kinase II site was also identified at serine 744 within sub-kinase domain III, and autokinase activity was significantly affected by mutation of this serine to an aspartic acid making this site appear constitutively phosphorylated. We have addressed the mechanism by which CaM kinase II phosphorylation of the EGFR might regulate receptor autokinase activity and show that this modification can hinder association of the cytoplasmic tail with the kinase domain to prevent an enzyme-substrate interaction.

Publications:

7

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262687	Ser1073	PPLQRGKsQQLTVSA	in vitro
pmid	sentence
14970204	Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. The Major Phosphorylation Sites, Serines 764/765, 1058, and 1123, All Contribute to Regulation of GAP Activity of synGAP by CaMKII

Identifier	Residue	Sequence	Organism
SIGNOR-262688	Ser1138	PSITKQHsQTPSTLN	in vitro
pmid	sentence
14970204	Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. We identify four major sites of phosphorylation, serines 1123, 1058, 750/751/756, and 764/765.

Identifier	Residue	Sequence	Organism
SIGNOR-262689	Ser779	FMARGLNsSMDMARL	in vitro
pmid	sentence
14970204	Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. The Major Phosphorylation Sites, Serines 764/765, 1058, and 1123, All Contribute to Regulation of GAP Activity of synGAP by CaMKII

Identifier	Residue	Sequence	Organism
SIGNOR-262690	Ser780	MARGLNSsMDMARLP	in vitro
pmid	sentence
14970204	Here we show that phosphorylation of synGAP by Ca(2+)/calmodulin-dependent protein kinase II increases its Ras GTPase-activating activity by 70-95%. We identify four major sites of phosphorylation, serines 1123, 1058, 750/751/756, and 764/765.

Identifier	Residue	Sequence	Organism
SIGNOR-262691	Thr1077	RGKSQQLtVSAAQKP	in vitro
pmid	sentence
15358237	Certain phosphopeptides were detected only in samples phosphorylated in vitro under conditions that favor CaMKII activity (Mg2+-ATP, Ca2+, calmodulin, and peptide inhibitors of PKA and PKC). In samples phosphorylated in vitro in the presence of Ca2+/calmodulin, we also detected the peptide (R)GKSQQLTVSAAQKPR with phosphorylated residues corresponding to S-1058 and T-1062 of synaptic ras GTPase activating protein (SynGAP).

Publications:

5

Organism:

In Vitro

Pathways:

Glutamatergic synapse

Identifier	Residue	Sequence
SIGNOR-275863	Ser109	ERHRRINsKKKESAW
pmid	sentence
14754994	Identification of an N-terminal amino acid of the CLC-3 chloride channel critical in phosphorylation-dependent activation of a CaMKII-activated chloride current\|The N-terminus of CLC-3, which contains a CaMKII consensus sequence, was phosphorylated by CaMKII in vitro, and mutation of the serine at position 109 (S109A) abolished the CaMKII-dependent Cl(-) conductance, indicating that this residue is important in the gating of CLC-3 at the plasma membrane.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-82966	Ser110	SFSEQTRsLDGRLQV	Homo sapiens
pmid	sentence
11027280	Smad2 is a target substrate for cam kinase ii in vitro at serine-110, -240, and -260. furthermore, cam kinase ii blocked nuclear accumulation of a smad2 and induced smad2-smad4 hetero-oligomerization independently of tgfbeta receptor activation, while preventing tgf-beta-dependent smad2-smad3 interactions.

Identifier	Residue	Sequence	Organism
SIGNOR-82970	Ser240	SDQQLNQsMDTGSPA	Homo sapiens
pmid	sentence
11027280	Smad2 is a target substrate for cam kinase ii in vitro at serine-110, -240, and -260. furthermore, cam kinase ii blocked nuclear accumulation of a smad2 and induced smad2-smad4 hetero-oligomerization independently of tgfbeta receptor activation, while preventing tgfbeta-dependent smad2-smad3 interactions.

Identifier	Residue	Sequence	Organism
SIGNOR-82974	Ser260	TLSPVNHsLDLQPVT	Homo sapiens
pmid	sentence
11027280	Smad2 is a target substrate for cam kinase ii in vitro at serine-110, -240, and -260. furthermore, cam kinase ii blocked nuclear accumulation of a smad2 and induced smad2-smad4 hetero-oligomerization independently of tgfbeta receptor activation, while preventing tgfbeta-dependent smad2-smad3 interactions.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-137614	Ser116	KDIIRQPsEEEIIKL	Homo sapiens
pmid	sentence
15916534	Pea-15 is a phosphoprotein containing a ser-104 phosphorylated by protein kinase c and a ser-116 phosphorylated by camkii (calcium/calmodulin-dependent protein kinase ii) or akt. Phosphorylation of ser-104 is implicated in the regulation of glucose metabolism, while phosphorylation at ser-116 is required for pea-15 recruitment to the disc (death-initiation signalling complex)

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-262684	Ser120	ARLAREKsQDGGELT	in vitro
pmid	sentence
18480293	Homer3 is phosphorylated at Ser120, Ser159, and Ser176 by CaMKII in vitro. Homer3 phosphorylation reduces its affinity for target molecules and modulates the Ca2+ signaling patterns induced by mGluR1α activation

Identifier	Residue	Sequence	Organism
SIGNOR-262685	Ser159	EKLFRSQsADAPGPT	in vitro
pmid	sentence
18480293	Homer3 is phosphorylated at Ser120, Ser159, and Ser176 by CaMKII in vitro. Homer3 phosphorylation reduces its affinity for target molecules and modulates the Ca2+ signaling patterns induced by mGluR1α activation

Identifier	Residue	Sequence	Organism
SIGNOR-262686	Ser176	ERLKKMLsEGSVGEV	in vitro
pmid	sentence
18480293	Homer3 is phosphorylated at Ser120, Ser159, and Ser176 by CaMKII in vitro. Homer3 phosphorylation reduces its affinity for target molecules and modulates the Ca2+ signaling patterns induced by mGluR1α activation

Publications:

3

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-250626	Ser13	ITSAARRsYVSSGEM	in vitro
pmid	sentence
7822264	On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II.

Identifier	Residue	Sequence	Organism
SIGNOR-250627	Ser17	ARRSYVSsGEMMVGG	in vitro
pmid	sentence
7822264	On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II.

Identifier	Residue	Sequence	Organism
SIGNOR-250628	Ser38	LGPGTRLsLARMPPP	in vitro
pmid	sentence
7822264	On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II.

Identifier	Residue	Sequence	Organism
SIGNOR-250629	Ser393	NLQIRETsLDTKSVS	in vitro
pmid	sentence
7822264	On the other hand, GFAP was phosphorylated to approximately 1.9 mol of phosphate/mol of GFAP by Ca(2+)-CaM-dependent protein kinase II, and this phosphorylation did induce disassembly of the filament. Sequential analysis of the purified phosphopeptides revealed that only Ser8 on GFAP was phosphorylated by cdc2 kinase, whereas Ser13, Ser17, Ser34, and Ser389 on GFAP were phosphorylated by Ca(2+)-CaM-dependent protein kinase II.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Cell Line
SIGNOR-250630	Ser1303	NKLRRQHsYDTFVDL	Hippocampal Cell Line
pmid	sentence
8940188	By peptide mapping, automated sequencing, and mass spectrometry, we identified the major site of phosphorylation on the fusion protein as Ser-383, corresponding to Ser-1303 of full-length NR2B. The Km for phosphorylation of this site in the fusion protein was approximately 50 nM, much lower than that of other known substrates for CaM kinase II, suggesting that the receptor is a high affinity substrate. We show that serine 1303 in the full-length NR2B and/or the cognate site in NR2A is a major site of phosphorylation of the receptor both in the postsynaptic density fraction and in living hippocampal neurons.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-59137	Ser142	RKILNDLsSDAPGVP	Homo sapiens
pmid	sentence
9668047	Phosphorylation of creb1 at ser142 and ser143 is selectively activated by ca(2+) influx;phosphorylation of ser142 and ser143, disrupts the interaction of creb with its cofactor cbp. Phosphorylation of serine 142 in creb by camkii leads to dissociation of the creb dimer.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-117344	Ser142	RKILNDLsSDAPGVP	Homo sapiens	Neuron
pmid	sentence
11970864	Phosphorylation of creb1 at ser142 and ser143 is selectively activated by ca(2+) influx;phosphorylation of ser142 and ser143, disrupts the interaction of creb with its cofactor cbp. Phosphorylation of serine 142 in creb by camkii leads to dissociation of the creb dimer.

Identifier	Residue	Sequence	Organism
SIGNOR-82501	Ser142	RKILNDLsSDAPGVP	Homo sapiens
pmid	sentence
11013247	Phosphorylation of creb1 at ser142 and ser143 is selectively activated by ca(2+) influx;phosphorylation of ser142 and ser143, disrupts the interaction of creb with its cofactor cbp. Phosphorylation of serine 142 in creb by camkii leads to dissociation of the creb dimer.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-250634	Ser1439	IQTKGQRsMDGYPEQ
pmid	sentence
11160423	In contrast, phosphorylation of densin-180 by CaMKII at serine-1397 only slightly decreases its affinity for CaMKII. The specific interaction of densin-180 with holoenzymes of CaMKII containing only alpha-subunit and the increased affinity of CaMKII for densin-180 after autophosphorylation suggest that densin-180 may be involved in localization of activated CaMKII synthesized in dendrites.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-156064	Ser155	CLEDIHTsRVVAHVL	Homo sapiens
pmid	sentence
17568776	Phosphorylation of pirh2 by calmodulin-dependent kinase ii impairs its ability to ubiquitinate p53

Identifier	Residue	Sequence	Organism
SIGNOR-156068	Thr154	ICLEDIHtSRVVAHV	Homo sapiens
pmid	sentence
17568776	Phosphorylation of pirh2 by calmodulin-dependent kinase ii impairs its ability to ubiquitinate p53

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-263113	Ser1575	PEICRTVsGDLAAEE	in vitro
pmid	sentence
20937870	To identify the regulatory sites of phosphorylation under physiologically relevant conditions, Ca(V)1.1 channels were purified from skeletal muscle and sites of phosphorylation on the α1 subunit were identified by mass spectrometry. Two phosphorylation sites were identified in the proximal C-terminal domain, serine 1575 (S1575) and threonine 1579 (T1579), which are conserved in cardiac Ca(V)1.2 channels (S1700 and T1704, respectively). In vitro phosphorylation revealed that Ca(V)1.1-S1575 is a substrate for both cAMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II, whereas Ca(V)1.1-T1579 is a substrate for casein kinase 2.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-59354	Ser16	KELEKRAsGQAFELI	Homo sapiens	JURKAT Cell
pmid	sentence
9686569	Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. In vitro, ser16 of recombinant human stathmin was phosphorylated also by purified cam kinase ii, and in vivo, cam kinase ii activity was indeed stimulated in cd2-triggered jurkat cells. Altogether, our results favor an association of cam kinase ii activity with costimulatory signals of t lymphocyte activation and phosphorylation of stathmin on ser16.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149640	Ser16	KELEKRAsGQAFELI	Homo sapiens	JURKAT Cell
pmid	sentence
16982419	Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. In vitro, ser16 of recombinant human stathmin was phosphorylated also by purified cam kinase ii, and in vivo, cam kinase ii activity was indeed stimulated in cd2-triggered jurkat cells. Altogether, our results favor an association of cam kinase ii activity with costimulatory signals of t lymphocyte activation and phosphorylation of stathmin on ser16.

Publications:

2

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-20912	Ser19	KGFRRAVsELDAKQA	Homo sapiens
pmid	sentence
1680128	This increase in ser19 phosphorylation was associated with enhanced th activity and was due, in part, to glutamate-receptor-mediated calcium influx and possibly calcium/calmodulin-dependent protein kinase ii (camkii) activation.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-260907	Ser192	NLEKNIPsSASGFSR	in vitro
pmid	sentence
16407128	CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit. \| these results implicate the 192RSST motif of Emi2 as a critical molecular target of CaMKII during CSF release

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-149684	Ser2120	ERRQPSSsSSEKQRF	Homo sapiens	Neuron
pmid	sentence
16982421	Here, we report a direct modulation of ca(v)2.2 channel inactivation properties by 14-3-3, a family of signaling proteins involved in a wide range of biological processes.Wild-type gst fusion proteins containing the putative 14-3-3-binding motif (aa 2076__?2140) werein vitro phosphorylated at s2126 by either camkii or pka, as detected by thesequence- and phosphorylation-specific antibody, anti-ps2126 (middle panel). Phosphorylation of s2126 significantly increases its binding to recombinant 14-3-3?

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Cell Line
SIGNOR-250631	Ser230	PKYSRQFsLEHVHGS	K-562 Cell
pmid	sentence
11447121	Ser230 is located in the regulatory domain of HSF1, and promotes the magnitude of the inducible transcriptional activity. Ser230 lies within a consensus site for calcium/calmodulin-dependent protein kinase II (CaMKII), and CaMKII overexpression enhances both the level of in vivo Ser230 phosphorylation and transactivation of HSF1. The importance of Ser230 was further established by the S230A HSF1 mutant showing markedly reduced activity relative to wild-type HSF1 when expressed in hsf1(-/-) cells.

Publications:

1

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250618	Ser232	ITLERGNsGLGFSIA	Chlorocebus aethiops	COS-7 Cell
pmid	sentence
12933808	Synapse-associated protein 97 (SAP97), a member of membrane-associated guanylate kinase protein family, has been implicated in the processes of targeting ionotropic glutamate receptors at postsynaptic sites. \| We show here that SAP97 is directly associated with NR2A through its PDZ1 domain, and CaMKII-dependent phosphorylation of SAP97-Ser-232 disrupts NR2A interaction both in an in vitro pull-out assay and in transfected COS-7 cells. Moreover, expression of SAP97(S232D) mutant has effects similar to those observed upon constitutively activating CaMKII.

Publications:

1

Organism:

Chlorocebus Aethiops

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103886	Ser242	PSAPPDRsKGAEPSQ	Homo sapiens	Neuron
pmid	sentence
12871946	Two serine residues in rim1 (ser-241 and ser-287) and one serine residue in rim2 (ser-335) were required for 14-3-3 binding. Incubation with ca2+/calmodulin-dependent protein kinase ii greatly stimulated the interaction of recombinant n-terminal rim but not the s241/287a mutant with 14-3-3,

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-103890	Ser288	NGKGALKsERKRVPK	Homo sapiens	Neuron
pmid	sentence
12871946	Two serine residues in rim1 (ser-241 and ser-287) and one serine residue in rim2 (ser-335) were required for 14-3-3 binding. Incubation with ca2+/calmodulin-dependent protein kinase ii greatly stimulated the interaction of recombinant n-terminal rim but not the s241/287a mutant with 14-3-3,

Publications:

2

Organism:

Homo Sapiens

Tissue:

Brain

Pathways:

Neurotransmitters release

Identifier	Residue	Sequence	Organism
SIGNOR-191773	Ser2426	ASGDRPPsVSSVHSE	Homo sapiens
pmid	sentence
22888005	We demonstrated that camkii directly bound and phosphorylated smrt at ser-1407, thereby facilitating smrt translocation from the nucleus to the cytoplasm and proteasome-dependent degradation.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-183596	Ser246	FPKSRLSsVSVTYCS	Homo sapiens
pmid	sentence
19182667	Camkii caused ets-2 phosphorylation.Serine 246, 310, and 313 were the targets. Camkii to phosphorylates ets-2, thus altering ets-2 binding to its downstream promoters

Identifier	Residue	Sequence	Organism
SIGNOR-183600	Ser310	LDVQRVPsFESFEDD	Homo sapiens
pmid	sentence
19182667	Camkii caused ets-2 phosphorylation.Serine 246, 310, and 313 were the targets. Camkii to phosphorylates ets-2, thus altering ets-2 binding to its downstream promoters

Identifier	Residue	Sequence	Organism
SIGNOR-183604	Ser313	QRVPSFEsFEDDCSQ	Homo sapiens
pmid	sentence
19182667	Camkii caused ets-2 phosphorylation.Serine 246, 310, and 313 were the targets. Camkii to phosphorylates ets-2, thus altering ets-2 binding to its downstream promoters

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-96330	Ser251	GKLGGQDsFESIESY	Homo sapiens	T-lymphocyte
pmid	sentence
12475968	Treatment of ets1 by t-cell nuclear extract or phosphorylation of these four serines by calmodulin-dependent kinase ii (camk ii) has recently been reported to decrease ets1 dna binding by reinforcing autoinhibition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-96334	Ser257	DSFESIEsYDSCDRL	Homo sapiens	T-lymphocyte
pmid	sentence
12475968	Treatment of ets1 by t-cell nuclear extract or phosphorylation of these four serines by calmodulin-dependent kinase ii (camk ii) has recently been reported to decrease ets1 dna binding by reinforcing autoinhibition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-96338	Ser282	NSLQRVPsYDSFDSE	Homo sapiens	T-lymphocyte
pmid	sentence
12475968	Treatment of ets1 by t-cell nuclear extract or phosphorylation of these four serines by calmodulin-dependent kinase ii (camk ii) has recently been reported to decrease ets1 dna binding by reinforcing autoinhibition

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-96342	Ser285	QRVPSYDsFDSEDYP	Homo sapiens	T-lymphocyte
pmid	sentence
12475968	Treatment of ets1 by t-cell nuclear extract or phosphorylation of these four serines by calmodulin-dependent kinase ii (camk ii) has recently been reported to decrease ets1 dna binding by reinforcing autoinhibition

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-158486	Ser261	CNLSRVDsTTCLFPV	Homo sapiens
pmid	sentence
17941647	Amp-activated protein kinase and calcium/calmodulin-dependent kinase ii were identified to phosphorylate specifically ser243 in vitro. Phosphorylation by these two kinases results in an increase of enzymatic activity by 1.4-fold. These findings suggest for the first time that hgfat1 may be regulated by kinases other than pka.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-79678	Ser268	LKSVRMLsGSKEKDR	Homo sapiens
pmid	sentence
10908300	The decrease in mu-opioid receptor activity after chronic agonist exposure (1 microm [d-ala(2),n-mephe(4),gly-ol(5)]-enkephalin) is largely due to kinase-mediated phosphorylation of intracellular receptor domains. We have recently shown that the substitution of two putative ca(2+)/calmodulin-dependent protein kinase ii (camk ii) phosphorylation sites, s261 and s266, by alanines in the third intracellular loop of the rat mu-opioid receptor (rmor1) confers resistance to camk ii-induced receptor desensitization.

Identifier	Residue	Sequence	Organism
SIGNOR-79682	Ser270	SVRMLSGsKEKDRNL	Homo sapiens
pmid	sentence
10908300	The decrease in mu-opioid receptor activity after chronic agonist exposure (1 microm [d-ala(2),n-mephe(4),gly-ol(5)]-enkephalin) is largely due to kinase-mediated phosphorylation of intracellular receptor domains. We have recently shown that the substitution of two putative ca(2+)/calmodulin-dependent protein kinase ii (camk ii) phosphorylation sites, s261 and s266, by alanines in the third intracellular loop of the rat mu-opioid receptor (rmor1) confers resistance to camk ii-induced receptor desensitization.

Identifier	Residue	Sequence	Organism
SIGNOR-79686	Thr372	STRIRQNtRDHPSTA	Homo sapiens
pmid	sentence
10908300	The decrease in mu-opioid receptor activity after chronic agonist exposure (1 microm [d-ala(2),n-mephe(4),gly-ol(5)]-enkephalin) is largely due to kinase-mediated phosphorylation of intracellular receptor domains. We have recently shown that the substitution of two putative ca(2+)/calmodulin-dependent protein kinase ii (camk ii) phosphorylation sites, s261 and s266, by alanines in the third intracellular loop of the rat mu-opioid receptor (rmor1) confers resistance to camk ii-induced receptor desensitization.

Publications:

3

Organism:

Homo Sapiens

Tissue:

Kidney

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-264408	Ser272	CSLERQLsLEQEVQQ	Homo sapiens	HeLa Cell
pmid	sentence
18978352	Phosphorylation of serine 271 on 5-lipoxygenase and its role in nuclear export\|We report here that 5-LO is constitutively phosphorylated on Ser-271 in transfected NIH 3T3 cells. This residue is nested in a classical nuclear export sequence, and phosphorylated Ser-271 5-LO was exclusively found in the nucleus by immunofluorescence and by fractionation techniques\|Nuclear export of 5-LO can also be induced by KN-93, an inhibitor of Ca2+/calmodulin-dependent kinase II, and the effects of SB 203,580 plus KN-93 are additive. Finally, HeLa cells, which lack nuclear 5-LO, also lack constitutive phosphorylation of Ser-271. Taken together, these results indicate that the phosphorylation of Ser-271 serves to inhibit the nuclear export of 5-LO.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276382	Ser31	LKLGSGPsIKALDGR	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276381	Ser87	PLKQKQPsFSAKKMT	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276383	Ser89	KQKQPSFsAKKMTEK	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-276377	Thr66	ATRKALGtVNRATEK	Homo sapiens	HeLa Cell
pmid	sentence
24781523	CaMKII phosphorylates securin at PP2A substrate site(s).Securin is destabilized by phosphorylation and stabilized by PP2A-dependent dephosphorylation on separase

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-17308	Ser314	MLATRNFsGGKSGGN	Homo sapiens
pmid	sentence
1324926	After removal of ca2+/calmodulin, the autonomous kinase undergoes a burst of inhibitory autophosphorylation at sites distinct from the autonomy site. Ca(2+)-independent autophosphorylation occurs within the calmodulin binding domain at thr305, thr306, and ser314

Identifier	Residue	Sequence	Organism
SIGNOR-17312	Thr305	KLKGAILtTMLATRN	Homo sapiens
pmid	sentence
1324926	After removal of ca2+/calmodulin, the autonomous kinase undergoes a burst of inhibitory autophosphorylation at sites distinct from the autonomy site. Ca(2+)-independent autophosphorylation occurs within the calmodulin binding domain at thr305, thr306, and ser314

Identifier	Residue	Sequence	Organism
SIGNOR-17316	Thr306	LKGAILTtMLATRNF	Homo sapiens
pmid	sentence
1324926	After removal of ca2+/calmodulin, the autonomous kinase undergoes a burst of inhibitory autophosphorylation at sites distinct from the autonomy site. Ca(2+)-independent autophosphorylation occurs within the calmodulin binding domain at thr305, thr306, and ser314

Publications:

3

Organism:

Homo Sapiens

Pathways:

Axon guidance, Glutamatergic synapse, Neurotransmitters release

Identifier	Residue	Sequence	Organism
SIGNOR-250617	Ser325	EQLSRELsTLRNLFK	in vitro
pmid	sentence
1314426	These studies implicate Ser276 of CIEBPP as the major in vim phosphorylation site for CaMKII. \| Phosphorylation of serine at position 276 within the leucine zipper of C/EBP beta appeared to confer calcium-regulated transcriptional stimulation of a promoter that contained binding sites for C/EBP beta.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-276429	Ser356	KAMGDEDsGDSDTSP	in vitro
pmid	sentence
23143515	CaMKIIα activated by the NMDA receptor phosphorylates GKAP Ser54 to induce polyubiquitination of GKAP.

Publications:

1

Organism:

In Vitro

Pathways:

Glutamatergic synapse

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-277367	Ser36	GEVVRCLsEQSVAIS	Homo sapiens	SK-N-SH Cell
pmid	sentence
29079782	Here we show that CaMKII can directly phosphorylate Beclin 1 at Ser90 to promote K63-linked ubiquitination of Beclin 1 and activation of autophagy.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266434	Ser362	FYTLNGSsVDSQPQS	Homo sapiens	E-18 Rat Primary Hippocampal Neuron
pmid	sentence
24614225	NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266442	Ser362	FYTLNGSsVDSQPQS	Homo sapiens	E-18 Rat Primary Hippocampal Neuron
pmid	sentence
24614225	NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266433	Ser772	LFKKIFPsLELNITD	Homo sapiens	E-18 Rat Primary Hippocampal Neuron
pmid	sentence
24614225	NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-266441	Ser772	LFKKIFPsLELNITD	Homo sapiens	E-18 Rat Primary Hippocampal Neuron
pmid	sentence
24614225	NMDA treatment of cultured hippocampal neurons causes recruitment of CYLD, as well as CaMKII, to the postsynaptic density (PSD), as shown by immunoelectron microscopy, […] Purified CaMKII phosphorylates CYLD on at least three residues (S-362, S-418, and S-772 on the human CYLD protein Q9NQC7-1) and promotes its deubiquitinase activity.

Publications:

4

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-250616	Ser38	KLKERWGsNELPAEE	Homo sapiens	HEK-293 Cell
pmid	sentence
7929371	SERCA2 and SERCA2 mutants S38A, S167A, and S531A were expressed in HEK-293 cells and tested for phosphorylation with CaM kinase. Mutant S38A was not phosphorylated, while mutants S167A and S531A were phosphorylated, suggesting that Ser38 is the site of CaM kinase phosphorylation in SERCA2. This conclusion was supported by the observation that phosphorylation of SERCA2 and mutants S167A and S531A by CaM kinase increased the Vmax for Ca2+ transport, while the Vmax for Ca2+ transport by mutant S38A was unaffected by exposure to a phosphorylation reaction mix.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-124344	Ser398	WKRLRSHsRQYVSGL	Homo sapiens
pmid	sentence
15107581	As we have shown previously, human h1r can be phosphorylated in vitro by several kinases includingpka, pkc, pkg, and camk ii in summary, these data suggest that thr140, thr142, ser396, ser398, and thr478 can be phosphorylated by the kinases described above (table 2).

Identifier	Residue	Sequence	Organism
SIGNOR-124348	Thr140	LRYLKYRtKTRASAT	Homo sapiens
pmid	sentence
15107581	As we have shown previously, human h1r can be phosphorylated in vitro by several kinases includingpka, pkc, pkg, and camk ii in summary, these data suggest that thr140, thr142, ser396, ser398, and thr478 can be phosphorylated by the kinases described above (table 2).

Publications:

2

Organism:

Homo Sapiens

Tissue:

Ovary

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275770	Ser516	LSLTRGLsRTSMKPR	Homo sapiens	Neuron
pmid	sentence
33410863	Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate–activated protein kinase (AMPK)–dependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).\|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. \| Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275771	Ser571	PWPLRRTsAQGQPSP	Homo sapiens	Neuron
pmid	sentence
33410863	Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate–activated protein kinase (AMPK)–dependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).\|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. \| Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5

Identifier	Residue	Sequence	Organism
SIGNOR-275772	Thr594	LHGKKNStVDCNGVV	Homo sapiens
pmid	sentence
33410863	Among the sites identified, only six were previously suggested to be the targets for specific kinases using in silico and/or in vitro analyses: S36 and S525 were attributed to the regulation by PKA; S484 and S664 were assigned to the serum- and glucocorticoid-inducible kinase 3 (SGK3); and S516 and S571 were ascribed to CaMKII (reviewed in Marionneau and Abriel, 2015). In marked contrast, several previously described phosphorylation sites were not detected in the present study, including the PKA-dependent S528, the CaMKII-associated T594, the PKC-dependent S1506, the adenosine monophosphate‚Äìactivated protein kinase (AMPK)‚Äìdependent T101 (Liu et al., 2019), and the six Fyn-dependent tyrosines (Ahern et al., 2005; Iqbal et al., 2018).\|The simplest interpretation of these findings is that these three phosphorylation clusters, at positions S457-S460, S483-T486, and S664-S671, are likely involved in regulating the basal and/or gating properties of native cardiac NaV1.5 channels. Conversely, the other phosphorylation sites, with lower stoichiometries, may play spatially or temporally distinct roles in the physiological or more pathophysiological regulation of channel expression or gating. \| Remarkably, this MS analysis also revealed that the vast majority of identified phosphorylation sites (at least 26) are clustered, suggesting concomitant phosphorylation and roles in regulating channel expression and/or function. Unexpectedly, however, except for S664, S667, and S671, no apparent effects of phosphomimetic or phosphosilent mutations were observed on heterologously expressed (in HEK-293 cells) NaV1.5

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-276329	Ser521	WTNRLYEsFKASDPL	in vitro
pmid	sentence
21642394	In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475.

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Cell Line
SIGNOR-250633	Ser53	ISVSRSTsFRGGMGS	NIH-3T3 Cell
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. Expression of K18 ser-52-->ala mutant in mammalian cells showed minimal phosphorylation but no distinguishable difference in filament assembly when compared with wild-type K18. In contrast, the ser-52 mutation played a clear but nonexclusive role in filament reorganization,

Publications:

1

Identifier	Residue	Sequence
SIGNOR-250636	Ser54	KEILRQMsSPQSRNG
pmid	sentence
11331285	In this study, we report that Pd was rapidly phosphorylated by Ca(2+)/calmodulin-dependent kinase II, resulting in 100-fold greater inhibition of Gbetagamma binding than cAMP-dependent protein kinase phosphorylation. Furthermore, Pd phosphorylation by Ca(2+)/calmodulin-dependent kinase II at Ser-54 and Ser-73 led to binding of the phosphoserine-binding protein 14-3-3.

Identifier	Residue	Sequence
SIGNOR-250637	Ser73	ERVSRKMsIQEYELI
pmid	sentence
11331285	In this study, we report that Pd was rapidly phosphorylated by Ca(2+)/calmodulin-dependent kinase II, resulting in 100-fold greater inhibition of Gbetagamma binding than cAMP-dependent protein kinase phosphorylation. Furthermore, Pd phosphorylation by Ca(2+)/calmodulin-dependent kinase II at Ser-54 and Ser-73 led to binding of the phosphoserine-binding protein 14-3-3.

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-276331	Ser544	RSVTMRKsQRSSKGS	in vitro
pmid	sentence
21642394	In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475.

Identifier	Residue	Sequence	Organism
SIGNOR-276332	Ser547	TMRKSQRsSKGSEIL	in vitro
pmid	sentence
21642394	In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475.

Identifier	Residue	Sequence	Organism
SIGNOR-276333	Ser548	MRKSQRSsKGSEILL	in vitro
pmid	sentence
21642394	In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475.

Identifier	Residue	Sequence	Organism
SIGNOR-276330	Thr540	KRLSRSVtMRKSQRS	in vitro
pmid	sentence
21642394	In vitro phosphorylation assays revealed that CAMKII can directly phosphorylate Nox5 on Thr494 and Ser498 as detected by phosphorylation state-specific antibodies. Mass spectrometry (MS) analysis revealed the phosphorylation of additional, novel sites at Ser475, Ser502, and Ser675. Of these phosphorylation sites, mutation of only Ser475 to alanine prevented CAMKII-induced increases in Nox5 activity. Together, these results suggest that CAMKII can positively regulate Nox5 activity via the phosphorylation of Ser475.

Publications:

4

Organism:

In Vitro

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249316	Ser552	VVRTPPKsPSSAKSR	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
10090741	We found that when tau was first phosphorylated by A-kinase, C-kinase, cdk5, or CaM kinase II and then by GSK-3, its binding to microtubules was inhibited by 45, 61, 78, and 79%, respectively. Further, the kinase combinations cdk5/GSK-3 and CaM kinase II/GSK-3 rapidly phosphorylated the sites Thr 231 and Ser 235. When these sites were individually replaced by Ala and the phosphorylation experiments repeated, tau binding to microtubules was inhibited by 54 and 71%, respectively. By comparison, when Ser 262 was replaced by Ala, tau binding to microtubules was inhibited by only 8% after phosphorylation by CaM kinase II.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249314	Ser579	NVKSKIGsTENLKHQ	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
10090741	We found that when tau was first phosphorylated by A-kinase, C-kinase, cdk5, or CaM kinase II and then by GSK-3, its binding to microtubules was inhibited by 45, 61, 78, and 79%, respectively. Further, the kinase combinations cdk5/GSK-3 and CaM kinase II/GSK-3 rapidly phosphorylated the sites Thr 231 and Ser 235. When these sites were individually replaced by Ala and the phosphorylation experiments repeated, tau binding to microtubules was inhibited by 54 and 71%, respectively. By comparison, when Ser 262 was replaced by Ala, tau binding to microtubules was inhibited by only 8% after phosphorylation by CaM kinase II.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-249315	Thr548	KKVAVVRtPPKSPSS	Homo sapiens	Alzheimer Disease Specific Cell Type
pmid	sentence
10090741	We found that when tau was first phosphorylated by A-kinase, C-kinase, cdk5, or CaM kinase II and then by GSK-3, its binding to microtubules was inhibited by 45, 61, 78, and 79%, respectively. Further, the kinase combinations cdk5/GSK-3 and CaM kinase II/GSK-3 rapidly phosphorylated the sites Thr 231 and Ser 235. When these sites were individually replaced by Ala and the phosphorylation experiments repeated, tau binding to microtubules was inhibited by 54 and 71%, respectively. By comparison, when Ser 262 was replaced by Ala, tau binding to microtubules was inhibited by only 8% after phosphorylation by CaM kinase II.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275784	Ser561	PFLSRHNsKSSIFSF	Homo sapiens	Neuron
pmid	sentence
32611770	CaMKII enhances voltage-gated sodium channel Nav1.6 activity and neuronal excitability\|mmobilized peptide arrays and nanoflow LC-electrospray ionization/MS of Nav1.6 reveal potential sites of CaMKII phosphorylation, specifically Ser-561 and Ser-641/Thr-642 within the first intracellular loop of the channel.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275785	Ser641	RRSVKRNsTVDCNGV	Homo sapiens	Neuron
pmid	sentence
32611770	CaMKII enhances voltage-gated sodium channel Nav1.6 activity and neuronal excitability\|mmobilized peptide arrays and nanoflow LC-electrospray ionization/MS of Nav1.6 reveal potential sites of CaMKII phosphorylation, specifically Ser-561 and Ser-641/Thr-642 within the first intracellular loop of the channel.

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-275786	Thr642	RSVKRNStVDCNGVV	Homo sapiens	Neuron
pmid	sentence
32611770	CaMKII enhances voltage-gated sodium channel Nav1.6 activity and neuronal excitability\|mmobilized peptide arrays and nanoflow LC-electrospray ionization/MS of Nav1.6 reveal potential sites of CaMKII phosphorylation, specifically Ser-561 and Ser-641/Thr-642 within the first intracellular loop of the channel.

Publications:

3

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-22631	Ser643	CFTPKGSsLKIEERA	Homo sapiens
pmid	sentence
2170388	Smooth muscle caldesmon was phosphorylated by smooth muscle calmodulin-dependent protein kinase. Ii

Identifier	Residue	Sequence	Organism
SIGNOR-22635	Ser656	RAEFLNKsVQKSSGV	Homo sapiens
pmid	sentence
2170388	Smooth muscle caldesmon was phosphorylated by smooth muscle calmodulin-dependent protein kinase. Ii

Publications:

2

Organism:

Homo Sapiens

Tissue:

Smooth Muscle

Identifier	Residue	Sequence	Organism
SIGNOR-57376	Ser706	LNGEASKsQEMVHLV	Homo sapiens
pmid	sentence
9580567	We demonstrate here that cd44 is phosphorylated to high stoichiometry in resting cells and that ca(2+)/calmodulin-dependent protein kinase ii is a cd44 ser(325) kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-109502	Ser706	LNGEASKsQEMVHLV	Homo sapiens	Fibroblast
pmid	sentence
11463356	In previous studies we have demonstrated that a key control point for this receptor is the phosphorylation of CD44 on a conserved cytoplasmic serine residue, Ser(325). This modification is not required for efficient ligand binding, but is an essential component of CD44-dependent cell migration on a hyaluronan substratum. We demonstrate here that cd44 is phosphorylated to high stoichiometry in resting cells and that ca(2+)/calmodulin-dependent protein kinase ii is a cd44 ser(325) kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence
SIGNOR-275539	Ser782	APLATMEsLSDTESL
pmid	sentence
23502535	Activated CaMKII interacted with the C-terminal domain of DGLalpha, phosphorylated two serine residues and inhibited DGLalpha activity. \|CaMKIIalpha phosphorylates DGLalpha at Ser808 and Ser782

Identifier	Residue	Sequence
SIGNOR-275540	Ser808	RSIRGSPsLHAVLER
pmid	sentence
23502535	Activated CaMKII interacted with the C-terminal domain of DGLalpha, phosphorylated two serine residues and inhibited DGLalpha activity. \|CaMKIIalpha phosphorylates DGLalpha at Ser808 and Ser782

Publications:

2

Identifier	Residue	Sequence	Organism
SIGNOR-135631	Ser843	DVRLSRGsIDREDGS	Homo sapiens
pmid	sentence
15845548	Furthermore, activated camkii directly phosphorylated the recombinant cooh-terminal region of fak at a residue equivalent to ser-843.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Axon guidance

Identifier	Residue	Sequence
SIGNOR-250635	Ser852	SYKVRFNsVSSYSDS
pmid	sentence
10400690	It was found that purified recombinant nNOS was phosphorylated by CaM-K Ialpha, CaM-K IIalpha, and CaM-K IV at Ser847 in vitro. Replacement of Ser847 with Ala (S847A) prevented phosphorylation by CaM kinases. Phosphorylated recombinant wild-type nNOS at Ser847 (approximately 0.5 mol of phosphate incorporation into nNOS) exhibited a 30% decrease of Vmax with little change of both the Km for L-arginine and Kact for CaM relative to unphosphorylated enzyme. The activity of mutant S847D was decreased to a level 50-60% as much as the wild-type enzyme. The decreased NOS enzyme activity of phosphorylated nNOS at Ser847 and mutant S847D was partially due to suppression of CaM binding, but not to impairment of dimer formation which is thought to be essential for enzyme activation.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-58251	Ser855	EPMRRSVsEAALAQP	Homo sapiens
pmid	sentence
9636039	Phosphorylation of bovine hormone-sensitive lipase by the amp-activated protein kinase.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism
SIGNOR-97546	Ser862	IRNKARLsITGSVGE	Homo sapiens
pmid	sentence
12536214	Receptor internalization, altered;intracellular localization

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-166846	Ser868	ITRGEWQsEAQDTMK	Homo sapiens	Neuron
pmid	sentence
20643921	Nmda-dependent internalization of gabab receptors requires activation of ca2+/calmodulin-dependent protein kinase ii (camkii), which associates with gabab receptors in vivo and phosphorylates serine 867 (s867) in the intracellular c terminus of the gabab1 subunit.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Sequence	Organism
SIGNOR-273553	Thr107	ELTHNWGtEDDETQS	in vitro
pmid	sentence
32966793	This study is able to show that a phosphorylation of threonine-107 (T107) in the (rate-limiting) Glyoxalase 1 (Glo1) protein, mediated by Ca2+/calmodulin-dependent kinase II delta (CamKIIδ), is associated with elevated catalytic efficiency of Glo1 (lower KM; higher Vmax).

Publications:

1

Organism:

In Vitro

Identifier	Residue	Sequence	Organism
SIGNOR-21797	Thr286	SCMHRQEtVDCLKKF	Homo sapiens
pmid	sentence
1849884	Role of threonine-286 as autophosphorylation site for appearance of ca2(+)-independent activity of calmodulin-dependent protein kinase ii alpha subunit

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary

Pathways:

Axon guidance, Glutamatergic synapse, Neurotransmitters release

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-124309	Thr286	SCMHRQEtVDCLKKF	Homo sapiens	Neuron
pmid	sentence
15140879	Ppm1f specifically dephosphorylates the phospho-thr-286 in autophosphorylated camkii substrate and thus deactivates the camkii in vitro.

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-48387	Thr311	EHAQRAVtKPRYMQW	Homo sapiens	Neuron
pmid	sentence
9155020	D-myo-inositol 1,4,5-trisphosphate 3-kinase a is activated by receptor activation through a calcium:calmodulin-dependent protein kinase ii phosphorylation mechanism. the phosphorylated residue was thr311.

Publications:

1

Organism:

Homo Sapiens

Tissue:

Ovary, Brain

Identifier	Residue	Sequence
SIGNOR-250632	Thr38	GGLSRSStVASLDTD
pmid	sentence
9813144	The point mutation T38D localized within the optimal CaMKII recognition motif of ICAP-1alpha results in a strong defect in cell spreading which cannot be overcome by the inhibition of the endogenous CaMKII. This fact strongly suggests that the phosphorylation of Threonine 38 by CaMKII modulates the alpha5beta1 integrin function. Conversely, the mutation T38A produces an analog of ICAP-1alpha that cannot be phosphorylated and that stimulates cell spreading on fibronectin to a similar extent when CaMKII is inhibited.

Publications:

1

Identifier	Residue	Sequence	Organism
SIGNOR-264778	Thr5	tRELFLNF	Rattus norvegicus
pmid	sentence
23455424	SLN is also phosphorylated by CaMKII at Thr 5, and a phosphorylation mimic (Thr5Glu mutation) abolishes the inhibitory function of ectopically expressed SLN in adult rat ventricular myocytes\| Thr 5 interacts with SERCA Trp 932, and phosphorylation at this site would cause a steric clash that destabilizes binding

Publications:

1

Organism:

Rattus Norvegicus

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-96628	Thr574	VDNIRSAtPEALAFV	Homo sapiens	Neuron
pmid	sentence
12486117	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:

1

Organism:

Homo Sapiens

Tissue:

Brain

Identifier	Residue	Organism	Cell Line
SIGNOR-264216		Homo sapiens	Neuron
pmid	sentence
11052931	The most abundant signaling protein in the PSD fraction is Ca2+/calmodulin–dependent protein kinase II (CaMKII), which makes up 1 to 2% of the total protein in the forebrain (21). CaMKII is a target for Ca2+ flowing through the NMDA receptor and is necessary for normal synaptic plasticity in pyramidal neurons. The cytosolic tails of the NR2 subunits of the NMDA receptor bind to CaMKII and thus can serve as docking sites for it in the PSD

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-270230		Homo sapiens
pmid	sentence
12536214	Receptor internalization, altered;intracellular localization

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glutamatergic synapse

Identifier	Residue	Organism	Cell Line
SIGNOR-264231		Homo sapiens	Neuron
pmid	sentence
27477489	CaMKII-mediated displacement of AIDA-1 out of the postsynaptic density core. The present study indicates that CaMKII activation is necessary for the NMDA-induced movement of AIDA-1 out of the PSD core.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Glutamatergic synapse

Identifier	Residue	Organism	Cell Line
SIGNOR-264217		Homo sapiens	Neuron
pmid	sentence
11052931	The most abundant signaling protein in the PSD fraction is Ca2+/calmodulin–dependent protein kinase II (CaMKII), which makes up 1 to 2% of the total protein in the forebrain (21). CaMKII is a target for Ca2+ flowing through the NMDA receptor and is necessary for normal synaptic plasticity in pyramidal neurons. The cytosolic tails of the NR2 subunits of the NMDA receptor bind to CaMKII and thus can serve as docking sites for it in the PSD

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255490
pmid	sentence
15621017	Thus, the increased immunoreactivity of CaMKII-α of the remaining neurons may be the consequence of the altered calcium dynamics in neurons. There is evidence indicating that CaMKII might participate in tau phosphorylation in AD.

Publications:

1

Identifier	Residue	Organism	Cell Line
SIGNOR-264215		Homo sapiens	Neuron
pmid	sentence
11052931	The most abundant signaling protein in the PSD fraction is Ca2+/calmodulin–dependent protein kinase II (CaMKII), which makes up 1 to 2% of the total protein in the forebrain (21). CaMKII is a target for Ca2+ flowing through the NMDA receptor and is necessary for normal synaptic plasticity in pyramidal neurons. The cytosolic tails of the NR2 subunits of the NMDA receptor bind to CaMKII and thus can serve as docking sites for it in the PSD

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Sequence	Organism	Cell Line
SIGNOR-255491
pmid	sentence
15621017	It has been reported that Aβ can result in an increase in intracellular Ca2+, which in turn can activates CaMK.

Publications:

1

Pathways:

Axon guidance, Glutamatergic synapse, Neurotransmitters release

Identifier	Residue	Organism
SIGNOR-268385		Homo sapiens
pmid	sentence
15363394	In this study, we have identified CaMKII and CaN-PP1 as the downstream effectors of localized Ca2+ signals in mediating attractive and repulsive turning responses of growth cones, respectively. Local Ca2+ elevation activates CaMKII and CaN-PP1 for attraction and repulsion, respectively.

Publications:

1

Organism:

Homo Sapiens

Pathways:

Axon guidance

Identifier	Residue	Organism	Cell Line
SIGNOR-264214		Homo sapiens	Neuron
pmid	sentence
11052931	The most abundant signaling protein in the PSD fraction is Ca2+/calmodulin–dependent protein kinase II (CaMKII), which makes up 1 to 2% of the total protein in the forebrain (21). CaMKII is a target for Ca2+ flowing through the NMDA receptor and is necessary for normal synaptic plasticity in pyramidal neurons. The cytosolic tails of the NR2 subunits of the NMDA receptor bind to CaMKII and thus can serve as docking sites for it in the PSD

Publications:

1

Organism:

Homo Sapiens

Identifier	Residue	Organism
SIGNOR-264699		in vitro
pmid	sentence
18480293	Homer3 is phosphorylated at Ser120, Ser159, and Ser176 by CaMKII in vitro. Homer3 phosphorylation reduces its affinity for target molecules and modulates the Ca2+ signaling patterns induced by mGluR1Î± activation

Publications:

1

Organism:

In Vitro

Pathways:

Glutamatergic synapse

Name	CAMK2A View Modifications
Full Name	Calcium/calmodulin-dependent protein kinase type II subunit alpha
Synonyms	CaM kinase II subunit alpha, CaMK-II subunit alpha \| CAMKA, KIAA0968
Primary ID	Q9UQM7
Links	- -
Type	protein
Relations	118
Pathways	Axon guidance, Glutamatergic synapse, Neurotransmitters release
Function	Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in synaptic plasticity, neurotransmitter release and long-term potentiation. Member of the NMDAR signaling complex in excitatory synapses, it regulates NMDAR-dependent potentiation of the AMPAR and therefore excitatory synaptic transmission (By similarity). Regulates dendritic spine development (PubMed:28130356). Also regulates the migration of developing neurons (PubMed:29100089). Phosphorylates the transcription factor FOXO3 to activate its transcriptional activity (PubMed:23805378). Acts as a negative regulator of 2-arachidonoylglycerol (2-AG)-mediated synaptic signaling via modulation of DAGLA activity (By similarity).

The SIGnaling Network
Open Resource

Summary

Viewer

Search Tools

▶Modifications Tables

Relations