| + |
CAMK4 | up-regulates 
phosphorylation
|
CREB1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153940 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
|
| pmid |
sentence |
| 17389598 |
Pka, ca2+-calmodulin-dependent kinase iv (camkiv), msk, p70s6k and rsk phosphorylate creb. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid Hormone Metabolism |
| + |
CAMK4 | up-regulates activity
phosphorylation
|
CREB1 |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-102722 |
Ser119 |
EILSRRPsYRKILND |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 12835716 |
Pka, ca2+-calmodulin-dependent kinase iv (camkiv), msk, p70s6k and rsk phosphorylate creb. All these kinases target CREB on S133 to activate CREB. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Thyroid Hormone Metabolism |
| + |
CAMK4 | down-regulates 
phosphorylation
|
STMN1 |
0.465 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34743 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
|
| pmid |
sentence |
| 7925472 |
Serine 16 of oncoprotein 18 is a major cytosolic target for the ca2+/calmodulin-dependent kinase-gr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK4 |
phosphorylation
|
NOVA2 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273519 |
Ser194 |
EQVHKAVsAIVQKVQ |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32492405 |
CaMKIV Phosphorylates Nova-2 and Regulates Its Nuclear Localization. CaMKIV Phosphorylates Nova-2 and Regulates Its Nuclear Localization. Conversely, Nova-2 with single or double mutations to alanine (2A and 1A2A) was predominantly nuclear, like the WT (Figures 5H and and5I).5I). In contrast, glutamate mutations at site 3 had no effect on Nova-2 localization (Figures 5H and and5I)5I) or on Nova-2 binding to RNA (Figure S5E). These results showed that active CaMKIV reduces Nova-2 nuclear localization by phosphorylating sites 1 and 2 (S25, T27). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK4 | up-regulates quantity
phosphorylation
|
NOVA2 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273521 |
Ser25 |
EVVCTKRsNTGEEGE |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32492405 |
CaMKIV Phosphorylates Nova-2 and Regulates Its Nuclear Localization. CaMKIV Phosphorylates Nova-2 and Regulates Its Nuclear Localization. Conversely, Nova-2 with single or double mutations to alanine (2A and 1A2A) was predominantly nuclear, like the WT (Figures 5H and and5I).5I). In contrast, glutamate mutations at site 3 had no effect on Nova-2 localization (Figures 5H and and5I)5I) or on Nova-2 binding to RNA (Figure S5E). These results showed that active CaMKIV reduces Nova-2 nuclear localization by phosphorylating sites 1 and 2 (S25, T27). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273520 |
Thr27 |
VCTKRSNtGEEGEYF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 32492405 |
CaMKIV Phosphorylates Nova-2 and Regulates Its Nuclear Localization. CaMKIV Phosphorylates Nova-2 and Regulates Its Nuclear Localization. Conversely, Nova-2 with single or double mutations to alanine (2A and 1A2A) was predominantly nuclear, like the WT (Figures 5H and and5I).5I). In contrast, glutamate mutations at site 3 had no effect on Nova-2 localization (Figures 5H and and5I)5I) or on Nova-2 binding to RNA (Figure S5E). These results showed that active CaMKIV reduces Nova-2 nuclear localization by phosphorylating sites 1 and 2 (S25, T27). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CAMK4 | down-regulates
phosphorylation
|
HDAC5 |
0.487 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85106 |
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.Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236571 |
Ser259 |
FPLRKTAsEPNLKVR |
Homo sapiens |
|
| pmid |
sentence |
| 12058061 |
Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-85110 |
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.Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-236575 |
Ser498 |
RPLSRTQsSPLPQSP |
Homo sapiens |
|
| pmid |
sentence |
| 12058061 |
Recently, camkiv, a calcium-calmodulindependent protein kinase, was also shown to activate mef2s by dissociating class ii histone deacetylases (e.g., Hdac5) from mef2s, thus relieving the transcriptional repressive effect of hdacs. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Muscle, Skeletal Muscle |
| Pathways: | IGF and Myogenesis |
| + |
CAMK4 | up-regulates activity
phosphorylation
|
CREBBP |
0.622 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250710 |
Ser302 |
PQLASKQsMVNSLPT |
|
Neuron |
| pmid |
sentence |
| 11970865 |
Ser301 of CBP was identified as a major target of CaMKIV phosphorylation in vitro and in vivo. CaM kinase inhibitors attenuated phosphorylation at Ser301 and blocked CBP-dependent transcription. Additionally, mutation of Ser301 impaired NMDA- and CaMKIV-stimulated transcription. These findings demonstrate that activity-induced CaMKIV signaling contributes to CREB/CBP-dependent transcription by phosphorylating CBP at Ser301. |
|
| Publications: |
1 |
| Pathways: | Thyroid Hormone Metabolism |
| + |
CAMK4 | down-regulates activity
phosphorylation
|
HDAC4 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250711 |
Ser467 |
RPLGRTQsAPLPQNA |
|
U2-OS Cell |
| pmid |
sentence |
| 11470791 |
CaMKIV phosphorylates HDAC4 in vitro and promotes its nuclear-cytoplasmic shuttling in vivo. | Thus, CaMKIV can phosphorylate HDAC4 at Ser-467 and/or Ser-632 in vitro. | Collectively, our results suggest that CaMKIV reverses the transcriptional repression activity of HDAC4 by stimulating the mobilization of HDAC4 out of the nucleus. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250712 |
Ser632 |
RPLSRAQsSPASATF |
|
|
| pmid |
sentence |
| 11470791 |
CaMKIV phosphorylates HDAC4 in vitro and promotes its nuclear-cytoplasmic shuttling in vivo. | Thus, CaMKIV can phosphorylate HDAC4 at Ser-467 and/or Ser-632 in vitro. | Collectively, our results suggest that CaMKIV reverses the transcriptional repression activity of HDAC4 by stimulating the mobilization of HDAC4 out of the nucleus. |
|
| Publications: |
2 |
| Pathways: | IGF and Myogenesis |
| + |
CAMK4 | up-regulates
phosphorylation
|
HNRNPL |
0.394 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-197367 |
Ser544 |
GKSERSSsGLLEWES |
Homo sapiens |
|
| pmid |
sentence |
| 22570490 |
Here we show that the regulation of the stress axis-regulated exon of the slo1 potassium channel transcripts by membrane depolarization requires a highly conserved camkiv target serine (ser-513) of the heterogeneous ribonucleoprotein l. Ser-513 phosphorylation within the rna recognition motif 4 enhanced heterogeneous ribonucleoprotein l interaction with the camkiv-responsive rna element 1 of stress axis-regulated exon and inhibited binding of the large subunit of the u2 auxiliary factor u2af65. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK4 | down-regulates activity
phosphorylation
|
NOS1 |
0.365 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250713 |
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 |
| + |
CAMK4 | down-regulates
phosphorylation
|
PHB2 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-174437 |
Ser91 |
RARPRKIsSPTGSKD |
Homo sapiens |
|
| pmid |
sentence |
| 21689744 |
Here we show that calcium/calmodulin-dependent kinase iv (camk iv) specifically binds to the c terminus of phb2 and phosphorylates phb2 at serine 91. Camk iv effectively decreased phb2-mediated repression of mef2 activity through phosphorylation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle |
| + |
CAMKK1 | up-regulates
phosphorylation
|
CAMK4 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124732 |
Thr200 |
EHQVLMKtVCGTPGY |
Homo sapiens |
|
| pmid |
sentence |
| 15143065 |
In response to an increase in intracellular Ca2+, CaMKIV binds Ca2+/CaM and becomes phosphorylated on T200 by CaMKK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134649 |
Thr200 |
EHQVLMKtVCGTPGY |
Homo sapiens |
|
| pmid |
sentence |
| 15769749 |
Phosphorylation of ca(2+)/cam-bound camkiv on its activation loop threonine (residue thr(200) in human camkiv) by ca(2+)/calmodulin-dependent kinase kinase leads to increased camkiv kinase activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232181 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10770941 |
Ca(2+)/calmodulin-dependent protein kinase kinase (CaM-KK) is a novel member of the CaM kinase family, which specifically phosphorylates and activates CaM kinase I and IV |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
| + |
CAMKK2 | up-regulates activity
phosphorylation
|
CAMK4 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250718 |
Thr200 |
EHQVLMKtVCGTPGY |
|
|
| pmid |
sentence |
| 7615569 |
Phosphorylation and activation of Ca(2+)-calmodulin-dependent protein kinase IV by Ca(2+)-calmodulin-dependent protein kinase Ia kinase. Phosphorylation of threonine 196 is essential for activation. |
|
| Publications: |
1 |
| Pathways: | Thyroid Hormone Metabolism |
| + |
CAMK4 | down-regulates
phosphorylation
|
HDAC4 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-83837 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11062529 |
Mckinsey et al. report that calcium/calmodulin-dependent kinase (camk), stimulates myogenesis and prevents formation of mef2/hdac complexes by inducing phosphorylation and nuclear export of hdacs 4 and 5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | IGF and Myogenesis |
3.0
CAMK4
- 
- 