Curated Information
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 > Curated Information Page > PubMed Id: 21965656
Zhang J, Petit CM, King DS, Lee AL (2011) Phosphorylation of a PDZ domain extension modulates binding affinity and interdomain interactions in postsynaptic density-95 (PSD-95) protein, a membrane-associated guanylate kinase (MAGUK). J Biol Chem 286, 41776-85 21965656
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.
Click on the protein name to open the protein page, and on the RSD number to open the site page.
Download

Y397-p - PSD-95 (rat)
Modsite: AQYKPEEysRFEAKI SwissProt Entrez-Gene
Orthologous residues
PSD‑95 (human): Y397‑p, PSD‑95 iso2 (human): Y440‑p, PSD‑95 (mouse): Y397‑p, PSD‑95 (rat): Y397‑p
Characterization
Methods used to characterize site in vivo mass spectrometry, mutation of modification site
Relevant cell lines - cell types - tissues:  E.coli (bacterial)
Cellular systems studied:  cell lines
Species studied:  bacteria
Downstream Regulation
Effect of modification (function):  protein conformation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CRIPT (human) SH3 Disrupts in vitro, affinity chromatography
Comments:  Y397E mutant showed dissociation, triple mutant Y397E/S415E/S418E showed stronger dissociation

S415-p - PSD-95 (rat)
Modsite: REQLMNSsLGsGtAs SwissProt Entrez-Gene
Orthologous residues
PSD‑95 (human): S415‑p, PSD‑95 iso2 (human): S458‑p, PSD‑95 (mouse): S415‑p, PSD‑95 (rat): S415‑p
Characterization
Methods used to characterize site in vivo mass spectrometry, mutation of modification site
Relevant cell lines - cell types - tissues:  E.coli (bacterial)
Cellular systems studied:  cell lines
Species studied:  bacteria
Downstream Regulation
Effect of modification (function):  protein conformation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CRIPT (human) SH3 Disrupts in vitro, affinity chromatography
Comments:  Y397E mutant showed dissociation, triple mutant Y397E/S415E/S418E showed stronger dissociation

S418-p - PSD-95 (rat)
Modsite: LMNSsLGsGtAsLRs SwissProt Entrez-Gene
Orthologous residues
PSD‑95 (human): S418‑p, PSD‑95 iso2 (human): S461‑p, PSD‑95 (mouse): S418‑p, PSD‑95 (rat): S418‑p
Characterization
Methods used to characterize site in vivo mass spectrometry, mutation of modification site
Relevant cell lines - cell types - tissues:  E.coli (bacterial)
Cellular systems studied:  cell lines
Species studied:  bacteria
Downstream Regulation
Effect of modification (function):  protein conformation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
CRIPT (human) SH3 Disrupts in vitro, affinity chromatography
Comments:  Y397E mutant showed dissociation, triple mutant Y397E/S415E/S418E showed stronger dissociation