Any feedback?
Literature summary for 2.7.11.17 extracted from
- Ca2+/calmodulin-dependent protein kinase kinase-alpha regulates skeletal muscle glucose uptake independent of AMP-activated protein kinase and Akt activation (2007), Diabetes, 56, 1403-1409.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Calmodulin | required | Mus musculus |  |
| additional information | CaMKI is phosphorylated at Thr177 and Thr180 by the Ca2+/calmodulin-dependent protein kinase kinase, CaMKKalpha, activating CaMKI, CaMKKK also activates CaMKIV | Mus musculus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | required | Mus musculus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | CaMKI is phosphorylated at Thr177 and Thr180 by the Ca2+/calmodulin-dependent protein kinase kinase, CaMKKalpha, activating CaMKI, CaMKIV is also a substrate for CaMKKK | Mus musculus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skeletal muscle | expression of CaMKI isozymes alpha, beta, and delta, not of CaMKIV | Mus musculus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CaMKI | - |
Mus musculus |
| CaMKIV | - |
Mus musculus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
