| UniProt ID | CDPK8_ARATH | |
|---|---|---|
| UniProt AC | Q42438 | |
| Protein Name | Calcium-dependent protein kinase 8 | |
| Gene Name | CPK8 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 533 | |
| Subcellular Localization |
Cell membrane Lipid-anchor . |
|
| Protein Description | May play a role in signal transduction pathways that involve calcium as a second messenger.. | |
| Protein Sequence | MGNCCASPGSETGSKKGKPKIKSNPFYSEAYTTNGSGTGFKLSVLKDPTGHDISLMYDLGREVGRGEFGITYLCTDIKTGEKYACKSISKKKLRTAVDIEDVRREVEIMKHMPRHPNIVSLKDAFEDDDAVHIVMELCEGGELFDRIVARGHYTERAAAAVMKTILEVVQICHKHGVMHRDLKPENFLFANKKETSALKAIDFGLSVFFKPGEGFNEIVGSPYYMAPEVLRRNYGPEVDIWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVIDFKRDPWPRVSETAKDLVRKMLEPDPKKRLSAAQVLEHSWIQNAKKAPNVSLGETVKARLKQFSVMNKLKKRALRVIAEHLSVEEVAGIKEAFEMMDSKKTGKINLEELKFGLHKLGQQQIPDTDLQILMEAADVDGDGTLNYGEFVAVSVHLKKMANDEHLHKAFSFFDQNQSDYIEIEELREALNDEVDTNSEEVVAAIMQDVDTDKDGRISYEEFAAMMKAGTDWRKASRQYSRERFNSLSLKLMREGSLQLEGEN | |
| 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 | ------MGNCCASPG ------CCCCCCCCC | 35.56 | - | |
| 23 | Phosphorylation | KGKPKIKSNPFYSEA CCCCCCCCCCCCCEE | 53.89 | 29797451 | |
| 28 | Phosphorylation | IKSNPFYSEAYTTNG CCCCCCCCEEEEECC | 19.01 | 19880383 | |
| 31 | Phosphorylation | NPFYSEAYTTNGSGT CCCCCEEEEECCCCC | 15.28 | 23110452 | |
| 32 | Phosphorylation | PFYSEAYTTNGSGTG CCCCEEEEECCCCCC | 22.34 | 19880383 | |
| 33 | Phosphorylation | FYSEAYTTNGSGTGF CCCEEEEECCCCCCE | 25.55 | 20374526 | |
| 36 | Phosphorylation | EAYTTNGSGTGFKLS EEEEECCCCCCEEEE | 34.94 | 30291188 | |
| 38 | Phosphorylation | YTTNGSGTGFKLSVL EEECCCCCCEEEEEE | 40.94 | 15308754 | |
| 221 | Phosphorylation | GFNEIVGSPYYMAPE CHHHHCCCCCCCCHH | 9.99 | - | |
| 285 | Phosphorylation | RDPWPRVSETAKDLV CCCCCCCCHHHHHHH | 30.43 | 28011693 | |
| 287 | Phosphorylation | PWPRVSETAKDLVRK CCCCCCHHHHHHHHH | 31.34 | 28011693 | |
| 488 | Phosphorylation | TDKDGRISYEEFAAM CCCCCCCCHHHHHHH | 25.73 | - | |
| 518 | Phosphorylation | RERFNSLSLKLMREG HHHHHHHHHHHHHHC | 24.23 | 23111157 | |
| 526 | Phosphorylation | LKLMREGSLQLEGEN HHHHHHCCCEEECCC | 14.27 | 19376835 |
| 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 CDPK8_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDPK8_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 CDPK8_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CATA3_ARATH | CAT3 | physical | 25966761 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks."; Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.; Plant Physiol. 150:889-903(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASSSPECTROMETRY. | |
| "Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY. | |
| "Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASSSPECTROMETRY. | |