Curated Information
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Curated Information Page
PubMed Id: 11741929 
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.
Poghosyan Z, et al. (2002) Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and Src family protein-tyrosine kinases. J Biol Chem 277, 4999-5007 11741929
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Y715-p - ADAM15 (human)
Orthologous residues
ADAM15 (human): Y715‑p, ADAM15 (mouse): Y716‑p
Characterization
 Methods used to characterize site in vivo phospho-antibody
 Relevant cell lines - cell types - tissues:  293T (epithelial), Jurkat (T lymphocyte), K562 (erythroid), THP1 (myeloid), U-937 (myeloid)
 Cellular systems studied:  cell lines
 Species studied:  human
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Lck (human)
KINASE Hck (human)
Upstream Regulation
 Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE Hck (human) genetic transfer of dominant-negative enzyme, genetic transfer of wild-type enzyme, genetic transfer of constitutively active upstream enzyme
KINASE Hck (human) genetic transfer of dominant-negative enzyme, genetic transfer of wild-type enzyme, genetic transfer of constitutively active upstream enzyme
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
phorbol ester increase
phorbol ester increase


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