| UniProt ID | CDPKA_ARATH | |
|---|---|---|
| UniProt AC | Q9M9V8 | |
| Protein Name | Calcium-dependent protein kinase 10 | |
| Gene Name | CPK10 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 545 | |
| Subcellular Localization |
Membrane Lipid-anchor . |
|
| Protein Description | May play a role in signal transduction pathways that involve calcium as a second messenger. May be a positive regulator controlling stress signal transduction.. | |
| Protein Sequence | MGNCNACVRPDSKESKPSSKPKKPNRDRKLNPFAGDFTRSPAPIRVLKDVIPMSNQTQISDKYILGRELGRGEFGITYLCTDRETHEALACKSISKRKLRTAVDIEDVRREVAIMSTLPEHPNVVKLKASYEDNENVHLVMELCEGGELFDRIVARGHYTERAAAAVARTIAEVVMMCHSNGVMHRDLKPENFLFANKKENSPLKAIDFGLSVFFKPGDKFTEIVGSPYYMAPEVLKRDYGPGVDVWSAGVIIYILLCGVPPFWAETEQGVALAILRGVLDFKRDPWPQISESAKSLVKQMLDPDPTKRLTAQQVLAHPWIQNAKKAPNVPLGDIVRSRLKQFSMMNRFKKKVLRVIAEHLSIQEVEVIKNMFSLMDDDKDGKITYPELKAGLQKVGSQLGEPEIKMLMEVADVDGNGFLDYGEFVAVIIHLQKIENDELFKLAFMFFDKDGSTYIELDELREALADELGEPDASVLSDIMREVDTDKDGRINYDEFVTMMKAGTDWRKASRQYSRERFKSLSINLMKDGSLHLHDALTGQTVPV | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Myristoylation | ------MGNCNACVR ------CCCCCCCCC | 47.61 | - | |
| 38 | Phosphorylation | NPFAGDFTRSPAPIR CCCCCCCCCCCCCCE | 34.67 | - | |
| 227 | Phosphorylation | KFTEIVGSPYYMAPE CHHHHCCCCCCCCHH | 9.99 | - | |
| 521 | Phosphorylation | YSRERFKSLSINLMK HHHHHHHHCEEEEEC | 25.33 | 25561503 | |
| 523 | Phosphorylation | RERFKSLSINLMKDG HHHHHHCEEEEECCC | 19.27 | 19880383 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of CDPKA_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDPKA_ARATH !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CDPKA_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CALM1_ARATH | CAM1 | physical | 25233328 | |
| CALM4_ARATH | CAM1 | physical | 25233328 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND MASSSPECTROMETRY. | |
| "A phyloproteomic characterization of in vitro autophosphorylation incalcium-dependent protein kinases."; Hegeman A.D., Rodriguez M., Han B.W., Uno Y., Phillips G.N. Jr.,Hrabak E.M., Cushman J.C., Harper J.F., Harmon A.C., Sussman M.R.; Proteomics 6:3649-3664(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38, AND MASSSPECTROMETRY. | |