UniProt ID | CDPK6_ARATH | |
---|---|---|
UniProt AC | Q38872 | |
Protein Name | Calcium-dependent protein kinase 6 | |
Gene Name | CPK6 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 544 | |
Subcellular Localization |
Cell membrane Lipid-anchor . Nucleus . |
|
Protein Description | May play a role in signal transduction pathways that involve calcium as a second messenger. Functions in abscisic acid (ABA) regulation of guard cell S-type anion-and Ca(2+)-permeable channels and stomatal closure. [PubMed: 17032064 Phosphorylates FD] | |
Protein Sequence | MGNSCRGSFKDKIYEGNHSRPEENSKSTTTTVSSVHSPTTDQDFSKQNTNPALVIPVKEPIMRRNVDNQSYYVLGHKTPNIRDLYTLSRKLGQGQFGTTYLCTDIATGVDYACKSISKRKLISKEDVEDVRREIQIMHHLAGHKNIVTIKGAYEDPLYVHIVMELCAGGELFDRIIHRGHYSERKAAELTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDDDFSLKAIDFGLSVFFKPGQIFKDVVGSPYYVAPEVLLKHYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGYIDFDTDPWPVISDSAKDLIRKMLCSSPSERLTAHEVLRHPWICENGVAPDRALDPAVLSRLKQFSAMNKLKKMALKVIAESLSEEEIAGLRAMFEAMDTDNSGAITFDELKAGLRRYGSTLKDTEIRDLMEAADVDNSGTIDYSEFIAATIHLNKLEREEHLVSAFQYFDKDGSGYITIDELQQSCIEHGMTDVFLEDIIKEVDQDNDGRIDYEEFVAMMQKGNAGVGRRTMKNSLNISMRDV | |
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 | N-myristoyl glycine | ------MGNSCRGSF ------CCCCCCCHH | 34.46 | - | |
2 | Myristoylation | ------MGNSCRGSF ------CCCCCCCHH | 34.46 | 19029837 | |
29 | Phosphorylation | EENSKSTTTTVSSVH CCCCCCCEEEEEECC | 27.79 | 30589143 | |
30 | Phosphorylation | ENSKSTTTTVSSVHS CCCCCCEEEEEECCC | 25.86 | 25561503 | |
31 | Phosphorylation | NSKSTTTTVSSVHSP CCCCCEEEEEECCCC | 19.12 | 25561503 | |
33 | Phosphorylation | KSTTTTVSSVHSPTT CCCEEEEEECCCCCC | 25.26 | 27532006 | |
34 | Phosphorylation | STTTTVSSVHSPTTD CCEEEEEECCCCCCC | 21.36 | 27532006 | |
37 | Phosphorylation | TTVSSVHSPTTDQDF EEEEECCCCCCCCCH | 23.06 | 17317660 | |
39 | Phosphorylation | VSSVHSPTTDQDFSK EEECCCCCCCCCHHH | 46.12 | 25561503 | |
40 | Phosphorylation | SSVHSPTTDQDFSKQ EECCCCCCCCCHHHC | 34.74 | 25561503 | |
49 | Phosphorylation | QDFSKQNTNPALVIP CCHHHCCCCCCEEEE | 39.83 | 23111157 | |
249 | Phosphorylation | IFKDVVGSPYYVAPE CHHHCCCCCCEECHH | 9.71 | - | |
532 | Phosphorylation | NAGVGRRTMKNSLNI CCCCCHHHHCHHCCC | 31.01 | 25561503 | |
536 | Phosphorylation | GRRTMKNSLNISMRD CHHHHCHHCCCCCCC | 19.78 | 30291188 | |
540 | Phosphorylation | MKNSLNISMRDV--- HCHHCCCCCCCC--- | 13.49 | 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 CDPK6_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDPK6_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 CDPK6_ARATH !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Myristoylation | |
Reference | PubMed |
"Experimental testing of predicted myristoylation targets involved inasymmetric cell division and calcium-dependent signalling."; Benetka W., Mehlmer N., Maurer-Stroh S., Sammer M., Koranda M.,Neumueller R., Betschinger J., Knoblich J.A., Teige M., Eisenhaber F.; Cell Cycle 7:3709-3719(2008). Cited for: MYRISTOYLATION, AND SUBCELLULAR LOCATION. | |
Phosphorylation | |
Reference | PubMed |
"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-540, AND MASSSPECTROMETRY. | |
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND MASSSPECTROMETRY. |