Curated Information
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Home > Curated Information Page > PubMed Id: 10764765
Strack S, McNeill RB, Colbran RJ (2000) Mechanism and regulation of calcium/calmodulin-dependent protein kinase II targeting to the NR2B subunit of the N-methyl-D-aspartate receptor. J Biol Chem 275, 23798-806 10764765
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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S1303-p - NMDAR2B (rat)
Modsite: NKLRRQHsyDtFVDL SwissProt Entrez-Gene
Orthologous residues
NMDAR2B (human): S1303‑p, NMDAR2B (mouse): S1303‑p, NMDAR2B (rat): S1303‑p
Characterization
Methods used to characterize site in vivo microscopy-colocalization with upstream kinase, mutation of modification site
Relevant cell lines - cell types - tissues:  293 (epithelial)
Cellular systems studied:  cell lines
Species studied:  human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CAMK2A (rat)
Upstream Regulation
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
A23187 increase Low increase in colocalization between NMDAR2B and CaMK2
Downstream Regulation
Effect of modification (function):  intracellular localization, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CAMK2A (human) Disrupts molecular association, regulation in vitro