| + |
CAMK2G | down-regulates activity 
phosphorylation
|
EGFR |
0.369 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250694 |
Ser1070 |
DSFLQRYsSDPTGAL |
|
A-431 Cell |
| pmid |
sentence |
| 1309762 |
The mechanism of desensitization of kinase activity can be accounted for, in part, by the EGF-stimulated phosphorylation of the receptor at Ser1046/7, a substrate for the multifunctional calmodulin-dependent protein kinase II in vitro. Mutation of Ser1046/7 by replacement with Ala residues blocks desensitization of the EGF receptor protein-tyrosine kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250695 |
Ser1071 |
SFLQRYSsDPTGALT |
Homo sapiens |
A-431 Cell |
| pmid |
sentence |
| 1309762 |
The mechanism of desensitization of kinase activity can be accounted for, in part, by the EGF-stimulated phosphorylation of the receptor at Ser1046/7, a substrate for the multifunctional calmodulin-dependent protein kinase II in vitro. Mutation of Ser1046/7 by replacement with Ala residues blocks desensitization of the EGF receptor protein-tyrosine kinase activity. |
|
| Publications: |
2 |
Organism: |
, Homo Sapiens |
| + |
CAMK2G | down-regulates activity
phosphorylation
|
ADCY3 |
0.36 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250691 |
Ser1076 |
NVASRMEsTGVMGNI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8798667 |
Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo. | Site-directed mutagenesis of a CaM kinase II consensus site (Ser-1076 to Ala-1076) in III-AC greatly reduced Ca2+-stimulated phosphorylation and inhibition of III-AC in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2G | down-regulates activity
phosphorylation
|
Adenylate_cyclase |
0.571 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267845 |
Ser1076 |
NVASRMEsTGVMGNI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 8798667 |
Phosphorylation and inhibition of type III adenylyl cyclase by calmodulin-dependent protein kinase II in vivo. | Site-directed mutagenesis of a CaM kinase II consensus site (Ser-1076 to Ala-1076) in III-AC greatly reduced Ca2+-stimulated phosphorylation and inhibition of III-AC in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2G |
phosphorylation
|
PEA15 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250701 |
Ser116 |
KDIIRQPsEEEIIKL |
|
Astrocyte |
| pmid |
sentence |
| 9721757 |
Partly purified PEA-15 was a substrate in vitro for CaMKII, but not for casein kinase II. Two-dimensional phosphopeptide mapping demonstrated that the site phosphorylated in vitro by CaMKII was also phosphorylated in intact astrocytes in response to endothelin. CaMKII phosphorylated selectively Ser116 and had no effect on Ser104, but in vitro phosphorylation by CaMKII appeared to facilitate further phosphorylation by protein kinase C. |
|
| Publications: |
1 |
| + |
CAMK2G | down-regulates activity
phosphorylation
|
MYLK |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250700 |
Ser1760 |
RAIGRLSsMAMISGL |
|
|
| pmid |
sentence |
| 2160950 |
Phosphorylation of MLC kinase by CaM protein kinase II increased the dissociation constant of MLC kinase for calmodulin about 10 times without changing the Vmax. The location of the phosphorylation sites was identified by isolating and sequencing the tryptic phosphopeptides of MLC kinase. The preferred site was identified as serine 512 and the second site as serine 525. These sites are the same as the sites phosphorylated by cAMP-dependent protein kinase. |
|
| Publications: |
1 |
| + |
CAMK2G | up-regulates activity 
phosphorylation
|
TH |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250709 |
Ser19 |
KGFRRAVsELDAKQA |
|
|
| pmid |
sentence |
| 1680128 |
In both isoforms, Ser-40 was found to be phosphorylated by PKA, and Ser-19 and Ser-40 were found to be phosphorylated by CaM-PK II. The putative phosphorylation site generated by alternative splicing (Ser-31) was phosphorylated specifically by CaM-PK II in TH-2 only. | Unlike TH-1, phosphorylation of TH-2 by CaM-PK II resulted in an increase of the Ki value for dopamine. |
|
| Publications: |
1 |
| + |
CAMK2G |
phosphorylation
|
SPR |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250705 |
Ser213 |
QQLARETsVDPDMRK |
|
|
| pmid |
sentence |
| 11825621 |
Phosphorylation sites of rat sepiapterin reductase (rSPR) by Ca2+/calmodulin-dependent protein kinase II were determined in the present study. Using specific monoclonal anti-phospho-Ser and -Thr antibodies, we found that only Ser residues of rSPR were phosphorylated. We constructed several point mutants of SPR by systematically replacing the three Ser residues by Ala ones. These mutants showed that all three Ser residues, i.e. S46, S196, and S214, of rSPR were phosphorylated. We also recognized that only Ser-213 of human SPR was phosphorylated. |
|
| Publications: |
1 |
| + |
CAMK2G | down-regulates
phosphorylation
|
NCOR2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-191777 |
Ser2407 |
AKVSGRPsSRKAKSP |
Homo sapiens |
|
| pmid |
sentence |
| 22888005 |
The kinase activity of camkii was essential for the activation of notch signaling. We also determined that camkii could enhance the association between notch1-ic and rbp-jk. Furthermore, the physical association between rbp-jk and smrt was substantially suppressed by camkii. 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 |
| + |
CAMK2G |
phosphorylation
|
FLNA |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250696 |
Ser2523 |
VTGPRLVsNHSLHET |
|
Pulmonary Artery Endothelial Cell |
| pmid |
sentence |
| 11290523 |
Our TER experiments using a CaM peptide, which functions as a specific competitive inhibitor of nonmuscle filamin phosphorylation by CaM kinase II, strongly suggest that filamin phosphorylation is involved in endothelial cell barrier regulation, although the exact mechanism is not clear and consequent signaling events are not well understood. |
|
| Publications: |
1 |
| + |
CAMK2G | down-regulates
phosphorylation
|
HDAC5 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85098 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85102 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 11114197 |
Camk phosphorylates serines -259 and -498 in hdac5, which subsequently serve as docking sites for 14-3-3. Our studies suggest that 14-3-3 binding to hdac5 is required for camk-dependent disruption of mef2hdac complexes and nuclear export of hdac5, and implicate 14-3-3 as a signal-dependent regulator of muscle cell differentiation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
CAMK2G |
phosphorylation
|
RRAD |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250703 |
Ser273 |
AGTRRREsLGKKAKR |
|
|
| pmid |
sentence |
| 9677319 |
Here we show that Rad serves as a substrate for phosphorylation by CaMKII, cAMP-dependent protein kinase (PKA), protein kinase C (PKC) and casein kinase II (CKII) with stoichiometries in vitro of 0.2-1.3 mol of phosphate/mol of Rad. By deletion and point mutation analysis we show that phosphorylation by CaMKII and PKA occurs on a single serine residue at position 273 |
|
| Publications: |
1 |
| + |
CAMK2G |
phosphorylation
|
RYR1 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250704 |
Ser2843 |
KKKTRKIsQSAQTYD |
|
|
| pmid |
sentence |
| 8380342 |
Phosphorylation of serine 2843 in ryanodine receptor-calcium release channel of skeletal muscle by cAMP-, cGMP- and CaM-dependent protein kinase. |
|
| Publications: |
1 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
SCN5A |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275779 |
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-275780 |
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-275781 |
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 |
| + |
CAMK2G |
phosphorylation
|
PLCB3 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250702 |
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 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
SCN8A |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275793 |
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-275794 |
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-275795 |
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 |
| + |
CAMK2G |
phosphorylation
|
SYN1 |
0.458 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250707 |
Ser568 |
PQATRQTsVSGPAPP |
|
|
| pmid |
sentence |
| 3118371 |
Sites 2 and 3 are serine residues phosphorylated by calcium/calmodulin-dependent protein kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250708 |
Ser605 |
AGPTRQAsQAGPVPR |
|
|
| pmid |
sentence |
| 3118371 |
Sites 2 and 3 are serine residues phosphorylated by calcium/calmodulin-dependent protein kinase II. |
|
| Publications: |
2 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
ATF1 |
0.303 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250692 |
Ser63 |
GILARRPsYRKILKD |
|
|
| pmid |
sentence |
| 8663317 |
Phosphopeptide mapping analysis and Western blotting studies demonstrated that in vitro, CaMK II phosphorylates only Ser63 (corresponding to Ser133 of CREB), which is essential for the activation, and not Ser72 (corresponding to Ser142 of CREB), which is a negative regulation site. |
|
| Publications: |
1 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
GRIA1 |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250697 |
Ser645 |
LTVERMVsPIESAED |
|
HEK-293 Cell |
| pmid |
sentence |
| 7877986 |
In this study, CaM-kinase II enhanced kainate currents of expressed glutamate receptor 6 in 293 cells and of wild-type glutamate receptor 1, but not the Ser-627 to Ala mutant, in Xenopus oocytes. | This CaM-kinase II regulatory phosphorylation site is conserved in all AMPA/kainate-type glutamate receptors, and its phosphorylation may be important in enhancing postsynaptic responsiveness as occurs during synaptic plasticity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250698 |
Ser849 |
FCLIPQQsINEAIRT |
|
|
| pmid |
sentence |
| 12609872 |
Direct phosphorylation of the GluR1 subunit of postsynaptic AMPA receptors by Ca(2+)/calmodulin-dependent protein kinase II (CaM-KII) is believed to be one of the major contributors to the enhanced strength of glutamatergic synapses in CA1 area of hippocampus during long-term potentiation. | Validity of the approach was confirmed by modeling, and silence analysis was applied then to the GluR1 AMPA receptor mutated at S831, the site phosphorylated by CaM-KII during long-term potentiation. Silence analysis indicates that a negative charge at S831 is a critical determinant for the enhanced channel function as a charge carrier. Silence and variance analyses, when applied to the same sets of data, were in agreement on the receptor regulation upon mutations. |
|
| Publications: |
2 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
STAT1 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250706 |
Ser727 |
TDNLLPMsPEEFDEV |
|
NIH-3T3 Cell |
| pmid |
sentence |
| 11972023 |
For maximal gene activation, S727 in the transcription activation domain of Stat1 also is inducibly phosphorylated by IFN-gamma. We previously purified a group of nuclear proteins that interact specifically with the Stat1 transcription activation domain. In this report, we identified one of them as the multifunctional Ca(2+)/calmodulin-dependent kinase (CaMK) II. We demonstrate that IFN-gamma mobilizes a Ca(2+) flux in cells and activates CaMKII. CaMKII can interact directly with Stat1 and phosphorylate Stat1 on S727 in vitro. Inhibition of Ca(2+) flux or CaMKII results in a lack of S727 phosphorylation and Stat1-dependent gene activation, suggesting in vivo phosphorylation of Stat1 S727 by CaMKII. |
|
| Publications: |
1 |
| + |
CAMK2G |
phosphorylation
|
GRIA4 |
0.507 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250699 |
Ser862 |
IRNKARLsITGSVGE |
|
|
| pmid |
sentence |
| 10366608 |
We found that GluR4 is phosphorylated on serine 842 within the C-terminal domain in vitro and in vivo. Serine 842 is phosphorylated by PKA, PKC, and CaMKII in vitro and is phosphorylated in transfected cells by PKA. |
|
| Publications: |
1 |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
CHAT |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250693 |
Thr574 |
VDNIRSAtPEALAFV |
|
Neuroblastoma Cell Line |
| pmid |
sentence |
| 12486117 |
Using mass spectrometry, we identified threonine 456 as a new phosphorylation site in choline acetyltransferase from A beta-(1-42)-treated cells and in purified recombinant ChAT phosphorylated in vitro by calcium/calmodulin-dependent protein kinase II (CaM kinase II). | This phosphorylation combination was observed in choline acetyltransferase from A beta-(1-42)-treated cells. Treatment of cells with A beta-(1-42) resulted in two phases of activation of choline acetyltransferase, the first within 30 min and associated with phosphorylation by protein kinase C and the second by 10 h and associated with phosphorylation by both CaM kinase II and protein kinase C. |
|
| Publications: |
1 |
| + |
CAMK2G | up-regulates
phosphorylation
|
MAP3K7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96422 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12482967 |
Camkii interacts with and phosphorylates tak1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2G | up-regulates activity
phosphorylation
|
AMPA |
0.614 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270234 |
|
|
|
|
| pmid |
sentence |
| 12609872 |
Direct phosphorylation of the GluR1 subunit of postsynaptic AMPA receptors by Ca(2+)/calmodulin-dependent protein kinase II (CaM-KII) is believed to be one of the major contributors to the enhanced strength of glutamatergic synapses in CA1 area of hippocampus during long-term potentiation. | Validity of the approach was confirmed by modeling, and silence analysis was applied then to the GluR1 AMPA receptor mutated at S831, the site phosphorylated by CaM-KII during long-term potentiation. Silence analysis indicates that a negative charge at S831 is a critical determinant for the enhanced channel function as a charge carrier. Silence and variance analyses, when applied to the same sets of data, were in agreement on the receptor regulation upon mutations. |
|
| Publications: |
1 |
| + |
calcium(2+) | up-regulates
chemical activation
|
CAMK2G |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198816 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22944199 |
Non-canonical Wnt/Ca2+ pathway has also been implicated in multiple functions including cell adhesion and cell movements during gastrulation. In this signaling cascade, binding of Wnt to the Fzd receptor leads to the release of intracellular Ca2+, a process which is mediated through heterotrimeric G proteins, PLC (phospholipase C) and CamKII (calcium-calmodulin-dependent kinae II) as well as PKC (protein kinase C). The increased intracellular Ca2+ concentration also activates the calcineurin phosphatase, leading to activation of the transcription factor NFAT (nuclear factor of activated T cell). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CAMK2G
- 
- 