| + |
CAMK1 |
phosphorylation
|
EIF4G3 |
0.486 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250613 |
Ser1156 |
NTFMRGGsSKDLLDN |
Homo sapiens |
|
| pmid |
sentence |
| 14507913 |
Endogenous eIF4GII immunoprecipitated from HEK293T cells was phosphorylated by CaMKI, in vitro as was a recombinant fragment of eIF4GII encompassing the central and C-terminal regions. The latter phosphorylation occurred with favorable kinetics (Km = 1 microm; kcat = 1.8 s-1) at a single site, Ser1156, located in a segment of eIF4GII aligning with the phosphoregion of eIF4GI. Phosphopeptide mapping and back phosphorylation experiments revealed [Ca2+]i-dependent, CaMKI site-specific, eIF4GII phosphorylation in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | up-regulates activity 
phosphorylation
|
PPME1 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276636 |
Ser15 |
MHLGRLPsRPPLPGS |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 24841198 |
When the CaMKI activity is elevated, it phosphorylates PME-1 at Ser15. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | down-regulates activity 
phosphorylation
|
PPME1 |
0.404 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265747 |
Ser15 |
MHLGRLPsRPPLPGS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24841198 |
CaMKI Is the Upstream Kinase for Phosphorylation of PME-1/Ser15|Our results also demonstrated that the phosphorylated levels of PME-1/Ser15 and CaMKI/Thr177 are inversely correlated with the phosphatase activity of SIK2·PP2A complex, further implying that the demethylase activity of phosphorylated PME-1/Ser15 may be higher than that of its unphosphorylated state. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | down-regulates
phosphorylation
|
HDAC5 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85018 |
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-85022 |
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 |
| + |
CAMK1 | down-regulates
phosphorylation
|
NUMB |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149993 |
Ser276 |
EQLARQGsFRGFPAL |
Homo sapiens |
|
| pmid |
sentence |
| 17022975 |
Based on experiments using numb mutants, both the initial phosphorylation of ser(264) and the subsequent phosphorylation of ser(283) are sufficient to abolish the binding of numb to ap-2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
GCM1 |
0.396 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262680 |
Ser47 |
YAKHIYSsEDKNAQR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 21791615 |
We show that Epac1 and Rap1, in response to cAMP, activate CaMKI to phosphorylate Ser47 in GCM1. This phosphorylation facilitates the interaction between GCM1 and the desumoylating enzyme SENP1 and thereby leads to GCM1 desumoylation and activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 |
phosphorylation
|
KRT18 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-27398 |
Ser53 |
ISVSRSTsFRGGMGS |
Homo sapiens |
|
| pmid |
sentence |
| 7523419 |
Ser-52 in k18 is not glycosylated and matches consensus sequences for phosphorylation by cam kinase..these kinases can phosphorylate k18 in vitro predominantly at that site |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
ATF1 |
0.502 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250611 |
Ser63 |
GILARRPsYRKILKD |
in vitro |
|
| 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 |
Organism: |
In Vitro |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
DNM1L |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262552 |
Ser637 |
VPVARKLsAREQRDC |
|
|
| pmid |
sentence |
| 31063459 |
For example, protein kinase A (PKA) phosphorylation of Drp1S600 has been reported to decrease Drp1 GTPase activity in vitro (23, 24), whereas phosphorylation of the same conserved serine residue by Ca2+-calmodulin–dependent protein kinase Iα (CaMKIα) in Drp1 isoform 3 has been reported to cause a significant increase in mitochondrial fission |
|
| Publications: |
1 |
| + |
CAMK1 | down-regulates activity
phosphorylation
|
NOS1 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250614 |
Ser852 |
SYKVRFNsVSSYSDS |
in vitro |
|
| 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 |
Organism: |
In Vitro |
| + |
CAMK1 | down-regulates activity
phosphorylation
|
SYN1 |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250615 |
Ser9 |
NYLRRRLsDSNFMAN |
in vitro |
|
| pmid |
sentence |
| 10571231 |
Synapsin phosphorylation in the A domain, at the only phosphorylation site shared by all synapsins, dissociates synapsins from synaptic vesicles.This site is located in the N-terminal A domain and is a substrate for both PKA and CaM Kinase I |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
CDKN1B |
0.309 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261195 |
Thr157 |
GIRKRPAtDDSSTQN |
Mus musculus |
|
| pmid |
sentence |
| 23707388 |
We also demonstrate that i) CaMKI phosphorylates p27 at Thr157and Thr198 in human cells and at Thr170and Thr197in mouse cells to modulate its subcellular localization; |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261194 |
Thr198 |
PGLRRRQt |
Mus musculus |
|
| pmid |
sentence |
| 23707388 |
We also demonstrate that i) CaMKI phosphorylates p27 at Thr157and Thr198 in human cells and at Thr170and Thr197in mouse cells to modulate its subcellular localization;|Collectively, these results suggest that CaMKI is involved in mediating G1 progression by promoting cyclin D1/cdk4 complex formation through site-specific p27 phosphorylation in human lung epithelia. |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
CAMKK2 | up-regulates activity
phosphorylation
|
CAMK1 |
0.422 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250716 |
Thr177 |
DPGSVLStACGTPGY |
|
|
| pmid |
sentence |
| 7641687 |
Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. |
|
| Publications: |
1 |
| + |
CAMKK1 | up-regulates activity
phosphorylation
|
CAMK1 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250717 |
Thr177 |
DPGSVLStACGTPGY |
|
|
| pmid |
sentence |
| 8253780 |
Human calcium-calmodulin dependent protein kinase I: cDNA cloning, domain structure and activation by phosphorylation at threonine-177 by calcium-calmodulin dependent protein kinase I kinase. |
|
| Publications: |
1 |
| + |
CAMK1 | up-regulates activity
phosphorylation
|
CAMK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250612 |
Thr177 |
DPGSVLStACGTPGY |
in vitro |
|
| pmid |
sentence |
| 8253780 |
CaM kinase I was autophosphorylated in a Ca2+/CaM-dependent manner at a threonyl residue (Thr-177) which is located at a position equivalent to that of the threonyl residue (Thr-197) autophosphorylated in cAMP-dependent protein kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPM1F | down-regulates activity
dephosphorylation
|
CAMK1 |
0.475 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277111 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11726284 |
Calmodulin-dependent protein kinase phosphatase (CaMKP) dephosphorylates and concomitantly deactivates multifunctional Ca(2+)/calmodulin-dependent protein kinases , such as CaMKI, CaMKII, and CaMKIV. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RAP1A | up-regulates activity 
|
CAMK1 |
0.296 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262683 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21791615 |
The present study indicates that Epac1 and Rap1 are involved in activation of CaMKI for Ser47 phosphorylation in GCM1. We found here that cAMP-dependent activation of Epac1 and Rap1 but not PKA is able to activate CaMKI to mediate Ser47 (S47) phosphorylation in GCM1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FBXL12 | down-regulates quantity
ubiquitination
|
CAMK1 |
0.489 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261193 |
|
|
Mus musculus |
MLE-12 Cell |
| pmid |
sentence |
| 23707388 |
Here, we show that a ubiquitin E3 ligase component, F-box protein Fbxl12, mediates CaMKI degradation via a proteasome-directed pathway leading to disruption of cyclin D1/cdk4 complex. Endogenous Fbxl12 and CaMKI interacted as demonstrated after Fbxl12 immuno-precipitation followed by immunoblot analysis with CaMKI antibodies assembly and resultantG1 arrest in lung epithelia. Fbxl12 targets CaMKI for ubiquitination. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
CAMK1
- 
- 