Phosphorylation of SHC by SYK kinase

Stable Identifier
Reaction [transition]
Homo sapiens
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SHC is an adapter protein that has been implicated in Ras activation. Mast cells express two isoforms of 46 and 52 kDa. Both isoforms of SHC have two domains, an N-terminal phosphotyrosine-binding (PTB) domain and a C-terminal SH2 domain that allows Shc to bind to proteins containing phosphorylated tyrosine residues. Following receptor stimulation, SHC is phosphorylated by Src kinases Syk on Y239, Y240 and Y317 (p56 isoform). Both phosphotyrosines Y239 and Y317 creates the binding site for the SH2 domain of GRB2.
Literature References
PubMed ID Title Journal Year
9199344 Shc contains two Grb2 binding sites needed for efficient formation of complexes with SOS in B lymphocytes

Harmer, SL, DeFranco, AL

Mol Cell Biol 1997
10523831 Phosphorylation of Shc by Src family kinases is necessary for stem cell factor receptor/c-kit mediated activation of the Ras/MAP kinase pathway and c-fos induction

Pontén, E, Carlberg, M, Hermanson, M, Blume-Jensen, P, Lennartsson, J, Rönnstrand, L

Oncogene 1999
8663278 Syk-dependent phosphorylation of Shc. A potential link between FcepsilonRI and the Ras/mitogen-activated protein kinase signaling pathway through SOS and Grb2

Zhang, C, Kinet, JP, Numerof, R, Scharenberg, AM, Paolini, R, Jabril-Cuenod, B, Beaven, MA

J. Biol. Chem. 1996
Catalyst Activity

protein tyrosine kinase activity of Clustered p:LYN:p-FCERI:IgE:allergen:p-6Y-SYK [plasma membrane]

Orthologous Events
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