dbPTM

KCC2B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KCC2B_MOUSE
UniProt AC	P28652
Protein Name	Calcium/calmodulin-dependent protein kinase type II subunit beta
Gene Name	Camk2b
Organism	Mus musculus (Mouse).
Sequence Length	542
Subcellular Localization	Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Sarcoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side. Cell junction, synapse .
Protein Description	Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in dendritic spine and synapse formation, neuronal plasticity and regulation of sarcoplasmic reticulum Ca(2+) transport in skeletal muscle. In neurons, plays an essential structural role in the reorganization of the actin cytoskeleton during plasticity by binding and bundling actin filaments in a kinase-independent manner. This structural function is required for correct targeting of CaMK2A, which acts downstream of NMDAR to promote dendritic spine and synapse formation and maintain synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In developing hippocampal neurons, promotes arborization of the dendritic tree and in mature neurons, promotes dendritic remodeling. Participates in the modulation of skeletal muscle function in response to exercise. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of triadin, a ryanodine receptor-coupling factor, and phospholamban (PLN/PLB), an endogenous inhibitor of SERCA2A/ATP2A2..
Protein Sequence	MATTVTCTRFTDEYQLYEDIGKGAFSVVRRCVKLCTGHEYAAKIINTKKLSARDHQKLEREARICRLLKHSNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILEAVLHCHQMGVVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKEAYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITAHEALKHPWVCQRSTVASMMHRQETVECLKKFNARRKLKGAILTTMLATRNFSVGRQTTAPATMSTAASGTTMGLVEQAKSLLNKKADGVKPQTNSTKNSSAITSPKGSLPPAALEPQTTVIHNPVDGIKESSDSTNTTIEDEDAKARKQEIIKTTEQLIEAVNNGDFEAYAKICDPGLTSFEPEALGNLVEGMDFHRFYFENLLAKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWQNVHFHCSGAPVAPLQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Phosphorylation	FTDEYQLYEDIGKGA CCCCCHHHHHHCCCH	8.95	20415495
22	Ubiquitination	QLYEDIGKGAFSVVR HHHHHHCCCHHHHHH	47.61	-
26	Phosphorylation	DIGKGAFSVVRRCVK HHCCCHHHHHHHHHH	21.11	18056256
33	Ubiquitination	SVVRRCVKLCTGHEY HHHHHHHHHHCCCHH	41.28	-
35	S-nitrosylation	VRRCVKLCTGHEYAA HHHHHHHHCCCHHHH	3.38	24895380
40	Phosphorylation	KLCTGHEYAAKIINT HHHCCCHHHHHHHHC	13.24	29899451
43	Ubiquitination	TGHEYAAKIINTKKL CCCHHHHHHHHCCCC	35.63	-
48	Acetylation	AAKIINTKKLSARDH HHHHHHCCCCCHHHH	47.42	7848607
48	Ubiquitination	AAKIINTKKLSARDH HHHHHHCCCCCHHHH	47.42	-
49	Ubiquitination	AKIINTKKLSARDHQ HHHHHCCCCCHHHHH	45.71	-
69	Ubiquitination	ARICRLLKHSNIVRL HHHHHHHHHCCEEEE	49.97	-
79	Phosphorylation	NIVRLHDSISEEGFH CEEEECCCCCCCCCE	19.78	-
138	Ubiquitination	GVVHRDLKPENLLLA CCCCCCCCHHHHHHH	55.35	-
146	Phosphorylation	PENLLLASKCKGAAV HHHHHHHHCCCCCCE	38.26	22817900
147	Ubiquitination	ENLLLASKCKGAAVK HHHHHHHCCCCCCEE	34.07	-
182	Phosphorylation	AGTPGYLSPEVLRKE CCCCCCCCHHHHHHH	15.55	23737553
227	Ubiquitination	HKLYQQIKAGAYDFP HHHHHHHHHCCCCCC	36.11	-
231	Phosphorylation	QQIKAGAYDFPSPEW HHHHHCCCCCCCCCH	19.73	24925903
235	Phosphorylation	AGAYDFPSPEWDTVT HCCCCCCCCCHHCCC	35.13	24925903
240	Phosphorylation	FPSPEWDTVTPEAKN CCCCCHHCCCHHHHH	27.61	24925903
242	Phosphorylation	SPEWDTVTPEAKNLI CCCHHCCCHHHHHHH	19.94	24925903
246	Ubiquitination	DTVTPEAKNLINQML HCCCHHHHHHHHHHH	51.10	-
254	Phosphorylation	NLINQMLTINPAKRI HHHHHHHCCCHHHCC	17.23	25521595
259	Ubiquitination	MLTINPAKRITAHEA HHCCCHHHCCCHHHH	45.66	-
268	Ubiquitination	ITAHEALKHPWVCQR CCHHHHHCCCCHHCH	55.45	-
276	Phosphorylation	HPWVCQRSTVASMMH CCCHHCHHHHHHHHH	11.01	25521595
277	Phosphorylation	PWVCQRSTVASMMHR CCHHCHHHHHHHHHH	23.45	25521595
280	Phosphorylation	CQRSTVASMMHRQET HCHHHHHHHHHHHHH	16.59	25521595
287	Phosphorylation	SMMHRQETVECLKKF HHHHHHHHHHHHHHH	17.17	25521595
290	S-nitrosylation	HRQETVECLKKFNAR HHHHHHHHHHHHCHH	6.16	24895380
299	Methylation	KKFNARRKLKGAILT HHHCHHHHHHHHHHH	49.34	-
301	Ubiquitination	FNARRKLKGAILTTM HCHHHHHHHHHHHHH	49.70	-
301	Methylation	FNARRKLKGAILTTM HCHHHHHHHHHHHHH	49.70	-
306	Phosphorylation	KLKGAILTTMLATRN HHHHHHHHHHHHCCC	12.21	20415495
307	Phosphorylation	LKGAILTTMLATRNF HHHHHHHHHHHCCCC	13.52	20415495
307	O-linked_Glycosylation	LKGAILTTMLATRNF HHHHHHHHHHHCCCC	13.52	4041595
311	Phosphorylation	ILTTMLATRNFSVGR HHHHHHHCCCCCCCC	23.37	20415495
315	Phosphorylation	MLATRNFSVGRQTTA HHHCCCCCCCCCCCC	27.49	28542873
320	Phosphorylation	NFSVGRQTTAPATMS CCCCCCCCCCCCCCC	24.46	29899451
321	Phosphorylation	FSVGRQTTAPATMST CCCCCCCCCCCCCCC	23.47	18056256
325	Phosphorylation	RQTTAPATMSTAASG CCCCCCCCCCCCCCC	15.59	25521595
325	O-linked_Glycosylation	RQTTAPATMSTAASG CCCCCCCCCCCCCCC	15.59	100712363
327	Phosphorylation	TTAPATMSTAASGTT CCCCCCCCCCCCCCC	15.56	20415495
327	O-linked_Glycosylation	TTAPATMSTAASGTT CCCCCCCCCCCCCCC	15.56	100712369
328	O-linked_Glycosylation	TAPATMSTAASGTTM CCCCCCCCCCCCCCH	18.54	68716875
328	Phosphorylation	TAPATMSTAASGTTM CCCCCCCCCCCCCCH	18.54	25521595
331	Phosphorylation	ATMSTAASGTTMGLV CCCCCCCCCCCHHHH	33.92	25521595
333	Phosphorylation	MSTAASGTTMGLVEQ CCCCCCCCCHHHHHH	15.89	19060867
334	Phosphorylation	STAASGTTMGLVEQA CCCCCCCCHHHHHHH	16.87	21183079
343	Phosphorylation	GLVEQAKSLLNKKAD HHHHHHHHHHHHCCC	40.90	22322096
347	Acetylation	QAKSLLNKKADGVKP HHHHHHHHCCCCCCC	49.67	7610711
356	Phosphorylation	ADGVKPQTNSTKNSS CCCCCCCCCCCCCCC	39.40	20415495
358	Phosphorylation	GVKPQTNSTKNSSAI CCCCCCCCCCCCCCC	44.11	25521595
359	Phosphorylation	VKPQTNSTKNSSAIT CCCCCCCCCCCCCCC	35.99	20415495
362	Phosphorylation	QTNSTKNSSAITSPK CCCCCCCCCCCCCCC	23.78	24925903
363	Phosphorylation	TNSTKNSSAITSPKG CCCCCCCCCCCCCCC	32.84	25521595
366	Phosphorylation	TKNSSAITSPKGSLP CCCCCCCCCCCCCCC	38.40	22324799
367	Phosphorylation	KNSSAITSPKGSLPP CCCCCCCCCCCCCCH	20.64	25521595
371	Phosphorylation	AITSPKGSLPPAALE CCCCCCCCCCHHHCC	43.77	22324799
381	Phosphorylation	PAALEPQTTVIHNPV HHHCCCCCEEEECCC	33.47	25521595
382	Phosphorylation	AALEPQTTVIHNPVD HHCCCCCEEEECCCC	16.53	25521595
394	Phosphorylation	PVDGIKESSDSTNTT CCCCCCCCCCCCCCC	34.15	25521595
395	Phosphorylation	VDGIKESSDSTNTTI CCCCCCCCCCCCCCC	36.35	25521595
397	Phosphorylation	GIKESSDSTNTTIED CCCCCCCCCCCCCCH	26.04	25521595
398	Phosphorylation	IKESSDSTNTTIEDE CCCCCCCCCCCCCHH	41.39	25521595
400	Phosphorylation	ESSDSTNTTIEDEDA CCCCCCCCCCCHHHH	29.28	25521595
401	Phosphorylation	SSDSTNTTIEDEDAK CCCCCCCCCCHHHHH	25.16	25521595
469	Ubiquitination	YFENLLAKNSKPIHT HHHHHHHCCCCCCEE	62.82	-
510	Phosphorylation	DGQGRPRTSQSEETR CCCCCCCCCCCCCCE	33.53	22807455
533	S-palmitoylation	WQNVHFHCSGAPVAP CEEEEEEECCCCCCC	3.82	28680068
533	S-nitrosylation	WQNVHFHCSGAPVAP CEEEEEEECCCCCCC	3.82	24895380

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
287	T	Phosphorylation	Kinase	CAMK2B	P28652	GPS
315	S	Phosphorylation	Kinase	PRKCG	P63318	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
287	T	Phosphorylation	16452087
Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin.
287	T	Phosphorylation	16452087
Phosphorylation of Thr-287 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 KCC2B_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of KCC2B_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of KCC2B_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-367; THR-287 ANDSER-397, AND MASS SPECTROMETRY.	17114649 [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-315, AND MASSSPECTROMETRY.	15572359 [Abstract]
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations."; Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.; Mol. Cell. Proteomics 5:914-922(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND MASSSPECTROMETRY.	16452087 [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-17, AND MASSSPECTROMETRY.	18034455 [Abstract]

show

show