UniProt ID | CDPKW_ARATH | |
---|---|---|
UniProt AC | Q6NLQ6 | |
Protein Name | Calcium-dependent protein kinase 32 {ECO:0000303|Ref.5} | |
Gene Name | CPK32 {ECO:0000303|Ref.5} | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 538 | |
Subcellular Localization |
Nucleus . Membrane Lipid-anchor . |
|
Protein Description | May play a role in signal transduction pathways that involve calcium as a second messenger. Involved in maintaining Ca2+ homeostasis in pollen tube tips by regulating CNGC18. [PubMed: 24121288 Functions as regulator of the calcium-mediated abscisic acid (ABA) signaling pathway] | |
Protein Sequence | MGNCCGTAGSLAQNDNKPKKGRKKQNPFSIDYGLHHGGGDGGGRPLKLIVLNDPTGREIESKYTLGRELGRGEFGVTYLCTDKETDDVFACKSILKKKLRTAVDIEDVRREVEIMRHMPEHPNVVTLKETYEDEHAVHLVMELCEGGELFDRIVARGHYTERAAAAVTKTIMEVVQVCHKHGVMHRDLKPENFLFGNKKETAPLKAIDFGLSVFFKPGERFNEIVGSPYYMAPEVLKRNYGPEVDIWSAGVILYILLCGVPPFWAETEQGVAQAIIRSVLDFRRDPWPKVSENAKDLIRKMLDPDQKRRLTAQQVLDHPWLQNAKTAPNVSLGETVRARLKQFTVMNKLKKRALRVIAEHLSDEEASGIREGFQIMDTSQRGKINIDELKIGLQKLGHAIPQDDLQILMDAGDIDRDGYLDCDEFIAISVHLRKMGNDEHLKKAFAFFDQNNNGYIEIEELREALSDELGTSEEVVDAIIRDVDTDKDGRISYEEFVTMMKTGTDWRKASRQYSRERFNSISLKLMQDASLQVNGDTR | |
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 | ------MGNCCGTAG ------CCCCCCHHH | 35.56 | - | |
227 | Phosphorylation | RFNEIVGSPYYMAPE CHHHHCCCCCCCCHH | 9.99 | - | |
362 | Phosphorylation | RVIAEHLSDEEASGI HHHHHHCCHHHHHCH | 44.90 | 30291188 | |
367 | Phosphorylation | HLSDEEASGIREGFQ HCCHHHHHCHHCCCE | 37.72 | 30407730 | |
378 | Phosphorylation | EGFQIMDTSQRGKIN CCCEEECCCCCCCCC | 14.91 | 15308754 | |
379 | Phosphorylation | GFQIMDTSQRGKINI CCEEECCCCCCCCCH | 17.39 | 15308754 | |
492 | Phosphorylation | TDKDGRISYEEFVTM CCCCCCCCHHHHHHH | 25.73 | - | |
520 | Phosphorylation | YSRERFNSISLKLMQ HHHHHHHHHHHHHHH | 15.73 | 25561503 | |
522 | Phosphorylation | RERFNSISLKLMQDA HHHHHHHHHHHHHHH | 21.19 | 25561503 | |
530 | Phosphorylation | LKLMQDASLQVNGDT HHHHHHHCCCCCCCC | 27.85 | 28011693 |
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 CDPKW_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDPKW_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 CDPKW_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
AI5L7_ARATH | ABF4 | physical | 16299177 | |
CNG18_ARATH | CNGC18 | physical | 24121288 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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-379, AND MASSSPECTROMETRY. |