{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P00533","secondaryAccessions":["O00688","O00732","P06268","Q14225","Q68GS5","Q92795","Q9BZS2","Q9GZX1","Q9H2C9","Q9H3C9","Q9UMD7","Q9UMD8","Q9UMG5"],"uniProtkbId":"EGFR_HUMAN","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1997-11-01","entryVersion":300,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Epidermal growth factor receptor"},"ecNumbers":[{"value":"2.7.10.1"}]},"alternativeNames":[{"fullName":{"value":"Proto-oncogene c-ErbB-1"}},{"fullName":{"value":"Receptor tyrosine-protein kinase erbB-1"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:3236"}],"value":"EGFR"},"synonyms":[{"value":"ERBB"},{"value":"ERBB1"},{"value":"HER1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q01279"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10805725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11116146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11483589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11602604"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12297049"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12297050"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12620237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12873986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15374980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15590694"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15611079"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17115032"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17909029"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19560417"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20462955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20837704"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21258366"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153536"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2790960"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35538033"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7679104"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8144591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9419975"}],"value":"Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:10805725, PubMed:27153536, PubMed:2790960, PubMed:35538033). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:12297049, PubMed:15611079, PubMed:17909029, PubMed:20837704, PubMed:27153536, PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975). Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Positively regulates cell migration via interaction with CCDC88A/GIV which retains EGFR at the cell membrane following ligand stimulation, promoting EGFR signaling which triggers cell migration (PubMed:20462955). Plays a role in enhancing learning and memory performance (By similarity). Plays a role in mammalian pain signaling (long-lasting hypersensitivity) (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"value":"Isoform 2 may act as an antagonist of EGF action"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21516087"}],"value":"(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10596"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:61978"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.10.1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU10028"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15374980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17349580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18046415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18227510"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19560417"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19563760"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15282549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15590694"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334392"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18046415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19836242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25922362"}],"value":"Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling. Up-regulated by NEU3-mediated desialylation of N-linked glycan at Asn-528"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q01279"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10026169"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10228163"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10805725"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11116146"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11483589"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12297050"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12620237"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12873986"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15282549"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15374980"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15590694"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15837620"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16140940"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16420529"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17115032"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17182860"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17334392"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17909029"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18046415"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18602463"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19172738"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19509291"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19560417"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19563760"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19749156"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19836242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20462955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20471394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20551055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20674546"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20837704"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21258366"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21518868"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22298428"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22888118"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23418353"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23589287"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23774213"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23912460"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25187647"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25311788"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26988023"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28479384"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35538033"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"39073202"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7657591"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8650580"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9852145"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.111"}],"value":"Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2 (PubMed:10805725). Forms a complex with CCDC88A/GIV (via SH2-like regions) and GNAI3 which leads to enhanced EGFR signaling and triggering of cell migration; binding to CCDC88A requires autophosphorylation of the EGFR C-terminal region, and ligand stimulation is required for recruitment of GNAI3 to the complex (PubMed:20462955, PubMed:25187647). Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation (PubMed:18046415). Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B (PubMed:10805725). Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation; interaction with CBL is reduced in the presence of tensin TNS4 (PubMed:23774213). Interacts with SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA (PubMed:17115032). Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2 (PubMed:10026169). Interacts with ATXN2. Interacts with GAREM1. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126 (PubMed:23418353). Interacts with GPRC5A (via its transmembrane domain) (PubMed:25311788). Interacts with FAM83B; positively regulates EGFR inducing its autophosphorylation in absence of stimulation by EGF (PubMed:23912460). Interacts with LAPTM4B; positively correlates with EGFR activation (PubMed:28479384). Interacts with STX19 (PubMed:16420529). Interacts with CD44 (PubMed:23589287). Interacts with PGRMC1; the interaction requires PGRMC1 homodimerization (PubMed:26988023). Interacts with PIKFYVE (PubMed:17909029). Interacts with NEU3. Interacts with TRAF4 (PubMed:30352854). Interacts with the ant venom OMEGA-myrmeciitoxin(02)-Mg1a (By similarity). Interacts with CD82; this interaction facilitates ligand-induced endocytosis of the receptor and its subsequent desensitization (PubMed:35538033). Interacts with SNX32; the interaction is required for endolysosomal EGFR trafficking 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Endocytosed upon activation by ligand (PubMed:17182860, PubMed:17909029, PubMed:27153536, PubMed:2790960). 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Dephosphorylated by PTPN1 and PTPN2"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q01279"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16543144"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22179831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22298428"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153536"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33996800"}],"value":"Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity). Ubiquitinated by ZNRF1 or CBL at different lysines in response to EGF stimulation; leading to recruitment of the ESCRT machinery and subsequent degradation in the lysosomes (PubMed:33996800). Deubiquitinated by UCHL1 leading to the inhibition of its degradation (By similarity)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27153536"}],"value":"Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28891468"}],"value":"Neddylated; by NEDD8 (PubMed:28891468). Neddylation results in localization to the cell membrane when activated by EGF. Neddylation also increases protein stability (PubMed:28891468)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19563760"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19836242"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21258366"}],"value":"Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Lung cancer","diseaseAccession":"DI-02205","acronym":"LNCR","description":"A common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. 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Some patients have chronic diarrhea, and necrotizing enterocolitis.","diseaseCrossReference":{"database":"MIM","id":"616069"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24691054"}]},"note":{"texts":[{"value":"The disease is caused by variants affecting the gene represented in this entry"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00159"}],"value":"Belongs to the protein kinase superfamily. Tyr protein kinase family. 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