KCC2A_HUMAN - dbPTM
KCC2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2A_HUMAN
UniProt AC Q9UQM7
Protein Name Calcium/calmodulin-dependent protein kinase type II subunit alpha
Gene Name CAMK2A
Organism Homo sapiens (Human).
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 (By similarity). Phosphorylates transcription factor FOXO3 on 'Ser-298'. [PubMed: 23805378 Activates FOXO3 transcriptional activity (By similarity]
Protein Sequence MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKSDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH
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
3Phosphorylation-----MATITCTRFT
-----CCEEEECCCC		18.6020068231
5Phosphorylation---MATITCTRFTEE
---CCEEEECCCCHH		11.9420068231
6S-nitrosocysteine--MATITCTRFTEEY
--CCEEEECCCCHHH		1.96-
6S-nitrosylation--MATITCTRFTEEY
--CCEEEECCCCHHH		1.9622178444
7Phosphorylation-MATITCTRFTEEYQ
-CCEEEECCCCHHHH		21.8420068231
10PhosphorylationTITCTRFTEEYQLFE
EEEECCCCHHHHHHH		25.3120068231
13PhosphorylationCTRFTEEYQLFEELG
ECCCCHHHHHHHHHC		12.3220068231
25PhosphorylationELGKGAFSVVRRCVK
HHCCCHHHHHHHHHH		21.1120068231
56UbiquitinationLSARDHQKLEREARI
CCHHHHHHHHHHHHH		49.23-
68UbiquitinationARICRLLKHPNIVRL
HHHHHHHCCCCEEEE		62.70-
78PhosphorylationNIVRLHDSISEEGHH
CEEEEECCCCCCCCE		19.78-
137UbiquitinationGVVHRDLKPENLLLA
CCCCCCCCHHHHHHH		55.35-
145PhosphorylationPENLLLASKLKGAAV
HHHHHHHHHHHCCHH		38.1928857561
181PhosphorylationAGTPGYLSPEVLRKD
CCCCCCCCHHHHHCC		15.5521815630
226 (in isoform 2)Ubiquitination-36.1121906983
226 (in isoform 1)Ubiquitination-36.1121906983
226AcetylationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.11132777
226UbiquitinationHRLYQQIKAGAYDFP
HHHHHHHHHCCCCCC		36.112190698
230PhosphorylationQQIKAGAYDFPSPEW
HHHHHCCCCCCCCCC		19.7328857561
234PhosphorylationAGAYDFPSPEWDTVT
HCCCCCCCCCCCCCC		35.1328857561
239PhosphorylationFPSPEWDTVTPEAKD
CCCCCCCCCCHHHHH		27.6128857561
245UbiquitinationDTVTPEAKDLINKML
CCCCHHHHHHHHHHH		51.94-
253PhosphorylationDLINKMLTINPSKRI
HHHHHHHCCCHHHCC		18.4020060891
257PhosphorylationKMLTINPSKRITAAE
HHHCCCHHHCCCHHH		30.0328787133
258TrimethylationMLTINPSKRITAAEA
HHCCCHHHCCCHHHH		49.42-
258MethylationMLTINPSKRITAAEA
HHCCCHHHCCCHHHH		49.4223644510
261PhosphorylationINPSKRITAAEALKH
CCHHHCCCHHHHHCC		24.6924719451
272PhosphorylationALKHPWISHRSTVAS
HHCCCCCCCHHHHHH		14.6922468782
275PhosphorylationHPWISHRSTVASCMH
CCCCCCHHHHHHHHC		23.0819060867
276PhosphorylationPWISHRSTVASCMHR
CCCCCHHHHHHHHCH		21.7625332170
279PhosphorylationSHRSTVASCMHRQET
CCHHHHHHHHCHHHH		13.9825332170
280S-nitrosylationHRSTVASCMHRQETV
CHHHHHHHHCHHHHH		1.6022178444
280S-nitrosocysteineHRSTVASCMHRQETV
CHHHHHHHHCHHHHH		1.60-
286PhosphorylationSCMHRQETVDCLKKF
HHHCHHHHHHHHHHH		17.2029255136
298MethylationKKFNARRKLKGAILT
HHHCHHHHHHHHHHH		49.34-
300MethylationFNARRKLKGAILTTM
HCHHHHHHHHHHHHH		49.70-
305PhosphorylationKLKGAILTTMLATRN
HHHHHHHHHHHHHCC		12.2117343827
306PhosphorylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCC		13.5217343827
306O-linked_GlycosylationLKGAILTTMLATRNF
HHHHHHHHHHHHCCC		13.5228657654
310PhosphorylationILTTMLATRNFSGGK
HHHHHHHHCCCCCCC		23.3721406692
314PhosphorylationMLATRNFSGGKSGGN
HHHHCCCCCCCCCCC		50.62-
318PhosphorylationRNFSGGKSGGNKKSD
CCCCCCCCCCCCCCC		56.03-
324PhosphorylationKSGGNKKSDGVKESS
CCCCCCCCCCCCCCC		41.0025332170
330PhosphorylationKSDGVKESSESTNTT
CCCCCCCCCCCCCCC		33.4224076635
331PhosphorylationSDGVKESSESTNTTI
CCCCCCCCCCCCCCC		36.3418510355
332 (in isoform 2)Phosphorylation-71.5118510355
333PhosphorylationGVKESSESTNTTIED
CCCCCCCCCCCCCCC		28.9818510355
333 (in isoform 2)Phosphorylation-28.9818510355
334 (in isoform 2)Phosphorylation-32.3118510355
334PhosphorylationVKESSESTNTTIEDE
CCCCCCCCCCCCCCC		32.3118510355
336PhosphorylationESSESTNTTIEDEDT
CCCCCCCCCCCCCCH		29.2818510355
337PhosphorylationSSESTNTTIEDEDTK
CCCCCCCCCCCCCHH		25.1620886841
342 (in isoform 2)Phosphorylation-65.2424076635
344 (in isoform 2)Phosphorylation-52.9818510355
348 (in isoform 2)Phosphorylation-36.2320886841
404PhosphorylationFYFENLWSRNSKPVH
HHHHCHHCCCCCCCE		25.4224076635
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
286TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
286TPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
305TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
306TPhosphorylationKinaseCAMK2AQ9UQM7
PSP
332SPhosphorylationKinaseCAMK1Q14012
GPS
332SPhosphorylationKinaseCAMK4Q16566
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
286TPhosphorylation

29100089
286TPhosphorylation

29100089
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCC2B_HUMANCAMK2Bphysical
17353931
KCC2D_HUMANCAMK2Dphysical
17353931
CHMP5_HUMANCHMP5physical
17353931
DLG1_HUMANDLG1physical
12933808
RIMS1_HUMANRIMS1physical
12871946
ATF1_HUMANATF1physical
8663317
CREB1_HUMANCREB1physical
8663317
NMDE2_HUMANGRIN2Bphysical
11459059
LRRC7_RATLrrc7physical
11160423
ACTN4_HUMANACTN4physical
11160423
1433B_HUMANYWHABphysical
12619878
HDAC5_HUMANHDAC5physical
18292392
GIT1_HUMANGIT1physical
18292392
1433T_HUMANYWHAQphysical
18292392
PLCG1_HUMANPLCG1physical
18292392
ZN363_HUMANRCHY1physical
17568776
PRS8_HUMANPSMC5physical
22496558
SC6A3_HUMANSLC6A3physical
22514303
TAU_HUMANMAPTphysical
17512525
ITA2B_HUMANITGA2Bphysical
1650365
PTTG1_HUMANPTTG1physical
24781523
KCC2D_HUMANCAMK2Dphysical
25852190
KCC2G_HUMANCAMK2Gphysical
25852190
ZMYM1_HUMANZMYM1physical
25852190
GNAO_HUMANGNAO1physical
26344197
KCC2A_HUMANCAMK2Aphysical
11559703
SMAD2_HUMANSMAD2physical
25241761
KCC2B_HUMANCAMK2Bphysical
27173435
SSBP2_HUMANSSBP2physical
27173435
ARL3_HUMANARL3physical
27173435
DCTN2_HUMANDCTN2physical
27173435
DCTN1_HUMANDCTN1physical
27173435
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2A_HUMAN

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Related Literatures of Post-Translational Modification

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