dbPTM

NMDZ1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NMDZ1_RAT
UniProt AC	P35439
Protein Name	Glutamate receptor ionotropic, NMDA 1
Gene Name	Grin1
Organism	Rattus norvegicus (Rat).
Sequence Length	938
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cell junction, synapse, postsynaptic cell membrane. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Enriched in postsynaptic plasma membrane and postsynaptic densities..
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	MSTMHLLTFALLFSCSFARAACDPKIVNIGAVLSTRKHEQMFREAVNQANKRHGSWKIQLNATSVTHKPNAIQMALSVCEDLISSQVYAILVSHPPTPNDHFTPTPVSYTAGFYRIPVLGLTTRMSIYSDKSIHLSFLRTVPPYSHQSSVWFEMMRVYNWNHIILLVSDDHEGRAAQKRLETLLEERESKAEKVLQFDPGTKNVTALLMEARELEARVIILSASEDDAATVYRAAAMLNMTGSGYVWLVGEREISGNALRYAPDGIIGLQLINGKNESAHISDAVGVVAQAVHELLEKENITDPPRGCVGNTNIWKTGPLFKRVLMSSKYADGVTGRVEFNEDGDRKFANYSIMNLQNRKLVQVGIYNGTHVIPNDRKIIWPGGETEKPRGYQMSTRLKIVTIHQEPFVYVKPTMSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTVPQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQADMIVAPLTINNERAQYIEFSKPFKYQGLTILVKKEIPRSTLDSFMQPFQSTLWLLVGLSVHVVAVMLYLLDRFSPFGRFKVNSEEEEEDALTLSSAMWFSWGVLLNSGIGEGAPRSFSARILGMVWAGFAMIIVASYTANLAAFLVLDRPEERITGINDPRLRNPSDKFIYATVKQSSVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLVTTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDSRSNAPATLTFENMAGVFMLVAGGIVAGIFLIFIEIAYKRHKDARRKQMQLAFAAVNVWRKNLQDRKSGRAEPDPKKKATFRAITSTLASSFKRRRSSKDTSTGGGRGALQNQKDTVLPRRAIEREEGQLQLCSRHRES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
61	N-linked_Glycosylation	GSWKIQLNATSVTHK CCEEEEEECEECCCC	25.46	-
203	N-linked_Glycosylation	QFDPGTKNVTALLME CCCCCCCCHHHHHHH	35.89	24876489
239	N-linked_Glycosylation	YRAAAMLNMTGSGYV HHHHHHHHCCCCCEE	16.94	-
276	N-linked_Glycosylation	LQLINGKNESAHISD EEEECCCCCCCCHHH	50.26	24876489
300	N-linked_Glycosylation	HELLEKENITDPPRG HHHHHHCCCCCCCCC	54.23	24876489
330	Phosphorylation	RVLMSSKYADGVTGR HHHHCCCCCCCCCEE	16.33	23800682
350	N-linked_Glycosylation	DGDRKFANYSIMNLQ CCCCCEEEEEEEECC	33.93	24090084
368	N-linked_Glycosylation	LVQVGIYNGTHVIPN EEEEEEECCCEECCC	47.14	24876489
440	N-linked_Glycosylation	KVICTGPNDTSPGSP EEEECCCCCCCCCCC	67.54	24876489
471	N-linked_Glycosylation	IKLARTMNFTYEVHL HHHHHHCCCEEEEEE	26.04	-
491	N-linked_Glycosylation	FGTQERVNNSNKKEW CCCHHCCCCCCHHHH	53.05	-
674	N-linked_Glycosylation	INDPRLRNPSDKFIY CCCHHHCCCCCCEEE	45.05	-
771	N-linked_Glycosylation	KDSPWKQNVSLSILK CCCCCCCCEEEEHHH	22.94	24090084
877 (in isoform 5)	Phosphorylation	-	59.80	22673903
879	Phosphorylation	PDPKKKATFRAITST CCHHHHHHHHHHHHH	23.64	21163614
880 (in isoform 5)	Phosphorylation	-	6.24	22673903
882 (in isoform 5)	Phosphorylation	-	12.76	22673903
883 (in isoform 5)	Phosphorylation	-	2.45	22673903
889	Phosphorylation	AITSTLASSFKRRRS HHHHHHHHHHCHHHC	39.15	9252405
890	Phosphorylation	ITSTLASSFKRRRSS HHHHHHHHHCHHHCC	29.22	15748156
896	Phosphorylation	SSFKRRRSSKDTSTG HHHCHHHCCCCCCCC	39.67	9252405
897	Phosphorylation	SFKRRRSSKDTSTGG HHCHHHCCCCCCCCC	32.51	9252405
898 (in isoform 7)	Phosphorylation	-	67.29	22673903
900	Phosphorylation	RRRSSKDTSTGGGRG HHHCCCCCCCCCCCH	31.74	21163614
901 (in isoform 7)	Phosphorylation	-	34.88	22673903
903 (in isoform 7)	Phosphorylation	-	36.00	22673903
904 (in isoform 7)	Phosphorylation	-	23.78	22673903
913	Ubiquitination	RGALQNQKDTVLPRR CHHHHCCCCCCCCHH	64.02	-
914 (in isoform 4)	Phosphorylation	-	32.08	22673903
917 (in isoform 4)	Phosphorylation	-	2.72	22673903
919 (in isoform 4)	Phosphorylation	-	36.18	22673903
920 (in isoform 4)	Phosphorylation	-	37.67	22673903

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
889	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
889	S	Phosphorylation	Kinase	PKC	-	Uniprot
890	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
890	S	Phosphorylation	Kinase	PKC	-	Uniprot
890	S	Phosphorylation	Kinase	PKCA	P05696	PSP
890	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
890	S	Phosphorylation	Kinase	PRKCG	P63319	GPS
896	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
896	S	Phosphorylation	Kinase	PKC	-	Uniprot
896	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
896	S	Phosphorylation	Kinase	PKCA	P05696	PSP
897	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
897	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
897	S	Phosphorylation	Kinase	PKCA	P05696	PSP
897	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
897	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
897	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
897	S	Phosphorylation		11588171
Dephosphorylated on Ser-897 probably by protein phosphatase 2A (PPP2CB).

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 NMDZ1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DRD1_RAT	Drd1	physical	12408866
NMDE1_RAT	Grin2a	physical	12408866
UBC_RAT	Ubc	physical	22405206
NMDE1_MOUSE	Grin2a	physical	7929101
NMDE3_MOUSE	Grin2c	physical	7929101
NMDE2_RAT	Grin2b	physical	20427654

Drug and Disease Associations

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

Regulatory Network of NMDZ1_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Serines 890 and 896 of the NMDA receptor subunit NR1 aredifferentially phosphorylated by protein kinase C isoforms."; Sanchez-Perez A.M., Felipo V.; Neurochem. Int. 47:84-91(2005). Cited for: PHOSPHORYLATION AT SER-890.	15936117 [Abstract]

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