EGFR_HUMAN
ID EGFR_HUMAN Reviewed; 1210 AA.
AC P00533; O00688; O00732; P06268; Q14225; Q68GS5; Q92795; Q9BZS2; Q9GZX1;
AC Q9H2C9; Q9H3C9; Q9UMD7; Q9UMD8; Q9UMG5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 282.
DE RecName: Full=Epidermal growth factor receptor {ECO:0000305};
DE EC=2.7.10.1;
DE AltName: Full=Proto-oncogene c-ErbB-1;
DE AltName: Full=Receptor tyrosine-protein kinase erbB-1;
DE Flags: Precursor;
GN Name=EGFR {ECO:0000312|HGNC:HGNC:3236}; Synonyms=ERBB, ERBB1, HER1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 25-32.
RX PubMed=6328312; DOI=10.1038/309418a0;
RA Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W.,
RA Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J.,
RA Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.;
RT "Human epidermal growth factor receptor cDNA sequence and aberrant
RT expression of the amplified gene in A431 epidermoid carcinoma cells.";
RL Nature 309:418-425(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=7654368; DOI=10.1002/mrd.1080410205;
RA Ilekis J.V., Stark B.C., Scoccia B.;
RT "Possible role of variant RNA transcripts in the regulation of epidermal
RT growth factor receptor expression in human placenta.";
RL Mol. Reprod. Dev. 41:149-156(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=8918811; DOI=10.1093/nar/24.20.4050;
RA Reiter J.L., Maihle N.J.;
RT "A 1.8 kb alternative transcript from the human epidermal growth factor
RT receptor gene encodes a truncated form of the receptor.";
RL Nucleic Acids Res. 24:4050-4056(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=9103388; DOI=10.1006/gyno.1996.4526;
RA Ilekis J.V., Gariti J., Niederberger C., Scoccia B.;
RT "Expression of a truncated epidermal growth factor receptor-like protein
RT (TEGFR) in ovarian cancer.";
RL Gynecol. Oncol. 65:36-41(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Placenta;
RX PubMed=11161793; DOI=10.1006/geno.2000.6341;
RA Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J.,
RA Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L.,
RA Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D., Maihle N.J.;
RT "Comparative genomic sequence analysis and isolation of human and mouse
RT alternative EGFR transcripts encoding truncated receptor isoforms.";
RL Genomics 71:1-20(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Xu L., Hong A., He X.;
RT "Cloning of the cDNA for a short EGF receptor from human placenta.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-98; ARG-266; LYS-521;
RP ILE-674; GLY-962 AND PRO-988.
RG NIEHS SNPs program;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-687.
RA Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M., Lampland A.L.,
RA Balasubramaniam S., Crossley T.O., Magnuson T.R., Maihle N.J.;
RT "Human and mouse alternative EGFR transcripts encoding only the
RT extracellular domain of the receptor.";
RL Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 713-924.
RX PubMed=6326261; DOI=10.1126/science.6326261;
RA Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M.,
RA Verma I.M., Gill G.N., Rosenfeld M.G.;
RT "Expression cloning of human EGF receptor complementary DNA: gene
RT amplification and three related messenger RNA products in A431 cells.";
RL Science 224:843-848(1984).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 150-962.
RX PubMed=6330563; DOI=10.1038/309806a0;
RA Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P.,
RA Roe B.A., Merlino G.T., Pastan I.;
RT "Human epidermal growth factor receptor cDNA is homologous to a variety of
RT RNAs overproduced in A431 carcinoma cells.";
RL Nature 309:806-810(1984).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1210.
RX PubMed=6093780; DOI=10.1016/0006-291x(84)90926-4;
RA Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G.,
RA O'Malley B.W.;
RT "Isolation of an evolutionarily conserved epidermal growth factor receptor
RT cDNA from human A431 carcinoma cells.";
RL Biochem. Biophys. Res. Commun. 124:125-132(1984).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=3329716;
RA Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A.,
RA Waterfield M.D.;
RT "The human EGF receptor gene: structure of the 110 kb locus and
RT identification of sequences regulating its transcription.";
RL Oncogene Res. 1:375-396(1987).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=1988448; DOI=10.1016/s0021-9258(18)52359-0;
RA Haley J.D., Waterfield M.D.;
RT "Contributory effects of de novo transcription and premature transcript
RT termination in the regulation of human epidermal growth factor receptor
RT proto-oncogene RNA synthesis.";
RL J. Biol. Chem. 266:1746-1753(1991).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=2991899; DOI=10.1073/pnas.82.15.4920;
RA Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.;
RT "Characterization and sequence of the promoter region of the human
RT epidermal growth factor receptor gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985).
RN [15]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 25-49.
RX PubMed=6324343; DOI=10.1126/science.6324343;
RA Weber W., Gill G.N., Spiess J.;
RT "Production of an epidermal growth factor receptor-related protein.";
RL Science 224:294-297(1984).
RN [16]
RP PROTEIN SEQUENCE OF 540.
RA Kohda D.;
RL Submitted (SEP-1997) to UniProtKB.
RN [17]
RP PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND 1068-1077,
RP AND PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND SER-1071.
RX PubMed=3138233; DOI=10.1016/s0021-9258(18)37684-1;
RA Heisermann G.J., Gill G.N.;
RT "Epidermal growth factor receptor threonine and serine residues
RT phosphorylated in vivo.";
RL J. Biol. Chem. 263:13152-13158(1988).
RN [18]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [19]
RP PROTEIN SEQUENCE OF 740-744 AND 746-747.
RX PubMed=2985580; DOI=10.1016/s0021-9258(18)89002-0;
RA Russo M.W., Lukas T.J., Cohen S., Staros J.V.;
RT "Identification of residues in the nucleotide binding site of the epidermal
RT growth factor receptor/kinase.";
RL J. Biol. Chem. 260:5205-5208(1985).
RN [20]
RP PROTEIN SEQUENCE OF 861-875 AND 914-932, UBIQUITINATION AT LYS-716;
RP LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and degradation by
RT multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [21]
RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
RX PubMed=9556602; DOI=10.1074/jbc.273.18.11150;
RA Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.;
RT "Disulfide bond structure of human epidermal growth factor receptor.";
RL J. Biol. Chem. 273:11150-11157(1998).
RN [22]
RP RECEPTOR ACTIVITY.
RX PubMed=6325948; DOI=10.1038/309270a0;
RA Mroczkowski B., Mosig G., Cohen S.;
RT "ATP-stimulated interaction between epidermal growth factor receptor and
RT supercoiled DNA.";
RL Nature 309:270-273(1984).
RN [23]
RP REVIEW.
RX PubMed=3039909; DOI=10.1146/annurev.bi.56.070187.004313;
RA Carpenter G.;
RT "Receptors for epidermal growth factor and other polypeptide mitogens.";
RL Annu. Rev. Biochem. 56:881-914(1987).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND LIGAND-BINDING.
RX PubMed=2790960; DOI=10.1016/0092-8674(89)90867-2;
RA Chen W.S., Lazar C.S., Lund K.A., Welsh J.B., Chang C.P., Walton G.M.,
RA Der C.J., Wiley H.S., Gill G.N., Rosenfeld M.G.;
RT "Functional independence of the epidermal growth factor receptor from a
RT domain required for ligand-induced internalization and calcium
RT regulation.";
RL Cell 59:33-43(1989).
RN [25]
RP PHOSPHORYLATION AT TYR-1110.
RX PubMed=2543678; DOI=10.1016/s0021-9258(18)81674-x;
RA Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M., Howk R.,
RA Givol D., Ullrich A., Schlessinger J.;
RT "All autophosphorylation sites of epidermal growth factor (EGF) receptor
RT and HER2/neu are located in their carboxyl-terminal tails. Identification
RT of a novel site in EGF receptor.";
RL J. Biol. Chem. 264:10667-10671(1989).
RN [26]
RP IDENTIFICATION OF AREG AS LIGAND, AND FUNCTION.
RX PubMed=7679104; DOI=10.1016/s0021-9258(18)53862-x;
RA Johnson G.R., Kannan B., Shoyab M., Stromberg K.;
RT "Amphiregulin induces tyrosine phosphorylation of the epidermal growth
RT factor receptor and p185erbB2. Evidence that amphiregulin acts exclusively
RT through the epidermal growth factor receptor at the surface of human
RT epithelial cells.";
RL J. Biol. Chem. 268:2924-2931(1993).
RN [27]
RP INTERACTION WITH ZPR1.
RX PubMed=8650580; DOI=10.1126/science.272.5269.1797;
RA Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T.,
RA Davis R.J.;
RT "Binding of zinc finger protein ZPR1 to the epidermal growth factor
RT receptor.";
RL Science 272:1797-1802(1996).
RN [28]
RP INTERACTION WITH ZPR1.
RX PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
RA Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
RT "Interaction of ZPR1 with translation elongation factor-1alpha in
RT proliferating cells.";
RL J. Cell Biol. 143:1471-1484(1998).
RN [29]
RP PHOSPHORYLATION AT THR-678 AND THR-693.
RX PubMed=10523301; DOI=10.1093/emboj/18.20.5567;
RA Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.;
RT "Cell-type specific phosphorylation of threonines T654 and T669 by PKD
RT defines the signal capacity of the EGF receptor.";
RL EMBO J. 18:5567-5576(1999).
RN [30]
RP IDENTIFICATION OF BETACELLULIN/BTC AS LIGAND.
RX PubMed=8144591; DOI=10.1016/s0021-9258(17)36977-6;
RA Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J., Igarashi K.,
RA Sasada R.;
RT "Recombinant human betacellulin. Molecular structure, biological
RT activities, and receptor interaction.";
RL J. Biol. Chem. 269:9966-9973(1994).
RN [31]
RP FUNCTION IN PHOSPHORYLATION OF CBL, AND INTERACTION WITH CBL.
RX PubMed=7657591; DOI=10.1074/jbc.270.35.20242;
RA Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.;
RT "Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and
RT association with epidermal growth factor (EGF) receptor upon EGF
RT stimulation.";
RL J. Biol. Chem. 270:20242-20245(1995).
RN [32]
RP GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
RX PubMed=8962717; DOI=10.3109/08977199609034572;
RA Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.;
RT "Analysis of the glycosylation patterns of the extracellular domain of the
RT epidermal growth factor receptor expressed in Chinese hamster ovary
RT fibroblasts.";
RL Growth Factors 13:121-132(1996).
RN [33]
RP IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND, AND FUNCTION.
RX PubMed=9419975; DOI=10.1038/sj.onc.1201458;
RA Komurasaki T., Toyoda H., Uchida D., Morimoto S.;
RT "Epiregulin binds to epidermal growth factor receptor and ErbB-4 and
RT induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-
RT 2, ErbB-3 and ErbB-4.";
RL Oncogene 15:2841-2848(1997).
RN [34]
RP PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN1 AND PTPN2.
RX PubMed=9488479; DOI=10.1128/mcb.18.3.1622;
RA Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.;
RT "Epidermal growth factor receptor and the adaptor protein p52Shc are
RT specific substrates of T-cell protein tyrosine phosphatase.";
RL Mol. Cell. Biol. 18:1622-1634(1998).
RN [35]
RP INTERACTION WITH AP2M1.
RX PubMed=10228163; DOI=10.1093/emboj/18.9.2489;
RA Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.;
RT "Inhibition of the receptor-binding function of clathrin adaptor protein
RT AP-2 by dominant-negative mutant mu2 subunit and its effects on
RT endocytosis.";
RL EMBO J. 18:2489-2499(1999).
RN [36]
RP INTERACTION WITH GRB2; NCK1 AND NCK2.
RX PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
RA Braverman L.E., Quilliam L.A.;
RT "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing
RT adapter protein having similar binding and biological properties to Nck.";
RL J. Biol. Chem. 274:5542-5549(1999).
RN [37]
RP GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
RX PubMed=10731668; DOI=10.1093/oxfordjournals.jbchem.a022585;
RA Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.;
RT "Characterization of the N-oligosaccharides attached to the atypical Asn-X-
RT Cys sequence of recombinant human epidermal growth factor receptor.";
RL J. Biochem. 127:65-72(2000).
RN [38]
RP FUNCTION IN PHOSPHORYLATION OF RGS16.
RX PubMed=11602604; DOI=10.1074/jbc.m108862200;
RA Derrien A., Druey K.M.;
RT "RGS16 function is regulated by epidermal growth factor receptor-mediated
RT tyrosine phosphorylation.";
RL J. Biol. Chem. 276:48532-48538(2001).
RN [39]
RP GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;
RP ASN-413; ASN-444; ASN-528; ASN-568; ASN-603 AND ASN-623.
RX PubMed=12731890; DOI=10.1021/bi027101p;
RA Zhen Y., Caprioli R.M., Staros J.V.;
RT "Characterization of glycosylation sites of the epidermal growth factor
RT receptor.";
RL Biochemistry 42:5478-5492(2003).
RN [40]
RP FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, AND PHOSPHORYLATION
RP AT TYR-1092 AND TYR-1110.
RX PubMed=12873986;
RA Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.;
RT "Identification and characterization of signal transducer and activator of
RT transcription 3 recruitment sites within the epidermal growth factor
RT receptor.";
RL Cancer Res. 63:3923-3930(2003).
RN [41]
RP ACTIVITY REGULATION, AND INTERACTION WITH LRIG1.
RX PubMed=15282549; DOI=10.1038/sj.emboj.7600342;
RA Gur G., Rubin C., Katz M., Amit I., Citri A., Nilsson J., Amariglio N.,
RA Henriksson R., Rechavi G., Hedman H., Wides R., Yarden Y.;
RT "LRIG1 restricts growth factor signaling by enhancing receptor
RT ubiquitylation and degradation.";
RL EMBO J. 23:3270-3281(2004).
RN [42]
RP FUNCTION IN EGFR SIGNALING, IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND
RP ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2, INTERACTION WITH
RP PIK3C2B, AND MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND
RP TYR-1197.
RX PubMed=10805725; DOI=10.1128/mcb.20.11.3817-3830.2000;
RA Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
RA Domin J.;
RT "Class II phosphoinositide 3-kinases are downstream targets of activated
RT polypeptide growth factor receptors.";
RL Mol. Cell. Biol. 20:3817-3830(2000).
RN [43]
RP FUNCTION IN NF-KAPPA-B ACTIVATION, AND INTERACTION WITH RIPK1.
RX PubMed=11116146; DOI=10.1074/jbc.m008458200;
RA Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S.,
RA Vartanian T.;
RT "The epidermal growth factor receptor engages receptor interacting protein
RT and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-
RT kappa B. Identification of a novel receptor-tyrosine kinase signalosome.";
RL J. Biol. Chem. 276:8865-8874(2001).
RN [44]
RP FUNCTION IN PHOSPHORYLATION OF MUC1, AND INTERACTION WITH MUC1.
RX PubMed=11483589; DOI=10.1074/jbc.c100359200;
RA Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III,
RA Kufe D.;
RT "The epidermal growth factor receptor regulates interaction of the human
RT DF3/MUC1 carcinoma antigen with c-Src and beta-catenin.";
RL J. Biol. Chem. 276:35239-35242(2001).
RN [45]
RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH SOCS5.
RX PubMed=15590694; DOI=10.1074/jbc.m408575200;
RA Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N.,
RA Rechavi G., Yarden Y.;
RT "Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor
RT receptor signaling.";
RL J. Biol. Chem. 280:7038-7048(2005).
RN [46]
RP IDENTIFICATION OF EPIGEN/EPGN AS A LIGAND, AND FUNCTION.
RX PubMed=15611079; DOI=10.1074/jbc.m413919200;
RA Kochupurakkal B.S., Harari D., Di-Segni A., Maik-Rachline G., Lyass L.,
RA Gur G., Kerber G., Citri A., Lavi S., Eilam R., Chalifa-Caspi V.,
RA Eshhar Z., Pikarsky E., Pinkas-Kramarski R., Bacus S.S., Yarden Y.;
RT "Epigen, the last ligand of ErbB receptors, reveals intricate relationships
RT between affinity and mitogenicity.";
RL J. Biol. Chem. 280:8503-8512(2005).
RN [47]
RP GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;
RP ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION AT THR-693;
RP SER-991 AND SER-1026, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16083266; DOI=10.1021/pr050113n;
RA Wu S.L., Kim J., Hancock W.S., Karger B.;
RT "Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS
RT platform for high sequence coverage of complex proteins with extensive
RT post-translational modifications-comprehensive analysis of beta-casein and
RT epidermal growth factor receptor (EGFR).";
RL J. Proteome Res. 4:1155-1170(2005).
RN [48]
RP INTERACTION WITH PELP1.
RX PubMed=16140940; DOI=10.1158/0008-5472.can-05-0614;
RA Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z.,
RA Sahin A.A., Kumar R.;
RT "Functional implications of altered subcellular localization of PELP1 in
RT breast cancer cells.";
RL Cancer Res. 65:7724-7732(2005).
RN [49]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1172 AND TYR-1197, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [50]
RP FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION,
RP INTERACTION WITH PCNA, AND SUBCELLULAR LOCATION.
RX PubMed=17115032; DOI=10.1038/ncb1501;
RA Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,
RA McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.;
RT "Tyrosine phosphorylation controls PCNA function through protein
RT stability.";
RL Nat. Cell Biol. 8:1359-1368(2006).
RN [51]
RP INTERACTION WITH STX19.
RX PubMed=16420529; DOI=10.1111/j.1600-0854.2005.00378.x;
RA Wang Y., Foo L.Y., Guo K., Gan B.Q., Zeng Q., Hong W., Tang B.L.;
RT "Syntaxin 9 is enriched in skin hair follicle epithelium and interacts with
RT the epidermal growth factor receptor.";
RL Traffic 7:216-226(2006).
RN [52]
RP INTERACTION WITH PIKFYVE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17909029; DOI=10.1158/0008-5472.can-07-1333;
RA Kim J., Jahng W.J., Di Vizio D., Lee J.S., Jhaveri R., Rubin M.A.,
RA Shisheva A., Freeman M.R.;
RT "The phosphoinositide kinase PIKfyve mediates epidermal growth factor
RT receptor trafficking to the nucleus.";
RL Cancer Res. 67:9229-9237(2007).
RN [53]
RP TISSUE SPECIFICITY.
RX PubMed=17671655; DOI=10.1172/jci31680;
RA Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D.,
RA Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E., Hoenderop J.G.,
RA Knoers N.V., Bindels R.J.;
RT "Impaired basolateral sorting of pro-EGF causes isolated recessive renal
RT hypomagnesemia.";
RL J. Clin. Invest. 117:2260-2267(2007).
RN [54]
RP INTERACTION WITH TNF2, AND SUBCELLULAR LOCATION.
RX PubMed=17182860; DOI=10.1091/mbc.e06-02-0142;
RA Shen F., Lin Q., Gu Y., Childress C., Yang W.;
RT "Activated Cdc42-associated kinase 1 is a component of EGF receptor
RT signaling complex and regulates EGF receptor degradation.";
RL Mol. Biol. Cell 18:732-742(2007).
RN [55]
RP INTERACTION WITH NEU3, AND ACTIVITY REGULATION.
RX PubMed=17334392; DOI=10.1038/sj.onc.1210341;
RA Wada T., Hata K., Yamaguchi K., Shiozaki K., Koseki K., Moriya S.,
RA Miyagi T.;
RT "A crucial role of plasma membrane-associated sialidase in the survival of
RT human cancer cells.";
RL Oncogene 26:2483-2490(2007).
RN [56]
RP INTERACTION WITH ATXN2.
RX PubMed=18602463; DOI=10.1016/j.cellsig.2008.05.018;
RA Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J.,
RA Auburger G.;
RT "Ataxin-2 associates with the endocytosis complex and affects EGF receptor
RT trafficking.";
RL Cell. Signal. 20:1725-1739(2008).
RN [57]
RP INTERACTION WITH GAB2.
RX PubMed=19172738; DOI=10.1038/emboj.2008.159;
RA Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
RA Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M.,
RA James D.E., Daly R.J.;
RT "Phosphorylation-dependent binding of 14-3-3 terminates signalling by the
RT Gab2 docking protein.";
RL EMBO J. 27:2305-2316(2008).
RN [58]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [59]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-1064;
RP SER-1081; SER-1166 AND TYR-1197, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [60]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; SER-995; TYR-998;
RP SER-1039; THR-1041; SER-1042; SER-1064 AND SER-1166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [61]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [62]
RP ACTIVITY REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197,
RP DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, AND INTERACTION WITH CBL
RP AND GRB2.
RX PubMed=19836242; DOI=10.1016/j.cub.2009.09.048;
RA Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F.,
RA Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.;
RT "An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase
RT controlling EGFR endocytosis.";
RL Curr. Biol. 19:1788-1798(2009).
RN [63]
RP INTERACTION WITH GAREM1.
RX PubMed=19509291; DOI=10.1074/jbc.m109.021139;
RA Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E.,
RA Taniguchi H., Konishi H.;
RT "GAREM, a novel adaptor protein for growth factor receptor-bound protein 2,
RT contributes to cellular transformation through the activation of
RT extracellular signal-regulated kinase signaling.";
RL J. Biol. Chem. 284:20206-20214(2009).
RN [64]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [65]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [66]
RP INTERACTION WITH GPER1.
RX PubMed=19749156; DOI=10.1210/me.2009-0120;
RA Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F.,
RA Fuqua S.A., Ando S., Maggiolini M.;
RT "G protein-coupled receptor 30 expression is up-regulated by EGF and TGF
RT alpha in estrogen receptor alpha-positive cancer cells.";
RL Mol. Endocrinol. 23:1815-1826(2009).
RN [67]
RP MUTAGENESIS OF 525-SER--ALA-1210; ASP-587; HIS-590 AND LYS-609.
RX PubMed=19718021; DOI=10.1038/nature08297;
RA Alvarado D., Klein D.E., Lemmon M.A.;
RT "ErbB2 resembles an autoinhibited invertebrate epidermal growth factor
RT receptor.";
RL Nature 461:287-291(2009).
RN [68]
RP INTERACTION WITH COPG1, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=20674546; DOI=10.1016/j.bbrc.2010.07.096;
RA Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.;
RT "COPI-mediated retrograde trafficking from the Golgi to the ER regulates
RT EGFR nuclear transport.";
RL Biochem. Biophys. Res. Commun. 399:498-504(2010).
RN [69]
RP INTERACTION WITH GPER1, AND SUBCELLULAR LOCATION.
RX PubMed=20551055; DOI=10.1158/0008-5472.can-10-0408;
RA Madeo A., Maggiolini M.;
RT "Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-
RT induced gene expression and migration in breast cancer-associated
RT fibroblasts.";
RL Cancer Res. 70:6036-6046(2010).
RN [70]
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH CCDC88A AND GNAI3, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RX PubMed=20462955; DOI=10.1091/mbc.e10-01-0028;
RA Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P.,
RA Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.;
RT "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor
RT and determines whether cells migrate or proliferate.";
RL Mol. Biol. Cell 21:2338-2354(2010).
RN [71]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1064 AND
RP TYR-1197, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [72]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [73]
RP PHOSPHORYLATION AT SER-229.
RX PubMed=21487020; DOI=10.1074/jbc.m111.240796;
RA Huang W.C., Chen Y.J., Li L.Y., Wei Y.L., Hsu S.C., Tsai S.L., Chiu P.C.,
RA Huang W.P., Wang Y.N., Chen C.H., Chang W.C., Chang W.C., Chen A.J.,
RA Tsai C.H., Hung M.C.;
RT "Nuclear translocation of epidermal growth factor receptor by Akt-dependent
RT phosphorylation enhances breast cancer-resistant protein expression in
RT gefitinib-resistant cells.";
RL J. Biol. Chem. 286:20558-20568(2011).
RN [74]
RP FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199
RP BY PRMT5, AND INTERACTION WITH PRMT5 AND PTPN6.
RX PubMed=21258366; DOI=10.1038/ncb2158;
RA Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J.,
RA Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T., Tsai C.H.,
RA Hung M.C.;
RT "Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation
RT negatively modulates EGFR-mediated ERK activation.";
RL Nat. Cell Biol. 13:174-181(2011).
RN [75]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21516087; DOI=10.1038/nm.2341;
RA Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
RA Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B., Zahid M.N.,
RA Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M., Pietschmann T.,
RA Patel A.H., Pessaux P., Doffoel M., Raffelsberger W., Poch O.,
RA McKeating J.A., Brino L., Baumert T.F.;
RT "EGFR and EphA2 are host factors for hepatitis C virus entry and possible
RT targets for antiviral therapy.";
RL Nat. Med. 17:589-595(2011).
RN [76]
RP INTERACTION WITH FER, AND PHOSPHORYLATION.
RX PubMed=21518868; DOI=10.1073/pnas.1105369108;
RA Guo C., Stark G.R.;
RT "FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine
RT through EGF-dependent activation of NF-kappaB.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011).
RN [77]
RP INTERACTION WITH ANKRD13A; ANKRD13B AND ANKRD13D, UBIQUITINATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22298428; DOI=10.1091/mbc.e11-09-0817;
RA Tanno H., Yamaguchi T., Goto E., Ishido S., Komada M.;
RT "The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor
RT endocytosis from the plasma membrane.";
RL Mol. Biol. Cell 23:1343-1353(2012).
RN [78]
RP UBIQUITINATION, AND DEUBIQUITINATION BY OTUD7B.
RX PubMed=22179831; DOI=10.1038/onc.2011.587;
RA Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F., Aulmann S.,
RA Ben-Chetrit N., Pines G., Navon R., Crosetto N., Kostler W., Carvalho S.,
RA Lavi S., Schmitt F., Dikic I., Yakhini Z., Sinn P., Mills G.B., Yarden Y.;
RT "Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression.";
RL Oncogene 31:4599-4608(2012).
RN [79]
RP INTERACTION WITH RNF115 AND RNF126.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
RN [80]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-1064, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [81]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1026 AND
RP SER-1166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [82]
RP INTERACTION WITH CCDC88A AND GNAI3.
RX PubMed=25187647; DOI=10.1091/mbc.e14-05-0978;
RA Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M.,
RA Kufareva I., Abagyan R., Ghosh P.;
RT "Structural basis for activation of trimeric Gi proteins by multiple growth
RT factor receptors via GIV/Girdin.";
RL Mol. Biol. Cell 25:3654-3671(2014).
RN [83]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CD44.
RX PubMed=23589287; DOI=10.1074/jbc.m113.451336;
RA Midgley A.C., Rogers M., Hallett M.B., Clayton A., Bowen T., Phillips A.O.,
RA Steadman R.;
RT "Transforming growth factor-beta1 (TGF-beta1)-stimulated fibroblast to
RT myofibroblast differentiation is mediated by hyaluronan (HA)-facilitated
RT epidermal growth factor receptor (EGFR) and CD44 co-localization in lipid
RT rafts.";
RL J. Biol. Chem. 288:14824-14838(2013).
RN [84]
RP INTERACTION WITH GPRC5A.
RX PubMed=25311788; DOI=10.1186/1476-4598-13-233;
RA Lin X., Zhong S., Ye X., Liao Y., Yao F., Yang X., Sun B., Zhang J., Li Q.,
RA Gao Y., Wang Y., Liu J., Han B., Chin Y.E., Zhou B.P., Deng J.;
RT "EGFR phosphorylates and inhibits lung tumor suppressor GPRC5A in lung
RT cancer.";
RL Mol. Cancer 13:233-233(2014).
RN [85]
RP INTERACTION WITH FAM83B.
RX PubMed=23912460; DOI=10.1038/onc.2013.293;
RA Cipriano R., Bryson B.L., Miskimen K.L., Bartel C.A., Hernandez-Sanchez W.,
RA Bruntz R.C., Scott S.A., Lindsley C.W., Brown H.A., Jackson M.W.;
RT "Hyperactivation of EGFR and downstream effector phospholipase D1 by
RT oncogenic FAM83B.";
RL Oncogene 33:3298-3306(2014).
RN [86]
RP GLYCOSYLATION AT ASN-528, AND ACTIVITY REGULATION.
RX PubMed=25922362; DOI=10.1093/glycob/cwv026;
RA Mozzi A., Forcella M., Riva A., Difrancesco C., Molinari F., Martin V.,
RA Papini N., Bernasconi B., Nonnis S., Tedeschi G., Mazzucchelli L.,
RA Monti E., Fusi P., Frattini M.;
RT "NEU3 activity enhances EGFR activation without affecting EGFR expression
RT and acts on its sialylation levels.";
RL Glycobiology 25:855-868(2015).
RN [87]
RP FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS
RP SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND
RP TYR-1197, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1048-ALA--ALA-1210;
RP CYS-1049 AND CYS-1146.
RX PubMed=27153536; DOI=10.1016/j.molcel.2016.04.003;
RA Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A.,
RA Witze E.S.;
RT "Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on
RT EGFR Signaling.";
RL Mol. Cell 62:385-396(2016).
RN [88]
RP INTERACTION WITH PGRMC1.
RX PubMed=26988023; DOI=10.1038/ncomms11030;
RA Kabe Y., Nakane T., Koike I., Yamamoto T., Sugiura Y., Harada E.,
RA Sugase K., Shimamura T., Ohmura M., Muraoka K., Yamamoto A., Uchida T.,
RA Iwata S., Yamaguchi Y., Krayukhina E., Noda M., Handa H., Ishimori K.,
RA Uchiyama S., Kobayashi T., Suematsu M.;
RT "Haem-dependent dimerization of PGRMC1/Sigma-2 receptor facilitates cancer
RT proliferation and chemoresistance.";
RL Nat. Commun. 7:11030-11030(2016).
RN [89]
RP INTERACTION WITH LAPTM4B.
RX PubMed=28479384; DOI=10.1016/j.gene.2017.05.006;
RA Tian M., Chen Y., Tian D., Qiao X., Ma Z., Li J.;
RT "Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer
RT cells.";
RL Gene 626:48-53(2017).
RN [90]
RP HYDROXYBUTYRYLATION AT LYS-745.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [91]
RP INTERACTION WITH TRAF4.
RX PubMed=30352854; DOI=10.1073/pnas.1809599115;
RA Cai G., Zhu L., Chen X., Sun K., Liu C., Sen G.C., Stark G.R., Qin J.,
RA Li X.;
RT "TRAF4 binds to the juxtamembrane region of EGFR directly and promotes
RT kinase activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:11531-11536(2018).
RN [92] {ECO:0007744|PDB:1MOX}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-525 IN COMPLEX WITH TGFA,
RP FUNCTION, GLYCOSYLATION AT ASN-56; ASN-196 AND ASN-352, AND DISULFIDE
RP BONDS.
RX PubMed=12297049; DOI=10.1016/s0092-8674(02)00940-6;
RA Garrett T.P., McKern N.M., Lou M., Elleman T.C., Adams T.E., Lovrecz G.O.,
RA Zhu H.J., Walker F., Frenkel M.J., Hoyne P.A., Jorissen R.N., Nice E.C.,
RA Burgess A.W., Ward C.W.;
RT "Crystal structure of a truncated epidermal growth factor receptor
RT extracellular domain bound to transforming growth factor alpha.";
RL Cell 110:763-773(2002).
RN [93] {ECO:0007744|PDB:1IVO}
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-646 IN COMPLEX WITH EGF,
RP FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION, SUBUNIT, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-56; ASN-175; ASN-196; ASN-352; ASN-361 AND ASN-444.
RX PubMed=12297050; DOI=10.1016/s0092-8674(02)00963-7;
RA Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H.,
RA Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.;
RT "Crystal structure of the complex of human epidermal growth factor and
RT receptor extracellular domains.";
RL Cell 110:775-787(2002).
RN [94] {ECO:0007744|PDB:1NQL}
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-642 IN COMPLEX WITH EGF,
RP FUNCTION, SUBUNIT, MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609, DISULFIDE
RP BONDS, AND GLYCOSYLATION AT ASN-352; ASN-361; ASN-444; ASN-528; ASN-568 AND
RP ASN-603.
RX PubMed=12620237; DOI=10.1016/s1097-2765(03)00047-9;
RA Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J.,
RA Lemmon M.A.;
RT "EGF activates its receptor by removing interactions that autoinhibit
RT ectodomain dimerization.";
RL Mol. Cell 11:507-517(2003).
RN [95] {ECO:0007744|PDB:1XKK}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH
RP GW572016, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=15374980; DOI=10.1158/0008-5472.can-04-1168;
RA Wood E.R., Truesdale A.T., McDonald O.B., Yuan D., Hassell A.,
RA Dickerson S.H., Ellis B., Pennisi C., Horne E., Lackey K., Alligood K.J.,
RA Rusnak D.W., Gilmer T.M., Shewchuk L.;
RT "A unique structure for epidermal growth factor receptor bound to GW572016
RT (Lapatinib): relationships among protein conformation, inhibitor off-rate,
RT and receptor activity in tumor cells.";
RL Cancer Res. 64:6652-6659(2004).
RN [96] {ECO:0007744|PDB:1YY9}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-642 IN COMPLEX WITH CETUXIMAB.
RX PubMed=15837620; DOI=10.1016/j.ccr.2005.03.003;
RA Li S., Schmitz K.R., Jeffrey P.D., Wiltzius J.J., Kussie P., Ferguson K.M.;
RT "Structural basis for inhibition of the epidermal growth factor receptor by
RT cetuximab.";
RL Cancer Cell 7:301-311(2005).
RN [97]
RP STRUCTURE BY NMR OF 669-721.
RX PubMed=15840573; DOI=10.1074/jbc.m502698200;
RA Choowongkomon K., Carlin C.R., Sonnichsen F.D.;
RT "A structural model for the membrane-bound form of the juxtamembrane domain
RT of the epidermal growth factor receptor.";
RL J. Biol. Chem. 280:24043-24052(2005).
RN [98] {ECO:0007744|PDB:2ITN, ECO:0007744|PDB:2ITO, ECO:0007744|PDB:2ITP, ECO:0007744|PDB:2ITQ, ECO:0007744|PDB:2ITT, ECO:0007744|PDB:2ITU, ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2J6M}
RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 696-1022 OF WILD-TYPE AND
RP VARIANTS SER-719 AND ARG-858 IN COMPLEXES WITH ATP ANALOGS AND SYNTHETIC
RP INHIBITORS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND CHARACTERIZATION
RP OF VARIANTS SER-719 AND ARG-858.
RX PubMed=17349580; DOI=10.1016/j.ccr.2006.12.017;
RA Yun C.H., Boggon T.J., Li Y., Woo M.S., Greulich H., Meyerson M., Eck M.J.;
RT "Structures of lung cancer-derived EGFR mutants and inhibitor complexes:
RT mechanism of activation and insights into differential inhibitor
RT sensitivity.";
RL Cancer Cell 11:217-227(2007).
RN [99]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH ERRFI1,
RP ACTIVITY REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, AND
RP INTERACTION WITH ERRFI1.
RX PubMed=18046415; DOI=10.1038/nature05998;
RA Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.;
RT "Inhibition of the EGF receptor by binding of MIG6 to an activating kinase
RT domain interface.";
RL Nature 450:741-744(2007).
RN [100] {ECO:0007744|PDB:2JIT, ECO:0007744|PDB:2JIU, ECO:0007744|PDB:2JIV}
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 695-1022 OF VARIANT MET-790,
RP CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT MET-790.
RX PubMed=18227510; DOI=10.1073/pnas.0709662105;
RA Yun C.H., Mengwasser K.E., Toms A.V., Woo M.S., Greulich H., Wong K.K.,
RA Meyerson M., Eck M.J.;
RT "The T790M mutation in EGFR kinase causes drug resistance by increasing the
RT affinity for ATP.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2070-2075(2008).
RN [101] {ECO:0007744|PDB:3GT8}
RP X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC ACTIVITY,
RP PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197, MUTAGENESIS OF LEU-688;
RP GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006, AND SUBUNIT.
RX PubMed=19563760; DOI=10.1016/j.cell.2009.04.025;
RA Jura N., Endres N.F., Engel K., Deindl S., Das R., Lamers M.H.,
RA Wemmer D.E., Zhang X., Kuriyan J.;
RT "Mechanism for activation of the EGF receptor catalytic domain by the
RT juxtamembrane segment.";
RL Cell 137:1293-1307(2009).
RN [102]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 669-1022 OF MUTANT MET-745,
RP CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LEU-688; VAL-689; GLU-690; LEU-692;
RP THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706 AND LYS-745.
RX PubMed=19560417; DOI=10.1016/j.molcel.2009.04.034;
RA Red Brewer M., Choi S.H., Alvarado D., Moravcevic K., Pozzi A.,
RA Lemmon M.A., Carpenter G.;
RT "The juxtamembrane region of the EGF receptor functions as an activation
RT domain.";
RL Mol. Cell 34:641-651(2009).
RN [103]
RP STRUCTURE BY NMR OF 634-677 IN COMPLEX WITH ERBB2, AND SUBUNIT.
RX PubMed=20471394; DOI=10.1016/j.jmb.2010.05.016;
RA Mineev K.S., Bocharov E.V., Pustovalova Y.E., Bocharova O.V., Chupin V.V.,
RA Arseniev A.S.;
RT "Spatial structure of the transmembrane domain heterodimer of ErbB1 and
RT ErbB2 receptor tyrosine kinases.";
RL J. Mol. Biol. 400:231-243(2010).
RN [104] {ECO:0007744|PDB:3NJP}
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-638 IN COMPLEX WITH EGF,
RP FUNCTION, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-56; ASN-73;
RP ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528.
RX PubMed=20837704; DOI=10.1128/mcb.00742-10;
RA Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Springer T.A.;
RT "Structural evidence for loose linkage between ligand binding and kinase
RT activation in the epidermal growth factor receptor.";
RL Mol. Cell. Biol. 30:5432-5443(2010).
RN [105]
RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1066-1076 IN COMPLEX WITH CBLB,
RP AND INTERACTION WITH CBLB.
RG Structural genomics consortium;
RT "Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069
RT peptide.";
RL Submitted (OCT-2010) to the PDB data bank.
RN [106]
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1062-1074 IN COMPLEX WITH CBLC,
RP PHOSPHORYLATION AT TYR-1069, INTERACTION WITH CBLC, AND MUTAGENESIS OF
RP GLN-1067; ARG-1068 AND TYR-1069.
RX PubMed=22888118; DOI=10.1093/jb/mvs085;
RA Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M.,
RA Yamanashi Y., Yamamoto T., Nakagawa A.;
RT "Structural flexibility regulates phosphopeptide-binding activity of the
RT tyrosine kinase binding domain of Cbl-c.";
RL J. Biochem. 152:487-495(2012).
RN [107]
RP VARIANTS ALA-709; GLY-709; CYS-719; SER-719; 746-GLU--ALA-750 DEL;
RP 746-GLU--THR-751 DELINS ALA; 746-GLU--SER-752 DELINS ASP; 747-LEU--THR-751
RP DEL; ILE-768; MET-769; VAL-833; LEU-835; VAL-838; ARG-858 AND GLN-861.
RX PubMed=15623594; DOI=10.1158/1078-0432.ccr-04-1245;
RA Huang S.F., Liu H.P., Li L.H., Ku Y.C., Fu Y.N., Tsai H.Y., Chen Y.T.,
RA Lin Y.F., Chang W.C., Kuo H.P., Wu Y.C., Chen Y.R., Tsai S.F.;
RT "High frequency of epidermal growth factor receptor mutations with complex
RT patterns in non-small cell lung cancers related to gefitinib responsiveness
RT in Taiwan.";
RL Clin. Cancer Res. 10:8195-8203(2004).
RN [108]
RP VARIANTS SER-719 AND ARG-858, AND POSSIBLE INVOLVEMENT IN LUNG CANCER.
RX PubMed=15118125; DOI=10.1126/science.1099314;
RA Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S.,
RA Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H.,
RA Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.;
RT "EGFR mutations in lung cancer: correlation with clinical response to
RT gefitinib therapy.";
RL Science 304:1497-1500(2004).
RN [109]
RP VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719; SER-724;
RP LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748;
RP 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858; ARG-858;
RP GLN-861 AND GLU-873, AND POSSIBLE INVOLVEMENT IN LUNG CANCER.
RX PubMed=16533793; DOI=10.1158/1078-0432.ccr-05-1981;
RA Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K., Lam W.K.,
RA Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.;
RT "Distinct epidermal growth factor receptor and KRAS mutation patterns in
RT non-small cell lung cancer patients with different tobacco exposure and
RT clinicopathologic features.";
RL Clin. Cancer Res. 12:1647-1653(2006).
RN [110]
RP CHARACTERIZATION OF VARIANTS ALA-709; GLY-709; SER-719; ILE-768; VAL-833;
RP LEU-835; VAL-838; ARG-858 AND GLN-861.
RX PubMed=16205628; DOI=10.1038/sj.onc.1209159;
RA Chen Y.R., Fu Y.N., Lin C.H., Yang S.T., Hu S.F., Chen Y.T., Tsai S.F.,
RA Huang S.F.;
RT "Distinctive activation patterns in constitutively active and gefitinib-
RT sensitive EGFR mutants.";
RL Oncogene 25:1205-1215(2006).
RN [111]
RP VARIANT 30-VAL--ARG-297 DEL, AND POSSIBLE INVOLVEMENT IN LUNG CANCER.
RX PubMed=16672372; DOI=10.1073/pnas.0510284103;
RA Ji H., Zhao X., Yuza Y., Shimamura T., Li D., Protopopov A., Jung B.L.,
RA McNamara K., Xia H., Glatt K.A., Thomas R.K., Sasaki H., Horner J.W.,
RA Eck M., Mitchell A., Sun Y., Al-Hashem R., Bronson R.T., Rabindran S.K.,
RA Discafani C.M., Maher E., Shapiro G.I., Meyerson M., Wong K.K.;
RT "Epidermal growth factor receptor variant III mutations in lung
RT tumorigenesis and sensitivity to tyrosine kinase inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7817-7822(2006).
RN [112]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [113]
RP VARIANT NISBD2 ASP-428, CHARACTERIZATION OF VARIANT NISBD2 ASP-428, AND
RP INVOLVEMENT IN NISBD2.
RX PubMed=24691054; DOI=10.1038/jid.2014.164;
RA Campbell P., Morton P.E., Takeichi T., Salam A., Roberts N.,
RA Proudfoot L.E., Mellerio J.E., Aminu K., Wellington C., Patil S.N.,
RA Akiyama M., Liu L., McMillan J.R., Aristodemou S., Ishida-Yamamoto A.,
RA Abdul-Wahab A., Petrof G., Fong K., Harnchoowong S., Stone K.L.,
RA Harper J.I., McLean W.H., Simpson M.A., Parsons M., McGrath J.A.;
RT "Epithelial inflammation resulting from an inherited loss-of-function
RT mutation in EGFR.";
RL J. Invest. Dermatol. 134:2570-2578(2014).
CC -!- FUNCTION: Receptor tyrosine kinase binding ligands of the EGF family
CC and activating several signaling cascades to convert extracellular cues
CC into appropriate cellular responses (PubMed:2790960, PubMed:10805725,
CC PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG,
CC epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-
CC binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591,
CC PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536,
CC PubMed:20837704, PubMed:17909029). Ligand binding triggers receptor
CC homo- and/or heterodimerization and autophosphorylation on key
CC cytoplasmic residues. The phosphorylated receptor recruits adapter
CC proteins like GRB2 which in turn activates complex downstream signaling
CC cascades. Activates at least 4 major downstream signaling cascades
CC including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs
CC modules (PubMed:27153536). May also activate the NF-kappa-B signaling
CC cascade (PubMed:11116146). Also directly phosphorylates other proteins
CC like RGS16, activating its GTPase activity and probably coupling the
CC EGF receptor signaling to the G protein-coupled receptor signaling
CC (PubMed:11602604). Also phosphorylates MUC1 and increases its
CC interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589).
CC Positively regulates cell migration via interaction with CCDC88A/GIV
CC which retains EGFR at the cell membrane following ligand stimulation,
CC promoting EGFR signaling which triggers cell migration
CC (PubMed:20462955). Plays a role in enhancing learning and memory
CC performance (By similarity). {ECO:0000250|UniProtKB:Q01279,
CC ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146,
CC ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:11602604,
CC ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050,
CC ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986,
CC ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:15590694,
CC ECO:0000269|PubMed:15611079, ECO:0000269|PubMed:17115032,
CC ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:19560417,
CC ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:20837704,
CC ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:27153536,
CC ECO:0000269|PubMed:2790960, ECO:0000269|PubMed:7679104,
CC ECO:0000269|PubMed:8144591, ECO:0000269|PubMed:9419975}.
CC -!- FUNCTION: Isoform 2 may act as an antagonist of EGF action.
CC -!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
CC virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV
CC entry by promoting the formation of the CD81-CLDN1 receptor complexes
CC that are essential for HCV entry and by enhancing membrane fusion of
CC cells expressing HCV envelope glycoproteins.
CC {ECO:0000269|PubMed:21516087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:17349580,
CC ECO:0000269|PubMed:18046415, ECO:0000269|PubMed:18227510,
CC ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19563760};
CC -!- ACTIVITY REGULATION: Endocytosis and inhibition of the activated EGFR
CC by phosphatases like PTPRJ and PTPRK constitute immediate regulatory
CC mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR
CC endocytosis and activity. Moreover, inducible feedback inhibitors
CC including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative
CC regulatory mechanisms for the EGFR signaling. Up-regulated by NEU3-
CC mediated desialylation of N-linked glycan at Asn-528.
CC {ECO:0000269|PubMed:15282549, ECO:0000269|PubMed:15590694,
CC ECO:0000269|PubMed:17334392, ECO:0000269|PubMed:18046415,
CC ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:25922362}.
CC -!- SUBUNIT: Binding of the ligand triggers homo- and/or heterodimerization
CC of the receptor triggering its autophosphorylation. Heterodimer with
CC ERBB2 (PubMed:10805725). Forms a complex with CCDC88A/GIV (via SH2-like
CC regions) and GNAI3 which leads to enhanced EGFR signaling and
CC triggering of cell migration; binding to CCDC88A requires
CC autophosphorylation of the EGFR C-terminal region, and ligand
CC stimulation is required for recruitment of GNAI3 to the complex
CC (PubMed:20462955, PubMed:25187647). Interacts with ERRFI1; inhibits
CC dimerization of the kinase domain and autophosphorylation
CC (PubMed:18046415). Part of a complex with ERBB2 and either PIK3C2A or
CC PIK3C2B (PubMed:10805725). Interacts with GRB2; an adapter protein
CC coupling the receptor to downstream signaling pathways. Interacts with
CC GAB2; involved in signaling downstream of EGFR. Interacts with STAT3;
CC mediates EGFR downstream signaling in cell proliferation. Interacts
CC with RIPK1; involved in NF-kappa-B activation. Interacts
CC (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR
CC ubiquitination and regulation. Interacts with SOCS5; regulates EGFR
CC degradation through ELOC- and ELOB-mediated ubiquitination and
CC proteasomal degradation. Interacts with PRMT5; methylates EGFR and
CC enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6;
CC inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1;
CC essential for regulation of EGF-dependent nuclear transport of EGFR by
CC retrograde trafficking from the Golgi to the ER. Interacts with TNK2;
CC this interaction is dependent on EGF stimulation and kinase activity of
CC EGFR. Interacts with PCNA; positively regulates PCNA (PubMed:17115032).
CC Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1.
CC Interacts with FER. May interact with EPS8; mediates EPS8
CC phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2
CC (PubMed:10026169). Interacts with ATXN2. Interacts with GAREM1.
CC Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct
CC and may regulate EGFR internalization after EGF stimulation. Interacts
CC with GPER1; the interaction occurs in an estrogen-dependent manner.
CC Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via
CC zinc fingers). Interacts with RNF115 and RNF126 (PubMed:23418353).
CC Interacts with GPRC5A (via its transmembrane domain) (PubMed:25311788).
CC Interacts with FAM83B; positively regulates EGFR inducing its
CC autophosphorylation in absence of stimulation by EGF (PubMed:23912460).
CC Interacts with LAPTM4B; positively correlates with EGFR activation
CC (PubMed:28479384). Interacts with STX19 (PubMed:16420529). Interacts
CC with CD44 (PubMed:23589287). Interacts with PGRMC1; the interaction
CC requires PGRMC1 homodimerization (PubMed:26988023). Interacts with
CC PIKFYVE (PubMed:17909029). Interacts with NEU3. Interacts with TRAF4
CC (PubMed:30352854). {ECO:0000269|PubMed:10026169,
CC ECO:0000269|PubMed:10228163, ECO:0000269|PubMed:10805725,
CC ECO:0000269|PubMed:11116146, ECO:0000269|PubMed:11483589,
CC ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
CC ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:15282549,
CC ECO:0000269|PubMed:15374980, ECO:0000269|PubMed:15590694,
CC ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:16140940,
CC ECO:0000269|PubMed:16420529, ECO:0000269|PubMed:17115032,
CC ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:17334392,
CC ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:18046415,
CC ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:19172738,
CC ECO:0000269|PubMed:19509291, ECO:0000269|PubMed:19560417,
CC ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19749156,
CC ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:20462955,
CC ECO:0000269|PubMed:20471394, ECO:0000269|PubMed:20551055,
CC ECO:0000269|PubMed:20674546, ECO:0000269|PubMed:20837704,
CC ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21518868,
CC ECO:0000269|PubMed:22298428, ECO:0000269|PubMed:22888118,
CC ECO:0000269|PubMed:23418353, ECO:0000269|PubMed:23589287,
CC ECO:0000269|PubMed:23912460, ECO:0000269|PubMed:25187647,
CC ECO:0000269|PubMed:25311788, ECO:0000269|PubMed:26988023,
CC ECO:0000269|PubMed:28479384, ECO:0000269|PubMed:7657591,
CC ECO:0000269|PubMed:8650580, ECO:0000269|PubMed:9852145,
CC ECO:0000269|Ref.105}.
CC -!- INTERACTION:
CC P00533; P00519: ABL1; NbExp=3; IntAct=EBI-297353, EBI-375543;
CC P00533; P42684: ABL2; NbExp=9; IntAct=EBI-297353, EBI-1102694;
CC P00533; Q15109: AGER; NbExp=2; IntAct=EBI-297353, EBI-1646426;
CC P00533; Q9UKV8: AGO2; NbExp=11; IntAct=EBI-297353, EBI-528269;
CC P00533; Q09666: AHNAK; NbExp=4; IntAct=EBI-297353, EBI-2555881;
CC P00533; O00170: AIP; NbExp=2; IntAct=EBI-297353, EBI-704197;
CC P00533; Q02952: AKAP12; NbExp=3; IntAct=EBI-297353, EBI-2562430;
CC P00533; Q92625: ANKS1A; NbExp=6; IntAct=EBI-297353, EBI-1048612;
CC P00533; P04083: ANXA1; NbExp=3; IntAct=EBI-297353, EBI-354007;
CC P00533; Q96CW1: AP2M1; NbExp=5; IntAct=EBI-297353, EBI-297683;
CC P00533; O00213: APBB1; NbExp=4; IntAct=EBI-297353, EBI-81694;
CC P00533; Q92870: APBB2; NbExp=7; IntAct=EBI-297353, EBI-79277;
CC P00533; O95704: APBB3; NbExp=2; IntAct=EBI-297353, EBI-286427;
CC P00533; Q9UKG1: APPL1; NbExp=2; IntAct=EBI-297353, EBI-741243;
CC P00533; O14965: AURKA; NbExp=4; IntAct=EBI-297353, EBI-448680;
CC P00533; P30530: AXL; NbExp=4; IntAct=EBI-297353, EBI-2850927;
CC P00533; Q9UQB8: BAIAP2; NbExp=3; IntAct=EBI-297353, EBI-525456;
CC P00533; Q9BXH1: BBC3; NbExp=10; IntAct=EBI-297353, EBI-519884;
CC P00533; Q14457: BECN1; NbExp=7; IntAct=EBI-297353, EBI-949378;
CC P00533; P51451: BLK; NbExp=3; IntAct=EBI-297353, EBI-2105445;
CC P00533; P62158: CALM3; NbExp=4; IntAct=EBI-297353, EBI-397435;
CC P00533; P49069: CAMLG; NbExp=3; IntAct=EBI-297353, EBI-1748958;
CC P00533; Q03135: CAV1; NbExp=7; IntAct=EBI-297353, EBI-603614;
CC P00533; P51636: CAV2; NbExp=3; IntAct=EBI-297353, EBI-603607;
CC P00533; P22681: CBL; NbExp=22; IntAct=EBI-297353, EBI-518228;
CC P00533; Q16543: CDC37; NbExp=11; IntAct=EBI-297353, EBI-295634;
CC P00533; P12830: CDH1; NbExp=4; IntAct=EBI-297353, EBI-727477;
CC P00533; P06493: CDK1; NbExp=3; IntAct=EBI-297353, EBI-444308;
CC P00533; P23528: CFL1; NbExp=3; IntAct=EBI-297353, EBI-352733;
CC P00533; Q9BZP6: CHIA; NbExp=2; IntAct=EBI-297353, EBI-14357960;
CC P00533; Q9NSE2: CISH; NbExp=4; IntAct=EBI-297353, EBI-617866;
CC P00533; Q7Z7G1: CLNK; NbExp=2; IntAct=EBI-297353, EBI-7878194;
CC P00533; P46108: CRK; NbExp=4; IntAct=EBI-297353, EBI-886;
CC P00533; P46108-1: CRK; NbExp=3; IntAct=EBI-297353, EBI-287556;
CC P00533; P46109: CRKL; NbExp=4; IntAct=EBI-297353, EBI-910;
CC P00533; O60716: CTNND1; NbExp=5; IntAct=EBI-297353, EBI-701927;
CC P00533; Q14247: CTTN; NbExp=4; IntAct=EBI-297353, EBI-351886;
CC P00533; Q6PKX4: DOK6; NbExp=2; IntAct=EBI-297353, EBI-2880244;
CC P00533; P01133: EGF; NbExp=29; IntAct=EBI-297353, EBI-640857;
CC P00533; P00533: EGFR; NbExp=29; IntAct=EBI-297353, EBI-297353;
CC P00533; Q6UW88: EPGN; NbExp=3; IntAct=EBI-297353, EBI-15482510;
CC P00533; Q12929: EPS8; NbExp=3; IntAct=EBI-297353, EBI-375576;
CC P00533; P04626: ERBB2; NbExp=25; IntAct=EBI-297353, EBI-641062;
CC P00533; P21860: ERBB3; NbExp=13; IntAct=EBI-297353, EBI-720706;
CC P00533; Q15303: ERBB4; NbExp=2; IntAct=EBI-297353, EBI-80371;
CC P00533; P07992: ERCC1; NbExp=21; IntAct=EBI-297353, EBI-750962;
CC P00533; O14944: EREG; NbExp=3; IntAct=EBI-297353, EBI-17272224;
CC P00533; Q9UJM3: ERRFI1; NbExp=13; IntAct=EBI-297353, EBI-2941912;
CC P00533; P03372: ESR1; NbExp=2; IntAct=EBI-297353, EBI-78473;
CC P00533; P03372-4: ESR1; NbExp=4; IntAct=EBI-297353, EBI-4309277;
CC P00533; Q92731: ESR2; NbExp=8; IntAct=EBI-297353, EBI-78505;
CC P00533; Q96A65: EXOC4; NbExp=2; IntAct=EBI-297353, EBI-355383;
CC P00533; P09769: FGR; NbExp=3; IntAct=EBI-297353, EBI-1383732;
CC P00533; Q14318: FKBP8; NbExp=4; IntAct=EBI-297353, EBI-724839;
CC P00533; Q13480: GAB1; NbExp=4; IntAct=EBI-297353, EBI-517684;
CC P00533; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-297353, EBI-975200;
CC P00533; P60520: GABARAPL2; NbExp=3; IntAct=EBI-297353, EBI-720116;
CC P00533; P04406: GAPDH; NbExp=7; IntAct=EBI-297353, EBI-354056;
CC P00533; Q8NBJ4: GOLM1; NbExp=13; IntAct=EBI-297353, EBI-712073;
CC P00533; Q14956: GPNMB; NbExp=3; IntAct=EBI-297353, EBI-7250369;
CC P00533; Q14956-1: GPNMB; NbExp=2; IntAct=EBI-297353, EBI-16191078;
CC P00533; O75791: GRAP2; NbExp=3; IntAct=EBI-297353, EBI-740418;
CC P00533; Q13322: GRB10; NbExp=3; IntAct=EBI-297353, EBI-80275;
CC P00533; P62993: GRB2; NbExp=45; IntAct=EBI-297353, EBI-401755;
CC P00533; Q99075: HBEGF; NbExp=3; IntAct=EBI-297353, EBI-7211558;
CC P00533; P08631: HCK; NbExp=3; IntAct=EBI-297353, EBI-346340;
CC P00533; Q9UBN7: HDAC6; NbExp=12; IntAct=EBI-297353, EBI-301697;
CC P00533; Q8WUI4: HDAC7; NbExp=3; IntAct=EBI-297353, EBI-1048378;
CC P00533; P07900: HSP90AA1; NbExp=7; IntAct=EBI-297353, EBI-296047;
CC P00533; P08238: HSP90AB1; NbExp=10; IntAct=EBI-297353, EBI-352572;
CC P00533; Q6PK50: HSP90AB1; NbExp=2; IntAct=EBI-297353, EBI-9356629;
CC P00533; P08107: HSPA1B; NbExp=6; IntAct=EBI-297353, EBI-629985;
CC P00533; P34932: HSPA4; NbExp=3; IntAct=EBI-297353, EBI-356933;
CC P00533; P11142: HSPA8; NbExp=7; IntAct=EBI-297353, EBI-351896;
CC P00533; P38646: HSPA9; NbExp=5; IntAct=EBI-297353, EBI-354932;
CC P00533; P17936: IGFBP3; NbExp=3; IntAct=EBI-297353, EBI-715709;
CC P00533; P46940: IQGAP1; NbExp=4; IntAct=EBI-297353, EBI-297509;
CC P00533; O14654: IRS4; NbExp=2; IntAct=EBI-297353, EBI-356594;
CC P00533; Q86VI4: LAPTM4B; NbExp=10; IntAct=EBI-297353, EBI-3267258;
CC P00533; O43561: LAT; NbExp=3; IntAct=EBI-297353, EBI-1222766;
CC P00533; Q13094: LCP2; NbExp=3; IntAct=EBI-297353, EBI-346946;
CC P00533; Q96FE5: LINGO1; NbExp=2; IntAct=EBI-297353, EBI-719955;
CC P00533; Q96JA1: LRIG1; NbExp=6; IntAct=EBI-297353, EBI-2865191;
CC P00533; O94898: LRIG2; NbExp=4; IntAct=EBI-297353, EBI-2830372;
CC P00533; Q38SD2: LRRK1; NbExp=2; IntAct=EBI-297353, EBI-1050422;
CC P00533; P07948: LYN; NbExp=7; IntAct=EBI-297353, EBI-79452;
CC P00533; P07948-1: LYN; NbExp=2; IntAct=EBI-297353, EBI-6895930;
CC P00533; Q12852: MAP3K12; NbExp=3; IntAct=EBI-297353, EBI-710223;
CC P00533; Q9UQF2: MAPK8IP1; NbExp=3; IntAct=EBI-297353, EBI-78404;
CC P00533; Q13387: MAPK8IP2; NbExp=5; IntAct=EBI-297353, EBI-722813;
CC P00533; Q9Y2H9: MAST1; NbExp=3; IntAct=EBI-297353, EBI-3385920;
CC P00533; P08581: MET; NbExp=8; IntAct=EBI-297353, EBI-1039152;
CC P00533; P14174: MIF; NbExp=3; IntAct=EBI-297353, EBI-372712;
CC P00533; P15941: MUC1; NbExp=4; IntAct=EBI-297353, EBI-2804728;
CC P00533; P16333: NCK1; NbExp=4; IntAct=EBI-297353, EBI-389883;
CC P00533; P46934: NEDD4; NbExp=3; IntAct=EBI-297353, EBI-726944;
CC P00533; P04150: NR3C1; NbExp=3; IntAct=EBI-297353, EBI-493507;
CC P00533; P16234: PDGFRA; NbExp=4; IntAct=EBI-297353, EBI-2861522;
CC P00533; O00750: PIK3C2B; NbExp=10; IntAct=EBI-297353, EBI-641107;
CC P00533; P27986: PIK3R1; NbExp=5; IntAct=EBI-297353, EBI-79464;
CC P00533; O00459: PIK3R2; NbExp=4; IntAct=EBI-297353, EBI-346930;
CC P00533; Q92569: PIK3R3; NbExp=7; IntAct=EBI-297353, EBI-79893;
CC P00533; P19174: PLCG1; NbExp=6; IntAct=EBI-297353, EBI-79387;
CC P00533; P16885: PLCG2; NbExp=6; IntAct=EBI-297353, EBI-617403;
CC P00533; P35813: PPM1A; NbExp=2; IntAct=EBI-297353, EBI-989143;
CC P00533; P17252: PRKCA; NbExp=3; IntAct=EBI-297353, EBI-1383528;
CC P00533; Q05397: PTK2; NbExp=7; IntAct=EBI-297353, EBI-702142;
CC P00533; P18031: PTPN1; NbExp=8; IntAct=EBI-297353, EBI-968788;
CC P00533; Q06124: PTPN11; NbExp=4; IntAct=EBI-297353, EBI-297779;
CC P00533; Q05209: PTPN12; NbExp=5; IntAct=EBI-297353, EBI-2266035;
CC P00533; Q9Y2R2: PTPN22; NbExp=3; IntAct=EBI-297353, EBI-1211241;
CC P00533; P18433: PTPRA; NbExp=3; IntAct=EBI-297353, EBI-2609645;
CC P00533; P23467: PTPRB; NbExp=3; IntAct=EBI-297353, EBI-1265766;
CC P00533; P08575: PTPRC; NbExp=2; IntAct=EBI-297353, EBI-1341;
CC P00533; P23470: PTPRG; NbExp=3; IntAct=EBI-297353, EBI-2258115;
CC P00533; Q9HD43: PTPRH; NbExp=3; IntAct=EBI-297353, EBI-1267176;
CC P00533; Q9UJ41: RABGEF1; NbExp=4; IntAct=EBI-297353, EBI-913954;
CC P00533; Q70E73: RAPH1; NbExp=2; IntAct=EBI-297353, EBI-3940924;
CC P00533; P20936: RASA1; NbExp=7; IntAct=EBI-297353, EBI-1026476;
CC P00533; Q13671: RIN1; NbExp=3; IntAct=EBI-297353, EBI-366017;
CC P00533; Q01973: ROR1; NbExp=8; IntAct=EBI-297353, EBI-6082337;
CC P00533; Q92622: RUBCN; NbExp=3; IntAct=EBI-297353, EBI-2952709;
CC P00533; P26447: S100A4; NbExp=6; IntAct=EBI-297353, EBI-717058;
CC P00533; P31947: SFN; NbExp=9; IntAct=EBI-297353, EBI-476295;
CC P00533; Q9NRF2: SH2B1; NbExp=4; IntAct=EBI-297353, EBI-310491;
CC P00533; Q9UQQ2: SH2B3; NbExp=2; IntAct=EBI-297353, EBI-7879749;
CC P00533; Q9BRG2: SH2D3A; NbExp=3; IntAct=EBI-297353, EBI-2339271;
CC P00533; P29353: SHC1; NbExp=34; IntAct=EBI-297353, EBI-78835;
CC P00533; P29353-7: SHC1; NbExp=4; IntAct=EBI-297353, EBI-9691288;
CC P00533; P98077: SHC2; NbExp=3; IntAct=EBI-297353, EBI-7256023;
CC P00533; Q6S5L8: SHC4; NbExp=3; IntAct=EBI-297353, EBI-9453524;
CC P00533; Q13239: SLA; NbExp=3; IntAct=EBI-297353, EBI-726214;
CC P00533; P13866: SLC5A1; NbExp=3; IntAct=EBI-297353, EBI-1772443;
CC P00533; Q07889: SOS1; NbExp=2; IntAct=EBI-297353, EBI-297487;
CC P00533; P12931: SRC; NbExp=9; IntAct=EBI-297353, EBI-621482;
CC P00533; P42224: STAT1; NbExp=7; IntAct=EBI-297353, EBI-1057697;
CC P00533; P40763: STAT3; NbExp=15; IntAct=EBI-297353, EBI-518675;
CC P00533; P42229: STAT5A; NbExp=4; IntAct=EBI-297353, EBI-749537;
CC P00533; P31948: STIP1; NbExp=3; IntAct=EBI-297353, EBI-1054052;
CC P00533; Q9UNE7: STUB1; NbExp=4; IntAct=EBI-297353, EBI-357085;
CC P00533; O43752: STX6; NbExp=3; IntAct=EBI-297353, EBI-2695795;
CC P00533; P43405: SYK; NbExp=6; IntAct=EBI-297353, EBI-78302;
CC P00533; P01135: TGFA; NbExp=4; IntAct=EBI-297353, EBI-1034374;
CC P00533; Q9Y490: TLN1; NbExp=2; IntAct=EBI-297353, EBI-2462036;
CC P00533; O60603: TLR2; NbExp=3; IntAct=EBI-297353, EBI-973722;
CC P00533; Q9Y6Q6-2: TNFRSF11A; NbExp=3; IntAct=EBI-297353, EBI-20899422;
CC P00533; Q68CZ2: TNS3; NbExp=5; IntAct=EBI-297353, EBI-1220488;
CC P00533; O75674: TOM1L1; NbExp=6; IntAct=EBI-297353, EBI-712991;
CC P00533; Q12933: TRAF2; NbExp=4; IntAct=EBI-297353, EBI-355744;
CC P00533; Q71U36: TUBA1A; NbExp=4; IntAct=EBI-297353, EBI-302552;
CC P00533; P10599: TXN; NbExp=5; IntAct=EBI-297353, EBI-594644;
CC P00533; P09936: UCHL1; NbExp=3; IntAct=EBI-297353, EBI-714860;
CC P00533; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-297353, EBI-1059156;
CC P00533; P07947: YES1; NbExp=3; IntAct=EBI-297353, EBI-515331;
CC P00533; P27348: YWHAQ; NbExp=7; IntAct=EBI-297353, EBI-359854;
CC P00533; P63104: YWHAZ; NbExp=6; IntAct=EBI-297353, EBI-347088;
CC P00533; P43403: ZAP70; NbExp=3; IntAct=EBI-297353, EBI-1211276;
CC P00533; Q53FC7; NbExp=3; IntAct=EBI-297353, EBI-9356749;
CC P00533; Q96BE0; NbExp=2; IntAct=EBI-297353, EBI-9356686;
CC P00533; P62161: Calm3; Xeno; NbExp=6; IntAct=EBI-297353, EBI-397530;
CC P00533; P22682: Cbl; Xeno; NbExp=2; IntAct=EBI-297353, EBI-640919;
CC P00533; Q9QZC5: Grb7; Xeno; NbExp=7; IntAct=EBI-297353, EBI-22085551;
CC P00533; P97313: Prkdc; Xeno; NbExp=4; IntAct=EBI-297353, EBI-2272005;
CC P00533; P20417: Ptpn1; Xeno; NbExp=11; IntAct=EBI-297353, EBI-916819;
CC P00533; Q80U62: Rubcn; Xeno; NbExp=2; IntAct=EBI-297353, EBI-3506572;
CC P00533; P0DTC2: S; Xeno; NbExp=4; IntAct=EBI-297353, EBI-25474821;
CC P00533; Q8K424: Trpv3; Xeno; NbExp=2; IntAct=EBI-297353, EBI-2650739;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17182860,
CC ECO:0000269|PubMed:20462955, ECO:0000269|PubMed:23589287,
CC ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:2790960}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:27153536}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:27153536}; Single-pass type I
CC membrane protein. Golgi apparatus membrane; Single-pass type I membrane
CC protein. Nucleus membrane; Single-pass type I membrane protein.
CC Endosome {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:27153536}.
CC Endosome membrane. Nucleus {ECO:0000269|PubMed:17115032,
CC ECO:0000269|PubMed:17909029, ECO:0000269|PubMed:20551055,
CC ECO:0000269|PubMed:20674546}. Note=In response to EGF, translocated
CC from the cell membrane to the nucleus via Golgi and ER
CC (PubMed:20674546, PubMed:17909029). Endocytosed upon activation by
CC ligand (PubMed:2790960, PubMed:17182860, PubMed:27153536,
CC PubMed:17909029). Colocalized with GPER1 in the nucleus of estrogen
CC agonist-induced cancer-associated fibroblasts (CAF) (PubMed:20551055).
CC {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:17909029,
CC ECO:0000269|PubMed:20674546, ECO:0000269|PubMed:27153536,
CC ECO:0000269|PubMed:2790960}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=p170;
CC IsoId=P00533-1; Sequence=Displayed;
CC Name=2; Synonyms=p60, Truncated, TEGFR;
CC IsoId=P00533-2; Sequence=VSP_002887, VSP_002888;
CC Name=3; Synonyms=p110;
CC IsoId=P00533-3; Sequence=VSP_002889, VSP_002890;
CC Name=4;
CC IsoId=P00533-4; Sequence=VSP_002891, VSP_002892;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is also expressed
CC in ovarian cancers. {ECO:0000269|PubMed:17671655}.
CC -!- PTM: Phosphorylated on Tyr residues in response to EGF
CC (PubMed:20462955, PubMed:27153536). Phosphorylation at Ser-695 is
CC partial and occurs only if Thr-693 is phosphorylated. Phosphorylation
CC at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1
CC activation. Dephosphorylation by PTPRJ prevents endocytosis and
CC stabilizes the receptor at the plasma membrane. Autophosphorylation at
CC Tyr-1197 is stimulated by methylation at Arg-1199 and enhances
CC interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110
CC recruits STAT3. Dephosphorylated by PTPN1 and PTPN2.
CC {ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:12873986,
CC ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19563760,
CC ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:20462955,
CC ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:2543678,
CC ECO:0000269|PubMed:27153536, ECO:0000269|PubMed:3138233}.
CC -!- PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation;
CC which does not affect tyrosine kinase activity or signaling capacity
CC but may play a role in lysosomal targeting (PubMed:27153536).
CC Polyubiquitin linkage is mainly through 'Lys-63', but linkage through
CC 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B
CC prevents degradation. Ubiquitinated by RNF115 and RNF126 (By
CC similarity). {ECO:0000250|UniProtKB:Q01279,
CC ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:22179831,
CC ECO:0000269|PubMed:22298428, ECO:0000269|PubMed:27153536}.
CC -!- PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits
CC internalization after ligand binding, and increases the persistence of
CC tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation
CC increases the amplitude and duration of EGFR signaling.
CC {ECO:0000269|PubMed:27153536}.
CC -!- PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates
CC phosphorylation at Tyr-1197. {ECO:0000269|PubMed:19563760,
CC ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:21258366}.
CC -!- DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy affecting
CC tissues of the lung. The most common form of lung cancer is non-small
CC cell lung cancer (NSCLC) that can be divided into 3 major histologic
CC subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung
CC cancer. NSCLC is often diagnosed at an advanced stage and has a poor
CC prognosis. {ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793,
CC ECO:0000269|PubMed:16672372}. Note=The gene represented in this entry
CC is involved in disease pathogenesis.
CC -!- DISEASE: Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)
CC [MIM:616069]: A disorder characterized by inflammatory features with
CC neonatal onset, involving the skin, hair, and gut. The skin lesions
CC involve perioral and perianal erythema, psoriasiform erythroderma, with
CC flares of erythema, scaling, and widespread pustules. Gastrointestinal
CC symptoms include malabsorptive diarrhea that is exacerbated by
CC intercurrent gastrointestinal infections. The hair is short or broken,
CC and the eyelashes and eyebrows are wiry and disorganized.
CC {ECO:0000269|PubMed:24691054}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/egfr/";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=EGFR entry;
CC URL="https://en.wikipedia.org/wiki/Epidermal_growth_factor_receptor";
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DR EMBL; X00588; CAA25240.1; -; mRNA.
DR EMBL; U95089; AAB53063.1; -; mRNA.
DR EMBL; U48722; AAC50802.1; -; mRNA.
DR EMBL; U48723; AAC50804.1; -; Genomic_DNA.
DR EMBL; U48724; AAC50796.1; -; Genomic_DNA.
DR EMBL; U48725; AAC50797.1; -; Genomic_DNA.
DR EMBL; U48726; AAC50798.1; -; Genomic_DNA.
DR EMBL; U48727; AAC50799.1; -; Genomic_DNA.
DR EMBL; U48728; AAC50800.1; -; Genomic_DNA.
DR EMBL; U48729; AAC50801.1; -; Genomic_DNA.
DR EMBL; AF288738; AAG35786.1; -; Genomic_DNA.
DR EMBL; AF288738; AAG35787.1; -; Genomic_DNA.
DR EMBL; AF288738; AAG35788.1; -; Genomic_DNA.
DR EMBL; AF288738; AAG35789.1; -; Genomic_DNA.
DR EMBL; AF288738; AAG35790.1; -; Genomic_DNA.
DR EMBL; AY698024; AAT97979.1; -; mRNA.
DR EMBL; AY588246; AAS83109.1; -; Genomic_DNA.
DR EMBL; AF277897; AAK01080.1; -; mRNA.
DR EMBL; AF125253; AAG43240.1; -; mRNA.
DR EMBL; AF125539; AAG43243.1; -; Genomic_DNA.
DR EMBL; AF125538; AAG43243.1; JOINED; Genomic_DNA.
DR EMBL; X06370; CAA29668.1; -; Genomic_DNA.
DR EMBL; X00663; CAA25282.1; -; mRNA.
DR EMBL; M38425; AAA63171.1; -; Genomic_DNA.
DR EMBL; M11234; AAA52370.1; -; Genomic_DNA.
DR CCDS; CCDS47587.1; -. [P00533-2]
DR CCDS; CCDS5514.1; -. [P00533-1]
DR CCDS; CCDS5515.1; -. [P00533-3]
DR CCDS; CCDS5516.1; -. [P00533-4]
DR PIR; A00641; GQHUE.
DR RefSeq; NP_005219.2; NM_005228.4. [P00533-1]
DR RefSeq; NP_958439.1; NM_201282.1. [P00533-4]
DR RefSeq; NP_958440.1; NM_201283.1. [P00533-2]
DR RefSeq; NP_958441.1; NM_201284.1. [P00533-3]
DR PDB; 1IVO; X-ray; 3.30 A; A/B=25-646.
DR PDB; 1M14; X-ray; 2.60 A; A=695-1022.
DR PDB; 1M17; X-ray; 2.60 A; A=695-1022.
DR PDB; 1MOX; X-ray; 2.50 A; A/B=25-525.
DR PDB; 1NQL; X-ray; 2.80 A; A=25-642.
DR PDB; 1XKK; X-ray; 2.40 A; A=695-1022.
DR PDB; 1YY9; X-ray; 2.60 A; A=25-642.
DR PDB; 1Z9I; NMR; -; A=669-721.
DR PDB; 2EB2; X-ray; 2.50 A; A=695-1022.
DR PDB; 2EB3; X-ray; 2.84 A; A=695-1022.
DR PDB; 2GS2; X-ray; 2.80 A; A=696-1022.
DR PDB; 2GS6; X-ray; 2.60 A; A=696-1022.
DR PDB; 2GS7; X-ray; 2.60 A; A/B=696-1022.
DR PDB; 2ITN; X-ray; 2.47 A; A=696-1022.
DR PDB; 2ITO; X-ray; 3.25 A; A=696-1022.
DR PDB; 2ITP; X-ray; 2.74 A; A=696-1022.
DR PDB; 2ITQ; X-ray; 2.68 A; A=696-1022.
DR PDB; 2ITT; X-ray; 2.73 A; A=696-1022.
DR PDB; 2ITU; X-ray; 2.80 A; A=696-1022.
DR PDB; 2ITV; X-ray; 2.47 A; A=696-1022.
DR PDB; 2ITW; X-ray; 2.88 A; A=696-1022.
DR PDB; 2ITX; X-ray; 2.98 A; A=696-1022.
DR PDB; 2ITY; X-ray; 3.42 A; A=696-1022.
DR PDB; 2ITZ; X-ray; 2.72 A; A=696-1022.
DR PDB; 2J5E; X-ray; 3.10 A; A=696-1022.
DR PDB; 2J5F; X-ray; 3.00 A; A=696-1022.
DR PDB; 2J6M; X-ray; 3.10 A; A=696-1022.
DR PDB; 2JIT; X-ray; 3.10 A; A/B=696-1022.
DR PDB; 2JIU; X-ray; 3.05 A; A/B=695-1022.
DR PDB; 2JIV; X-ray; 3.50 A; A/B=695-1022.
DR PDB; 2KS1; NMR; -; B=634-677.
DR PDB; 2M0B; NMR; -; A/B=634-677.
DR PDB; 2M20; NMR; -; A/B=642-697.
DR PDB; 2N5S; NMR; -; A=642-690.
DR PDB; 2RF9; X-ray; 3.50 A; A/B=696-1022.
DR PDB; 2RFD; X-ray; 3.60 A; A/B=702-1022.
DR PDB; 2RFE; X-ray; 2.90 A; A/B/C/D=702-1022.
DR PDB; 2RGP; X-ray; 2.00 A; A=702-1016.
DR PDB; 3B2U; X-ray; 2.58 A; A/B/E/I/M/P/S/V=335-538.
DR PDB; 3B2V; X-ray; 3.30 A; A=25-642.
DR PDB; 3BEL; X-ray; 2.30 A; A=702-1016.
DR PDB; 3BUO; X-ray; 2.60 A; A/C=1063-1075.
DR PDB; 3C09; X-ray; 3.20 A; A/D=336-538.
DR PDB; 3G5V; X-ray; 2.00 A; C=311-326.
DR PDB; 3G5Y; X-ray; 1.59 A; E=311-326.
DR PDB; 3GOP; X-ray; 2.80 A; A=669-1022.
DR PDB; 3GT8; X-ray; 2.96 A; A/B/C/D=696-1022.
DR PDB; 3IKA; X-ray; 2.90 A; A/B=694-1022.
DR PDB; 3LZB; X-ray; 2.70 A; A/B/C/D/E/F/G/H=696-983.
DR PDB; 3NJP; X-ray; 3.30 A; A/B=25-638.
DR PDB; 3OB2; X-ray; 2.10 A; A=1063-1074.
DR PDB; 3OP0; X-ray; 2.52 A; C/D=1066-1076.
DR PDB; 3P0Y; X-ray; 1.80 A; A=334-538.
DR PDB; 3PFV; X-ray; 2.27 A; C/D=1066-1076.
DR PDB; 3POZ; X-ray; 1.50 A; A=696-1022.
DR PDB; 3QWQ; X-ray; 2.75 A; A=1-642.
DR PDB; 3UG1; X-ray; 2.75 A; A=695-1022.
DR PDB; 3UG2; X-ray; 2.50 A; A=695-1022.
DR PDB; 3VJN; X-ray; 2.34 A; A=695-1022.
DR PDB; 3VJO; X-ray; 2.64 A; A=695-1022.
DR PDB; 3VRP; X-ray; 1.52 A; B=1062-1074.
DR PDB; 3VRR; X-ray; 2.00 A; C=1062-1074.
DR PDB; 3W2O; X-ray; 2.35 A; A=698-1022.
DR PDB; 3W2P; X-ray; 2.05 A; A=698-1022.
DR PDB; 3W2Q; X-ray; 2.20 A; A=698-1022.
DR PDB; 3W2R; X-ray; 2.05 A; A=698-1022.
DR PDB; 3W2S; X-ray; 1.90 A; A=696-1022.
DR PDB; 3W32; X-ray; 1.80 A; A=696-1022.
DR PDB; 3W33; X-ray; 1.70 A; A=696-1022.
DR PDB; 4G5J; X-ray; 2.80 A; A=696-1022.
DR PDB; 4G5P; X-ray; 3.17 A; A/B=696-1022.
DR PDB; 4HJO; X-ray; 2.75 A; A=696-1022.
DR PDB; 4I1Z; X-ray; 3.00 A; A=695-1022.
DR PDB; 4I20; X-ray; 3.34 A; A=695-1022.
DR PDB; 4I21; X-ray; 3.37 A; A/B=695-1022.
DR PDB; 4I22; X-ray; 1.71 A; A=695-1022.
DR PDB; 4I23; X-ray; 2.80 A; A=695-1022.
DR PDB; 4I24; X-ray; 1.80 A; A/B=695-1022.
DR PDB; 4JQ7; X-ray; 2.73 A; A=696-1021.
DR PDB; 4JQ8; X-ray; 2.83 A; A=696-1021.
DR PDB; 4JR3; X-ray; 2.70 A; A=696-1021.
DR PDB; 4JRV; X-ray; 2.80 A; A=696-1021.
DR PDB; 4KRL; X-ray; 2.85 A; A=335-538.
DR PDB; 4KRM; X-ray; 2.66 A; A/C/E/G/I/K=335-538.
DR PDB; 4KRO; X-ray; 3.05 A; A=25-642.
DR PDB; 4KRP; X-ray; 2.82 A; A=25-642.
DR PDB; 4LI5; X-ray; 2.64 A; A=696-1020.
DR PDB; 4LL0; X-ray; 4.00 A; A/B=694-1022.
DR PDB; 4LQM; X-ray; 2.50 A; A=694-1022.
DR PDB; 4LRM; X-ray; 3.53 A; A/B/C/D/E=694-1022.
DR PDB; 4R3P; X-ray; 2.90 A; A=696-1018.
DR PDB; 4R3R; X-ray; 3.25 A; A=696-1018.
DR PDB; 4R5S; X-ray; 3.00 A; A=696-1022.
DR PDB; 4RIW; X-ray; 3.10 A; B/D=682-1022.
DR PDB; 4RIX; X-ray; 3.10 A; B/D=682-1022.
DR PDB; 4RIY; X-ray; 2.98 A; B/D=682-1022.
DR PDB; 4RJ4; X-ray; 2.78 A; A=695-1022.
DR PDB; 4RJ5; X-ray; 3.10 A; A=695-1022.
DR PDB; 4RJ6; X-ray; 2.70 A; A=695-1022.
DR PDB; 4RJ7; X-ray; 2.55 A; A=695-1022.
DR PDB; 4RJ8; X-ray; 2.50 A; A=695-1022.
DR PDB; 4TKS; X-ray; 3.20 A; A=695-1022.
DR PDB; 4UIP; X-ray; 2.95 A; A=26-637.
DR PDB; 4UV7; X-ray; 2.10 A; A=25-645.
DR PDB; 4WD5; X-ray; 3.30 A; A/B=694-1022.
DR PDB; 4WKQ; X-ray; 1.85 A; A=696-1022.
DR PDB; 4WRG; X-ray; 1.90 A; A=696-1022.
DR PDB; 4ZAU; X-ray; 2.80 A; A=696-1022.
DR PDB; 4ZJV; X-ray; 2.70 A; A/B=695-1022.
DR PDB; 4ZSE; X-ray; 1.97 A; A/B/C/D=695-1022.
DR PDB; 5C8K; X-ray; 3.00 A; A=695-1022.
DR PDB; 5C8M; X-ray; 2.90 A; A=695-1022.
DR PDB; 5C8N; X-ray; 2.40 A; A=695-1022.
DR PDB; 5CAL; X-ray; 2.70 A; A=695-1022.
DR PDB; 5CAN; X-ray; 2.80 A; A=695-1022.
DR PDB; 5CAO; X-ray; 2.60 A; A=695-1022.
DR PDB; 5CAP; X-ray; 2.40 A; A=695-1022.
DR PDB; 5CAQ; X-ray; 2.50 A; A=695-1022.
DR PDB; 5CAS; X-ray; 2.10 A; A=695-1022.
DR PDB; 5CAU; X-ray; 2.25 A; A=695-1022.
DR PDB; 5CAV; X-ray; 2.73 A; A=695-1022.
DR PDB; 5CNN; X-ray; 1.90 A; A/B=696-1042.
DR PDB; 5CNO; X-ray; 1.55 A; A/B/X=696-1022.
DR PDB; 5CZH; X-ray; 2.80 A; A=694-1022.
DR PDB; 5CZI; X-ray; 2.60 A; A=694-1022.
DR PDB; 5D41; X-ray; 2.31 A; A/B=695-1022.
DR PDB; 5EDP; X-ray; 2.90 A; A=695-1022.
DR PDB; 5EDQ; X-ray; 2.80 A; A=695-1022.
DR PDB; 5EDR; X-ray; 2.60 A; A=695-1022.
DR PDB; 5EM5; X-ray; 2.65 A; A=695-1022.
DR PDB; 5EM6; X-ray; 2.78 A; A=695-1022.
DR PDB; 5EM7; X-ray; 2.81 A; A=695-1022.
DR PDB; 5EM8; X-ray; 2.80 A; A=695-1022.
DR PDB; 5FED; X-ray; 2.65 A; A=696-1022.
DR PDB; 5FEE; X-ray; 2.70 A; A=696-1022.
DR PDB; 5FEQ; X-ray; 3.40 A; A=696-1022.
DR PDB; 5GMP; X-ray; 2.80 A; A=696-1022.
DR PDB; 5GNK; X-ray; 1.80 A; A=696-988.
DR PDB; 5GTY; X-ray; 3.14 A; A/B/C/D/E/F/G/H=696-1022.
DR PDB; 5GTZ; X-ray; 3.00 A; A=696-1022.
DR PDB; 5HCX; X-ray; 2.60 A; A=696-1022.
DR PDB; 5HCY; X-ray; 2.46 A; A=696-1022.
DR PDB; 5HCZ; X-ray; 2.62 A; A=696-1022.
DR PDB; 5HG5; X-ray; 1.52 A; A=695-1022.
DR PDB; 5HG7; X-ray; 1.85 A; A=695-1022.
DR PDB; 5HG8; X-ray; 1.42 A; A=695-1022.
DR PDB; 5HG9; X-ray; 2.15 A; A=695-1022.
DR PDB; 5HIB; X-ray; 2.85 A; A=695-1022.
DR PDB; 5HIC; X-ray; 2.60 A; A=695-1022.
DR PDB; 5J9Y; X-ray; 2.80 A; A=697-1019.
DR PDB; 5J9Z; X-ray; 2.50 A; A=696-1020.
DR PDB; 5JEB; X-ray; 3.30 A; A=696-1022.
DR PDB; 5LV6; NMR; -; A/B=634-677.
DR PDB; 5SX4; X-ray; 2.80 A; M/N=335-525.
DR PDB; 5SX5; X-ray; 2.50 A; M/N=335-525.
DR PDB; 5U8L; X-ray; 1.60 A; A=695-1022.
DR PDB; 5UG8; X-ray; 1.46 A; A=695-1022.
DR PDB; 5UG9; X-ray; 1.33 A; A=695-1022.
DR PDB; 5UGA; X-ray; 1.82 A; A=695-1022.
DR PDB; 5UGB; X-ray; 2.53 A; A=695-1022.
DR PDB; 5UGC; X-ray; 1.58 A; A=695-1022.
DR PDB; 5UWD; X-ray; 3.06 A; A=695-1022.
DR PDB; 5WB7; X-ray; 2.94 A; A/B/C/D=25-525.
DR PDB; 5WB8; X-ray; 3.00 A; A/D=25-525.
DR PDB; 5X26; X-ray; 2.95 A; A=696-1022.
DR PDB; 5X27; X-ray; 2.95 A; A=696-1022.
DR PDB; 5X28; X-ray; 2.95 A; A=696-1022.
DR PDB; 5X2A; X-ray; 1.85 A; A/B/C/D=696-1022.
DR PDB; 5X2C; X-ray; 2.05 A; A/B=696-1022.
DR PDB; 5X2F; X-ray; 2.20 A; A/B/C/D=696-1022.
DR PDB; 5X2K; X-ray; 3.20 A; A=696-1022.
DR PDB; 5XDK; X-ray; 2.35 A; A=696-1022.
DR PDB; 5XDL; X-ray; 2.70 A; A=696-1022.
DR PDB; 5XGM; X-ray; 2.95 A; A=696-1022.
DR PDB; 5XGN; X-ray; 3.00 A; A/B=696-1022.
DR PDB; 5XWD; X-ray; 2.89 A; A=1-643.
DR PDB; 5Y25; X-ray; 3.10 A; A=698-1022.
DR PDB; 5Y9T; X-ray; 3.25 A; A=695-1022.
DR PDB; 5YU9; X-ray; 1.95 A; A/B/C/D=696-1022.
DR PDB; 5ZTO; X-ray; 2.65 A; A=696-1022.
DR PDB; 5ZWJ; X-ray; 2.90 A; A=675-1022.
DR PDB; 6ARU; X-ray; 3.20 A; A=25-640.
DR PDB; 6B3S; X-ray; 2.80 A; A/B/E/I=335-538.
DR PDB; 6D8E; X-ray; 2.54 A; A=696-1022.
DR PDB; 6DUK; X-ray; 2.20 A; A/B/C/D/E/F=695-1022.
DR PDB; 6JRJ; X-ray; 2.94 A; A=696-1022.
DR PDB; 6JRK; X-ray; 2.80 A; A=696-1022.
DR PDB; 6JRX; X-ray; 2.20 A; A=696-1022.
DR PDB; 6JWL; X-ray; 2.55 A; A=696-1022.
DR PDB; 6JX0; X-ray; 2.53 A; A=696-1022.
DR PDB; 6JX4; X-ray; 2.53 A; A=696-1022.
DR PDB; 6JXT; X-ray; 2.31 A; A=696-1022.
DR PDB; 6JZ0; X-ray; 2.86 A; A=696-1021.
DR PDB; 6LUB; X-ray; 2.31 A; A=695-1022.
DR PDB; 6LUD; X-ray; 2.05 A; A=695-1022.
DR PDB; 6P1D; X-ray; 2.40 A; A/B/C/D=696-1022.
DR PDB; 6P1L; X-ray; 2.80 A; A/B/C/D=696-1022.
DR PDB; 6P8Q; X-ray; 1.90 A; A/B/C/D=696-1022.
DR PDB; 6S89; X-ray; 2.70 A; A=695-1022.
DR PDB; 6S8A; X-ray; 2.60 A; A=695-1022.
DR PDB; 6S9B; X-ray; 3.25 A; A=697-1022.
DR PDB; 6S9C; X-ray; 2.73 A; A=696-1022.
DR PDB; 6S9D; X-ray; 2.67 A; A=696-1022.
DR PDB; 6TFU; X-ray; 2.00 A; A/B=695-1022.
DR PDB; 6TFV; X-ray; 1.50 A; A/B=695-1022.
DR PDB; 6TFW; X-ray; 2.00 A; A/B=695-1022.
DR PDB; 6TFY; X-ray; 1.70 A; A/B=695-1022.
DR PDB; 6TFZ; X-ray; 1.80 A; A/B=695-1022.
DR PDB; 6TG0; X-ray; 1.50 A; A/B=695-1022.
DR PDB; 6TG1; X-ray; 1.60 A; A/B=695-1022.
DR PDB; 6V5N; X-ray; 2.40 A; A/B/C/D=695-1022.
DR PDB; 6V5P; X-ray; 2.30 A; A/B/C/D=695-1022.
DR PDB; 6V66; X-ray; 1.79 A; A/B/C/D=696-1022.
DR PDB; 6V6K; X-ray; 2.20 A; A/B/C/D/E/F/G/H=696-1022.
DR PDB; 6V6O; X-ray; 2.10 A; A/B/C/D/E/F/G/H=696-1022.
DR PDB; 6VH4; X-ray; 2.80 A; A=696-1022.
DR PDB; 6VHN; X-ray; 2.40 A; A=696-1022.
DR PDB; 6VHP; X-ray; 3.60 A; A=696-1022.
DR PDB; 6WA2; X-ray; 2.40 A; A/B/C/D=695-1022.
DR PDB; 6WAK; X-ray; 2.40 A; A/B/C/D=695-1022.
DR PDB; 6WXN; X-ray; 1.76 A; A/B/C/D=695-1022.
DR PDB; 6XL4; X-ray; 2.06 A; A/B/C/D=695-1022.
DR PDB; 6Z4B; X-ray; 2.50 A; A/B=695-1022.
DR PDB; 6Z4D; X-ray; 2.00 A; A/B=695-1022.
DR PDB; 7A2A; X-ray; 1.90 A; A/B=695-1022.
DR PDB; 7A6I; X-ray; 2.40 A; A=695-1022.
DR PDB; 7A6J; X-ray; 2.00 A; A/B=695-1022.
DR PDB; 7A6K; X-ray; 2.00 A; A/B/C/D=695-1022.
DR PDB; 7AEI; X-ray; 2.65 A; A=695-1022.
DR PDB; 7AEM; X-ray; 2.65 A; A=695-1022.
DR PDB; 7B85; X-ray; 2.50 A; A=695-1022.
DR PDB; 7JXI; X-ray; 3.00 A; A/B/C/D=695-1022.
DR PDB; 7JXK; X-ray; 3.10 A; A/B/C/D/E/F=695-1022.
DR PDB; 7JXL; X-ray; 2.40 A; A/B/C/D=695-1022.
DR PDB; 7JXM; X-ray; 2.19 A; A/B/C/D=695-1022.
DR PDB; 7JXP; X-ray; 2.16 A; A/B/C/D/E/F=695-1022.
DR PDB; 7JXQ; X-ray; 1.83 A; A/B/C/D=695-1022.
DR PDB; 7JXW; X-ray; 2.50 A; A/B/C/D=695-1022.
DR PDB; 7K1H; X-ray; 2.60 A; A/B/C/D/E/F=695-1022.
DR PDB; 7K1I; X-ray; 3.20 A; A=695-1022.
DR PDB; 7KXZ; X-ray; 2.40 A; A=695-1022.
DR PDB; 7KY0; X-ray; 3.10 A; A/B/C/D=695-1022.
DR PDB; 7LEN; X-ray; 2.90 A; A/B=25-525.
DR PDB; 7LFR; X-ray; 3.20 A; A/B=25-525.
DR PDB; 7LFS; X-ray; 3.50 A; A/B/C/D=25-525.
DR PDB; 7LG8; X-ray; 2.93 A; A/B/C/D=695-1022.
DR PDB; 7LGS; X-ray; 3.10 A; A/B/C/D=696-1022.
DR PDB; 7LTX; X-ray; 2.30 A; A/B/C/D=695-1022.
DR PDB; 7OM4; X-ray; 6.05 A; A=25-645.
DR PDB; 7OXB; X-ray; 2.56 A; A=696-1020.
DR PDB; 7SYD; EM; 3.10 A; A/B=1-1210.
DR PDB; 7SYE; EM; 3.30 A; A/B=1-1210.
DR PDB; 7SZ0; EM; 3.30 A; A/B=1-1210.
DR PDB; 7SZ1; EM; 3.40 A; A/B=1-1210.
DR PDB; 7SZ5; EM; 3.60 A; A/B=1-1210.
DR PDB; 7SZ7; EM; 3.40 A; A/B=1-1210.
DR PDB; 7TVD; X-ray; 2.96 A; A=696-1022.
DR PDBsum; 1IVO; -.
DR PDBsum; 1M14; -.
DR PDBsum; 1M17; -.
DR PDBsum; 1MOX; -.
DR PDBsum; 1NQL; -.
DR PDBsum; 1XKK; -.
DR PDBsum; 1YY9; -.
DR PDBsum; 1Z9I; -.
DR PDBsum; 2EB2; -.
DR PDBsum; 2EB3; -.
DR PDBsum; 2GS2; -.
DR PDBsum; 2GS6; -.
DR PDBsum; 2GS7; -.
DR PDBsum; 2ITN; -.
DR PDBsum; 2ITO; -.
DR PDBsum; 2ITP; -.
DR PDBsum; 2ITQ; -.
DR PDBsum; 2ITT; -.
DR PDBsum; 2ITU; -.
DR PDBsum; 2ITV; -.
DR PDBsum; 2ITW; -.
DR PDBsum; 2ITX; -.
DR PDBsum; 2ITY; -.
DR PDBsum; 2ITZ; -.
DR PDBsum; 2J5E; -.
DR PDBsum; 2J5F; -.
DR PDBsum; 2J6M; -.
DR PDBsum; 2JIT; -.
DR PDBsum; 2JIU; -.
DR PDBsum; 2JIV; -.
DR PDBsum; 2KS1; -.
DR PDBsum; 2M0B; -.
DR PDBsum; 2M20; -.
DR PDBsum; 2N5S; -.
DR PDBsum; 2RF9; -.
DR PDBsum; 2RFD; -.
DR PDBsum; 2RFE; -.
DR PDBsum; 2RGP; -.
DR PDBsum; 3B2U; -.
DR PDBsum; 3B2V; -.
DR PDBsum; 3BEL; -.
DR PDBsum; 3BUO; -.
DR PDBsum; 3C09; -.
DR PDBsum; 3G5V; -.
DR PDBsum; 3G5Y; -.
DR PDBsum; 3GOP; -.
DR PDBsum; 3GT8; -.
DR PDBsum; 3IKA; -.
DR PDBsum; 3LZB; -.
DR PDBsum; 3NJP; -.
DR PDBsum; 3OB2; -.
DR PDBsum; 3OP0; -.
DR PDBsum; 3P0Y; -.
DR PDBsum; 3PFV; -.
DR PDBsum; 3POZ; -.
DR PDBsum; 3QWQ; -.
DR PDBsum; 3UG1; -.
DR PDBsum; 3UG2; -.
DR PDBsum; 3VJN; -.
DR PDBsum; 3VJO; -.
DR PDBsum; 3VRP; -.
DR PDBsum; 3VRR; -.
DR PDBsum; 3W2O; -.
DR PDBsum; 3W2P; -.
DR PDBsum; 3W2Q; -.
DR PDBsum; 3W2R; -.
DR PDBsum; 3W2S; -.
DR PDBsum; 3W32; -.
DR PDBsum; 3W33; -.
DR PDBsum; 4G5J; -.
DR PDBsum; 4G5P; -.
DR PDBsum; 4HJO; -.
DR PDBsum; 4I1Z; -.
DR PDBsum; 4I20; -.
DR PDBsum; 4I21; -.
DR PDBsum; 4I22; -.
DR PDBsum; 4I23; -.
DR PDBsum; 4I24; -.
DR PDBsum; 4JQ7; -.
DR PDBsum; 4JQ8; -.
DR PDBsum; 4JR3; -.
DR PDBsum; 4JRV; -.
DR PDBsum; 4KRL; -.
DR PDBsum; 4KRM; -.
DR PDBsum; 4KRO; -.
DR PDBsum; 4KRP; -.
DR PDBsum; 4LI5; -.
DR PDBsum; 4LL0; -.
DR PDBsum; 4LQM; -.
DR PDBsum; 4LRM; -.
DR PDBsum; 4R3P; -.
DR PDBsum; 4R3R; -.
DR PDBsum; 4R5S; -.
DR PDBsum; 4RIW; -.
DR PDBsum; 4RIX; -.
DR PDBsum; 4RIY; -.
DR PDBsum; 4RJ4; -.
DR PDBsum; 4RJ5; -.
DR PDBsum; 4RJ6; -.
DR PDBsum; 4RJ7; -.
DR PDBsum; 4RJ8; -.
DR PDBsum; 4TKS; -.
DR PDBsum; 4UIP; -.
DR PDBsum; 4UV7; -.
DR PDBsum; 4WD5; -.
DR PDBsum; 4WKQ; -.
DR PDBsum; 4WRG; -.
DR PDBsum; 4ZAU; -.
DR PDBsum; 4ZJV; -.
DR PDBsum; 4ZSE; -.
DR PDBsum; 5C8K; -.
DR PDBsum; 5C8M; -.
DR PDBsum; 5C8N; -.
DR PDBsum; 5CAL; -.
DR PDBsum; 5CAN; -.
DR PDBsum; 5CAO; -.
DR PDBsum; 5CAP; -.
DR PDBsum; 5CAQ; -.
DR PDBsum; 5CAS; -.
DR PDBsum; 5CAU; -.
DR PDBsum; 5CAV; -.
DR PDBsum; 5CNN; -.
DR PDBsum; 5CNO; -.
DR PDBsum; 5CZH; -.
DR PDBsum; 5CZI; -.
DR PDBsum; 5D41; -.
DR PDBsum; 5EDP; -.
DR PDBsum; 5EDQ; -.
DR PDBsum; 5EDR; -.
DR PDBsum; 5EM5; -.
DR PDBsum; 5EM6; -.
DR PDBsum; 5EM7; -.
DR PDBsum; 5EM8; -.
DR PDBsum; 5FED; -.
DR PDBsum; 5FEE; -.
DR PDBsum; 5FEQ; -.
DR PDBsum; 5GMP; -.
DR PDBsum; 5GNK; -.
DR PDBsum; 5GTY; -.
DR PDBsum; 5GTZ; -.
DR PDBsum; 5HCX; -.
DR PDBsum; 5HCY; -.
DR PDBsum; 5HCZ; -.
DR PDBsum; 5HG5; -.
DR PDBsum; 5HG7; -.
DR PDBsum; 5HG8; -.
DR PDBsum; 5HG9; -.
DR PDBsum; 5HIB; -.
DR PDBsum; 5HIC; -.
DR PDBsum; 5J9Y; -.
DR PDBsum; 5J9Z; -.
DR PDBsum; 5JEB; -.
DR PDBsum; 5LV6; -.
DR PDBsum; 5SX4; -.
DR PDBsum; 5SX5; -.
DR PDBsum; 5U8L; -.
DR PDBsum; 5UG8; -.
DR PDBsum; 5UG9; -.
DR PDBsum; 5UGA; -.
DR PDBsum; 5UGB; -.
DR PDBsum; 5UGC; -.
DR PDBsum; 5UWD; -.
DR PDBsum; 5WB7; -.
DR PDBsum; 5WB8; -.
DR PDBsum; 5X26; -.
DR PDBsum; 5X27; -.
DR PDBsum; 5X28; -.
DR PDBsum; 5X2A; -.
DR PDBsum; 5X2C; -.
DR PDBsum; 5X2F; -.
DR PDBsum; 5X2K; -.
DR PDBsum; 5XDK; -.
DR PDBsum; 5XDL; -.
DR PDBsum; 5XGM; -.
DR PDBsum; 5XGN; -.
DR PDBsum; 5XWD; -.
DR PDBsum; 5Y25; -.
DR PDBsum; 5Y9T; -.
DR PDBsum; 5YU9; -.
DR PDBsum; 5ZTO; -.
DR PDBsum; 5ZWJ; -.
DR PDBsum; 6ARU; -.
DR PDBsum; 6B3S; -.
DR PDBsum; 6D8E; -.
DR PDBsum; 6DUK; -.
DR PDBsum; 6JRJ; -.
DR PDBsum; 6JRK; -.
DR PDBsum; 6JRX; -.
DR PDBsum; 6JWL; -.
DR PDBsum; 6JX0; -.
DR PDBsum; 6JX4; -.
DR PDBsum; 6JXT; -.
DR PDBsum; 6JZ0; -.
DR PDBsum; 6LUB; -.
DR PDBsum; 6LUD; -.
DR PDBsum; 6P1D; -.
DR PDBsum; 6P1L; -.
DR PDBsum; 6P8Q; -.
DR PDBsum; 6S89; -.
DR PDBsum; 6S8A; -.
DR PDBsum; 6S9B; -.
DR PDBsum; 6S9C; -.
DR PDBsum; 6S9D; -.
DR PDBsum; 6TFU; -.
DR PDBsum; 6TFV; -.
DR PDBsum; 6TFW; -.
DR PDBsum; 6TFY; -.
DR PDBsum; 6TFZ; -.
DR PDBsum; 6TG0; -.
DR PDBsum; 6TG1; -.
DR PDBsum; 6V5N; -.
DR PDBsum; 6V5P; -.
DR PDBsum; 6V66; -.
DR PDBsum; 6V6K; -.
DR PDBsum; 6V6O; -.
DR PDBsum; 6VH4; -.
DR PDBsum; 6VHN; -.
DR PDBsum; 6VHP; -.
DR PDBsum; 6WA2; -.
DR PDBsum; 6WAK; -.
DR PDBsum; 6WXN; -.
DR PDBsum; 6XL4; -.
DR PDBsum; 6Z4B; -.
DR PDBsum; 6Z4D; -.
DR PDBsum; 7A2A; -.
DR PDBsum; 7A6I; -.
DR PDBsum; 7A6J; -.
DR PDBsum; 7A6K; -.
DR PDBsum; 7AEI; -.
DR PDBsum; 7AEM; -.
DR PDBsum; 7B85; -.
DR PDBsum; 7JXI; -.
DR PDBsum; 7JXK; -.
DR PDBsum; 7JXL; -.
DR PDBsum; 7JXM; -.
DR PDBsum; 7JXP; -.
DR PDBsum; 7JXQ; -.
DR PDBsum; 7JXW; -.
DR PDBsum; 7K1H; -.
DR PDBsum; 7K1I; -.
DR PDBsum; 7KXZ; -.
DR PDBsum; 7KY0; -.
DR PDBsum; 7LEN; -.
DR PDBsum; 7LFR; -.
DR PDBsum; 7LFS; -.
DR PDBsum; 7LG8; -.
DR PDBsum; 7LGS; -.
DR PDBsum; 7LTX; -.
DR PDBsum; 7OM4; -.
DR PDBsum; 7OXB; -.
DR PDBsum; 7SYD; -.
DR PDBsum; 7SYE; -.
DR PDBsum; 7SZ0; -.
DR PDBsum; 7SZ1; -.
DR PDBsum; 7SZ5; -.
DR PDBsum; 7SZ7; -.
DR PDBsum; 7TVD; -.
DR AlphaFoldDB; P00533; -.
DR BMRB; P00533; -.
DR SMR; P00533; -.
DR BioGRID; 108276; 1683.
DR CORUM; P00533; -.
DR DIP; DIP-405N; -.
DR ELM; P00533; -.
DR IntAct; P00533; 622.
DR MINT; P00533; -.
DR STRING; 9606.ENSP00000275493; -.
DR BindingDB; P00533; -.
DR ChEMBL; CHEMBL203; -.
DR DrugBank; DB15327; Abivertinib.
DR DrugBank; DB08916; Afatinib.
DR DrugBank; DB03496; Alvocidib.
DR DrugBank; DB16695; Amivantamab.
DR DrugBank; DB06021; AV-412.
DR DrugBank; DB12267; Brigatinib.
DR DrugBank; DB05424; Canertinib.
DR DrugBank; DB00002; Cetuximab.
DR DrugBank; DB11963; Dacomitinib.
DR DrugBank; DB11731; Depatuxizumab mafodotin.
DR DrugBank; DB00530; Erlotinib.
DR DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB00317; Gefitinib.
DR DrugBank; DB11737; Icotinib.
DR DrugBank; DB04988; IGN311.
DR DrugBank; DB01259; Lapatinib.
DR DrugBank; DB00281; Lidocaine.
DR DrugBank; DB05101; Matuzumab.
DR DrugBank; DB16390; Mobocertinib.
DR DrugBank; DB09559; Necitumumab.
DR DrugBank; DB11828; Neratinib.
DR DrugBank; DB13164; Olmutinib.
DR DrugBank; DB09330; Osimertinib.
DR DrugBank; DB01269; Panitumumab.
DR DrugBank; DB07662; PD-168393.
DR DrugBank; DB05524; Pelitinib.
DR DrugBank; DB05374; Rindopepimut.
DR DrugBank; DB07602; S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE.
DR DrugBank; DB05294; Vandetanib.
DR DrugBank; DB05944; Varlitinib.
DR DrugBank; DB12202; Zalutumumab.
DR DrugBank; DB15035; Zanubrutinib.
DR DrugCentral; P00533; -.
DR GuidetoPHARMACOLOGY; 1797; -.
DR MoonDB; P00533; Predicted.
DR GlyConnect; 137; 81 N-Linked glycans (10 sites).
DR GlyGen; P00533; 18 sites, 101 N-linked glycans (15 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P00533; -.
DR MetOSite; P00533; -.
DR PhosphoSitePlus; P00533; -.
DR SwissPalm; P00533; -.
DR BioMuta; EGFR; -.
DR DMDM; 2811086; -.
DR SWISS-2DPAGE; P00533; -.
DR CPTAC; CPTAC-1043; -.
DR CPTAC; CPTAC-1560; -.
DR CPTAC; CPTAC-1781; -.
DR CPTAC; CPTAC-802; -.
DR EPD; P00533; -.
DR jPOST; P00533; -.
DR MassIVE; P00533; -.
DR MaxQB; P00533; -.
DR PaxDb; P00533; -.
DR PeptideAtlas; P00533; -.
DR PRIDE; P00533; -.
DR ProteomicsDB; 51261; -. [P00533-1]
DR ProteomicsDB; 51262; -. [P00533-2]
DR ProteomicsDB; 51263; -. [P00533-3]
DR ProteomicsDB; 51264; -. [P00533-4]
DR ABCD; P00533; 112 sequenced antibodies.
DR Antibodypedia; 718; 10079 antibodies from 64 providers.
DR CPTC; P00533; 13 antibodies.
DR DNASU; 1956; -.
DR Ensembl; ENST00000275493.7; ENSP00000275493.2; ENSG00000146648.20. [P00533-1]
DR Ensembl; ENST00000342916.7; ENSP00000342376.3; ENSG00000146648.20. [P00533-4]
DR Ensembl; ENST00000344576.7; ENSP00000345973.2; ENSG00000146648.20. [P00533-3]
DR Ensembl; ENST00000420316.6; ENSP00000413843.2; ENSG00000146648.20. [P00533-2]
DR GeneID; 1956; -.
DR KEGG; hsa:1956; -.
DR MANE-Select; ENST00000275493.7; ENSP00000275493.2; NM_005228.5; NP_005219.2.
DR UCSC; uc003tqh.4; human. [P00533-1]
DR CTD; 1956; -.
DR DisGeNET; 1956; -.
DR GeneCards; EGFR; -.
DR HGNC; HGNC:3236; EGFR.
DR HPA; ENSG00000146648; Tissue enhanced (placenta).
DR MalaCards; EGFR; -.
DR MIM; 131550; gene.
DR MIM; 211980; phenotype.
DR MIM; 616069; phenotype.
DR neXtProt; NX_P00533; -.
DR OpenTargets; ENSG00000146648; -.
DR Orphanet; 251579; Giant cell glioblastoma.
DR Orphanet; 251576; Gliosarcoma.
DR Orphanet; 294023; Neonatal inflammatory skin and bowel disease.
DR Orphanet; 357191; Selection of therapeutic option in non-small cell lung carcinoma.
DR PharmGKB; PA7360; -.
DR VEuPathDB; HostDB:ENSG00000146648; -.
DR eggNOG; KOG1025; Eukaryota.
DR GeneTree; ENSGT00940000155450; -.
DR HOGENOM; CLU_003384_0_2_1; -.
DR InParanoid; P00533; -.
DR OMA; CYVGNIR; -.
DR PhylomeDB; P00533; -.
DR TreeFam; TF106002; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P00533; -.
DR Reactome; R-HSA-1227986; Signaling by ERBB2.
DR Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR Reactome; R-HSA-1236394; Signaling by ERBB4.
DR Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
DR Reactome; R-HSA-1251932; PLCG1 events in ERBB2 signaling.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-177929; Signaling by EGFR.
DR Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
DR Reactome; R-HSA-180292; GAB1 signalosome.
DR Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
DR Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
DR Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
DR Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-445144; Signal transduction by L1.
DR Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
DR Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8857538; PTK6 promotes HIF1A stabilization.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
DR Reactome; R-HSA-9009391; Extra-nuclear estrogen signaling.
DR Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR SignaLink; P00533; -.
DR SIGNOR; P00533; -.
DR BioGRID-ORCS; 1956; 148 hits in 1121 CRISPR screens.
DR ChiTaRS; EGFR; human.
DR EvolutionaryTrace; P00533; -.
DR GeneWiki; Epidermal_growth_factor_receptor; -.
DR GenomeRNAi; 1956; -.
DR Pharos; P00533; Tclin.
DR PRO; PR:P00533; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P00533; protein.
DR Bgee; ENSG00000146648; Expressed in nipple and 204 other tissues.
DR ExpressionAtlas; P00533; baseline and differential.
DR Genevisible; P00533; HS.
DR GO; GO:0009925; C:basal plasma membrane; IBA:GO_Central.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097708; C:intracellular vesicle; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR GO; GO:0097489; C:multivesicular body, internal vesicle lumen; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0032587; C:ruffle membrane; IDA:ARUK-UCL.
DR GO; GO:0070435; C:Shc-EGFR complex; ISS:BHF-UCL.
DR GO; GO:0044214; C:spanning component of plasma membrane; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051117; F:ATPase binding; ISS:ARUK-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; NAS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0048408; F:epidermal growth factor binding; IBA:GO_Central.
DR GO; GO:0005006; F:epidermal growth factor receptor activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; NAS:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IEA:Ensembl.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007202; P:activation of phospholipase C activity; TAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
DR GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
DR GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
DR GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0038134; P:ERBB2-EGFR signaling pathway; IDA:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1905208; P:negative regulation of cardiocyte differentiation; IMP:BHF-UCL.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0001503; P:ossification; NAS:UniProtKB.
DR GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:UniProtKB.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:BHF-UCL.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:BHF-UCL.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; IMP:BHF-UCL.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:CAFA.
DR GO; GO:0010750; P:positive regulation of nitric oxide mediated signal transduction; IDA:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
DR GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR GO; GO:0051205; P:protein insertion into membrane; TAS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:CAFA.
DR GO; GO:0046328; P:regulation of JNK cascade; IMP:CAFA.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:CAFA.
DR GO; GO:0070141; P:response to UV-A; IDA:BHF-UCL.
DR GO; GO:0007435; P:salivary gland morphogenesis; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd00064; FU; 3.
DR DisProt; DP00309; -.
DR Gene3D; 3.80.20.20; -; 2.
DR IDEAL; IID00262; -.
DR InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR032778; GF_recep_IV.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR000494; Rcpt_L-dom.
DR InterPro; IPR036941; Rcpt_L-dom_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR Pfam; PF00757; Furin-like; 1.
DR Pfam; PF14843; GF_recep_IV; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF01030; Recep_L_domain; 2.
DR PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00261; FU; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Developmental protein; Direct protein sequencing; Disease variant;
KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
KW Golgi apparatus; Host cell receptor for virus entry;
KW Host-virus interaction; Hydroxylation; Isopeptide bond; Kinase;
KW Lipoprotein; Membrane; Methylation; Nucleotide-binding; Nucleus; Palmitate;
KW Phosphoprotein; Proto-oncogene; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:6328312, ECO:0000269|Ref.16"
FT CHAIN 25..1210
FT /note="Epidermal growth factor receptor"
FT /id="PRO_0000016665"
FT TOPO_DOM 25..645
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 646..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..1210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 75..300
FT /note="Approximate"
FT REPEAT 390..600
FT /note="Approximate"
FT DOMAIN 712..979
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 688..704
FT /note="Important for dimerization, phosphorylation and
FT activation"
FT REGION 1097..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 837
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 718..726
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:19563760,
FT ECO:0007744|PDB:2GS7, ECO:0007744|PDB:3GT8,
FT ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN,
FT ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41"
FT BINDING 745
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17349580,
FT ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3,
FT ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN,
FT ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN,
FT ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW,
FT ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE,
FT ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO,
FT ECO:0007744|PDB:5D41"
FT BINDING 790..791
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17349580,
FT ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3,
FT ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN,
FT ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX,
FT ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN,
FT ECO:0007744|PDB:3VJO, ECO:0007744|PDB:4RIW,
FT ECO:0007744|PDB:4RIX, ECO:0007744|PDB:4RIY,
FT ECO:0007744|PDB:4ZSE, ECO:0007744|PDB:5CNN,
FT ECO:0007744|PDB:5CNO, ECO:0007744|PDB:5D41"
FT BINDING 855
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17349580,
FT ECO:0000269|PubMed:19563760, ECO:0007744|PDB:2EB3,
FT ECO:0007744|PDB:2GS7, ECO:0007744|PDB:2ITN,
FT ECO:0007744|PDB:2ITV, ECO:0007744|PDB:2ITX,
FT ECO:0007744|PDB:3GT8, ECO:0007744|PDB:3VJN,
FT ECO:0007744|PDB:4RIW, ECO:0007744|PDB:4RIX,
FT ECO:0007744|PDB:4RIY, ECO:0007744|PDB:4ZSE,
FT ECO:0007744|PDB:5CNN, ECO:0007744|PDB:5CNO,
FT ECO:0007744|PDB:5D41"
FT SITE 1016
FT /note="Important for interaction with PIK3C2B"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21487020"
FT MOD_RES 678
FT /note="Phosphothreonine; by PKC and PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:10523301"
FT MOD_RES 693
FT /note="Phosphothreonine; by PKD/PRKD1"
FT /evidence="ECO:0000269|PubMed:10523301,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:3138233,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3138233,
FT ECO:0007744|PubMed:18691976"
FT MOD_RES 745
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 995
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 998
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19563760,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1016
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19563760"
FT MOD_RES 1026
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16083266,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1041
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1042
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1064
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1069
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:22888118"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3138233"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3138233"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 1092
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12873986,
FT ECO:0000269|PubMed:27153536"
FT MOD_RES 1110
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:12873986,
FT ECO:0000269|PubMed:2543678"
FT MOD_RES 1166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:24275569"
FT MOD_RES 1172
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:27153536,
FT ECO:0007744|PubMed:17081983"
FT MOD_RES 1197
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19563760,
FT ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:27153536,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1199
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:21258366"
FT LIPID 1049
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:27153536"
FT LIPID 1146
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:27153536"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) (complex) asparagine; atypical;
FT partial"
FT /evidence="ECO:0000269|PubMed:10731668,
FT ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050,
FT ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:20837704, ECO:0007744|PDB:1IVO,
FT ECO:0007744|PDB:1MOX, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ"
FT /id="CAR_000227"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:3NJP"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:8962717"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12297050,
FT ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:8962717,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:3NJP"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:3NJP"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10731668,
FT ECO:0000269|PubMed:12297049, ECO:0000269|PubMed:12297050,
FT ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:20837704, ECO:0007744|PDB:1IVO,
FT ECO:0007744|PDB:1MOX, ECO:0007744|PDB:1NQL,
FT ECO:0007744|PDB:1YY9, ECO:0007744|PDB:3B2U,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10731668,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:20837704, ECO:0007744|PDB:1IVO,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL,
FT ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UV7"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:8962717, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP"
FT CARBOHYD 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12297050,
FT ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:20837704,
FT ECO:0000269|PubMed:8962717, ECO:0007744|PDB:1IVO,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3P0Y,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL,
FT ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:12731890, ECO:0000269|PubMed:16083266,
FT ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:25922362,
FT ECO:0000269|PubMed:8962717, ECO:0007744|PDB:1NQL,
FT ECO:0007744|PDB:1YY9, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:10731668,
FT ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19159218,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9"
FT CARBOHYD 603
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:10731668,
FT ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12731890,
FT ECO:0000269|PubMed:16083266, ECO:0007744|PDB:1NQL,
FT ECO:0007744|PDB:1YY9"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000305|PubMed:12731890"
FT DISULFID 31..58
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 157..187
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD"
FT DISULFID 190..199
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD"
FT DISULFID 194..207
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD"
FT DISULFID 215..223
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 219..231
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 232..240
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 236..248
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 251..260
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 264..291
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD"
FT DISULFID 295..307
FT /evidence="ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD"
FT DISULFID 311..326
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3G5V,
FT ECO:0007744|PDB:3G5Y, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 329..333
FT /evidence="ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD"
FT DISULFID 337..362
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3C09, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5SX4, ECO:0007744|PDB:5SX5,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD, ECO:0007744|PDB:6B3S"
FT DISULFID 470..499
FT /evidence="ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3C09, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5SX4, ECO:0007744|PDB:5SX5,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD, ECO:0007744|PDB:6B3S"
FT DISULFID 506..515
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3NJP, ECO:0007744|PDB:3P0Y,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL,
FT ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5SX4,
FT ECO:0007744|PDB:5SX5, ECO:0007744|PDB:5WB7,
FT ECO:0007744|PDB:5WB8, ECO:0007744|PDB:5XWD,
FT ECO:0007744|PDB:6B3S"
FT DISULFID 510..523
FT /evidence="ECO:0000269|PubMed:12297049,
FT ECO:0000269|PubMed:12297050, ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1IVO, ECO:0007744|PDB:1MOX,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2U, ECO:0007744|PDB:3B2V,
FT ECO:0007744|PDB:3C09, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3P0Y, ECO:0007744|PDB:3QWQ,
FT ECO:0007744|PDB:4KRL, ECO:0007744|PDB:4KRM,
FT ECO:0007744|PDB:4KRO, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UIP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5SX4, ECO:0007744|PDB:5SX5,
FT ECO:0007744|PDB:5WB7, ECO:0007744|PDB:5WB8,
FT ECO:0007744|PDB:5XWD, ECO:0007744|PDB:6B3S"
FT DISULFID 526..535
FT /evidence="ECO:0000269|PubMed:12297050,
FT ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:15837620,
FT ECO:0000269|PubMed:20837704, ECO:0007744|PDB:1IVO,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRL,
FT ECO:0007744|PDB:4KRM, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT DISULFID 539..555
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT DISULFID 558..571
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT DISULFID 562..579
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT DISULFID 582..591
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UV7,
FT ECO:0007744|PDB:5XWD"
FT DISULFID 595..617
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT DISULFID 620..628
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRO,
FT ECO:0007744|PDB:4KRP, ECO:0007744|PDB:4UIP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT DISULFID 624..636
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:15837620, ECO:0000269|PubMed:20837704,
FT ECO:0007744|PDB:1NQL, ECO:0007744|PDB:1YY9,
FT ECO:0007744|PDB:3B2V, ECO:0007744|PDB:3NJP,
FT ECO:0007744|PDB:3QWQ, ECO:0007744|PDB:4KRP,
FT ECO:0007744|PDB:4UV7, ECO:0007744|PDB:5XWD"
FT CROSSLNK 716
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144"
FT CROSSLNK 737
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144"
FT CROSSLNK 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144"
FT CROSSLNK 867
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144"
FT CROSSLNK 929
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144"
FT CROSSLNK 970
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144"
FT VAR_SEQ 404..405
FT /note="FL -> LS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7654368,
FT ECO:0000303|PubMed:8918811, ECO:0000303|PubMed:9103388,
FT ECO:0000303|Ref.6"
FT /id="VSP_002887"
FT VAR_SEQ 406..1210
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7654368,
FT ECO:0000303|PubMed:8918811, ECO:0000303|PubMed:9103388,
FT ECO:0000303|Ref.6"
FT /id="VSP_002888"
FT VAR_SEQ 628..705
FT /note="CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFMRRRHIVRKRTL
FT RRLLQERELVEPLTPSGEAPNQALLR -> PGNESLKAMLFCLFKLSSCNQSNDGSVSH
FT QSGSPAAQESCLGWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11161793"
FT /id="VSP_002889"
FT VAR_SEQ 628
FT /note="C -> S (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11161793"
FT /id="VSP_002891"
FT VAR_SEQ 629..1210
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11161793"
FT /id="VSP_002892"
FT VAR_SEQ 706..1210
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11161793"
FT /id="VSP_002890"
FT VARIANT 30..297
FT /note="Missing (variant EGFR vIII; found in a lung cancer
FT sample; somatic mutation; induces lung cancer when
FT exogenously expressed)"
FT /evidence="ECO:0000269|PubMed:16672372"
FT /id="VAR_066493"
FT VARIANT 98
FT /note="R -> Q (in dbSNP:rs17289589)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019293"
FT VARIANT 266
FT /note="P -> R (in dbSNP:rs17336639)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019294"
FT VARIANT 428
FT /note="G -> D (in NISBD2; loss of function; the mutant does
FT not localize to the cell membrane; has diffuse cytoplasmic
FT localization; dbSNP:rs606231253)"
FT /evidence="ECO:0000269|PubMed:24691054"
FT /id="VAR_072435"
FT VARIANT 521
FT /note="R -> K (in dbSNP:rs2227983)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.7"
FT /id="VAR_019295"
FT VARIANT 674
FT /note="V -> I (in dbSNP:rs17337079)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019296"
FT VARIANT 709
FT /note="E -> A (found in a lung cancer sample; more
FT sensitive to gefitinib than wild-type; dbSNP:rs397517085)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628, ECO:0000269|PubMed:16533793"
FT /id="VAR_026084"
FT VARIANT 709
FT /note="E -> G (found in a lung cancer sample;
FT constitutively activated kinase with higher levels of basal
FT autophosphorylation; more sensitive to gefitinib than wild-
FT type; dbSNP:rs397517085)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628"
FT /id="VAR_069498"
FT VARIANT 709
FT /note="E -> K (found in a lung cancer sample;
FT dbSNP:rs727504256)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026085"
FT VARIANT 719
FT /note="G -> A (found in a lung cancer sample;
FT dbSNP:rs121913428)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026086"
FT VARIANT 719
FT /note="G -> C (found in a lung cancer sample;
FT dbSNP:rs28929495)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16533793"
FT /id="VAR_026087"
FT VARIANT 719
FT /note="G -> D (found in a lung cancer sample;
FT dbSNP:rs121913428)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026088"
FT VARIANT 719
FT /note="G -> S (found in a lung cancer sample; somatic
FT mutation; strongly increased kinase activity;
FT constitutively activated kinase with higher levels of basal
FT autophosphorylation; more sensitive to gefitinib than wild-
FT type; dbSNP:rs28929495)"
FT /evidence="ECO:0000269|PubMed:15118125,
FT ECO:0000269|PubMed:15623594, ECO:0000269|PubMed:16205628,
FT ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:17349580"
FT /id="VAR_019297"
FT VARIANT 724
FT /note="G -> S (found in a lung cancer sample;
FT dbSNP:rs1051753269)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026089"
FT VARIANT 734
FT /note="E -> K (found in a lung cancer sample;
FT dbSNP:rs121913420)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026090"
FT VARIANT 746..752
FT /note="ELREATS -> D (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:15623594"
FT /id="VAR_069499"
FT VARIANT 746..751
FT /note="ELREAT -> A (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:15623594"
FT /id="VAR_069500"
FT VARIANT 746..750
FT /note="Missing (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:15623594"
FT /id="VAR_026092"
FT VARIANT 746
FT /note="Missing (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026091"
FT VARIANT 747..751
FT /note="Missing (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:15623594"
FT /id="VAR_069501"
FT VARIANT 747..749
FT /note="Missing (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026094"
FT VARIANT 747
FT /note="L -> F (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026093"
FT VARIANT 748
FT /note="R -> P (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026095"
FT VARIANT 752..759
FT /note="Missing (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026096"
FT VARIANT 768
FT /note="S -> I (found in a lung cancer sample;
FT constitutively activated kinase with higher levels of basal
FT autophosphorylation; more sensitive to gefitinib than wild-
FT type; dbSNP:rs121913465)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628"
FT /id="VAR_069502"
FT VARIANT 769
FT /note="V -> M (found in a lung cancer sample;
FT dbSNP:rs147149347)"
FT /evidence="ECO:0000269|PubMed:15623594"
FT /id="VAR_069503"
FT VARIANT 787
FT /note="Q -> R (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026097"
FT VARIANT 790
FT /note="T -> M (found in a lung cancer sample; increased
FT kinase activity; dbSNP:rs121434569)"
FT /evidence="ECO:0000269|PubMed:16533793,
FT ECO:0000269|PubMed:18227510"
FT /id="VAR_026098"
FT VARIANT 833
FT /note="L -> V (found in a lung cancer sample; more
FT sensitive to gefitinib than wild-type; dbSNP:rs397517126)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628, ECO:0000269|PubMed:16533793"
FT /id="VAR_026099"
FT VARIANT 834
FT /note="V -> L (found in a lung cancer sample;
FT dbSNP:rs397517127)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026100"
FT VARIANT 835
FT /note="H -> L (found in a lung cancer sample; more
FT sensitive to gefitinib than wild-type; dbSNP:rs397517128)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628"
FT /id="VAR_069504"
FT VARIANT 838
FT /note="L -> V (found in a lung cancer sample; more
FT sensitive to gefitinib than wild-type; dbSNP:rs864621996)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628"
FT /id="VAR_069505"
FT VARIANT 858
FT /note="L -> M (found in a lung cancer sample;
FT dbSNP:rs121913443)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026101"
FT VARIANT 858
FT /note="L -> R (found in a lung cancer sample; somatic
FT mutation; constitutively activated enzyme with strongly
FT increased kinase activity; more sensitive to gefitinib than
FT wild-type; dbSNP:rs121434568)"
FT /evidence="ECO:0000269|PubMed:15118125,
FT ECO:0000269|PubMed:15623594, ECO:0000269|PubMed:16205628,
FT ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:17349580"
FT /id="VAR_019298"
FT VARIANT 861
FT /note="L -> Q (found in a lung cancer sample;
FT constitutively activated kinase with higher levels of basal
FT autophosphorylation; more sensitive to gefitinib than wild-
FT type; dbSNP:rs121913444)"
FT /evidence="ECO:0000269|PubMed:15623594,
FT ECO:0000269|PubMed:16205628, ECO:0000269|PubMed:16533793"
FT /id="VAR_026102"
FT VARIANT 873
FT /note="G -> E (found in a lung cancer sample)"
FT /evidence="ECO:0000269|PubMed:16533793"
FT /id="VAR_026103"
FT VARIANT 962
FT /note="R -> G (in dbSNP:rs17337451)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019299"
FT VARIANT 988
FT /note="H -> P (in dbSNP:rs17290699)"
FT /evidence="ECO:0000269|Ref.7"
FT /id="VAR_019300"
FT VARIANT 1034
FT /note="L -> R (in dbSNP:rs34352568)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042095"
FT VARIANT 1210
FT /note="A -> V (in dbSNP:rs35918369)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042096"
FT MUTAGEN 275
FT /note="Y->A: Strongly reduced autophosphorylation and
FT activation of downstream kinases; when associated with A-
FT 309."
FT /evidence="ECO:0000269|PubMed:12297050"
FT MUTAGEN 287
FT /note="F->A: Strongly reduced autophosphorylation and
FT activation of downstream kinases; when associated with A-
FT 309."
FT /evidence="ECO:0000269|PubMed:12297050"
FT MUTAGEN 309
FT /note="R->S: Strongly reduced autophosphorylation and
FT activation of downstream kinases; when associated with A-
FT 275. Strongly reduced autophosphorylation and activation of
FT downstream kinases; when associated with A-287."
FT /evidence="ECO:0000269|PubMed:12297050"
FT MUTAGEN 429
FT /note="R->E: Abolishes autophosphorylation and activation
FT of downstream kinases."
FT /evidence="ECO:0000269|PubMed:12297050"
FT MUTAGEN 525..1210
FT /note="Missing: Increased EGF binding."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 587..590
FT /note="DGPH->AGPA: Decreases intramolecular interactions
FT and facilitates EGF binding."
FT /evidence="ECO:0000269|PubMed:12620237"
FT MUTAGEN 587
FT /note="D->A: Increased EGF binding; when associated with A-
FT 590 and A-609."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 590
FT /note="H->A: Increased EGF binding; when associated with A-
FT 587; A-590 and A-609."
FT /evidence="ECO:0000269|PubMed:19718021"
FT MUTAGEN 609
FT /note="K->A: Decreases intramolecular interactions and
FT facilitates EGF binding. Increased EGF binding; when
FT associated with A-587; A-590 and A-609."
FT /evidence="ECO:0000269|PubMed:12620237,
FT ECO:0000269|PubMed:19718021"
FT MUTAGEN 688
FT /note="L->A: Strongly reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417,
FT ECO:0000269|PubMed:19563760"
FT MUTAGEN 689
FT /note="V->A: Reduced autophosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 689
FT /note="V->M: Constitutively activated kinase."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 690
FT /note="E->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417,
FT ECO:0000269|PubMed:19563760"
FT MUTAGEN 692
FT /note="L->A,P: Strongly reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417,
FT ECO:0000269|PubMed:19563760"
FT MUTAGEN 693
FT /note="T->A: Increased phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 693
FT /note="T->D: Strongly reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 694
FT /note="P->A: Strongly reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 699
FT /note="P->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 700
FT /note="N->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 704
FT /note="L->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 705
FT /note="R->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 706
FT /note="I->A: Abolishes phosphorylation."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 745
FT /note="K->A,M: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:19560417"
FT MUTAGEN 974
FT /note="D->A: Strongly reduced phosphorylation."
FT MUTAGEN 977
FT /note="R->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:19563760"
FT MUTAGEN 1005..1006
FT /note="ED->RK: Constitutively activated kinase."
FT /evidence="ECO:0000269|PubMed:19563760"
FT MUTAGEN 1016
FT /note="Y->F: 50% decrease in interaction with PIK3C2B. 65%
FT decrease in interaction with PIK3C2B; when associated with
FT F-1197. Abolishes interaction with PIK3C2B; when associated
FT with F-1197 and F-1092."
FT /evidence="ECO:0000269|PubMed:10805725"
FT MUTAGEN 1048..1210
FT /note="Missing: Abolishes palmitoylation."
FT /evidence="ECO:0000269|PubMed:27153536"
FT MUTAGEN 1049
FT /note="C->A: Decreased palmitoylation."
FT /evidence="ECO:0000269|PubMed:27153536"
FT MUTAGEN 1067
FT /note="Q->G: No effect on interaction with CBLC."
FT /evidence="ECO:0000269|PubMed:22888118"
FT MUTAGEN 1068
FT /note="R->G: Strongly decreases interaction with CBLC."
FT /evidence="ECO:0000269|PubMed:22888118"
FT MUTAGEN 1069
FT /note="Y->F: Abolishes interaction with CBLC."
FT /evidence="ECO:0000269|PubMed:22888118"
FT MUTAGEN 1092
FT /note="Y->F: No change in interaction with PIK3C2B.
FT Abolishes interaction with PIK3C2B; when associated with F-
FT 1197 and F-1016."
FT /evidence="ECO:0000269|PubMed:10805725"
FT MUTAGEN 1110
FT /note="Y->F: No change in interaction with PIK3C2B."
FT /evidence="ECO:0000269|PubMed:10805725"
FT MUTAGEN 1146
FT /note="C->A: Decreased palmitoylation."
FT /evidence="ECO:0000269|PubMed:27153536"
FT MUTAGEN 1172
FT /note="Y->F: No change in interaction with PIK3C2B."
FT /evidence="ECO:0000269|PubMed:10805725"
FT MUTAGEN 1197
FT /note="Y->F: No change in interaction with PIK3C2B. 65%
FT decrease in interaction with PIK3C2B; when associated with
FT F-1016. Abolishes interaction with PIK3C2B; when associated
FT with F-1092 and F-1016."
FT /evidence="ECO:0000269|PubMed:10805725"
FT CONFLICT 540
FT /note="N -> K (in Ref. 1; CAA25240)"
FT /evidence="ECO:0000305"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3QWQ"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 60..69
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1IVO"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 125..129
FT /evidence="ECO:0007829|PDB:1MOX"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1MOX"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5XWD"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:1MOX"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:5XWD"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:4UV7"
FT TURN 245..247
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 248..256
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:4UV7"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:4UV7"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3B2V"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:7LEN"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:4KRP"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3B2V"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:3G5Y"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3G5Y"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3P0Y"
FT TURN 340..342
FT /evidence="ECO:0007829|PDB:3QWQ"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:3P0Y"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:3P0Y"
FT TURN 380..383
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:3P0Y"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 477..480
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:1YY9"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 496..501
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:5SX4"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:3P0Y"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:3P0Y"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:4KRL"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:1YY9"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:4KRO"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:1YY9"
FT STRAND 570..575
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 578..587
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 597..602
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 606..611
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 615..619
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:7SYE"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:4UV7"
FT HELIX 633..635
FT /evidence="ECO:0007829|PDB:4UV7"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:2KS1"
FT HELIX 648..669
FT /evidence="ECO:0007829|PDB:2KS1"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:1Z9I"
FT HELIX 679..684
FT /evidence="ECO:0007829|PDB:3GOP"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:3GOP"
FT STRAND 688..692
FT /evidence="ECO:0007829|PDB:1Z9I"
FT STRAND 694..697
FT /evidence="ECO:0007829|PDB:1Z9I"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:3POZ"
FT HELIX 709..711
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 712..721
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 724..731
FT /evidence="ECO:0007829|PDB:5UG9"
FT TURN 734..736
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 740..747
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:2ITU"
FT TURN 753..755
FT /evidence="ECO:0007829|PDB:3W2S"
FT HELIX 756..767
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:6JRJ"
FT STRAND 777..791
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 794..797
FT /evidence="ECO:0007829|PDB:5ZWJ"
FT HELIX 798..804
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 811..830
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 840..842
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 843..847
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 850..853
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 858..862
FT /evidence="ECO:0007829|PDB:3POZ"
FT TURN 863..865
FT /evidence="ECO:0007829|PDB:3POZ"
FT STRAND 867..870
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 871..873
FT /evidence="ECO:0007829|PDB:6V66"
FT STRAND 875..877
FT /evidence="ECO:0007829|PDB:5CZH"
FT HELIX 878..880
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 883..888
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 893..908
FT /evidence="ECO:0007829|PDB:5UG9"
FT TURN 909..911
FT /evidence="ECO:0007829|PDB:7JXW"
FT TURN 914..917
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 920..922
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 923..928
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:5ZWJ"
FT HELIX 941..950
FT /evidence="ECO:0007829|PDB:5UG9"
FT STRAND 951..953
FT /evidence="ECO:0007829|PDB:5JEB"
FT HELIX 955..957
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 961..972
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 975..977
FT /evidence="ECO:0007829|PDB:5UG9"
FT HELIX 984..986
FT /evidence="ECO:0007829|PDB:5HG8"
FT TURN 992..998
FT /evidence="ECO:0007829|PDB:5HG8"
FT TURN 999..1003
FT /evidence="ECO:0007829|PDB:6S89"
FT STRAND 1004..1010
FT /evidence="ECO:0007829|PDB:3W2S"
FT HELIX 1013..1016
FT /evidence="ECO:0007829|PDB:3POZ"
FT STRAND 1068..1070
FT /evidence="ECO:0007829|PDB:3PFV"
SQ SEQUENCE 1210 AA; 134277 MW; D8A2A50B4EFB6ED2 CRC64;
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA
VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF
QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC
TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK
NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF
ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL
FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN
LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV
ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS
GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI
CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA
RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK
FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ
QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED
SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN
TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV
APQSSEFIGA
