EGFR is a receptor for EGF, but also for other members of the EGF family, as TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30 and vaccinia virus growth factor. Phospho-EGFR (Tyr1110) is the phosphorylated, active form of the epidermal growth factor receptor (EGFR) at tyrosine 1110 within the C-terminal tail. This modification is catalyzed by EGFR itself or SRC-family kinases upon ligand (EGF, TGF-α) binding or oxidative stress. Phosphorylation at Tyr1110 creates a docking site for SH2-domain-containing proteins, propagating downstream signals through the RAS-RAF-MEK-ERK and PI3K-AKT pathways. Some scientists call EGFR Tyr1110 as EGFR Tyr1086, the site where the signaling peptide is removed.