KCC2A_RAT - dbPTM
KCC2A_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2A_RAT
UniProt AC P11275
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit alpha
Gene Name Camk2a
Organism Rattus norvegicus (Rat).
Sequence Length 478
Subcellular Localization Cell junction, synapse, presynaptic cell membrane . Cell junction, synapse . Postsynaptic lipid rafts.
Protein Description CaM-kinase II (CAMK2) is a prominent kinase in the central nervous system that may function in long-term potentiation and neurotransmitter release. Member of the NMDAR signaling complex in excitatory synapses it may regulate NMDAR-dependent potentiation of the AMPAR and synaptic plasticity. [PubMed: 15312654 Phosphorylates transcription factor FOXO3 on 'Ser-298'. Activates FOXO3 transcriptional activity (By similarity]
Protein Sequence MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKNDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH
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
13PhosphorylationCTRFTEEYQLFEELG
ECCCCHHHHHHHHHC		12.32-
21UbiquitinationQLFEELGKGAFSVVR
HHHHHHCCCHHHHHH		60.74-
21AcetylationQLFEELGKGAFSVVR
HHHHHHCCCHHHHHH		60.7422902405
25PhosphorylationELGKGAFSVVRRCVK
HHCCCHHHHHHHHHH		21.1125403869
32UbiquitinationSVVRRCVKVLAGQEY
HHHHHHHHHHCCCHH		34.85-
39PhosphorylationKVLAGQEYAAKIINT
HHHCCCHHHHHHHCC		12.17-
42AcetylationAGQEYAAKIINTKKL
CCCHHHHHHHCCCCC		35.6322902405
42UbiquitinationAGQEYAAKIINTKKL
CCCHHHHHHHCCCCC		35.63-
47UbiquitinationAAKIINTKKLSARDH
HHHHHCCCCCCHHHH		47.42-
48UbiquitinationAKIINTKKLSARDHQ
HHHHCCCCCCHHHHH		45.71-
56AcetylationLSARDHQKLEREARI
CCHHHHHHHHHHHHH		49.2372607917
68AcetylationARICRLLKHPNIVRL
HHHHHHHCCCCEEEE		62.7022902405
68UbiquitinationARICRLLKHPNIVRL
HHHHHHHCCCCEEEE		62.70-
80PhosphorylationVRLHDSISEEGHHYL
EEEECCCCCCCCEEE		33.28-
106PhosphorylationEDIVAREYYSEADAS
HHHHHHHHCCCCCHH		13.51-
137UbiquitinationGVVHRDLKPENLLLA
CCCCCCCCHHHHHHH		55.35-
137AcetylationGVVHRDLKPENLLLA
CCCCCCCCHHHHHHH		55.357768123
145PhosphorylationPENLLLASKLKGAAV
HHHHHHHHHHHCCHH		38.1927097102
146AcetylationENLLLASKLKGAAVK
HHHHHHHHHHCCHHH		48.9222902405
146UbiquitinationENLLLASKLKGAAVK
HHHHHHHHHHCCHHH		48.92-
148UbiquitinationLLLASKLKGAAVKLA
HHHHHHHHCCHHHHH		50.68-
153UbiquitinationKLKGAAVKLADFGLA
HHHCCHHHHHHCCEE		32.98-
181PhosphorylationAGTPGYLSPEVLRKD
CCCCCCCCHHHHHCC		15.5530181290
220DimethylationFWDEDQHRLYQQIKA
CCCHHHHHHHHHHHH		29.47-
220MethylationFWDEDQHRLYQQIKA
CCCHHHHHHHHHHHH		29.47-
222PhosphorylationDEDQHRLYQQIKAGA
CHHHHHHHHHHHHCC		9.79-
226AcetylationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.11140695
226UbiquitinationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.11-
230PhosphorylationQQIKAGAYDFPSPEW
HHHHHCCCCCCCCCC		19.73-
234PhosphorylationAGAYDFPSPEWDTVT
HCCCCCCCCCCCCCC		35.1328551015
239PhosphorylationFPSPEWDTVTPEAKD
CCCCCCCCCCHHHHH		27.61-
241PhosphorylationSPEWDTVTPEAKDLI
CCCCCCCCHHHHHHH		19.94-
245UbiquitinationDTVTPEAKDLINKML
CCCCHHHHHHHHHHH		51.94-
250UbiquitinationEAKDLINKMLTINPS
HHHHHHHHHHCCCHH		28.44-
250AcetylationEAKDLINKMLTINPS
HHHHHHHHHHCCCHH		28.4422902405
253PhosphorylationDLINKMLTINPSKRI
HHHHHHHCCCHHHCC		18.4018514171
257PhosphorylationKMLTINPSKRITAAE
HHHCCCHHHCCCHHH		30.0325403869
258UbiquitinationMLTINPSKRITAAEA
HHCCCHHHCCCHHHH		49.42-
258AcetylationMLTINPSKRITAAEA
HHCCCHHHCCCHHHH		49.4222902405
267AcetylationITAAEALKHPWISHR
CCHHHHHCCCCCCCH		55.4522902405
267UbiquitinationITAAEALKHPWISHR
CCHHHHHCCCCCCCH		55.45-
275PhosphorylationHPWISHRSTVASCMH
CCCCCCHHHHHHHHC		23.0827097102
276PhosphorylationPWISHRSTVASCMHR
CCCCCHHHHHHHHCH		21.7630411139
279PhosphorylationSHRSTVASCMHRQET
CCHHHHHHHHCHHHH		13.9825403869
286PhosphorylationSCMHRQETVDCLKKF
HHHCHHHHHHHHHHH		17.2012218416
291AcetylationQETVDCLKKFNARRK
HHHHHHHHHHCHHHH		62.7422902405
291UbiquitinationQETVDCLKKFNARRK
HHHHHHHHHHCHHHH		62.74-
292UbiquitinationETVDCLKKFNARRKL
HHHHHHHHHCHHHHH		30.79-
298UbiquitinationKKFNARRKLKGAILT
HHHCHHHHHHHHHHH		49.34-
300UbiquitinationFNARRKLKGAILTTM
HCHHHHHHHHHHHHH		49.70-
305PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHHCC		12.2120592192
306PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCC		13.5220592192
310PhosphorylationILTTMLATRNFSGGK
HHHHHHHHCCCCCCC		23.3727097102
314PhosphorylationMLATRNFSGGKSGGN
HHHHCCCCCCCCCCC		50.6225403869
322UbiquitinationGGKSGGNKKNDGVKE
CCCCCCCCCCCCCCC		57.11-
323UbiquitinationGKSGGNKKNDGVKES
CCCCCCCCCCCCCCC		65.36-
328UbiquitinationNKKNDGVKESSESTN
CCCCCCCCCCCCCCC		58.36-
330PhosphorylationKNDGVKESSESTNTT
CCCCCCCCCCCCCCC		33.4225403869
331PhosphorylationNDGVKESSESTNTTI
CCCCCCCCCCCCCCC		36.3430411139
333PhosphorylationGVKESSESTNTTIED
CCCCCCCCCCCCCCC		28.9830411139
334PhosphorylationVKESSESTNTTIEDE
CCCCCCCCCCCCCCC		32.3130411139
336PhosphorylationESSESTNTTIEDEDT
CCCCCCCCCCCCCCH		29.2830411139
337PhosphorylationSSESTNTTIEDEDTK
CCCCCCCCCCCCCHH		25.1630411139
343PhosphorylationTTIEDEDTKVRKQEI
CCCCCCCHHHHHHHH		29.4128551015
344UbiquitinationTIEDEDTKVRKQEII
CCCCCCHHHHHHHHH		52.98-
347UbiquitinationDEDTKVRKQEIIKVT
CCCHHHHHHHHHHHH		56.10-
352UbiquitinationVRKQEIIKVTEQLIE
HHHHHHHHHHHHHHH		49.09-
404PhosphorylationFYFENLWSRNSKPVH
HHHHCHHCCCCCCCE		25.4227097102
408UbiquitinationNLWSRNSKPVHTTIL
CHHCCCCCCCEEEEE		55.39-
435PhosphorylationCIAYIRITQYLDAGG
HHHHHHHHHHHHCCC		11.00-
437PhosphorylationAYIRITQYLDAGGIP
HHHHHHHHHHCCCCC		9.63-
461AcetylationVWHRRDGKWQIVHFH
EEECCCCCEEEEEEE		39.9722902405
461UbiquitinationVWHRRDGKWQIVHFH
EEECCCCCEEEEEEE		39.97-
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
253TPhosphorylationKinaseCAMK2AP11275
PSP
253TPhosphorylationKinaseCAMK2BP08413
PSP
279SPhosphorylationKinaseCAMK2AP11275
PSP
286TPhosphorylationKinaseCAMK2AP11275
PSP
286TPhosphorylationKinaseCAMK2BP08413
PSP
286TPhosphorylationKinasePRKCAP05696
GPS
286TPhosphorylationKinaseCAMK2-FAMILY-GPS
286TPhosphorylationKinaseCAM-KII_GROUP-PhosphoELM
305TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
305TPhosphorylationKinaseCAMK2AP11275
PSP
306TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
306TPhosphorylationKinaseCAMK2AP11275
PSP
310TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
314SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
314SPhosphorylationKinaseCAMK2AP11275
PSP
314SPhosphorylationKinaseCAMK2BP08413
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
286TPhosphorylation

2842767
286TPhosphorylation

2842767
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS8_RATPsmc5physical
19638347
GYS1_HUMANGYS1physical
8280084
LBR_RATLbrphysical
8598227
GRM4_RATGrm4physical
15494036
GRM7_RATGrm7physical
15494036
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2A_RAT

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Ca2+/calmodulin-dependent protein kinase II: identification ofthreonine-286 as the autophosphorylation site in the alpha subunitassociated with the generation of Ca2+-independent activity.";
Thiel G., Czernik A.J., Gorelick F., Nairn A.C., Greengard P.;
Proc. Natl. Acad. Sci. U.S.A. 85:6337-6341(1988).
Cited for: PROTEIN SEQUENCE OF 282-299, AND PHOSPHORYLATION AT THR-286.

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