| + |
CAMK2B | up-regulates activity 
phosphorylation
|
GRIN2B |
0.589 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250688 |
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 |
| + |
CAMK2B | up-regulates activity
phosphorylation
|
RETREG1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273554 |
Ser151 |
AQLWRSLsESWEVIN |
in vitro |
|
| pmid |
sentence |
| 31930741 |
Under ER-stress conditions, activated CAMK2B phosphorylates the reticulon-homology domain of FAM134B, which enhances FAM134B oligomerization and activity in membrane fragmentation to accommodate high demand for ER-phagy. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAMK2B | down-regulates 
phosphorylation
|
STMN1 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59358 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 9686569 |
Stimulation via cd2 activated multiple signal transduction pathways, resulting in phosphorylation of distinct sites of stathmin. 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. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | down-regulates
phosphorylation
|
GSK3A |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167962 |
Ser21 |
SGRARTSsFAEPGGG |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 20841359 |
Inhibitory phosphorylation of gsk-3 by camkii couples depolarization to neuronal survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | down-regulates activity
phosphorylation
|
ETS1 |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250684 |
Ser251 |
GKLGGQDsFESIESY |
|
DG-75 Cell |
| pmid |
sentence |
| 12475968 |
Increased Transactivation of the GM-CSF Promoter/Enhancer by Ets1 with Mutated CaMK II Sites | Significantly, phosphorylation of Ets1 by Ca2+-dependent pathways is thought to inhibit DNA binding in vitro. To analyze the role of these four serines, S251, S257, S282, and S285, in transcription, we constructed three mutant derivatives of human Ets1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250685 |
Ser257 |
DSFESIEsYDSCDRL |
|
DG-75 Cell |
| pmid |
sentence |
| 12475968 |
Increased Transactivation of the GM-CSF Promoter/Enhancer by Ets1 with Mutated CaMK II Sites | Significantly, phosphorylation of Ets1 by Ca2+-dependent pathways is thought to inhibit DNA binding in vitro. To analyze the role of these four serines, S251, S257, S282, and S285, in transcription, we constructed three mutant derivatives of human Ets1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250686 |
Ser282 |
NSLQRVPsYDSFDSE |
|
DG-75 Cell |
| pmid |
sentence |
| 12475968 |
Increased Transactivation of the GM-CSF Promoter/Enhancer by Ets1 with Mutated CaMK II Sites | Significantly, phosphorylation of Ets1 by Ca2+-dependent pathways is thought to inhibit DNA binding in vitro. To analyze the role of these four serines, S251, S257, S282, and S285, in transcription, we constructed three mutant derivatives of human Ets1 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250687 |
Ser285 |
QRVPSYDsFDSEDYP |
|
DG-75 Cell |
| pmid |
sentence |
| 12475968 |
Increased Transactivation of the GM-CSF Promoter/Enhancer by Ets1 with Mutated CaMK II Sites | Significantly, phosphorylation of Ets1 by Ca2+-dependent pathways is thought to inhibit DNA binding in vitro. To analyze the role of these four serines, S251, S257, S282, and S285, in transcription, we constructed three mutant derivatives of human Ets1 |
|
| Publications: |
4 |
| + |
CAMK2B | up-regulates
phosphorylation
|
CYLD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-25334 |
Ser362 |
FYTLNGSsVDSQPQS |
Homo sapiens |
|
| pmid |
sentence |
| 24614225 |
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-91403 |
Ser772 |
LFKKIFPsLELNITD |
Homo sapiens |
|
| pmid |
sentence |
| 24614225 |
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: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | up-regulates activity
phosphorylation
|
CYLD |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-25329 |
Ser418 |
TTENRFHsLPFSLTK |
Homo sapiens |
|
| pmid |
sentence |
| 24614225 |
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: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | up-regulates activity
phosphorylation
|
SCN5A |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275773 |
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-275774 |
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 |
Cell Line |
| SIGNOR-275775 |
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–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 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CAMK2B |
phosphorylation
|
PLCB3 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250689 |
Ser537 |
PSLEPQKsLGDEGLN |
|
|
| pmid |
sentence |
| 11325525 |
CaMK II phosphorylated PLCbeta3 but not PLCbeta1 in vitro. Phosphorylation occurred exclusively on 537Ser in the X-Y linker region of PLCbeta3. 537Ser was also phosphorylated in the basal state in cells and phosphorylation was enhanced by ionomycin treatment |
|
| Publications: |
1 |
| + |
CAMK2B | down-regulates
phosphorylation
|
CTNNB1 |
0.294 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202825 |
Ser552 |
QDTQRRTsMGGTQQQ |
Homo sapiens |
|
| pmid |
sentence |
| 24117889 |
Camkii represses transcriptionally active beta-catenin to mediate acute ethanol neurodegeneration and can phosphorylate beta-catenin. Using targeted mutagenesis we identified camkii phosphorylation sites within human beta-catenin at t332, t472, and s552 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202829 |
Thr332 |
VNIMRTYtYEKLLWT |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24117889 |
Camkii represses transcriptionally active _-catenin to mediate acute ethanol neurodegeneration and can phosphorylate _-catenincamkii can directly phosphorylate _-catenin. Using targeted mutagenesis we identified camkii phosphorylation sites within human _-catenin at t332, t472, and s552. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-202833 |
Thr472 |
ICALRHLtSRHQEAE |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24117889 |
Camkii represses transcriptionally active _-catenin to mediate acute ethanol neurodegeneration and can phosphorylate _-catenincamkii can directly phosphorylate _-catenin. Using targeted mutagenesis we identified camkii phosphorylation sites within human _-catenin at t332, t472, and s552. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | up-regulates activity
phosphorylation
|
SCN8A |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275787 |
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-275788 |
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-275789 |
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 |
| + |
CAMK2B | up-regulates
phosphorylation
|
STAT1 |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154771 |
Ser727 |
TDNLLPMsPEEFDEV |
Homo sapiens |
|
| pmid |
sentence |
| 17502367 |
All stats are phosphorylated on at least one serine residue in their tad specifically, ser727 in stats 1 and 3 and ser721 in stat4. Stat serine kinases have been identified through the use of inhibitors, dominant-negative alleles, and in vitro kinase assays. They include mapk (p38mapk: stats 1, 3, 4;erk: stat3, 5;jnk: stat3), pkc_ (stat1, stat3), mtor (stat3), nlk (stat3 (42)), and camkii and ikk_ (stat1 (39, 40, 43)).STAT Serine phosphorylation regulates transcriptional activity (see below). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | up-regulates
phosphorylation
|
PRKAA1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-138360 |
Thr183 |
SDGEFLRtSCGSPNY |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15980064 |
These data indicate that the camkks function in intact cells as ampkks, predicting wider roles for these kinases in regulating ampk activity in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | up-regulates activity
phosphorylation
|
CAMK2B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250640 |
Thr287 |
SMMHRQEtVECLKKF |
|
|
| pmid |
sentence |
| 2842767 |
Ca2+/calmodulin-dependent protein kinase II: identification of threonine-286 as the autophosphorylation site in the alpha subunit associated with the generation of Ca2+-independent activity. |
|
| Publications: |
1 |
| + |
CAMK2B | up-regulates
phosphorylation
|
AMPK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217493 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15980064 |
These data indicate that the camkks function in intact cells as ampkks, predicting wider roles for these kinases in regulating ampk activity in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CAMK2B
- 
- 