Epidermal growth factor receptor information

EGFR
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1IVO, 1M14, 1M17, 1MOX, 1NQL, 1XKK, 1YY9, 1Z9I, 2EB2, 2EB3, 2GS2, 2GS6, 2GS7, 2ITN, 2ITO, 2ITP, 2ITQ, 2ITT, 2ITU, 2ITV, 2ITW, 2ITY, 2ITZ, 2J5E, 2J5F, 2J6M, 2JIT, 2JIU, 2JIV, 2KS1, 2M0B, 2M20, 2RF9, 2RFD, 2RFE, 2RGP, 3B2U, 3B2V, 3BEL, 3BUO, 3C09, 3G5V, 3G5Y, 3GOP, 3GT8, 3IKA, 3LZB, 3NJP, 3OB2, 3OP0, 3P0Y, 3PFV, 3POZ, 3QWQ, 3UG1, 3UG2, 3VJN, 3VJO, 3VRP, 3VRR, 3W2O, 3W2P, 3W2Q, 3W2R, 3W2S, 3W32, 3W33, 4G5J, 4G5P, 4HJO, 4I1Z, 4I20, 4I21, 4I22, 4I23, 4I24, 4JQ7, 4JQ8, 4JR3, 4JRV, 4KRL, 4KRM, 4KRO, 4KRP, 4LI5, 4LL0, 4LQM, 4LRM, 4R3P, 4R3R, 4R5S, 4RIW, 4RIX, 4RIY, 4RJ4, 4RJ5, 4RJ6, 4RJ7, 4RJ8, 4TKS, 4WKQ, 4WRG, 4ZJV, 5CNN, 5CNO, 5CAN, 2N5S, 5CAL, 5C8M, 4UV7, 5CAV, 5CZI, 5EDQ, 5CAS, 5CAO, 5CAP, 5EM5, 5HG5, 5EDR, 5EM8, 5EDP, 5HG7, 5CAU, 5C8K, 5C8N, 5CZH, 5CAQ, 5EM6, 4UIP, 5HG9, 5EM7, 5HG8, 4ZSE, 5HIB, 5HIC, 5D41, 4WD5
Identifiers
Aliases	EGFR, ERBB, ERBB1, HER1, NISBD2, PIG61, mENA, epidermal growth factor receptor, Genes, erbB-1, ERRP
External IDs	OMIM: 131550 MGI: 95294 HomoloGene: 74545 GeneCards: EGFR
Gene location (Human)
Chr.	Chromosome 7 (human)
End	55,211,628 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	16,868,158 bp
RNA expression pattern
	Top expressed in
	nipple; ; gums; ; placenta; ; vulva; ; superficial temporal artery; ; human penis; ; urethra; ; saphenous vein; ; lower lobe of lung; ; oral cavity;
	Top expressed in
	left lobe of liver; ; rib; ; external carotid artery; ; skin of abdomen; ; conjunctival fornix; ; hair follicle; ; phalanx of foot; ; calvaria; ; right ventricle; ; skin of back;
	More reference expression data
	https://ncbi.nlm.nih.gov/gene?cmd=retrieve&dopt=default&rn=1&list_uids=1956/ More reference expression data
Gene ontology
Molecular function	kinase activity; nitric-oxide synthase regulator activity; transmembrane receptor protein tyrosine kinase activity; protein phosphatase binding; ATP binding; protein kinase activity; enzyme binding; MAP kinase kinase kinase activity; transferase activity; chromatin binding; actin filament binding; double-stranded DNA binding; transmembrane signaling receptor activity; nucleotide binding; signal transducer activity; identical protein binding; signaling receptor binding; protein tyrosine kinase activity; calmodulin binding; protein kinase binding; phosphatidylinositol-4,5-bisphosphate 3-kinase activity; protein heterodimerization activity; integrin binding; epidermal growth factor binding; epidermal growth factor-activated receptor activity; ubiquitin protein ligase binding; cadherin binding; virus receptor activity; protein binding;
Cellular component	cytoplasm; endosome; multivesicular body, internal vesicle lumen; nuclear membrane; membrane; focal adhesion; extracellular region; perinuclear region of cytoplasm; nucleus; cell surface; endoplasmic reticulum; integral component of membrane; Golgi apparatus; early endosome membrane; receptor complex; plasma membrane; endocytic vesicle; intracellular anatomical structure; AP-2 adaptor complex; endosome membrane; endoplasmic reticulum membrane; Golgi membrane; basolateral plasma membrane; Shc-EGFR complex; membrane raft; apical plasma membrane; synapse; extracellular space; clathrin-coated vesicle membrane; integral component of plasma membrane; basal plasma membrane; protein-containing complex;
Biological process	positive regulation of protein phosphorylation; negative regulation of epidermal growth factor receptor signaling pathway; positive regulation of MAP kinase activity; protein phosphorylation; cell surface receptor signaling pathway; protein insertion into membrane; cell population proliferation; morphogenesis of an epithelial fold; ossification; negative regulation of protein catabolic process; transmembrane receptor protein tyrosine kinase signaling pathway; positive regulation of fibroblast proliferation; activation of phospholipase C activity; epidermis development; learning or memory; protein autophosphorylation; positive regulation of phosphorylation; cerebral cortex cell migration; digestive tract morphogenesis; hair follicle development; phosphorylation; positive regulation of epithelial cell proliferation; embryonic placenta development; eyelid development in camera-type eye; activation of phospholipase A2 activity; positive regulation of DNA replication; response to UV-A; regulation of peptidyl-tyrosine phosphorylation; positive regulation of cell migration; positive regulation of nitric oxide biosynthetic process; cellular response to estradiol stimulus; positive regulation of DNA repair; response to stress; regulation of nitric-oxide synthase activity; salivary gland morphogenesis; MAPK cascade; cellular response to epidermal growth factor stimulus; multicellular organism development; regulation of cell population proliferation; cell morphogenesis; cellular response to amino acid stimulus; signal transduction; positive regulation of transcription by RNA polymerase II; lung development; positive regulation of synaptic transmission, glutamatergic; positive regulation of ERK1 and ERK2 cascade; phosphatidylinositol phosphate biosynthetic process; circadian rhythm; positive regulation of superoxide anion generation; positive regulation of cell population proliferation; positive regulation of vasoconstriction; response to osmotic stress; tongue development; negative regulation of apoptotic process; response to cobalamin; liver regeneration; response to calcium ion; wound healing; cellular response to dexamethasone stimulus; negative regulation of mitotic cell cycle; cellular response to growth factor stimulus; hydrogen peroxide metabolic process; response to oxidative stress; response to lipid; regulation of cell motility; intracellular signal transduction; response to organic cyclic compound; magnesium ion homeostasis; protein biosynthesis; positive regulation of production of miRNAs involved in gene silencing by miRNA; positive regulation of smooth muscle cell proliferation; positive regulation of bone resorption; midgut development; positive regulation of inflammatory response; liver development; diterpenoid metabolic process; ERBB2 signaling pathway; response to estradiol; positive regulation of cell growth; positive regulation of prolactin secretion; astrocyte activation; cellular response to mechanical stimulus; response to hydroxyisoflavone; neuron projection morphogenesis; ovulation cycle; regulation of transcription by RNA polymerase II; peptidyl-tyrosine phosphorylation; membrane organization; positive regulation of protein kinase C activity; negative regulation of ERBB signaling pathway; positive regulation of protein localization to plasma membrane; negative regulation of cardiocyte differentiation; cellular response to reactive oxygen species; positive regulation of transcription, DNA-templated; regulation of JNK cascade; regulation of ERK1 and ERK2 cascade; cellular response to cadmium ion; positive regulation of NIK/NF-kappaB signaling; viral entry into host cell; epidermal growth factor receptor signaling pathway; positive regulation of peptidyl-serine phosphorylation; peptidyl-tyrosine autophosphorylation; cell-cell adhesion; regulation of phosphatidylinositol 3-kinase signaling; positive regulation of protein kinase B signaling; positive regulation of nitric oxide mediated signal transduction; cell differentiation; positive regulation of cyclin-dependent protein serine/threonine kinase activity; negative regulation of Notch signaling pathway; positive regulation of canonical Wnt signaling pathway; positive regulation of G1/S transition of mitotic cell cycle;
	Sources:Amigo / QuickGO
Orthologs
	1956,https://ncbi.nlm.nih.gov/gene?cmd=retrieve&dopt=default&rn=1&list_uids=1956; 1956,https://ncbi.nlm.nih.gov/gene?cmd=retrieve&dopt=default&rn=1&list_uids=1956
	13649
	ENSG00000146648
	ENSMUSG00000020122
	P00533
	Q01279
NM_001346897; NM_001346898; NM_001346899; NM_001346900; NM_001346941;
	NM_005228; NM_201282; NM_201283; NM_201284
	NM_007912; NM_207655
NP_001333826; NP_001333827; NP_001333828; NP_001333829; NP_001333870;
	NP_005219; NP_958439; NP_958440; NP_958441
	NP_031938; NP_997538
	Wikidata
View/Edit Human	View/Edit Mouse

The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is a transmembrane protein that is a receptor for members of the epidermal growth factor family (EGF family) of extracellular protein ligands.^[5]

The epidermal growth factor receptor is a member of the ErbB family of receptors, a subfamily of four closely related receptor tyrosine kinases: EGFR (ErbB-1), HER2/neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4). In many cancer types, mutations affecting EGFR expression or activity could result in cancer.^[6]

Epidermal growth factor and its receptor was discovered by Stanley Cohen of Vanderbilt University. Cohen shared the 1986 Nobel Prize in Medicine with Rita Levi-Montalcini for their discovery of growth factors.

Deficient signaling of the EGFR and other receptor tyrosine kinases in humans is associated with diseases such as Alzheimer's, while over-expression is associated with the development of a wide variety of tumors. Interruption of EGFR signalling, either by blocking EGFR binding sites on the extracellular domain of the receptor or by inhibiting intracellular tyrosine kinase activity, can prevent the growth of EGFR-expressing tumours and improve the patient's condition^{[citation needed]}.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000146648 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000020122 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Herbst RS (2004). "Review of epidermal growth factor receptor biology". International Journal of Radiation Oncology, Biology, Physics. 59 (2 Suppl): 21–6. doi:10.1016/j.ijrobp.2003.11.041. PMID 15142631.
^ Zhang H, Berezov A, Wang Q, Zhang G, Drebin J, Murali R, Greene MI (August 2007). "ErbB receptors: from oncogenes to targeted cancer treatment". The Journal of Clinical Investigation. 117 (8): 2051–8. doi:10.1172/JCI32278. PMC 1934579. PMID 17671639.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000146648 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000020122 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid15142631-5] Herbst RS (2004). "Review of epidermal growth factor receptor biology". International Journal of Radiation Oncology, Biology, Physics. 59 (2 Suppl): 21–6. doi:10.1016/j.ijrobp.2003.11.041. PMID 15142631.

[pmid17671639-6] Zhang H, Berezov A, Wang Q, Zhang G, Drebin J, Murali R, Greene MI (August 2007). "ErbB receptors: from oncogenes to targeted cancer treatment". The Journal of Clinical Investigation. 117 (8): 2051–8. doi:10.1172/JCI32278. PMC 1934579. PMID 17671639.

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