KCC2A_DROME - dbPTM
KCC2A_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2A_DROME
UniProt AC Q00168
Protein Name Calcium/calmodulin-dependent protein kinase type II alpha chain
Gene Name CaMKII
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 530
Subcellular Localization
Protein Description A key regulator of plasticity in synaptic physiology and behavior, alterations in its activity produce pleiotrophic effects that involve synaptic transmission and development as well as various aspects of behavior. Directly modulates eag potassium channels..
Protein Sequence MAAPAACTRFSDNYDIKEELGKGAFSIVKRCVQKSTGFEFAAKIINTKKLTARDFQKLEREARICRKLHHPNIVRLHDSIQEENYHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGVVHRDLKPENLLLASKAKGAAVKLADFGLAIEVQGDHQAWFGFAGTPGYLSPEVLKKEPYGKSVDIWACGVILYILLVGYPPFWDEDQHRLYSQIKAGAYDYPSPEWDTVTPEAKNLINQMLTVNPNKRITAAEALKHPWICQRERVASVVHRQETVDCLKKFNARRKLKGAILTTMLATRNFSSRSMITKKGEGSQVKESTDSSSTTLEDDDIKEDKKGTVDRSTTVVSKEPEDIRILCPAKTYQQNIGNSQCSSARRQEIIKITEQLIEAINSGDFDGYTKICDPHLTAFEPEALGNLVEGIDFHKFYFENVLGKNCKAINTTILNPHVHLLGEEAACIAYVRLTQYIDKQGHAHTHQSEETRVWHKRDNKWQNVHFHRSASAKISGATTFDFIPQK
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
280PhosphorylationCQRERVASVVHRQET
HCHHHHHHHHCHHHH
23.0919429919
287PhosphorylationSVVHRQETVDCLKKF
HHHCHHHHHHHHHHH
17.2016880127
306PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHHCC
12.2114687552
307PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCC
13.5214687552
311PhosphorylationILTTMLATRNFSSRS
HHHHHHHHCCCCCCC
23.3721082442
315PhosphorylationMLATRNFSSRSMITK
HHHHCCCCCCCCEEE
28.5230478224
316PhosphorylationLATRNFSSRSMITKK
HHHCCCCCCCCEEEC
25.0030478224
318PhosphorylationTRNFSSRSMITKKGE
HCCCCCCCCEEECCC
19.2427794539
327PhosphorylationITKKGEGSQVKESTD
EEECCCCCCCEECCC
27.741910789
332PhosphorylationEGSQVKESTDSSSTT
CCCCCEECCCCCCCC
31.6219429919
333PhosphorylationGSQVKESTDSSSTTL
CCCCEECCCCCCCCC
40.7819429919
335PhosphorylationQVKESTDSSSTTLED
CCEECCCCCCCCCCC
26.6927794539
336PhosphorylationVKESTDSSSTTLEDD
CEECCCCCCCCCCCC
34.2219429919
337PhosphorylationKESTDSSSTTLEDDD
EECCCCCCCCCCCCC
29.3919429919
338PhosphorylationESTDSSSTTLEDDDI
ECCCCCCCCCCCCCC
37.0319429919
339PhosphorylationSTDSSSTTLEDDDIK
CCCCCCCCCCCCCCC
30.0519429919
352PhosphorylationIKEDKKGTVDRSTTV
CCCCCCCCCCCCEEE
28.2827794539
352 (in isoform 2)Phosphorylation-28.2827794539
352 (in isoform 3)Phosphorylation-28.2827794539
358PhosphorylationGTVDRSTTVVSKEPE
CCCCCCEEEECCCHH
21.8421082442
358 (in isoform 2)Phosphorylation-21.8427794539
358 (in isoform 3)Phosphorylation-21.8427794539
383PhosphorylationYQQNIGNSQCSSARR
CHHHCCCCCCCHHHH
27.6127794539
523PhosphorylationAKISGATTFDFIPQK
CEECCCEEECCCCCC
22.2221082442

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
287TPhosphorylationKinaseKCC2AQ00168
PhosphoELM
287TPhosphorylationKinaseCAMK2-FAMILY-GPS
306TPhosphorylationKinaseKCC2AQ00168
PhosphoELM
306TPhosphorylationKinaseCAMK2-FAMILY-GPS
307TPhosphorylationKinaseKCC2AQ00168
PhosphoELM
307TPhosphorylationKinaseCAMK2-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCC2A_DROME !!

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 KCC2A_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCDCX_DROMECG32809physical
14605208
CSKP_DROMECASKgenetic
23543616
CSKP_DROMECASKgenetic
24062638
DLG1_DROMEdlg1physical
10458610
CALM_DROMECamphysical
8702694
CSKP_DROMECASKphysical
14687552
KCC2A_DROMECaMKIIphysical
10458610
KCC2A_DROMECaMKIIphysical
8769895

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2A_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND MASSSPECTROMETRY.
"Activity-dependent gating of CaMKII autonomous activity by DrosophilaCASK.";
Hodge J.J., Mullasseril P., Griffith L.C.;
Neuron 51:327-337(2006).
Cited for: AUTOPHOSPHORYLATION AT THR-287, AND ENZYME REGULATION.
"Regulation of the Ca2+/CaM-responsive pool of CaMKII by scaffold-dependent autophosphorylation.";
Lu C.S., Hodge J.J., Mehren J., Sun X.X., Griffith L.C.;
Neuron 40:1185-1197(2003).
Cited for: FUNCTION, INTERACTION WITH CASK, AUTOPHOSPHORYLATION AT THR-287;THR-306 AND THR-307, AND MUTAGENESIS OF THR-306 AND THR-307.

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