SYK autophosphorylates

Stable Identifier
Homo sapiens
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SYK can autophosphorylate and autophosphorylation increases its activity. It is more readily activated by autophosphorylation although it is rapidly activated by Src family kinases. SYK has multiple sites of phosphorylation which both regulate its activity and serve as docking sites for other proteins (Sada et al. 2001). Some of these sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, and Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997).

Literature References
PubMed ID Title Journal Year
9042338 Identification of the major sites of autophosphorylation of the murine protein-tyrosine kinase Syk

Ashendel, CL, Furlong, MT, Geahlen, RL, Harrison, ML, Kim, KH, Mahrenholz, AM

Biochim Biophys Acta 1997
18818202 Molecular mechanism of the Syk activation switch

Shaw, D, Papp, E, Gandhi, S, Tsang, E, Giannetti, AM, Tse, JK, Dinh, M, Wang, S, Ho, H, Bradshaw, JM

J Biol Chem 2008
Catalyst Activity

protein tyrosine kinase activity of pathogens:CLEC6A,CLEC4E:p-Y65,Y76-FCER1G dimer:SYK [plasma membrane]

Orthologous Events
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