CDPKB_ARATH - dbPTM
CDPKB_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDPKB_ARATH
UniProt AC Q39016
Protein Name Calcium-dependent protein kinase 11
Gene Name CPK11
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 495
Subcellular Localization Cytoplasm . Nucleus .
Protein Description May play a role in signal transduction pathways that involve calcium as a second messenger. Functions as regulator of the calcium-mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-responsive transcription factors ABF1 and ABF4 in vitro..
Protein Sequence METKPNPRRPSNTVLPYQTPRLRDHYLLGKKLGQGQFGTTYLCTEKSTSANYACKSIPKRKLVCREDYEDVWREIQIMHHLSEHPNVVRIKGTYEDSVFVHIVMEVCEGGELFDRIVSKGHFSEREAVKLIKTILGVVEACHSLGVMHRDLKPENFLFDSPKDDAKLKATDFGLSVFYKPGQYLYDVVGSPYYVAPEVLKKCYGPEIDVWSAGVILYILLSGVPPFWAETESGIFRQILQGKLDFKSDPWPTISEAAKDLIYKMLERSPKKRISAHEALCHPWIVDEQAAPDKPLDPAVLSRLKQFSQMNKIKKMALRVIAERLSEEEIGGLKELFKMIDTDNSGTITFEELKAGLKRVGSELMESEIKSLMDAADIDNSGTIDYGEFLAATLHMNKMEREENLVAAFSYFDKDGSGYITIDELQSACTEFGLCDTPLDDMIKEIDLDNDGKIDFSEFTAMMRKGDGVGRSRTMMKNLNFNIADAFGVDGEKSDD
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
11PhosphorylationKPNPRRPSNTVLPYQ
CCCCCCCCCCCCCCC		43.2319880383
13PhosphorylationNPRRPSNTVLPYQTP
CCCCCCCCCCCCCCC		27.9722631563
48PhosphorylationYLCTEKSTSANYACK
EEECCCCCCCCHHCC		42.8228295753
52PhosphorylationEKSTSANYACKSIPK
CCCCCCCHHCCCCCC		17.0628295753
56PhosphorylationSANYACKSIPKRKLV
CCCHHCCCCCCCCEE		43.9628295753
190PhosphorylationYLYDVVGSPYYVAPE
EEEECCCCCCCCCHH		9.71-
230PhosphorylationVPPFWAETESGIFRQ
CCCCHHHCCCCHHHH		27.9215308754
232PhosphorylationPFWAETESGIFRQIL
CCHHHCCCCHHHHHH		44.6115308754
274PhosphorylationRSPKKRISAHEALCH
HCCCCCCCHHHHHCC		27.8325368622
301PhosphorylationPLDPAVLSRLKQFSQ
CCCHHHHHHHHHHHH		29.0325368622
307PhosphorylationLSRLKQFSQMNKIKK
HHHHHHHHHHHHHHH		26.4825368622
361PhosphorylationAGLKRVGSELMESEI
HHHHHHHHHHHHHHH		25.3825561503
493PhosphorylationFGVDGEKSDD-----
HCCCCCCCCC-----		42.5830291188
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 CDPKB_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDPKB_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 CDPKB_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2AV3_ARATHHTA9physical
19130088
DI191_ARATHDI19physical
19130088
BT2_ARATHBT2physical
19130088
CHLP_ARATHAT1G74470physical
19130088
ADF3_ARATHADF3physical
19130088
TOC33_ARATHTOC33physical
19130088
ACPM2_ARATHmtACP2physical
19130088
THF1_ARATHPSB29physical
19130088
ZHD14_ARATHHB32physical
19130088
PIN7_ARATHPIN7physical
19130088
NAGS1_ARATHNAGS1physical
19130088
CPL1_ARATHCPL1physical
19130088
RL183_ARATHAT5G27850physical
19130088
6PGD2_ARATHAT5G41670physical
19130088
DI191_ARATHDI19physical
16438971
CDPKO_ARATHCPK24physical
23449501
CDPKB_ARATHCDPK2physical
20118232
P2C75_ARATHAHG1physical
23007729
P2C37_ARATHPP2CAphysical
23007729
AI5L4_ARATHABF1physical
23007729
AI5L6_ARATHABF3physical
23007729
ABI5_ARATHABI5physical
23007729
AI5L4_ARATHABF1physical
17921317
AI5L7_ARATHABF4physical
17921317
CDPKB_ARATHCDPK2physical
17921317
H32_ARATHAT5G65360physical
17921317
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDPKB_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-361, AND MASSSPECTROMETRY.

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