| + |
CAMK2D | down-regulates activity 
phosphorylation
|
ANKRD28 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264793 |
Ser1011 |
TNTSKTVsFEALPIM |
in vitro |
|
| pmid |
sentence |
| 17023142 |
We provide evidence for a dual kinase-mediated regulation of the PITK holoenzyme whereby PITK phosphorylation at S1017 is catalyzed by calcium/calmodulin-dependent kinase II-delta (CaMKIIdelta), promoting the subsequent phosphorylation of S1013 by glycogen synthase kinase-3 (GSK3) in vitro.|the phosphorylation of PITK at these specific residues altered PP1 binding and subsequent PITK-directed dephosphorylation of hnRNP K |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAMK2D | down-regulates activity
phosphorylation
|
ITPR2 |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262692 |
Ser150 |
EKNAMRVsLDAAGNE |
Chlorocebus aethiops |
COS-1 Cell |
| pmid |
sentence |
| 23019322 |
Phopho-specific antibodies demonstrate that InsP(3)R2 Ser-150 is phosphorylated in vivo by CaMKIIδ. The results of this study show that serine 150 of the InsP(3)R2 is phosphorylated by CaMKII and results in a decrease in the channel open probability. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
CAMK2D |
phosphorylation
|
TPD52 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-168550 |
Ser176 |
KNSPTFKsFEEKVEN |
Homo sapiens |
|
| pmid |
sentence |
| 20946871 |
Here we demonstrate, using site-specific mutations, that ca(2+)-sensitive phosphorylation at serine 136 modulates the accumulation of d52 at the plasma membrane within 2 min of cell stimulation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162630 |
Ser176 |
KNSPTFKsFEEKVEN |
Homo sapiens |
|
| pmid |
sentence |
| 20032513 |
Here we demonstrate, using site-specific mutations, that ca(2+)-sensitive phosphorylation at serine 136 modulates the accumulation of d52 at the plasma membrane within 2 min of cell stimulation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | up-regulates activity 
phosphorylation
|
SCN5A |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275782 |
Ser1934 |
LFRQQAGsGLSEEDA |
|
|
| pmid |
sentence |
| 28882890 |
C-terminal phosphorylation of NaV1.5 impairs FGF13-dependent regulation of channel inactivation| Of 19 native NaV1.5 phosphorylation sites identified, two C-terminal phosphoserines at positions 1938 and 1989 showed increased phosphorylation in the CaMKIIδc-Tg compared with the WT ventricles. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275783 |
Ser1985 |
DSVTRATsDNLQVRG |
|
|
| pmid |
sentence |
| 28882890 |
C-terminal phosphorylation of NaV1.5 impairs FGF13-dependent regulation of channel inactivation| Of 19 native NaV1.5 phosphorylation sites identified, two C-terminal phosphoserines at positions 1938 and 1989 showed increased phosphorylation in the CaMKIIδc-Tg compared with the WT ventricles. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275776 |
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-275777 |
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-275778 |
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: |
5 |
Organism: |
, Homo Sapiens |
| + |
CAMK2D | up-regulates
phosphorylation
|
HDAC4 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-151418 |
Ser210 |
YGKTQHSsLDQSSPP |
Homo sapiens |
|
| pmid |
sentence |
| 17179159 |
These results demonstrate that camkiideltab preferentially targets hdac4, and this involves serine 210overexpression of camkiideltab in primary neonatal cardiomyocytes increases the activity of the mef2 transcription factor and completely rescues hdac4-mediated repression of mef2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | down-regulates activity
phosphorylation
|
KCNQ1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275479 |
Ser484 |
PHFMRTNsFAEDLDL |
|
|
| pmid |
sentence |
| 29410121 |
CaMKII regulates KCNQ1 at S484 during sustained β-AR stimulation to inhibit IKs. The ability of CaMKII to inhibit IKs may contribute to arrhythmogenicity during HF. |
|
| Publications: |
1 |
| + |
CAMK2D | down-regulates
phosphorylation
|
SCN5A |
0.48 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197058 |
Ser516 |
LSLTRGLsRTSMKPR |
Homo sapiens |
|
| pmid |
sentence |
| 22514276 |
A stable interaction between ?(C)-camkii and the intracellular loop between domains 1 and 2 of na(v)1.5 was observed. This region was also phosphorylated by ?(C)-camkii, specifically at the ser-516 and thr-594 sites.Wild-type (wt) and phosphomutant hna(v)1.5 were co-expressed with gfp-?(C)-camkii in hek293 cells, and i(na) was recorded. As observed in myocytes, camkii shifted wt i(na) availability to a more negative membrane potential and enhanced accumulation of i(na) into an intermediate inactivated state, but these effects were abolished by mutating either of these sites to non-phosphorylatable ala residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197067 |
Thr594 |
LHGKKNStVDCNGVV |
Homo sapiens |
|
| pmid |
sentence |
| 22514276 |
A stable interaction between ?(C)-camkii and the intracellular loop between domains 1 and 2 of na(v)1.5 was observed. This region was also phosphorylated by ?(C)-camkii, specifically at the ser-516 and thr-594 sites.Wild-type (wt) and phosphomutant hna(v)1.5 were co-expressed with gfp-?(C)-camkii in hek293 cells, and i(na) was recorded. As observed in myocytes, camkii shifted wt i(na) availability to a more negative membrane potential and enhanced accumulation of i(na) into an intermediate inactivated state, but these effects were abolished by mutating either of these sites to non-phosphorylatable ala residues. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | up-regulates activity
phosphorylation
|
SCN8A |
0.285 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275790 |
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-275791 |
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-275792 |
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 |
| + |
CAMK2D |
phosphorylation
|
VIM |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250690 |
Ser83 |
GVRLLQDsVDFSLAD |
|
Vero Cell |
| pmid |
sentence |
| 16140754 |
Interestingly, viral DNA replication also resulted in the activation of calcium calmodulin-dependent protein kinase II (CaM kinase II) and phosphorylation of the N-terminal domain of vimentin on serine 82. Immunostaining showed that vimentin within the cage was phosphorylated on serine 82. |
|
| Publications: |
1 |
| + |
CAMK2D | down-regulates
phosphorylation
|
KCNJ11 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-200027 |
Thr224 |
MQVVRKTtSPEGEVV |
Homo sapiens |
|
| pmid |
sentence |
| 23223335 |
Results showed that activation of camkii triggered dynamin-dependent internalization of k(atp) channels. This process required phosphorylation of threonine at 180 and 224 and an intact (330)yskf(333) endocytosis motif of the k(atp) channel kir6.2 pore-forming subunit. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | up-regulates
phosphorylation
|
CEACAM1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203402 |
Thr457 |
CFLHFGKtGRASDQR |
Homo sapiens |
|
| pmid |
sentence |
| 24302721 |
Camkiid specifically phosphorylates thr-457 on ceacam1-sf, which in turn regulates the process of lumen formation via apoptosis of the central acinar cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Breast |
| + |
CAMK2D | up-regulates
phosphorylation
|
CACNB2 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164067 |
Thr554 |
RGLSRQEtFDSETQE |
Homo sapiens |
|
| pmid |
sentence |
| 20194790 |
We recently identified ca(v)1.2 beta(2a) residues critical for camkii phosphorylation (thr 498) beta(2a) thr 498 and leu 493 are required for ca(v)1.2 activation by camkii in native cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | up-regulates
phosphorylation
|
CAMK2D |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255954 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19725819 |
Upon binding of the Ca2+/calmodulin complex to the binding domain of CaMKII, it is activated via autophosphorylation, then remaining active independent of of Ca2+ levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | up-regulates 
|
Myoblast_fusion |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255955 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19725819 |
In the cytoplasm where the activated CaMKII localises it induces signalling pathways that are mainly involved in mitochondrial biogenesis and expression of contractile protein |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2D | up-regulates
|
MEF2A |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255956 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19725819 |
In response toincreases in intracellular Ca2+ levels, activated CaMKII translocates into the nucleus where it phosphorylates and deactivates HDAC4 which, as a result, dissociates from theDNA-binding domain of MEF2. This dissociation allows MEF2 to bind to its DNA-binding domain to activate transcription of the MEF2-dependent target gene products MyoD and myogenin |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
calcium(2+) | up-regulates activity
chemical activation
|
CAMK2D |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255953 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19725819 |
Upon binding of the Ca2+/calmodulin complex to the binding domain of CaMKII, it is activated via autophosphorylation, then remaining active independent of of Ca2+ levels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CAMK2D
- 
- 