Ser890
Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage PhosphoSitePlus® v6.5.9.3
Powered by Cell Signaling Technology
Home > Phosphorylation Site Page: > Ser890  -  NMDAR1 (rat)

Site Information
ITSTLAssFKRRRss   SwissProt Entrez-Gene
Blast this site against: NCBI  SwissProt  PDB 
Site Group ID: 447737

In vivo Characterization
Methods used to characterize site in vivo:
[32P] bio-synthetic labeling ( 11 ) , mutation of modification site ( 1 , 3 , 11 ) , phospho-antibody ( 2 , 4 , 5 , 6 , 7 , 8 , 10 ) , phosphoamino acid analysis ( 11 ) , phosphopeptide mapping ( 2 , 11 ) , western blotting ( 4 , 5 , 8 )
Disease tissue studied:
Parkinson's disease ( 2 )
Relevant cell line - cell type - tissue:
'brain, hippocampus' ( 5 , 6 , 7 , 10 ) , 'brain, striatum' ( 2 ) , 'brain, substantia nigra' ( 8 ) , 'neuron, cortical' ( 11 ) , 293 (epithelial) ( 1 , 3 , 10 , 11 ) , neuron-'brain, cerebral cortex' ( 4 ) , QT-6 (fibroblast) ( 10 )

Upstream Regulation
Putative in vivo kinases:
PKCG (rat) ( 4 )
Kinases, in vitro:
PKCA (human) ( 9 ) , PKCA (rat) ( 10 )
Treatments:
6-OHDA ( 8 ) , colforsin ( 10 ) , DHPG ( 4 ) , dopaminergic_lesion ( 2 ) , Go_6976 ( 4 ) , ischemia/reperfusion ( 6 ) , levodopa ( 2 , 8 ) , okadaic_acid ( 7 ) , phorbol_ester ( 7 , 10 ) , PKC-theta_pseudosubstrate ( 4 ) , PKCalpha_peptide_inhibitor ( 4 ) , PKCbeta1_peptide_inhibitor ( 4 ) , PKCbeta2_peptide_inhibitor ( 4 ) , PKCgamma_peptide_inhibitor ( 4 ) , rottlerin ( 4 ) , status epilepticus ( 5 )

Downstream Regulation
Effects of modification on NMDAR1:
activity, inhibited ( 1 ) , intracellular localization ( 10 ) , molecular association, regulation ( 9 )
Inhibit interaction with:
Calmodulin (rat) ( 9 )

Disease / Diagnostics Relevance
Relevant diseases:
Parkinson's disease ( 2 )

References 

1

Xu M, Smothers CT, Woodward JJ (2011) Effects of ethanol on phosphorylation site mutants of recombinant N-methyl-D-aspartate receptors. Alcohol 45, 373-80
21163614   Curated Info

2

Kong M, Ba M, Song L, Liu Z (2009) Comparative effects of acute or chronic administration of levodopa to 6-OHDA-lesioned rats on the expression and phosphorylation of N-methyl-D-aspartate receptor NR1 subunits in the striatum. Neurochem Res 34, 1513-21
19283475   Curated Info

3

Jackson MF, et al. (2006) Protein kinase C enhances glycine-insensitive desensitization of NMDA receptors independently of previously identified protein kinase C sites. J Neurochem 96, 1509-18
16417568   Curated Info

4

Sánchez-Pérez AM, Felipo V (2005) Serines 890 and 896 of the NMDA receptor subunit NR1 are differentially phosphorylated by protein kinase C isoforms. Neurochem Int 47, 84-91
15936117   Curated Info

5

Niimura M, et al. (2005) Changes in phosphorylation of the NMDA receptor in the rat hippocampus induced by status epilepticus. J Neurochem 92, 1377-85
15748156   Curated Info

6

Cheung HH, Teves L, Wallace MC, Gurd JW (2001) Increased phosphorylation of the NR1 subunit of the NMDA receptor following cerebral ischemia. J Neurochem 78, 1179-82
11553692   Curated Info

7

Grosshans DR, Browning MD (2001) Protein kinase C activation induces tyrosine phosphorylation of the NR2A and NR2B subunits of the NMDA receptor. J Neurochem 76, 737-44
11158244   Curated Info

8

Dunah AW, et al. (2000) Alterations in subunit expression, composition, and phosphorylation of striatal N-methyl-D-aspartate glutamate receptors in a rat 6-hydroxydopamine model of Parkinson's disease. Mol Pharmacol 57, 342-52
10648644   Curated Info

9

Hisatsune C, et al. (1997) Phosphorylation-dependent regulation of N-methyl-D-aspartate receptors by calmodulin. J Biol Chem 272, 20805-10
9252405   Curated Info

10

Tingley WG, et al. (1997) Characterization of protein kinase A and protein kinase C phosphorylation of the N-methyl-D-aspartate receptor NR1 subunit using phosphorylation site-specific antibodies. J Biol Chem 272, 5157-66
9030583   Curated Info

11

Tingley WG, Roche KW, Thompson AK, Huganir RL (1993) Regulation of NMDA receptor phosphorylation by alternative splicing of the C-terminal domain. Nature 364, 70-3
8316301   Curated Info