Curated Information
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PubMed Id: 14551197 
Shivakrupa R, Radha V, Sudhakar Ch, Swarup G (2003) Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain. J Biol Chem 278, 52188-94 14551197
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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Y504-p - RAPGEF1 (human)
Orthologous residues
RAPGEF1 (human): Y504‑p, RAPGEF1 iso2 (human): Y465‑p, RAPGEF1 (mouse): Y514‑p, RAPGEF1 iso2 (mouse): Y476‑p, RAPGEF1 (rat): Y389‑p
 Methods used to characterize site in vivo [32P] bio-synthetic labeling, mutation of modification site, phospho-antibody
 Relevant cell lines - cell types - tissues:  COS (fibroblast), HeLa (cervical), J774 (macrophage), MCF-7 (breast cell)
 Cellular systems studied:  cell lines
 Species studied:  human, monkey, mouse
 Enzymes shown to modify site in vitro
Type Enzyme
KINASE Hck (human)
Upstream Regulation
 Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
mercuric chloride increase

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