dbPTM

NMDE2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NMDE2_RAT
UniProt AC	Q00960
Protein Name	Glutamate receptor ionotropic, NMDA 2B
Gene Name	Grin2b
Organism	Rattus norvegicus (Rat).
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: 1350383]
Protein Sequence	MKPSAECCSPKFWLVLAVLAVSGSKARSQKSPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMSDRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSIEQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLDDGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVPSEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIYQSNMLNRYLINVTFEGRNLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYVWPRMCPETEEQEDDHLSIVTLEEAPFVIVESVDPLSGTCMRNTVPCQKRIISENKTDEEPGYIKKCCKGFCIDILKKISKSVKFTYDLYLVTNGKHGKKINGTWNGMIGEVVMKRAYMAVGSLTINEERSEVVDFSVPFIETGISVMVSRSNGTVSPSAFLEPFSADVWVMMFVMLLIVSAVAVFVFEYFSPVGYNRCLADGREPGGPSFTIGKAIWLLWGLVFNNSVPVQNPKGTTSKIMVSVWAFFAVIFLASYTANLAAFMIQEEYVDQVSGLSDKKFQRPNDFSPPFRFGTVPNGSTERNIRNNYAEMHAYMGKFNQRGVDDALLSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGKVFASTGYGIAIQKDSGWKRQVDLAILQLFGDGEMEELEALWLTGICHNEKNEVMSSQLDIDNMAGVFYMLGAAMALSLITFICEHLFYWQFRHCFMGVCSGKPGMVFSISRGIYSCIHGVAIEERQSVMNSPTATMNNTHSNILRLLRTAKNMANLSGVNGSPQSALDFIRRESSVYDISEHRRSFTHSDCKSYNNPPCEENLFSDYISEVERTFGNLQLKDSNVYQDHYHHHHRPHSIGSTSSIDGLYDCDNPPFTTQPRSISKKPLDIGLPSSKHSQLSDLYGKFSFKSDRYSGHDDLIRSDVSDISTHTVTYGNIEGNAAKRRKQQYKDSLKKRPASAKSRREFDEIELAYRRRPPRSPDHKRYFRDKEGLRDFYLDQFRTKENSPHWEHVDLTDIYKERSDDFKRDSVSGGGPCTNRSHLKHGTGEKHGVVGGVPAPWEKNLTNVDWEDRSGGNFCRSCPSKLHNYSSTVAGQNSGRQACIRCEACKKAGNLYDISEDNSLQELDQPAAPVAVTSNASSTKYPQSPTNSKAQKKNRNKLRRQHSYDTFVDLQKEEAALAPRSVSLKDKGRFMDGSPYAHMFEMPAGESSFANKSSVPTAGHHHNNPGSGYMLSKSLYPDRVTQNPFIPTFGDDQCLLHGSKSYFFRQPTVAGASKTRPDFRALVTNKPVVVTLHGAVPGRFQKDICIGNQSNPCVPNNKNPRAFNGSSNGHVYEKLSSIESDV

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	24876489
338	Phosphorylation	QSNMLNRYLINVTFE HHCCCCCEEEEEEEE	15.74	-
341	N-linked_Glycosylation	MLNRYLINVTFEGRN CCCCEEEEEEEECCC	24.96	24876489
348	N-linked_Glycosylation	NVTFEGRNLSFSEDG EEEEECCCCCCCCCC	51.39	-
383	Phosphorylation	VGKWKDKSLQMKYYV CCCCCCCCHHCEEEE	33.69	8940188
444	N-linked_Glycosylation	QKRIISENKTDEEPG HHHEECCCCCCCCCC	45.82	-
471	Phosphorylation	ILKKISKSVKFTYDL HHHHHCCCCCEEEEE	24.61	28432305
475	Phosphorylation	ISKSVKFTYDLYLVT HCCCCCEEEEEEEEE	15.48	28432305
476	Phosphorylation	SKSVKFTYDLYLVTN CCCCCEEEEEEEEEC	13.69	28432305
479	Phosphorylation	VKFTYDLYLVTNGKH CCEEEEEEEEECCCC	9.02	28432305
482	Phosphorylation	TYDLYLVTNGKHGKK EEEEEEEECCCCCCE	35.34	28432305
491	N-linked_Glycosylation	GKHGKKINGTWNGMI CCCCCEECCCCCCHH	51.20	-
542	N-linked_Glycosylation	SVMVSRSNGTVSPSA EEEEECCCCCCCHHH	49.39	-
688	N-linked_Glycosylation	FRFGTVPNGSTERNI CCCCCCCCCCCHHHH	53.35	24876489
849	S-palmitoylation	FYWQFRHCFMGVCSG HHHHHHHHHHHHHCC	1.88	19874789
854	S-palmitoylation	RHCFMGVCSGKPGMV HHHHHHHHCCCCCCE	3.53	19874789
871	S-palmitoylation	ISRGIYSCIHGVAIE ECCCHHHHHHCCHHH	1.17	19874789
882	Phosphorylation	VAIEERQSVMNSPTA CHHHHHHHHHCCCCH	29.56	30240740
886	Phosphorylation	ERQSVMNSPTATMNN HHHHHHCCCCHHHCC	12.92	30240740
888	Phosphorylation	QSVMNSPTATMNNTH HHHHCCCCHHHCCHH	34.28	22673903
890	Phosphorylation	VMNSPTATMNNTHSN HHCCCCHHHCCHHHH	23.94	30240740
912	Phosphorylation	AKNMANLSGVNGSPQ HHHHHHHCCCCCCHH	40.27	27097102
917	Phosphorylation	NLSGVNGSPQSALDF HHCCCCCCHHHHHHH	17.98	27097102
920	Phosphorylation	GVNGSPQSALDFIRR CCCCCHHHHHHHHHH	33.90	27097102
929	Phosphorylation	LDFIRRESSVYDISE HHHHHHCCCCCCHHH	24.24	25403869
930	Phosphorylation	DFIRRESSVYDISEH HHHHHCCCCCCHHHH	21.68	-
932	Phosphorylation	IRRESSVYDISEHRR HHHCCCCCCHHHHHC	14.98	25403869
935	Phosphorylation	ESSVYDISEHRRSFT CCCCCCHHHHHCCCC	25.18	-
940	Phosphorylation	DISEHRRSFTHSDCK CHHHHHCCCCHHHHH	34.16	25403869
942	Phosphorylation	SEHRRSFTHSDCKSY HHHHCCCCHHHHHHC	23.01	25403869
944	Phosphorylation	HRRSFTHSDCKSYNN HHCCCCHHHHHHCCC	41.46	25403869
948	Phosphorylation	FTHSDCKSYNNPPCE CCHHHHHHCCCCCCH	39.15	-
949	Phosphorylation	THSDCKSYNNPPCEE CHHHHHHCCCCCCHH	12.40	-
960	Phosphorylation	PCEENLFSDYISEVE CCHHCCCHHHHHHHH	32.44	-
962	Phosphorylation	EENLFSDYISEVERT HHCCCHHHHHHHHHH	12.73	-
964	Phosphorylation	NLFSDYISEVERTFG CCCHHHHHHHHHHHC	29.39	-
981	Phosphorylation	QLKDSNVYQDHYHHH EECCCCCCCCCCCCC	16.69	-
985	Phosphorylation	SNVYQDHYHHHHRPH CCCCCCCCCCCCCCC	15.90	-
993	Phosphorylation	HHHHRPHSIGSTSSI CCCCCCCCCCCCCCC	31.18	-
1004	Phosphorylation	TSSIDGLYDCDNPPF CCCCCCCCCCCCCCC	21.76	-
1030	Phosphorylation	LDIGLPSSKHSQLSD CCCCCCCCCCHHHHH	32.23	-
1033	Phosphorylation	GLPSSKHSQLSDLYG CCCCCCCHHHHHHHC	36.23	-
1036	Phosphorylation	SSKHSQLSDLYGKFS CCCCHHHHHHHCCCC	20.24	-
1039	Phosphorylation	HSQLSDLYGKFSFKS CHHHHHHHCCCCCCC	24.22	30411139
1043	Phosphorylation	SDLYGKFSFKSDRYS HHHHCCCCCCCCCCC	34.94	23298284
1046	Phosphorylation	YGKFSFKSDRYSGHD HCCCCCCCCCCCCCH	25.88	-
1049	Phosphorylation	FSFKSDRYSGHDDLI CCCCCCCCCCCHHHH	24.80	-
1050	Phosphorylation	SFKSDRYSGHDDLIR CCCCCCCCCCHHHHH	30.46	-
1058	Phosphorylation	GHDDLIRSDVSDIST CCHHHHHCCCCCCCC	35.06	25403869
1061	Phosphorylation	DLIRSDVSDISTHTV HHHHCCCCCCCCCEE	33.93	25403869
1064	Phosphorylation	RSDVSDISTHTVTYG HCCCCCCCCCEEECC	21.08	25403869
1065	Phosphorylation	SDVSDISTHTVTYGN CCCCCCCCCEEECCC	23.15	25403869
1067	Phosphorylation	VSDISTHTVTYGNIE CCCCCCCEEECCCCC	18.03	25403869
1069	Phosphorylation	DISTHTVTYGNIEGN CCCCCEEECCCCCCH	27.20	-
1070	Phosphorylation	ISTHTVTYGNIEGNA CCCCEEECCCCCCHH	12.11	-
1109	Phosphorylation	FDEIELAYRRRPPRS HHHHHHHHHCCCCCC	19.78	-
1116	Phosphorylation	YRRRPPRSPDHKRYF HHCCCCCCCCCHHHC	40.22	25403869
1133	Phosphorylation	KEGLRDFYLDQFRTK CCCCCHHHHHHHCCC	17.41	-
1139	Phosphorylation	FYLDQFRTKENSPHW HHHHHHCCCCCCCCC	43.96	-
1143	Phosphorylation	QFRTKENSPHWEHVD HHCCCCCCCCCCCCC	21.16	-
1152	Phosphorylation	HWEHVDLTDIYKERS CCCCCCHHHHHHHCC	18.85	-
1155	Phosphorylation	HVDLTDIYKERSDDF CCCHHHHHHHCCCCC	15.03	-
1166	Phosphorylation	SDDFKRDSVSGGGPC CCCCCCCCCCCCCCC	23.40	25403869
1221	Ubiquitination	FCRSCPSKLHNYSST CCCCCCHHHCCCCCC	38.62	-
1225	Phosphorylation	CPSKLHNYSSTVAGQ CCHHHCCCCCCCCCC	8.02	-
1226	Phosphorylation	PSKLHNYSSTVAGQN CHHHCCCCCCCCCCC	25.50	-
1227	Phosphorylation	SKLHNYSSTVAGQNS HHHCCCCCCCCCCCC	19.28	-
1228	Phosphorylation	KLHNYSSTVAGQNSG HHCCCCCCCCCCCCC	14.40	-
1252	Phosphorylation	CKKAGNLYDISEDNS HHHHCCEECCCCCCC	18.41	22673903
1255	Phosphorylation	AGNLYDISEDNSLQE HCCEECCCCCCCCCC	35.68	22673903
1259	Phosphorylation	YDISEDNSLQELDQP ECCCCCCCCCCCCCC	43.69	22673903
1284	Phosphorylation	SSTKYPQSPTNSKAQ CCCCCCCCCCCCHHH	29.23	28551015
1303	Phosphorylation	NKLRRQHSYDTFVDL HHHHHHHCHHHHHHH	19.16	17156796
1304	Phosphorylation	KLRRQHSYDTFVDLQ HHHHHHCHHHHHHHH	19.51	25403869
1306	Phosphorylation	RRQHSYDTFVDLQKE HHHHCHHHHHHHHHH	19.82	25403869
1323	Phosphorylation	ALAPRSVSLKDKGRF HHCCCCCCCCCCCCC	30.83	22335236
1334	Phosphorylation	KGRFMDGSPYAHMFE CCCCCCCCCCCEEEE	15.52	-
1336	Phosphorylation	RFMDGSPYAHMFEMP CCCCCCCCCEEEECC	15.73	22817900
1367	Phosphorylation	HHHNNPGSGYMLSKS CCCCCCCCCCCCCCC	28.18	-
1369	Phosphorylation	HNNPGSGYMLSKSLY CCCCCCCCCCCCCCC	9.15	-
1400	Ubiquitination	QCLLHGSKSYFFRQP CEEECCCEEEECCCC	54.49	-
1402	Phosphorylation	LLHGSKSYFFRQPTV EECCCEEEECCCCCC	15.52	-
1472	Phosphorylation	GSSNGHVYEKLSSIE CCCCCCHHHHHHCCC	11.15	15748156
1476	Phosphorylation	GHVYEKLSSIESDV- CCHHHHHHCCCCCC-	40.10	25403869
1477	Phosphorylation	HVYEKLSSIESDV-- CHHHHHHCCCCCC--	40.59	25403869
1480	Phosphorylation	EKLSSIESDV----- HHHHCCCCCC-----	41.84	25403869

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
383	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
383	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
1303	S	Phosphorylation	Kinase	DAPK1	F1LNN8	PSP
1303	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
1303	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
1303	S	Phosphorylation	Kinase	PKCD	Q05655	PSP
1303	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
1303	S	Phosphorylation	Kinase	CAM-KII_GROUP	-	PhosphoELM
1336	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
1472	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
1472	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
1480	S	Phosphorylation	Kinase	CK2A1	P68400	PSP
1480	S	Phosphorylation	Kinase	CSNK2A1	P19139	GPS
1480	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1303	S	Phosphorylation		22673903
Phosphorylation at Ser-1303 by DAPK1 enhances synaptic NMDA receptor channel activity (By similarity).

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
DLG4_RAT	Dlg4	physical	8601796
DLG1_RAT	Dlg1	physical	8601796

Drug and Disease Associations

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

Regulatory Network of NMDE2_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structure of the zinc-bound amino-terminal domain of the NMDAreceptor NR2B subunit."; Karakas E., Simorowski N., Furukawa H.; EMBO J. 28:3910-3920(2009). Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 32-394 IN COMPLEX WITH ZINCION, GLYCOSYLATION AT ASN-74; HIS-127; ASP-283; GLU-284 AND ASN-341,MUTAGENESIS OF HIS-60; HIS-311 AND HIS-359, AND DISULFIDE BOND.	19910922 [Abstract]

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