dbPTM

NMDE2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NMDE2_MOUSE
UniProt AC	Q01097
Protein Name	Glutamate receptor ionotropic, NMDA 2B
Gene Name	Grin2b
Organism	Mus musculus (Mouse).
Sequence Length	1482
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane Multi-pass membrane protein .
Protein Description	Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). [PubMed: 1377365]
Protein Sequence	MKPSAECCSPKFWLVLAVLAVSGSKARSQKSAPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVLADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPSEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIISENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSTSSIDGLYDCDNPPFTTQPRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHLKHGTGDKHGVVGGVPAPWEKNLTNVDWEDRSGGNFCRSCPSKLHNYSSTVAGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVSSNASTTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMPAGESSFANKSSVTTAGHHHNNPGSGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKTRPDFRALVTNKPVVSALHGAVPGRFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
74	N-linked_Glycosylation	RVELVAMNETDPKSI CEEEEECCCCCHHHH	39.00	-
330	Phosphorylation	NTHEKRIYQSNMLNR CCCHHHHHHHCCCCC	15.21	30635358
332	Phosphorylation	HEKRIYQSNMLNRYL CHHHHHHHCCCCCEE	13.77	30635358
338	Phosphorylation	QSNMLNRYLINVTFE HHCCCCCEEEEEEEE	15.74	30635358
341	N-linked_Glycosylation	MLNRYLINVTFEGRN CCCCEEEEEEEECCC	24.96	-
343	Phosphorylation	NRYLINVTFEGRNLS CCEEEEEEEECCCCC	16.10	30635358
348	N-linked_Glycosylation	NVTFEGRNLSFSEDG EEEEECCCCCCCCCC	51.39	-
444	N-linked_Glycosylation	QKRIISENKTDEEPG HHHEECCCCCCCCCC	45.82	-
471	Phosphorylation	ILKKISKSVKFTYDL HHHHHCCCCCEEEEE	24.61	29895711
475	Phosphorylation	ISKSVKFTYDLYLVT HCCCCCEEEEEEEEE	15.48	29895711
479	Phosphorylation	VKFTYDLYLVTNGKH CCEEEEEEEEECCCC	9.02	29895711
482	Phosphorylation	TYDLYLVTNGKHGKK EEEEEEEECCCCCCE	35.34	29895711
491	N-linked_Glycosylation	GKHGKKINGTWNGMI CCCCCEECCCCCCHH	51.20	-
542	N-linked_Glycosylation	SVMVSRSNGTVSPSA EEEEECCCCCCCHHH	49.39	-
688	N-linked_Glycosylation	FRFGTVPNGSTERNI CCCCCCCCCCCHHHH	53.35	-
855	Phosphorylation	HCFMGVCSGKPGMVF HHHHHHHCCCCCCEE	47.66	-
871	S-palmitoylation	ISRGIYSCIHGVAIE ECCCHHHHHHCCHHH	1.17	28680068
882	Phosphorylation	VAIEERQSVMNSPTA CHHHHHHHHHCCCCH	29.56	25521595
886	Phosphorylation	ERQSVMNSPTATMNN HHHHHHCCCCHHHCC	12.92	25521595
888	Phosphorylation	QSVMNSPTATMNNTH HHHHCCCCHHHCCHH	34.28	25521595
890	Phosphorylation	VMNSPTATMNNTHSN HHCCCCHHHCCHHHH	23.94	22324799
894	Phosphorylation	PTATMNNTHSNILRL CCHHHCCHHHHHHHH	22.98	29899451
906	Ubiquitination	LRLLRTAKNMANLSG HHHHHHHHHHHHHCC	46.79	-
912	Phosphorylation	AKNMANLSGVNGSPQ HHHHHHHCCCCCCHH	40.27	22817900
917	Phosphorylation	NLSGVNGSPQSALDF HHCCCCCCHHHHHHH	17.98	25521595
920	Phosphorylation	GVNGSPQSALDFIRR CCCCCHHHHHHHHHH	33.90	22324799
929	Phosphorylation	LDFIRRESSVYDISE HHHHHHCCCCCCHHH	24.24	22817900
930	Phosphorylation	DFIRRESSVYDISEH HHHHHCCCCCCHHHH	21.68	22817900
932	Phosphorylation	IRRESSVYDISEHRR HHHCCCCCCHHHHHC	14.98	22817900
935	Phosphorylation	ESSVYDISEHRRSFT CCCCCCHHHHHCCCC	25.18	29899451
940	Phosphorylation	DISEHRRSFTHSDCK CHHHHHCCCCHHHHH	34.16	22324799
942	Phosphorylation	SEHRRSFTHSDCKSY HHHHCCCCHHHHHHC	23.01	23335269
944	Phosphorylation	HRRSFTHSDCKSYNN HHCCCCHHHHHHCCC	41.46	29899451
949	Phosphorylation	THSDCKSYNNPPCEE CHHHHHHCCCCCCHH	12.40	29899451
954	S-palmitoylation	KSYNNPPCEENLFSD HHCCCCCCHHCCCHH	12.35	28680068
960	Phosphorylation	PCEENLFSDYISEVE CCHHCCCHHHHHHHH	32.44	29899451
962	Phosphorylation	EENLFSDYISEVERT HHCCCHHHHHHHHHH	12.73	22817900
964	Phosphorylation	NLFSDYISEVERTFG CCCHHHHHHHHHHHC	29.39	29899451
978	Phosphorylation	GNLQLKDSNVYQDHY CCEEECCCCCCCCCC	26.97	-
1017	Phosphorylation	PFTTQPRSISKKPLD CCCCCCCCCCCCCCC	37.59	-
1019	Phosphorylation	TTQPRSISKKPLDIG CCCCCCCCCCCCCCC	35.55	-
1021	Ubiquitination	QPRSISKKPLDIGLP CCCCCCCCCCCCCCC	43.98	-
1029	Phosphorylation	PLDIGLPSSKHSQLS CCCCCCCCCCCHHHH	58.00	29899451
1030	Phosphorylation	LDIGLPSSKHSQLSD CCCCCCCCCCHHHHH	32.23	29899451
1031	Ubiquitination	DIGLPSSKHSQLSDL CCCCCCCCCHHHHHH	52.17	-
1033	Phosphorylation	GLPSSKHSQLSDLYG CCCCCCCHHHHHHHC	36.23	29899451
1036	Phosphorylation	SSKHSQLSDLYGKFS CCCCHHHHHHHCCCC	20.24	22324799
1039	Phosphorylation	HSQLSDLYGKFSFKS CHHHHHHHCCCCCCC	24.22	25521595
1041	Ubiquitination	QLSDLYGKFSFKSDR HHHHHHCCCCCCCCC	25.03	-
1043	Phosphorylation	SDLYGKFSFKSDRYS HHHHCCCCCCCCCCC	34.94	20139300
1046	Phosphorylation	YGKFSFKSDRYSGHD HCCCCCCCCCCCCCH	25.88	22817900
1049	Phosphorylation	FSFKSDRYSGHDDLI CCCCCCCCCCCHHHH	24.80	22817900
1050	Phosphorylation	SFKSDRYSGHDDLIR CCCCCCCCCCHHHHH	30.46	22817900
1058	Phosphorylation	GHDDLIRSDVSDIST CCHHHHHCCCCCCCC	35.06	22817900
1061	Phosphorylation	DLIRSDVSDISTHTV HHHHCCCCCCCCCEE	33.93	29899451
1064	Phosphorylation	RSDVSDISTHTVTYG HCCCCCCCCCEEECC	21.08	22817900
1065	Phosphorylation	SDVSDISTHTVTYGN CCCCCCCCCEEECCC	23.15	29899451
1067	Phosphorylation	VSDISTHTVTYGNIE CCCCCCCEEECCCCC	18.03	22817900
1069	Phosphorylation	DISTHTVTYGNIEGN CCCCCEEECCCCCCH	27.20	29899451
1070	Phosphorylation	ISTHTVTYGNIEGNA CCCCEEECCCCCCHH	12.11	29899451
1085	Phosphorylation	AKRRKQQYKDSLKKR HHHHHHHHHHHHHHC	17.80	29899451
1088	Phosphorylation	RKQQYKDSLKKRPAS HHHHHHHHHHHCCCC	37.63	29899451
1098	Phosphorylation	KRPASAKSRREFDEI HCCCCHHHHHHHHHH	35.97	29899451
1109	Phosphorylation	FDEIELAYRRRPPRS HHHHHHHHHCCCCCC	19.78	22817900
1116	Phosphorylation	YRRRPPRSPDHKRYF HHCCCCCCCCCHHHC	40.22	22817900
1126	Ubiquitination	HKRYFRDKEGLRDFY CHHHCCCCCCCCHHH	49.80	-
1133	Phosphorylation	KEGLRDFYLDQFRTK CCCCCHHHHHHHCCC	17.41	29899451
1139	Phosphorylation	FYLDQFRTKENSPHW HHHHHHCCCCCCCCC	43.96	22817900
1143	Phosphorylation	QFRTKENSPHWEHVD HHCCCCCCCCCCCCC	21.16	25521595
1152	Phosphorylation	HWEHVDLTDIYKERS CCCCCCHHHHHHHCC	18.85	22817900
1155	Phosphorylation	HVDLTDIYKERSDDF CCCHHHHHHHCCCCC	15.03	22817900
1159	Phosphorylation	TDIYKERSDDFKRDS HHHHHHCCCCCCCCC	42.49	29899451
1166	Phosphorylation	SDDFKRDSVSGGGPC CCCCCCCCCCCCCCC	23.40	25521595
1168	Phosphorylation	DFKRDSVSGGGPCTN CCCCCCCCCCCCCCC	35.35	20415495
1215	S-palmitoylation	DRSGGNFCRSCPSKL CCCCCCCCCCCCHHH	3.48	30846936
1218	S-palmitoylation	GGNFCRSCPSKLHNY CCCCCCCCCHHHCCC	1.97	30846936
1225	Phosphorylation	CPSKLHNYSSTVAGQ CCHHHCCCCCCCCCC	8.02	29899451
1228	Phosphorylation	KLHNYSSTVAGQNSG HHCCCCCCCCCCCCC	14.40	29899451
1234	Phosphorylation	STVAGQNSGRQACIR CCCCCCCCCCCEEHH	27.71	29899451
1239	S-palmitoylation	QNSGRQACIRCEACK CCCCCCEEHHHHHHH	1.20	30846936
1242	S-palmitoylation	GRQACIRCEACKKAG CCCEEHHHHHHHHHC	1.65	30846936
1245	S-palmitoylation	ACIRCEACKKAGNLY EEHHHHHHHHHCCEE	1.86	30846936
1252	Phosphorylation	CKKAGNLYDISEDNS HHHHCCEECCCCCCC	18.41	29899451
1255	Phosphorylation	AGNLYDISEDNSLQE HCCEECCCCCCCCCC	35.68	22817900
1259	Phosphorylation	YDISEDNSLQELDQP ECCCCCCCCCCCCCC	43.69	22817900
1281	Phosphorylation	SNASTTKYPQSPTNS CCCCCCCCCCCCCCH	12.38	20415495
1284	Phosphorylation	STTKYPQSPTNSKAQ CCCCCCCCCCCHHHH	29.23	25521595
1286	Phosphorylation	TKYPQSPTNSKAQKK CCCCCCCCCHHHHHH	58.32	25521595
1288	Phosphorylation	YPQSPTNSKAQKKNR CCCCCCCHHHHHHHH	31.67	20415495
1303	Phosphorylation	NKLRRQHSYDTFVDL HHHHHHHCHHHHHHH	19.16	25521595
1304	Phosphorylation	KLRRQHSYDTFVDLQ HHHHHHCHHHHHHHH	19.51	25521595
1306	Phosphorylation	RRQHSYDTFVDLQKE HHHHCHHHHHHHHHH	19.82	22324799
1321	Phosphorylation	EAALAPRSVSLKDKG HHHHCCCCCCCCCCC	18.26	22324799
1323	Phosphorylation	ALAPRSVSLKDKGRF HHCCCCCCCCCCCCC	30.83	11306676
1334	Phosphorylation	KGRFMDGSPYAHMFE CCCCCCCCCCCEEEE	15.52	19060867
1336	Phosphorylation	RFMDGSPYAHMFEMP CCCCCCCCCEEEECC	15.73	22817900
1369	Phosphorylation	HNNPGSGYMLSKSLY CCCCCCCCCCCCCCC	9.15	29899451
1374	Phosphorylation	SGYMLSKSLYPDRVT CCCCCCCCCCCCCCC	29.74	29899451
1399	Phosphorylation	DQCLLHGSKSYFFRQ CCEEECCCEEEECCC	14.00	29899451
1401	Phosphorylation	CLLHGSKSYFFRQPT EEECCCEEEECCCCC	28.95	29899451
1426	Acetylation	FRALVTNKPVVSALH HHHHHCCCCHHHHCC	29.80	19861867
1426	Ubiquitination	FRALVTNKPVVSALH HHHHHCCCCHHHHCC	29.80	-
1458	Ubiquitination	NPCVPNNKNPRAFNG CCCCCCCCCCCCCCC	74.99	-
1472	Phosphorylation	GSSNGHVYEKLSSIE CCCCCCHHHHHHCCC	11.15	20427654
1477	Phosphorylation	HVYEKLSSIESDV-- CHHHHHHCCCCCC--	40.59	25521595
1480	Phosphorylation	EKLSSIESDV----- HHHHCCCCCC-----	41.84	25521595

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
932	Y	Phosphorylation	Kinase	FYN	P39688	PhosphoELM
1039	Y	Phosphorylation	Kinase	FYN	P39688	PhosphoELM
1070	Y	Phosphorylation	Kinase	FRK	Q922K9	PSP
1070	Y	Phosphorylation	Kinase	FYN	P06241	PSP
1070	Y	Phosphorylation	Kinase	FYN	P39688	PhosphoELM
1109	Y	Phosphorylation	Kinase	FYN	P39688	PhosphoELM
1116	S	Phosphorylation	Kinase	CDK5	P49615	PSP
1252	Y	Phosphorylation	Kinase	FYN	P39688	PSP
1303	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
1303	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
1303	S	Phosphorylation	Kinase	PKACA	P05132	PSP
1303	S	Phosphorylation	Kinase	DAPK1	Q80YE7	Uniprot
1323	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
1323	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
1336	Y	Phosphorylation	Kinase	FYN	P39688	PSP
1472	Y	Phosphorylation	Kinase	PKACA	P05132	PSP
1472	Y	Phosphorylation	Kinase	SRC	P05480	PSP
1472	Y	Phosphorylation	Kinase	FYN	P39688	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1303	S	Phosphorylation		20141836
Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity.

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 NMDE2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOS1_MOUSE	Nos1	physical	10862698
SYGP1_MOUSE	Syngap1	physical	10862698
DLGP1_MOUSE	Dlgap1	physical	10862698
CTRO_MOUSE	Cit	physical	10862698
NMDZ1_MOUSE	Grin1	physical	10862698
NMDE1_MOUSE	Grin2a	physical	10862698
DLG4_MOUSE	Dlg4	physical	10862698
DLG2_MOUSE	Dlg2	physical	10862698
GRM1_MOUSE	Grm1	physical	10862698
HOME1_MOUSE	Homer1	physical	10862698
DLG3_MOUSE	Dlg3	physical	10862698
SHAN2_MOUSE	Shank2	physical	10862698
AKAP9_MOUSE	Akap9	physical	10862698
AKAP5_MOUSE	Akap5	physical	10862698
NSF_MOUSE	Nsf	physical	10862698
KAPCA_MOUSE	Prkaca	physical	10862698
KAP3_MOUSE	Prkar2b	physical	10862698
KPCB_MOUSE	Prkcb	physical	10862698
KPCG_MOUSE	Prkcg	physical	10862698
KPCE_MOUSE	Prkce	physical	10862698
KCC2B_MOUSE	Camk2b	physical	10862698
PP1G_MOUSE	Ppp1cc	physical	10862698
PP2AA_MOUSE	Ppp2ca	physical	10862698
PP2BA_MOUSE	Ppp3ca	physical	10862698
PPP5_MOUSE	Ppp5c	physical	10862698
PTN11_MOUSE	Ptpn11	physical	10862698
SRC_MOUSE	Src	physical	10862698
FAK2_MOUSE	Ptk2b	physical	10862698
MK01_MOUSE	Mapk1	physical	10862698
MK03_MOUSE	Mapk3	physical	10862698
MP2K1_MOUSE	Map2k1	physical	10862698
MP2K2_MOUSE	Map2k2	physical	10862698
DUS4_MOUSE	Dusp4	physical	10862698
KS6A1_MOUSE	Rps6ka1	physical	10862698
KS6A3_MOUSE	Rps6ka3	physical	10862698
RAF1_MOUSE	Raf1	physical	10862698
RAC1_MOUSE	Rac1	physical	10862698
RAP1A_MOUSE	Rap1a	physical	10862698
NF1_MOUSE	Nf1	physical	10862698
RASH_MOUSE	Hras	physical	10862698
RALA_MOUSE	Rala	physical	10862698
P85A_MOUSE	Pik3r1	physical	10862698
PLCG1_MOUSE	Plcg1	physical	10862698
PA24A_MOUSE	Pla2g4a	physical	10862698
ARC_MOUSE	Arc	physical	10862698
CADH2_MOUSE	Cdh2	physical	10862698
DSG1A_MOUSE	Dsg1a	physical	10862698
CTNB1_MOUSE	Ctnnb1	physical	10862698
CTND1_MOUSE	Ctnnd1	physical	10862698
MTAP2_MOUSE	Map2	physical	10862698
ACTC_MOUSE	Actc1	physical	10862698
ACTN2_MOUSE	Actn2	physical	10862698
SPTA1_MOUSE	Spta1	physical	10862698
TBA1A_MOUSE	Tuba1a	physical	10862698
SRC8_MOUSE	Cttn	physical	10862698
CLH1_MOUSE	Cltc	physical	10862698
DYN1_MOUSE	Dnm1	physical	10862698
HS71B_MOUSE	Hspa1b	physical	10862698
NMDZ1_MOUSE	Grin1	physical	16554481
NMDE1_MOUSE	Grin2a	physical	16554481
NMDE1_MOUSE	Grin2a	physical	14645471
NMDZ1_MOUSE	Grin1	physical	14645471
DLG4_MOUSE	Dlg4	physical	15663482
LRP1_MOUSE	Lrp1	physical	23760271

Drug and Disease Associations

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

Regulatory Network of NMDE2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"DAPK1 interaction with NMDA receptor NR2B subunits mediates braindamage in stroke."; Tu W., Xu X., Peng L., Zhong X., Zhang W., Soundarapandian M.M.,Balel C., Wang M., Jia N., Zhang W., Lew F., Chan S.L., Chen Y.,Lu Y.; Cell 140:222-234(2010). Cited for: FUNCTION, PHOSPHORYLATION AT SER-1303, AND INTERACTION WITH DAPK1.	20141836 [Abstract]
"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-917 AND SER-1303, ANDMASS SPECTROMETRY.	17114649 [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 SER-930; TYR-932; TYR-949;TYR-962; TYR-1039; TYR-1049; SER-1061; THR-1065; TYR-1070; TYR-1109;TYR-1155; TYR-1252; SER-1303 AND TYR-1304, AND MASS SPECTROMETRY.	18034455 [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 SER-1166 AND SER-1303, ANDMASS SPECTROMETRY.	16452087 [Abstract]
"Regulation of NMDA receptor function by Fyn-mediated tyrosinephosphorylation."; Nakazawa T., Tezuka T., Yamamoto T.; Nihon Shinkei Seishin Yakurigaku Zasshi 22:165-167(2002). Cited for: PHOSPHORYLATION AT TYR-1472.	12451687 [Abstract]

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