Curated Information
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Home > Curated Information Page > PubMed Id: 10506185
Bardelli A, et al. (1999) A peptide representing the carboxyl-terminal tail of the met receptor inhibits kinase activity and invasive growth. J Biol Chem 274, 29274-81 10506185
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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Y1349-p - Met (human)
Modsite: stFIGEHyVHVNAty SwissProt Entrez-Gene
Orthologous residues
Met (human): Y1349‑p, Met iso2 (human): Y1367‑p, Met (mouse): Y1347‑p, Met (rat): Y1350‑p
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Met (human) Induces sequence-specific competitor, functional assay, in vitro
Comments:  peptide Y1349-Y1356 inhibited Met autophosphorylation

Y1356-p - Met (human)
Modsite: yVHVNAtyVNVKCVA SwissProt Entrez-Gene
Orthologous residues
Met (human): Y1356‑p, Met iso2 (human): Y1374‑p, Met (mouse): Y1354‑p, Met (rat): Y1357‑p
Downstream Regulation
Effect of modification (function):  enzymatic activity, induced, molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
Met (human) Induces sequence-specific competitor, functional assay, in vitro
Comments:  peptide Y1349-Y1356 inhibited Met autophosphorylation