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PubMed Id: 1330535

This page summarizes selected information from the article 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.

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

Y751-p - PDGFRb (human)

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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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