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EGFR — PTK6

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: PTK6 — EGFR (direct interaction, unspecified method) Jones et al., Nature 2006
• IRef Biogrid Interaction: PTK6 — EGFR (physical association, affinity chromatography technology) Kamalati et al., J Biol Chem 1996*
• IRef Hprd Interaction: PTK6 — EGFR (in vivo) Kamalati et al., J Biol Chem 1996*
• IRef Intact Interaction: PTK6 — EGFR (direct interaction, protein array) Jones et al., Nature 2006
• IRef Ophid Interaction: PTK6 — EGFR (aggregation, confirmational text mining) Jones et al., Nature 2006
• IRef Ophid Interaction: PTK6 — EGFR (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Poppleton et al., Arch Biochem Biophys 2000 : A peptide betaIII-2 corresponding to amino acids Arg259-Lys273 in the beta2-adrenergic receptor which competes for association of Galpha ( s ) with the EGFR and increases protein tyrosine kinase activity of the EGFR could mimic the effects of EGFR-13
Kawanabe et al., Am J Physiol Heart Circ Physiol 2002 : ET-1 induced EGFR PTK transactivation was completely inhibited by AG-1478, which is a specific inhibitor of EGFR PTK ... In the absence of extracellular Ca ( 2+ ), the magnitude of EGFR PTK transactivation was near the basal level ... Based on sensitivity to nifedipine, which is a specific blocker of voltage operated Ca ( 2+ ) channels ( VOCCs ), VOCCs have minor roles in EGFR PTK transactivation ... In contrast, Ca ( 2+ ) influx through VICCs plays an important role in EGFR PTK transactivation ... In summary, Ca ( 2+ ) influx through VICCs plays an essential role in ET-1 induced EGFR PTK transactivation in rabbit internal carotid artery vascular smooth muscle cells
Sini et al., Clin Cancer Res 2005 (Neoplasms, Experimental) : Both ErbB inhibitors significantly enhanced the antitumor activity of PTK787/ZK222584
Kang et al., J Biol Chem 2010 (Breast Neoplasms) : These results demonstrate that PTK6 enhances EGFR signaling by inhibition of EGFR down-regulation through phosphorylation of ARAP1 in breast cancer cells
King et al., J Biol Chem 1986 : The possible role of epidermal growth factor (EGF) receptor phosphorylation at threonine 654 in modulating the protein-tyrosine kinase activity of EGF treated A431 cells has been studied
Sherrill et al., Biochemistry 1996 : The binding of epidermal growth factor (EGF) to epidermal growth factor receptor ( EGF receptor ) induces dimerization of the receptor and activation of its protein tyrosine kinase