ID  Q01279;
PN  Epidermal growth factor receptor;
GN  Egfr;
OS  10090;
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: Q01279;
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 (PubMed:8404850). 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 (PubMed:20639532). {ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:10953014, ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:8404850}.
DE  Reference Proteome: Yes;
DE  Interaction: P42567; IntAct: EBI-7373206; Score: 0.44
DE  Interaction: O70469; IntAct: EBI-7588761; Score: 0.40
DE  Interaction: O54928; IntAct: EBI-7477248; Score: 0.40
DE  Interaction: P01132; IntAct: EBI-7853849; Score: 0.40
DE  Interaction: P18031; IntAct: EBI-7945363; Score: 0.40
DE  Interaction: P01133; IntAct: EBI-8618729; Score: 0.44
DE  Interaction: P35831; IntAct: EBI-8614373; Score: 0.40
DE  Interaction: P32883; IntAct: EBI-6296299; Score: 0.46
DE  Interaction: P22682; IntAct: EBI-8846800; Score: 0.50
DE  Interaction: Q60631; IntAct: EBI-8846800; Score: 0.35
DE  Interaction: Q15109; IntAct: EBI-15599433; Score: 0.52
DE  Interaction: O54890; IntAct: EBI-15645972; Score: 0.40
DE  Interaction: Q9D1T0; IntAct: EBI-15654918; Score: 0.40
DE  Interaction: P62991; IntAct: EBI-15844305; Score: 0.40
DE  Interaction: Q91XA9; IntAct: EBI-16880617; Score: 0.27
DE  Interaction: P70193; IntAct: EBI-25424163; Score: 0.40
DE  Interaction: Q9JKY5; IntAct: EBI-27088765; Score: 0.40
GO  GO:0016324;
GO  GO:0009925;
GO  GO:0016323;
GO  GO:0030054;
GO  GO:0009986;
GO  GO:0005737;
GO  GO:0031901;
GO  GO:0030139;
GO  GO:0005789;
GO  GO:0005768;
GO  GO:0010008;
GO  GO:0000139;
GO  GO:0005887;
GO  GO:0097708;
GO  GO:0016020;
GO  GO:0045121;
GO  GO:0097489;
GO  GO:0031965;
GO  GO:0005634;
GO  GO:0048471;
GO  GO:0005886;
GO  GO:0032991;
GO  GO:0043235;
GO  GO:0032587;
GO  GO:0044214;
GO  GO:0045202;
GO  GO:0051015;
GO  GO:0005524;
GO  GO:0005516;
GO  GO:0003682;
GO  GO:0019899;
GO  GO:0048408;
GO  GO:0005006;
GO  GO:0042802;
GO  GO:0005178;
GO  GO:0016301;
GO  GO:0019900;
GO  GO:0030235;
GO  GO:0019901;
GO  GO:0019903;
GO  GO:0030296;
GO  GO:0004713;
GO  GO:0044877;
GO  GO:0005102;
GO  GO:0030297;
GO  GO:0004714;
GO  GO:0004888;
GO  GO:0031625;
GO  GO:0048143;
GO  GO:0030154;
GO  GO:0000902;
GO  GO:0008283;
GO  GO:0007166;
GO  GO:0098609;
GO  GO:0071230;
GO  GO:0071276;
GO  GO:0071549;
GO  GO:0071364;
GO  GO:0071392;
GO  GO:0071363;
GO  GO:0071260;
GO  GO:0034614;
GO  GO:0071466;
GO  GO:0021795;
GO  GO:0007623;
GO  GO:0048546;
GO  GO:0016101;
GO  GO:0001892;
GO  GO:0007173;
GO  GO:0008544;
GO  GO:0050673;
GO  GO:0038134;
GO  GO:0061029;
GO  GO:0001942;
GO  GO:0042743;
GO  GO:0035556;
GO  GO:0007611;
GO  GO:0097421;
GO  GO:0030324;
GO  GO:0010960;
GO  GO:0007494;
GO  GO:0060571;
GO  GO:0043066;
GO  GO:1905208;
GO  GO:0045930;
GO  GO:0042177;
GO  GO:0048812;
GO  GO:0042698;
GO  GO:0038083;
GO  GO:0018108;
GO  GO:0045780;
GO  GO:0090263;
GO  GO:0030307;
GO  GO:0030335;
GO  GO:0008284;
GO  GO:0045737;
GO  GO:0045739;
GO  GO:0045740;
GO  GO:0045893;
GO  GO:0050679;
GO  GO:0070374;
GO  GO:0048146;
GO  GO:1900087;
GO  GO:0060252;
GO  GO:0050729;
GO  GO:0033674;
GO  GO:0043406;
GO  GO:0043410;
GO  GO:1903800;
GO  GO:0070257;
GO  GO:1901224;
GO  GO:0010750;
GO  GO:0033138;
GO  GO:0042327;
GO  GO:1902722;
GO  GO:0051897;
GO  GO:1900020;
GO  GO:1902966;
GO  GO:1903078;
GO  GO:0001934;
GO  GO:0048661;
GO  GO:0032930;
GO  GO:0051968;
GO  GO:0045944;
GO  GO:0045907;
GO  GO:0046777;
GO  GO:0042127;
GO  GO:0070372;
GO  GO:0046328;
GO  GO:0050999;
GO  GO:0050730;
GO  GO:0014066;
GO  GO:0051592;
GO  GO:0033590;
GO  GO:0033594;
GO  GO:0006970;
GO  GO:0070141;
GO  GO:0007435;
GO  GO:0007165;
GO  GO:0043586;
GO  GO:0006412;
GO  GO:0007169;
GO  GO:0042311;
GO  GO:0042060;
TP  Membrane Topology: Transmembrane; Source: UniProt - Sequence Analysis {ECO:0000255};
SQ  MRPSGTARTTLLVLLTALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMYNNCEVVLGNLEITYVQRNYDLSFLK
SQ  TIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAILSNYGTNRTGLRELPMRNLQEILIGAVRFSNNPILCNMD
SQ  TIQWRDIVQNVFMSNMSMDLQSHPSSCPKCDPSCPNGSCWGGGEENCQKLTKIICAQQCSHRCRGRSPSDCCHNQCAAGC
SQ  TGPRESDCLVCQKFQDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEE
SQ  DGIRKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKE
SQ  ITGFLLIQAWPDNWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKL
SQ  FGTPNQKTKIMNNRAEKDCKAVNHVCNPLCSSEGCWGPEPRDCVSCQNVSRGRECVEKCNILEGEPREFVENSECIQCHP
SQ  ECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGIMGENNTLVWKYADANNVCHLCHANCTYGCAGPGLQGCEVWP
SQ  SGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVL
SQ  GSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCL
SQ  LDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPI
SQ  KWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASDISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSR
SQ  PKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSL
SQ  SATSNNSTVACINRNGSCRVKEDAFLQRYSSDPTGAVTEDNIDDAFLPVPEYVNQSVPKRPAGSVQNPVYHNQPLHPAPG
SQ  RDLHYQNPHSNAVGNPEYLNTAQPTCLSSGFNSPALWIQKGSHQMSLDNPDYQQDFFPKETKPNGIFKGPTAENAEYLRV
SQ  APPSSEFIGA
//