| UniProt ID | CDPKL_ARATH | |
|---|---|---|
| UniProt AC | Q9ZSA2 | |
| Protein Name | Calcium-dependent protein kinase 21 | |
| Gene Name | CPK21 | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 531 | |
| Subcellular Localization |
Cell membrane Lipid-anchor . |
|
| Protein Description | May play a role in signal transduction pathways that involve calcium as a second messenger. Mediates the phosphorylation and activation of the S-type anion efflux channel SLAC1.. | |
| Protein Sequence | MGCFSSKHRKTQNDGGEKSIPINPVQTHVVPEHRKPQTPTPKPMTQPIHQQISTPSSNPVSVRDPDTILGKPFEDIRKFYSLGKELGRGQFGITYMCKEIGTGNTYACKSILKRKLISKQDKEDVKREIQIMQYLSGQPNIVEIKGAYEDRQSIHLVMELCAGGELFDRIIAQGHYSERAAAGIIRSIVNVVQICHFMGVVHRDLKPENFLLSSKEENAMLKATDFGLSVFIEEGKVYRDIVGSAYYVAPEVLRRSYGKEIDIWSAGVILYILLSGVPPFWAENEKGIFDEVIKGEIDFVSEPWPSISESAKDLVRKMLTKDPKRRITAAQVLEHPWIKGGEAPDKPIDSAVLSRMKQFRAMNKLKKLALKVIAESLSEEEIKGLKTMFANIDTDKSGTITYEELKTGLTRLGSRLSETEVKQLMEAADVDGNGTIDYYEFISATMHRYKLDRDEHVYKAFQHFDKDNSGHITRDELESAMKEYGMGDEASIKEVISEVDTDNDGRINFEEFCAMMRSGSTQPQGKLLPFH | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Myristoylation | ------MGCFSSKHR ------CCCCCCCCC | 22.60 | - | |
| 19 | Phosphorylation | QNDGGEKSIPINPVQ CCCCCCCCCCCCCCE | 29.33 | 27288362 | |
| 27 | Phosphorylation | IPINPVQTHVVPEHR CCCCCCEECCCCCCC | 19.51 | 23111157 | |
| 38 | Phosphorylation | PEHRKPQTPTPKPMT CCCCCCCCCCCCCCC | 37.34 | 25561503 | |
| 244 | Phosphorylation | VYRDIVGSAYYVAPE EEEHHCCHHHHHCHH | 11.38 | 15308754 | |
| 376 | Phosphorylation | ALKVIAESLSEEEIK HHHHHHHHCCHHHHC | 28.33 | 17317660 | |
| 417 | Phosphorylation | TRLGSRLSETEVKQL HHHHHCCCHHHHHHH | 41.17 | 25561503 | |
| 419 | Phosphorylation | LGSRLSETEVKQLME HHHCCCHHHHHHHHH | 42.58 | 25561503 | |
| 469 | Phosphorylation | QHFDKDNSGHITRDE HHHCCCCCCCCCHHH | 41.71 | 30291188 |
| 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 CDPKL_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDPKL_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 CDPKL_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| P2C56_ARATH | ABI1 | physical | 20385816 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Phosphorylation | |
| Reference | PubMed |
| "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-244, AND MASSSPECTROMETRY. | |