Curated Information
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Curated Information Page
PubMed Id: 1330535 
Panayotou G, et al. (1992) Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J 11, 4261-72 1330535
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, 2012,40:D261-70). To learn more about the scope of PhosphoSitePlus®, click here.
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Y751-p - PDGFRB (human)
Orthologous residues
PDGFRB (human): Y751‑p, PDGFRB (mouse): Y750‑p, PDGFRB (rat): Y750‑p
Downstream Regulation
 Effect of modification (function):  molecular association, regulation, protein conformation
 Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
PIK3R1 (human) SH2 Induces protein conformation in vitro
 Comments:  recombinant SH2 domain-containing peptide of P85-alpha interaction with a 17 residue PDGFRb peptide containg Y751

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