dbPTM

CCG2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CCG2_MOUSE
UniProt AC	O88602
Protein Name	Voltage-dependent calcium channel gamma-2 subunit
Gene Name	Cacng2
Organism	Mus musculus (Mouse).
Sequence Length	323
Subcellular Localization	Membrane Multi-pass membrane protein. Cell junction, synapse, synaptosome .
Protein Description	Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state (By similarity)..
Protein Sequence	MGLFDRGVQMLLTTVGAFAAFSLMTIAVGTDYWLYSRGVCKTKSVSENETSKKNEEVMTHSGLWRTCCLEGNFKGLCKQIDHFPEDADYEADTAEYFLRAVRASSIFPILSVILLFMGGLCIAASEFYKTRHNIILSAGIFFVSAGLSNIIGIIVYISANAGDPSKSDSKKNSYSYGWSFYFGALSFIIAEMVGVLAVHMFIDRHKQLRATARATDYLQASAITRIPSYRYRYQRRSRSSSRSTEPSHSRDASPVGVKGFNTLPSTEISMYTLSRDPLKAATTPTATYNSDRDNSFLQVHNCIQKDSKDSLHANTANRRTTPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
42	Phosphorylation	YSRGVCKTKSVSENE EECCCCCCCCCCCCC	24.35	28576409
48	N-linked_Glycosylation	KTKSVSENETSKKNE CCCCCCCCCCCCCCH	50.79	-
217	Phosphorylation	ATARATDYLQASAIT HHHHHHHHHHHHHHH	9.07	25521595
221	Phosphorylation	ATDYLQASAITRIPS HHHHHHHHHHHCCCC	13.77	22817900
228	Phosphorylation	SAITRIPSYRYRYQR HHHHCCCCHHHHHHC	21.63	22817900
229	Phosphorylation	AITRIPSYRYRYQRR HHHCCCCHHHHHHCC	13.30	-
237	Phosphorylation	RYRYQRRSRSSSRST HHHHHCCCCCCCCCC	38.41	22817900
239	Phosphorylation	RYQRRSRSSSRSTEP HHHCCCCCCCCCCCC	33.63	22817900
240	Phosphorylation	YQRRSRSSSRSTEPS HHCCCCCCCCCCCCC	28.76	22817900
241	Phosphorylation	QRRSRSSSRSTEPSH HCCCCCCCCCCCCCC	31.34	22817900
243	Phosphorylation	RSRSSSRSTEPSHSR CCCCCCCCCCCCCCC	38.79	22817900
244	Phosphorylation	SRSSSRSTEPSHSRD CCCCCCCCCCCCCCC	51.29	29899451
247	Phosphorylation	SSRSTEPSHSRDASP CCCCCCCCCCCCCCC	28.06	22817900
249	Phosphorylation	RSTEPSHSRDASPVG CCCCCCCCCCCCCCC	35.87	22817900
253	Phosphorylation	PSHSRDASPVGVKGF CCCCCCCCCCCCCCC	25.14	25521595
271	Phosphorylation	PSTEISMYTLSRDPL CCCEEEEEEECCCCC	9.57	22817900
274	Phosphorylation	EISMYTLSRDPLKAA EEEEEEECCCCCCCC	27.17	29899451
282	Phosphorylation	RDPLKAATTPTATYN CCCCCCCCCCCCCCC	37.86	29899451
283	Phosphorylation	DPLKAATTPTATYNS CCCCCCCCCCCCCCC	17.57	29899451
287	Phosphorylation	AATTPTATYNSDRDN CCCCCCCCCCCCCCC	26.22	-
288	Phosphorylation	ATTPTATYNSDRDNS CCCCCCCCCCCCCCC	15.37	19060867
290	Phosphorylation	TPTATYNSDRDNSFL CCCCCCCCCCCCCCC	24.49	19060867
295	Phosphorylation	YNSDRDNSFLQVHNC CCCCCCCCCCHHEEE	31.46	29899451
305	Ubiquitination	QVHNCIQKDSKDSLH HHEEEECCCCCCCCC	44.02	22790023
310	Phosphorylation	IQKDSKDSLHANTAN ECCCCCCCCCCCCCC	26.28	29899451
321	Phosphorylation	NTANRRTTPV----- CCCCCCCCCC-----	21.90	11805122

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
321	T	Phosphorylation	Kinase	PRKACA	P05132	GPS
321	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
321	T	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
321	T	Phosphorylation		11805122
Phosphorylation of Thr-321 by PKA impairs interaction with DLG1 and DLG4.

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 CCG2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
GRIA1_MOUSE	Gria1	physical	15883194

Drug and Disease Associations

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

Regulatory Network of CCG2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-253, AND MASSSPECTROMETRY.	16452087 [Abstract]
"Phosphorylation of stargazin by protein kinase A regulates itsinteraction with PSD-95."; Choi J., Ko J., Park E., Lee J.-R., Yoon J., Lim S., Kim E.; J. Biol. Chem. 277:12359-12363(2002). Cited for: PHOSPHORYLATION AT THR-321, INTERACTION WITH DLG1 AND DLG4, ANDMUTAGENESIS OF THR-321 AND VAL-323.	11805122 [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-271, AND MASSSPECTROMETRY.	18034455 [Abstract]

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