dbPTM

KCC2A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCC2A_MOUSE
UniProt AC	P11798
Protein Name	Calcium/calmodulin-dependent protein kinase type II subunit alpha
Gene Name	Camk2a
Organism	Mus musculus (Mouse).
Sequence Length	478
Subcellular Localization	Isoform Alpha KAP: Cytoplasm . 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. Phosphorylates transcription factor FOXO3 on 'Ser-298' (By similarity). Activates FOXO3 transcriptional activity. [PubMed: 23805378]
Protein Sequence	MATITCTRFTEEYQLFEELGKGAFSVVRRCVKVLAGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGHHYLIFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKLKGAAVKLADFGLAIEVEGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDLWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPSKRITAAEALKHPWISHRSTVASCMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSGGKSGGNKKNDGVKESSESTNTTIEDEDTKVRKQEIIKVTEQLIEAISNGDFESYTKMCDPGMTAFEPEALGNLVEGLDFHRFYFENLWSRNSKPVHTTILNPHIHLMGDESACIAYIRITQYLDAGGIPRTAQSEETRVWHRRDGKWQIVHFHRSGAPSVLPH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MATITCTRFTEE ---CCEEEECCCCHH	11.94	29895711
6	S-palmitoylation	--MATITCTRFTEEY --CCEEEECCCCHHH	1.96	28680068
10	Phosphorylation	TITCTRFTEEYQLFE EEEECCCCHHHHHHH	25.31	19737024
13	Phosphorylation	CTRFTEEYQLFEELG ECCCCHHHHHHHHHC	12.32	18034455
21	Ubiquitination	QLFEELGKGAFSVVR HHHHHHCCCHHHHHH	60.74	-
25	Phosphorylation	ELGKGAFSVVRRCVK HHCCCHHHHHHHHHH	21.11	22817900
32	Ubiquitination	SVVRRCVKVLAGQEY HHHHHHHHHHCCCHH	34.85	-
39	Phosphorylation	KVLAGQEYAAKIINT HHHCCCHHHHHHHCC	12.17	-
42	Acetylation	AGQEYAAKIINTKKL CCCHHHHHHHCCCCC	35.63	11994385
42	Ubiquitination	AGQEYAAKIINTKKL CCCHHHHHHHCCCCC	35.63	-
43 (in isoform 2)	Phosphorylation	-	2.23	29899451
44 (in isoform 2)	Phosphorylation	-	5.44	25521595
45 (in isoform 2)	Phosphorylation	-	49.68	25521595
46 (in isoform 2)	Phosphorylation	-	21.10	25521595
47	Ubiquitination	AAKIINTKKLSARDH HHHHHCCCCCCHHHH	47.42	-
47	Acetylation	AAKIINTKKLSARDH HHHHHCCCCCCHHHH	47.42	19859547
48	Ubiquitination	AKIINTKKLSARDHQ HHHHCCCCCCHHHHH	45.71	-
52 (in isoform 2)	Phosphorylation	-	38.27	25521595
53 (in isoform 2)	Phosphorylation	-	48.57	25521595
55 (in isoform 2)	Phosphorylation	-	57.21	25521595
56 (in isoform 2)	Phosphorylation	-	49.23	29899451
58 (in isoform 2)	Phosphorylation	-	56.35	29899451
59 (in isoform 2)	Phosphorylation	-	54.00	29899451
68	Ubiquitination	ARICRLLKHPNIVRL HHHHHHHCCCCEEEE	62.70	-
137	Ubiquitination	GVVHRDLKPENLLLA CCCCCCCCHHHHHHH	55.35	-
145	Phosphorylation	PENLLLASKLKGAAV HHHHHHHHHHHCCHH	38.19	20415495
146	Ubiquitination	ENLLLASKLKGAAVK HHHHHHHHHHCCHHH	48.92	-
148	Ubiquitination	LLLASKLKGAAVKLA HHHHHHHHCCHHHHH	50.68	-
181	Phosphorylation	AGTPGYLSPEVLRKD CCCCCCCCHHHHHCC	15.55	23737553
226	Acetylation	HRLYQQIKAGAYDFP HHHHHHHHHCCCCCC	36.11	23236377
226	Ubiquitination	HRLYQQIKAGAYDFP HHHHHHHHHCCCCCC	36.11	-
230	Phosphorylation	QQIKAGAYDFPSPEW HHHHHCCCCCCCCCC	19.73	25521595
234	Phosphorylation	AGAYDFPSPEWDTVT HCCCCCCCCCCCCCC	35.13	25521595
239	Phosphorylation	FPSPEWDTVTPEAKD CCCCCCCCCCHHHHH	27.61	24925903
241	Phosphorylation	SPEWDTVTPEAKDLI CCCCCCCCHHHHHHH	19.94	20415495
245	Ubiquitination	DTVTPEAKDLINKML CCCCHHHHHHHHHHH	51.94	-
250	Ubiquitination	EAKDLINKMLTINPS HHHHHHHHHHCCCHH	28.44	-
253	O-linked_Glycosylation	DLINKMLTINPSKRI HHHHHHHCCCHHHCC	18.40	26741
253	Phosphorylation	DLINKMLTINPSKRI HHHHHHHCCCHHHCC	18.40	22817900
257	Phosphorylation	KMLTINPSKRITAAE HHHCCCHHHCCCHHH	30.03	22324799
258	Ubiquitination	MLTINPSKRITAAEA HHCCCHHHCCCHHHH	49.42	-
258	Acetylation	MLTINPSKRITAAEA HHCCCHHHCCCHHHH	49.42	129341
261	Phosphorylation	INPSKRITAAEALKH CCHHHCCCHHHHHCC	24.69	22324799
267	Ubiquitination	ITAAEALKHPWISHR CCHHHHHCCCCCCCH	55.45	-
272	Phosphorylation	ALKHPWISHRSTVAS HHCCCCCCCHHHHHH	14.69	25521595
275	Phosphorylation	HPWISHRSTVASCMH CCCCCCHHHHHHHHC	23.08	25521595
276	Phosphorylation	PWISHRSTVASCMHR CCCCCHHHHHHHHCH	21.76	25521595
279	Phosphorylation	SHRSTVASCMHRQET CCHHHHHHHHCHHHH	13.98	22817900
280	S-nitrosocysteine	HRSTVASCMHRQETV CHHHHHHHHCHHHHH	1.60	-
280	S-nitrosylation	HRSTVASCMHRQETV CHHHHHHHHCHHHHH	1.60	19101475
286	Phosphorylation	SCMHRQETVDCLKKF HHHCHHHHHHHHHHH	17.20	12198546
291	Ubiquitination	QETVDCLKKFNARRK HHHHHHHHHHCHHHH	62.74	-
292	Ubiquitination	ETVDCLKKFNARRKL HHHHHHHHHCHHHHH	30.79	-
298	Methylation	KKFNARRKLKGAILT HHHCHHHHHHHHHHH	49.34	-
300	Methylation	FNARRKLKGAILTTM HCHHHHHHHHHHHHH	49.70	-
300	Ubiquitination	FNARRKLKGAILTTM HCHHHHHHHHHHHHH	49.70	-
305	Phosphorylation	KLKGAILTTMLATRN HHHHHHHHHHHHHCC	12.21	22324799
306	O-linked_Glycosylation	LKGAILTTMLATRNF HHHHHHHHHHHHCCC	13.52	15497
306	Phosphorylation	LKGAILTTMLATRNF HHHHHHHHHHHHCCC	13.52	29899451
310	Phosphorylation	ILTTMLATRNFSGGK HHHHHHHHCCCCCCC	23.37	29899451
314	Phosphorylation	MLATRNFSGGKSGGN HHHHCCCCCCCCCCC	50.62	22817900
318	Phosphorylation	RNFSGGKSGGNKKND CCCCCCCCCCCCCCC	56.03	20415495
328	Ubiquitination	NKKNDGVKESSESTN CCCCCCCCCCCCCCC	58.36	-
330	Phosphorylation	KNDGVKESSESTNTT CCCCCCCCCCCCCCC	33.42	25521595
331	Phosphorylation	NDGVKESSESTNTTI CCCCCCCCCCCCCCC	36.34	25521595
333	Phosphorylation	GVKESSESTNTTIED CCCCCCCCCCCCCCC	28.98	25521595
334	Phosphorylation	VKESSESTNTTIEDE CCCCCCCCCCCCCCC	32.31	25521595
336	Phosphorylation	ESSESTNTTIEDEDT CCCCCCCCCCCCCCH	29.28	25521595
337	Phosphorylation	SSESTNTTIEDEDTK CCCCCCCCCCCCCHH	25.16	25521595
343	Phosphorylation	TTIEDEDTKVRKQEI CCCCCCCHHHHHHHH	29.41	25521595
344	Ubiquitination	TIEDEDTKVRKQEII CCCCCCHHHHHHHHH	52.98	-
362	Phosphorylation	EQLIEAISNGDFESY HHHHHHHHCCCHHHH	41.63	29899451
368	Phosphorylation	ISNGDFESYTKMCDP HHCCCHHHHHHCCCC	37.79	29899451
369	Phosphorylation	SNGDFESYTKMCDPG HCCCHHHHHHCCCCC	11.81	29899451
370	Phosphorylation	NGDFESYTKMCDPGM CCCHHHHHHCCCCCC	22.91	29899451
404	Phosphorylation	FYFENLWSRNSKPVH HHHHCHHCCCCCCCE	25.42	22324799
470	Phosphorylation	QIVHFHRSGAPSVLP EEEEEEECCCCCCCC	30.64	-

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
286	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
286	T	Phosphorylation	Kinase	CAMK2A	P11798	PSP
305	T	Phosphorylation	Kinase	CAMK2A	P11798	PSP
306	T	Phosphorylation	Kinase	CAMK2A	P11798	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
286	T	Phosphorylation	23805378
Autophosphorylation of Thr-286 following activation by Ca(2+)/calmodulin.
286	T	Phosphorylation	23805378
Phosphorylation of Thr-286 locks the kinase into an activated state.

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RHG32_MOUSE	Arhgap32	physical	12531901
NMDE2_MOUSE	Grin2b	physical	24734203
NMDZ1_MOUSE	Grin1	physical	24734203

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KCC2A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; THR-286; SER-333;THR-334 AND THR-337, AND MASS SPECTROMETRY.	17114649 [Abstract]
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.	15648052 [Abstract]
"Proteomic analysis of in vivo phosphorylated synaptic proteins."; Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.; J. Biol. Chem. 280:5972-5982(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASSSPECTROMETRY.	15572359 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, AND MASSSPECTROMETRY.	18034455 [Abstract]

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