PTPN12 dephosphorylates EGFR at Y1148 (Y1172)

Stable Identifier
R-HSA-8864029
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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PTPN12 protein tyrosine phosphatase dephosphorylates activated EGFR at tyrosine residue Y1148 (Y1148 corresponds to Y1172 in the nascent EGFR sequence which includes the 24 amino acid long signal peptide at the N-terminus). PTPN12-mediated dephosphorylation of activated EGFR inhibits SHC1 recruitment to the p-Y1148 docking site, thus attenuating downstream RAS activation (Sun et al. 2011). The recruitment of SHC1 to p-Y1148 of EGFR is mediated by the N-terminal phosphotyrosine interaction domain (PID) of SHC1 (Batzer et al. 1995, Songyang et al. 1995).

Literature References
PubMed ID Title Journal Year
21376233 Activation of multiple proto-oncogenic tyrosine kinases in breast cancer via loss of the PTPN12 phosphatase

Sun, T, Aceto, N, Meerbrey, KL, Kessler, JD, Zhou, C, Migliaccio, I, Nguyen, DX, Pavlova, NN, Botero, M, Huang, J, Bernardi, RJ, Schmitt, E, Hu, G, Li, MZ, Dephoure, N, Gygi, SP, Rao, M, Creighton, CJ, Hilsenbeck, SG, Shaw, CA, Muzny, D, Gibbs, RA, Wheeler, DA, Osborne, CK, Schiff, R, Bentires-Alj, M, Elledge, SJ, Westbrook, TF

Cell 2011
7542744 The phosphotyrosine interaction domain of Shc binds an LXNPXY motif on the epidermal growth factor receptor

Batzer, AG, Blaikie, P, Nelson, K, Schlessinger, J, Margolis, B

Mol. Cell. Biol. 1995
7541030 The phosphotyrosine interaction domain of SHC recognizes tyrosine-phosphorylated NPXY motif

Songyang, Z, Margolis, B, Chaudhuri, M, Shoelson, SE, Cantley, LC

J. Biol. Chem. 1995
Participants
Participant Of
Event Information
Catalyst Activity
Catalyst Activity
Title
protein tyrosine phosphatase activity of PTPN12 [cytosol]
Physical Entity
Activity
Orthologous Events
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Reviewed
Created