ID  P55245;
PN  Epidermal growth factor receptor;
GN  EGFR;
OS  9544;
SL  Nucleus Position: SL-0178;
SL  Nucleus Position: SL-0182;
SL  Comments: Cell membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P00533}; Single- pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Nucleus membrane {ECO:0000250|UniProtKB:P00533}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P00533}. Endosome {ECO:0000250|UniProtKB:P00533}. Endosome membrane {ECO:0000250|UniProtKB:P00533}. Nucleus {ECO:0000250|UniProtKB:P00533}. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF). {ECO:0000250|UniProtKB:P00533}.
DR  UNIPROT: P55245;
DR  UNIPROT: F6YXS7;
DR  UNIPROT: G7ML99;
DR  UNIPROT: H9FAB2;
DR  Pfam: PF00757;
DR  Pfam: PF14843;
DR  Pfam: PF07714;
DR  Pfam: PF01030;
DR  PROSITE: PS00107;
DR  PROSITE: PS50011;
DR  PROSITE: PS00109;
DE  Function: Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. 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. May also activate the NF-kappa-B signaling cascade. 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. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (By similarity). 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 (By similarity). Plays a role in enhancing learning and memory performance (By similarity). {ECO:0000250|UniProtKB:P00533, ECO:0000250|UniProtKB:Q01279}.
DE  Reference Proteome: Yes;
GO  GO:0009925;
GO  GO:0005737;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0010008;
GO  GO:0000139;
GO  GO:0005887;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0005886;
GO  GO:0043235;
GO  GO:0005524;
GO  GO:0003682;
GO  GO:0048408;
GO  GO:0005006;
GO  GO:0004713;
GO  GO:0004714;
GO  GO:0030154;
GO  GO:0071364;
GO  GO:0071392;
GO  GO:0007173;
GO  GO:0007611;
GO  GO:0043066;
GO  GO:0030307;
GO  GO:0008284;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0033674;
GO  GO:1902966;
GO  GO:0001934;
GO  GO:0045944;
GO  GO:0046777;
GO  GO:0007169;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFLK
SQ  TIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVE
SQ  SIQWRDIVSSEFLSNMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC
SQ  TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEE
SQ  DGVRKCKKCEGPCRKVCNGIGIGEFKDTLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKE
SQ  ITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL
SQ  FGTSSQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCQNVSRGRECVDKCNVLEGEPREFVENSECIQCHP
SQ  ECLPQVMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCARNG
SQ  PKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS
SQ  GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLD
SQ  YVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKW
SQ  MALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK
SQ  FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQGFFSSPSTSRTPLLSSLSA
SQ  TSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTEDSIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPS
SQ  RDPHYQDPHSTAVGNPEYLNTVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV
SQ  APQSSEFIGA
//