| + |
PRKACA | down-regulates activity 
phosphorylation
|
CAMKK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256115 |
Thr108 |
SPRAWRRPtIESHHVAI |
Rattus norvegicus |
|
| pmid |
sentence |
| 10187789 |
In vitro, CaMKK is phosphorylated by PKA and this is associated with inhibition of enzyme activity. The major site of phosphorylation is threonine 108, although additional sites are phosphorylated with lower efficiency. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CAMKK1 | up-regulates activity 
phosphorylation
|
CAMK1 |
0.413 |
| 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 |
| + |
CAMKK1 | up-regulates activity
phosphorylation
|
CAMK1D |
0.415 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250715 |
Thr180 |
GKGDVMStACGTPGY |
|
HeLa Cell |
| pmid |
sentence |
| 12935886 |
CaM-KIdelta exhibits Ca(2+)/CaM-dependent activity that is enhanced (approximately 30-fold) in vitro by phosphorylation of its Thr180 by CaM-K kinase (CaM-KK)alpha, consistent with detection of CaM-KIdelta-activating activity in HeLa cells. | This sustained activation of CaM-KIdelta was completely abolished by Thr180Ala mutation and inhibited by CaM-KK inhibitor, STO-609, indicating a functional CaM-KK/CaM-KIdelta cascade in HeLa cells. |
|
| Publications: |
1 |
| + |
CAMKK1 | up-regulates
phosphorylation
|
PRKAA1 |
0.46 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-176598 |
Thr183 |
SDGEFLRtSCGSPNY |
Homo sapiens |
|
| pmid |
sentence |
| 21918180 |
Ampka1 activators increased phosphorylation level and cytoplasmic localization (reduced nuclear/cytoplasmic ratio). Ampka1 activators reduced rna synthesis in the nucleoli. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMKK1 | up-regulates
phosphorylation
|
CAMK4 |
0.621 |
| 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-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-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 |
| + |
CAMKK1 | up-regulates activity
phosphorylation
|
AKT |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250714 |
Thr308 |
KDGATMKtFCGTPEY |
|
|
| pmid |
sentence |
| 10833263 |
Protein kinase B (PKB) was recently reported to be activated on the phosphorylation of Thr(308) by Ca(2+)/calmodulin-dependent protein kinase kinase alpha (CaM-kinase kinase alpha), suggesting that PKB was regulated through not only the phosphoinositide 3-kinase pathway but also the Ca(2+)/calmodulin protein kinase pathway. |
|
| Publications: |
1 |
| + |
CAMKK1 | up-regulates activity
phosphorylation
|
AKT1 |
0.378 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252609 |
Thr308 |
KDGATMKtFCGTPEY |
|
|
| pmid |
sentence |
| 10833263 |
Protein kinase B (PKB) was recently reported to be activated on the phosphorylation of Thr(308) by Ca(2+)/calmodulin-dependent protein kinase kinase alpha (CaM-kinase kinase alpha), suggesting that PKB was regulated through not only the phosphoinositide 3-kinase pathway but also the Ca(2+)/calmodulin protein kinase pathway. |
|
| Publications: |
1 |
| Pathways: | IGF and Myogenesis |
| + |
CAMKK1 | up-regulates activity
phosphorylation
|
BRSK1 |
0.306 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280202 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18324781 |
In transfected COS-7 cells, kinase activity and Thr (189) phosphorylation of overexpressed SAD-B were significantly enhanced by coexpression of constitutively active CaMKKalpha (residues 1-434) in a manner similar to that observed with coexpression of LKB1, STRAD, and MO25.|Taken together, these results indicate that CaMKKalpha is capable of activating SAD-B through phosphorylation of Thr (189) both in vitro and in vivo and demonstrate for the first time that CaMKK may be an alternative activating kinase for SAD-B. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM2 | up-regulates
binding
|
CAMKK1 |
0.485 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266328 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10770941 |
The binding of Ca2+/CaM to CaM-KK is absolutely required for its activation and efficient phosphorylation of target protein kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM3 | up-regulates
binding
|
CAMKK1 |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266344 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10770941 |
The binding of Ca2+/CaM to CaM-KK is absolutely required for its activation and efficient phosphorylation of target protein kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CALM1 | up-regulates
binding
|
CAMKK1 |
0.753 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-232178 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10770941 |
The binding of Ca2+/CaM to CaM-KK is absolutely required for its activation and efficient phosphorylation of target protein kinases |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
CAMKK1
- 
- 