epidermal growth factor receptor; receptor tyrosine-protein kinase ErbB-1 (EGFR, ERBB1, HER1)
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Function
- tyrosine kinase receptor
- receptor for EGF, & other members of the EGF family including:
- role in RAS signal transduction & MAP kinase pathways
- role in control of cell growth & differentiation
- phosphorylates MUC1 in breast cancer cells & increases the interaction of MUC1 with C-SRC & CTNNB1/beta-catenin
- isoform 2/truncated isoform may act as an antagonist
- binds RIPK1
- CBL interacts with the autophosphorylated C-terminal tail of the EGF receptor
- part of a complex with ERBB2 & either PIK3C2A or PIK3C2B
- autophosphorylated form interacts with PIK3C2B, maybe indirectly
- interacts with PELP1
- binds MUC1
- phosphorylation of Ser-695 is partial & occurs only if Thr-693 is phosphorylated
- monoubiquitinated & polyubiquitinated upon EGF stimulation which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting
- polyubiquitin linkage is mainly through Lys-63, but linkage through Lys-48, Lys-11 & Lys-29 also occur
- binding of EGF to the receptor leads to dimerization, internalization, induction of tyrosine kinase activity, stimulation of cell DNA synthesis, & cell proliferation
Structure
- belongs to the protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily
- contains 1 protein kinase domain
Compartment
Alternative splicing
named isoforms=4
Expression
- ubiquitously expressed
Pathology
- defects in EGFR are associated with NSCLC (non-small cell lung carcinoma)
- isoform 2 is also expressed in ovarian cancers
More general terms
Additional terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P00533.html
- ↑ GeneReviews https://www.genecards.org/cgi-bin/carddisp.pl?gene=EGFR
- ↑ Wikipedia; Note: EGFR entry http://en.wikipedia.org/wiki/epidermal_growth_factor_receptor
- ↑ Nishibe S et al Selectivity of phospholipase C phosphorylation by the epidermal growth factor receptor, the insulin receptor, and their cytoplasmic domains. Proc Natl Acad Sci U S A. 1990 Jan;87(1):424-8. Erratum in: Proc Natl Acad Sci U S A 1990 Apr;87(8):3253. Kim JJ [corrected to Kim JW]. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2153302
- ↑ Wang KK et al Calmodulin-binding proteins as calpain substrates. Biochem J 262:693 1989 PMID: https://www.ncbi.nlm.nih.gov/pubmed/2556106
- ↑ Hollenberg MD. Structure-activity relationships for transmembrane signaling: the receptor's turn. FASEB J. 1991 Feb;5(2):178-86. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/1848518
- ↑ Harrison's Principles of Internal Medicine, 13th ed. Isselbacher et al (eds), McGraw-Hill Inc. NY, 1994, pg 769
- ↑ Pawson T Protein modules and signalling networks Nature 373:573 1995 PMID: https://www.ncbi.nlm.nih.gov/pubmed/7531822
- ↑ Kemp BE, Pearson RB. Protein kinase recognition sequence motifs. Trends Biochem Sci. 1990 Sep;15(9):342-6. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/2238044
Patient information
epidermal growth factor [EGF] receptor patient information