CDPK5_ARATH - dbPTM
CDPK5_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDPK5_ARATH
UniProt AC Q38871
Protein Name Calcium-dependent protein kinase 5
Gene Name CPK5
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 556
Subcellular Localization Membrane
Lipid-anchor .
Protein Description May play a role in signal transduction pathways that involve calcium as a second messenger..
Protein Sequence MGNSCRGSFKDKLDEGDNNKPEDYSKTSTTNLSSNSDHSPNAADIIAQEFSKDNNSNNNSKDPALVIPLREPIMRRNPDNQAYYVLGHKTPNIRDIYTLSRKLGQGQFGTTYLCTEIASGVDYACKSISKRKLISKEDVEDVRREIQIMHHLAGHGSIVTIKGAYEDSLYVHIVMELCAGGELFDRIIQRGHYSERKAAELTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDDDFSLKAIDFGLSVFFKPGQIFTDVVGSPYYVAPEVLLKRYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGYIDFESDPWPVISDSAKDLIRRMLSSKPAERLTAHEVLRHPWICENGVAPDRALDPAVLSRLKQFSAMNKLKKMALKVIAESLSEEEIAGLREMFQAMDTDNSGAITFDELKAGLRKYGSTLKDTEIHDLMDAADVDNSGTIDYSEFIAATIHLNKLEREEHLVAAFQYFDKDGSGFITIDELQQACVEHGMADVFLEDIIKEVDQNNDGKIDYGEFVEMMQKGNAGVGRRTMRNSLNISMRDA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGNSCRGSF
------CCCCCCCCH
34.46-
8PhosphorylationMGNSCRGSFKDKLDE
CCCCCCCCHHCCCCC
15.1230291188
27PhosphorylationKPEDYSKTSTTNLSS
CCCCCCCCCCCCCCC
25.9323111157
28PhosphorylationPEDYSKTSTTNLSSN
CCCCCCCCCCCCCCC
36.6530407730
29PhosphorylationEDYSKTSTTNLSSNS
CCCCCCCCCCCCCCC
25.5730407730
30PhosphorylationDYSKTSTTNLSSNSD
CCCCCCCCCCCCCCC
33.6530407730
33PhosphorylationKTSTTNLSSNSDHSP
CCCCCCCCCCCCCCC
29.5523111157
34PhosphorylationTSTTNLSSNSDHSPN
CCCCCCCCCCCCCCC
43.4426811356
36PhosphorylationTTNLSSNSDHSPNAA
CCCCCCCCCCCCCHH
38.3523111157
39PhosphorylationLSSNSDHSPNAADII
CCCCCCCCCCHHHHH
25.4923111157
56PhosphorylationEFSKDNNSNNNSKDP
HHHCCCCCCCCCCCC
47.3825561503
60PhosphorylationDNNSNNNSKDPALVI
CCCCCCCCCCCCEEE
40.3325561503
261PhosphorylationIFTDVVGSPYYVAPE
EEECCCCCCCEECHH
9.71-
544PhosphorylationNAGVGRRTMRNSLNI
CCCCCHHHHHHHHCC
21.0823776212
548PhosphorylationGRRTMRNSLNISMRD
CHHHHHHHHCCCCCC
16.6630291188
552PhosphorylationMRNSLNISMRDA---
HHHHHCCCCCCC---
13.4930291188

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 CDPK5_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDPK5_ARATH !!

Disease-associated PTM Sites based on SAP

* 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 CDPK5_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CDPK5_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDPK5_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-552, 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 SER-8, AND MASSSPECTROMETRY.

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