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Database: UniProt
Entry: P00533
LinkDB: P00533
Original site: P00533 
ID   EGFR_HUMAN              Reviewed;        1210 AA.
AC   P00533; O00688; O00732; P06268; Q14225; Q68GS5; Q92795; Q9BZS2;
AC   Q9GZX1; Q9H2C9; Q9H3C9; Q9UMD7; Q9UMD8; Q9UMG5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   31-JUL-2019, entry version 265.
DE   RecName: Full=Epidermal growth factor receptor;
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; Synonyms=ERBB, ERBB1, HER1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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
RT   epidermal 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
RT   factor 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
RT   protein (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.,
RA   Maihle N.J.;
RT   "Comparative genomic sequence analysis and isolation of human and
RT   mouse alternative EGFR transcripts encoding truncated receptor
RT   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;
RP   LYS-521; 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.,
RA   Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R.,
RA   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
RT   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
RT   variety of 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
RT   receptor 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;
RA   Haley J.D., Waterfield M.D.;
RT   "Contributory effects of de novo transcription and premature
RT   transcript termination in the regulation of human epidermal growth
RT   factor receptor 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
RP   1068-1077, AND PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND
RP   SER-1071.
RX   PubMed=3138233;
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
RT   verified cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
RN   [19]
RP   PROTEIN SEQUENCE OF 740-744 AND 746-747.
RX   PubMed=2985580;
RA   Russo M.W., Lukas T.J., Cohen S., Staros J.V.;
RT   "Identification of residues in the nucleotide binding site of the
RT   epidermal 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
RP   MASS 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
RT   degradation by 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
RT   and 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
RT   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
RT   a 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;
RA   Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M.,
RA   Howk R., Givol D., Ullrich A., Schlessinger J.;
RT   "All autophosphorylation sites of epidermal growth factor (EGF)
RT   receptor and HER2/neu are located in their carboxyl-terminal tails.
RT   Identification 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;
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
RT   exclusively through the epidermal growth factor receptor at the
RT   surface of human 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.,
RA   Barrett T., 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;
RA   Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J.,
RA   Igarashi K., 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
RT   and 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
RT   the epidermal growth factor receptor expressed in Chinese hamster
RT   ovary 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,
RT   ErbB-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
RT   protein AP-2 by dominant-negative mutant mu2 subunit and its effects
RT   on 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-
RT   containing adapter protein having similar binding and biological
RT   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
RT   Asn-X-Cys sequence of recombinant human epidermal growth factor
RT   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-
RT   mediated 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
RT   factor receptor.";
RL   Biochemistry 42:5478-5492(2003).
RN   [40]
RP   FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, AND
RP   PHOSPHORYLATION 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
RT   activator of transcription 3 recruitment sites within the epidermal
RT   growth factor 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.,
RA   Amariglio N., Henriksson R., Rechavi G., Hedman H., Wides R.,
RA   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
RP   AND ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2,
RP   INTERACTION WITH PIK3C2B, AND MUTAGENESIS OF TYR-1016; TYR-1092;
RP   TYR-1110; TYR-1172 AND 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
RT   activated 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
RT   protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to
RT   activate NF-kappa B. Identification of a novel receptor-tyrosine
RT   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
RT   human 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
RT   factor 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.,
RA   Lyass L., Gur G., Kerber G., Citri A., Lavi S., Eilam R.,
RA   Chalifa-Caspi V., Eshhar Z., Pikarsky E., Pinkas-Kramarski R.,
RA   Bacus S.S., Yarden Y.;
RT   "Epigen, the last ligand of ErbB receptors, reveals intricate
RT   relationships 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
RP   THR-693; SER-991 AND SER-1026, AND IDENTIFICATION BY MASS
RP   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
RT   and 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
RT   in 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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling 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
RT   with the epidermal growth factor receptor.";
RL   Traffic 7:216-226(2006).
RN   [52]
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.,
RA   Hoenderop J.G., Knoers N.V., Bindels R.J.;
RT   "Impaired basolateral sorting of pro-EGF causes isolated recessive
RT   renal hypomagnesemia.";
RL   J. Clin. Invest. 117:2260-2267(2007).
RN   [53]
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   [54]
RP   INTERACTION WITH ATX2.
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
RT   receptor trafficking.";
RL   Cell. Signal. 20:1725-1739(2008).
RN   [55]
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.,
RA   Guilhaus M., James D.E., Daly R.J.;
RT   "Phosphorylation-dependent binding of 14-3-3 terminates signalling by
RT   the Gab2 docking protein.";
RL   EMBO J. 27:2305-2316(2008).
RN   [56]
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.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [57]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-1064;
RP   SER-1081; SER-1166 AND TYR-1197, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [58]
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
RP   IDENTIFICATION BY 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   [59]
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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [60]
RP   ACTIVITY REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197,
RP   DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   CBL 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   [61]
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
RT   protein 2, contributes to cellular transformation through the
RT   activation of extracellular signal-regulated kinase signaling.";
RL   J. Biol. Chem. 284:20206-20214(2009).
RN   [62]
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
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [63]
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   [64]
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.,
RA   De Amicis F., Fuqua S.A., Ando S., Maggiolini M.;
RT   "G protein-coupled receptor 30 expression is up-regulated by EGF and
RT   TGF alpha in estrogen receptor alpha-positive cancer cells.";
RL   Mol. Endocrinol. 23:1815-1826(2009).
RN   [65]
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
RT   regulates EGFR nuclear transport.";
RL   Biochem. Biophys. Res. Commun. 399:498-504(2010).
RN   [66]
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   [67]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1064
RP   AND TYR-1197, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [68]
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.,
RA   Buerckstuemmer T., 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   [69]
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.,
RA   Chiu P.C., Huang W.P., Wang Y.N., Chen C.H., Chang W.C., Chang W.C.,
RA   Chen A.J., Tsai C.H., Hung M.C.;
RT   "Nuclear translocation of epidermal growth factor receptor by Akt-
RT   dependent phosphorylation enhances breast cancer-resistant protein
RT   expression in gefitinib-resistant cells.";
RL   J. Biol. Chem. 286:20558-20568(2011).
RN   [70]
RP   FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT
RP   ARG-1199 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.,
RA   Tsai C.H., 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   [71]
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.,
RA   Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M.,
RA   Pietschmann T., Patel A.H., Pessaux P., Doffoel M., Raffelsberger W.,
RA   Poch O., McKeating J.A., Brino L., Baumert T.F.;
RT   "EGFR and EphA2 are host factors for hepatitis C virus entry and
RT   possible targets for antiviral therapy.";
RL   Nat. Med. 17:589-595(2011).
RN   [72]
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
RT   quinacrine through EGF-dependent activation of NF-kappaB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011).
RN   [73]
RP   INTERACTION WITH ANKRD13A; ANKRD13B AND ALKRD13D, 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   [74]
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.,
RA   Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N.,
RA   Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z.,
RA   Sinn P., Mills G.B., Yarden Y.;
RT   "Deubiquitination of EGFR by Cezanne-1 contributes to cancer
RT   progression.";
RL   Oncogene 31:4599-4608(2012).
RN   [75]
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
RT   sorting of the epidermal growth factor receptor.";
RL   J. Cell Sci. 126:1366-1380(2013).
RN   [76]
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   [77]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1026
RP   AND SER-1166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [78]
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.,
RA   Phillips A.O., Steadman R.;
RT   "Transforming growth factor-beta1 (TGF-beta1)-stimulated fibroblast to
RT   myofibroblast differentiation is mediated by hyaluronan (HA)-
RT   facilitated epidermal growth factor receptor (EGFR) and CD44 co-
RT   localization in lipid rafts.";
RL   J. Biol. Chem. 288:14824-14838(2013).
RN   [79]
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.,
RA   Li Q., 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   [80]
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.,
RA   Hernandez-Sanchez W., Bruntz R.C., Scott S.A., Lindsley C.W.,
RA   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   [81]
RP   FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY
RP   MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092;
RP   TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   1048-ALA--ALA-1210; 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.,
RA   Garcia B.A., Witze E.S.;
RT   "Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a
RT   Dependence on EGFR Signaling.";
RL   Mol. Cell 62:385-396(2016).
RN   [82]
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
RT   cancer cells.";
RL   Gene 626:48-53(2017).
RN   [83] {ECO:0000244|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.,
RA   Lovrecz G.O., Zhu H.J., Walker F., Frenkel M.J., Hoyne P.A.,
RA   Jorissen R.N., Nice E.C., 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   [84] {ECO:0000244|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
RP   LOCATION, MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429,
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-56; ASN-175; ASN-196;
RP   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   [85] {ECO:0000244|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,
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-352; ASN-361; ASN-444;
RP   ASN-528; ASN-568 AND 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   [86] {ECO:0000244|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.,
RA   Alligood K.J., Rusnak D.W., Gilmer T.M., Shewchuk L.;
RT   "A unique structure for epidermal growth factor receptor bound to
RT   GW572016 (Lapatinib): relationships among protein conformation,
RT   inhibitor off-rate, and receptor activity in tumor cells.";
RL   Cancer Res. 64:6652-6659(2004).
RN   [87] {ECO:0000244|PDB:1YY9}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-642 IN COMPLEX WITH
RP   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.,
RA   Ferguson K.M.;
RT   "Structural basis for inhibition of the epidermal growth factor
RT   receptor by cetuximab.";
RL   Cancer Cell 7:301-311(2005).
RN   [88]
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
RT   domain of the epidermal growth factor receptor.";
RL   J. Biol. Chem. 280:24043-24052(2005).
RN   [89] {ECO:0000244|PDB:2ITN, ECO:0000244|PDB:2ITO, ECO:0000244|PDB:2ITP, ECO:0000244|PDB:2ITQ, ECO:0000244|PDB:2ITT, ECO:0000244|PDB:2ITU, ECO:0000244|PDB:2ITV, ECO:0000244|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
RP   SYNTHETIC INHIBITORS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND
RP   CHARACTERIZATION 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.,
RA   Eck M.J.;
RT   "Structures of lung cancer-derived EGFR mutants and inhibitor
RT   complexes: mechanism of activation and insights into differential
RT   inhibitor sensitivity.";
RL   Cancer Cell 11:217-227(2007).
RN   [90]
RP   X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH
RP   ERRFI1, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
RP   SUBUNIT, AND 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
RT   kinase domain interface.";
RL   Nature 450:741-744(2007).
RN   [91] {ECO:0000244|PDB:2JIT, ECO:0000244|PDB:2JIU, ECO:0000244|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.,
RA   Wong K.K., Meyerson M., Eck M.J.;
RT   "The T790M mutation in EGFR kinase causes drug resistance by
RT   increasing the affinity for ATP.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2070-2075(2008).
RN   [92] {ECO:0000244|PDB:3GT8}
RP   X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC
RP   ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197,
RP   MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND
RP   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   [93]
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;
RP   LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706
RP   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
RT   activation domain.";
RL   Mol. Cell 34:641-651(2009).
RN   [94]
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.,
RA   Chupin V.V., Arseniev A.S.;
RT   "Spatial structure of the transmembrane domain heterodimer of ErbB1
RT   and ErbB2 receptor tyrosine kinases.";
RL   J. Mol. Biol. 400:231-243(2010).
RN   [95] {ECO:0000244|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;
RP   ASN-73; 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.,
RA   Springer T.A.;
RT   "Structural evidence for loose linkage between ligand binding and
RT   kinase activation in the epidermal growth factor receptor.";
RL   Mol. Cell. Biol. 30:5432-5443(2010).
RN   [96]
RP   X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1066-1076 IN COMPLEX WITH
RP   CBLB, 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   [97]
RP   X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1062-1074 IN COMPLEX WITH
RP   CBLC, PHOSPHORYLATION AT TYR-1069, INTERACTION WITH CBLC, AND
RP   MUTAGENESIS OF 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
RT   the tyrosine kinase binding domain of Cbl-c.";
RL   J. Biochem. 152:487-495(2012).
RN   [98]
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;
RP   747-LEU--THR-751 DEL; ILE-768; MET-769; VAL-833; LEU-835; VAL-838;
RP   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
RT   complex patterns in non-small cell lung cancers related to gefitinib
RT   responsiveness in Taiwan.";
RL   Clin. Cancer Res. 10:8195-8203(2004).
RN   [99]
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   [100]
RP   VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719;
RP   SER-724; 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;
RP   ARG-858; 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.,
RA   Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.;
RT   "Distinct epidermal growth factor receptor and KRAS mutation patterns
RT   in non-small cell lung cancer patients with different tobacco exposure
RT   and clinicopathologic features.";
RL   Clin. Cancer Res. 12:1647-1653(2006).
RN   [101]
RP   CHARACTERIZATION OF VARIANTS ALA-709; GLY-709; SER-719; ILE-768;
RP   VAL-833; 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.,
RA   Tsai S.F., Huang S.F.;
RT   "Distinctive activation patterns in constitutively active and
RT   gefitinib-sensitive EGFR mutants.";
RL   Oncogene 25:1205-1215(2006).
RN   [102]
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.,
RA   Jung B.L., McNamara K., Xia H., Glatt K.A., Thomas R.K., Sasaki H.,
RA   Horner J.W., Eck M., Mitchell A., Sun Y., Al-Hashem R., Bronson R.T.,
RA   Rabindran S.K., Discafani C.M., Maher E., Shapiro G.I., Meyerson M.,
RA   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   [103]
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.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [104]
RP   VARIANT NISBD2 ASP-428, CHARACTERIZATION OF VARIANT NISBD2 ASP-428,
RP   AND 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
CC       family and activating several signaling cascades to convert
CC       extracellular cues into appropriate cellular responses
CC       (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands
CC       include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin,
CC       epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:2790960,
CC       PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079,
CC       PubMed:12297049, PubMed:27153536, PubMed:20837704). Ligand binding
CC       triggers receptor homo- and/or heterodimerization and
CC       autophosphorylation on key cytoplasmic residues. The
CC       phosphorylated receptor recruits adapter proteins like GRB2 which
CC       in turn activates complex downstream signaling cascades. Activates
CC       at least 4 major downstream signaling cascades including the RAS-
CC       RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules
CC       (PubMed:27153536). May also activate the NF-kappa-B signaling
CC       cascade (PubMed:11116146). Also directly phosphorylates other
CC       proteins like RGS16, activating its GTPase activity and probably
CC       coupling the EGF receptor signaling to the G protein-coupled
CC       receptor signaling (PubMed:11602604). Also phosphorylates MUC1 and
CC       increases its interaction with SRC and CTNNB1/beta-catenin
CC       (PubMed:11483589). 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:19560417, 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.
CC       Mediates HCV entry by promoting the formation of the CD81-CLDN1
CC       receptor complexes that are essential for HCV entry and by
CC       enhancing membrane fusion of cells expressing HCV envelope
CC       glycoproteins. {ECO:0000269|PubMed:21516087}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-
CC         tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136,
CC         Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         EC=2.7.10.1; 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
CC       EGFR by phosphatases like PTPRJ and PTPRK constitute immediate
CC       regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that
CC       regulates EGFR endocytosis and activity. Moreover, inducible
CC       feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1
CC       constitute alternative regulatory mechanisms for the EGFR
CC       signaling. {ECO:0000269|PubMed:15282549,
CC       ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:18046415,
CC       ECO:0000269|PubMed:19836242}.
CC   -!- SUBUNIT: Binding of the ligand triggers homo- and/or
CC       heterodimerization of the receptor triggering its
CC       autophosphorylation. Heterodimer with ERBB2 (PubMed:10805725).
CC       Interacts with ERRFI1; inhibits dimerization of the kinase domain
CC       and autophosphorylation (PubMed:18046415). Part of a complex with
CC       ERBB2 and either PIK3C2A or PIK3C2B (PubMed:10805725). Interacts
CC       with GRB2; an adapter protein coupling the receptor to downstream
CC       signaling pathways. Interacts with GAB2; involved in signaling
CC       downstream of EGFR. Interacts with STAT3; mediates EGFR downstream
CC       signaling in cell proliferation. Interacts with RIPK1; involved in
CC       NF-kappa-B activation. Interacts (autophosphorylated) with CBL,
CC       CBLB and CBLC; involved in EGFR ubiquitination and regulation.
CC       Interacts with SOCS5; regulates EGFR degradation through ELOC- and
CC       ELOB-mediated ubiquitination and proteasomal degradation.
CC       Interacts with PRMT5; methylates EGFR and enhances interaction
CC       with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-
CC       dependent activation of MAPK/ERK. Interacts with COPG1; essential
CC       for regulation of EGF-dependent nuclear transport of EGFR by
CC       retrograde trafficking from the Golgi to the ER. Interacts with
CC       TNK2; this interaction is dependent on EGF stimulation and kinase
CC       activity of EGFR. Interacts with PCNA; positively regulates PCNA
CC       (PubMed:17115032). Interacts with PELP1. Interacts with MUC1.
CC       Interacts with AP2M1. Interacts with FER. May interact with EPS8;
CC       mediates EPS8 phosphorylation. Interacts (via SH2 domains) with
CC       GRB2, NCK1 and NCK2 (PubMed:10026169). Interacts with ATX2.
CC       Interacts with GAREM1. Interacts (ubiquitinated) with
CC       ANKRD13A/B/D; the interaction is direct and may regulate EGFR
CC       internalization after EGF stimulation. Interacts with GPER1; the
CC       interaction occurs in an estrogen-dependent manner. Interacts (via
CC       C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc
CC       fingers). Interacts with RNF115 and RNF126 (PubMed:23418353).
CC       Interacts with GPRC5A (via its transmembrane domain)
CC       (PubMed:25311788). Interacts with FAM83B; positively regulates
CC       EGFR inducing its autophosphorylation in absence of stimulation by
CC       EGF (PubMed:23912460). Interacts with LAPTM4B; positively
CC       correlates with EGFR activation (PubMed:28479384). Interacts with
CC       STX19 (PubMed:16420529). Interacts with CD44 (PubMed:23589287).
CC       {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:10228163,
CC       ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146,
CC       ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:12297050,
CC       ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986,
CC       ECO:0000269|PubMed:15282549, ECO:0000269|PubMed:15374980,
CC       ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:15837620,
CC       ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:16420529,
CC       ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17182860,
CC       ECO:0000269|PubMed:18046415, ECO:0000269|PubMed:18602463,
CC       ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19509291,
CC       ECO:0000269|PubMed:19560417, ECO:0000269|PubMed:19563760,
CC       ECO:0000269|PubMed:19749156, ECO:0000269|PubMed:19836242,
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:25311788,
CC       ECO:0000269|PubMed:28479384, ECO:0000269|PubMed:7657591,
CC       ECO:0000269|PubMed:8650580, ECO:0000269|PubMed:9852145,
CC       ECO:0000269|Ref.96}.
CC   -!- INTERACTION:
CC       Self; NbExp=26; IntAct=EBI-297353, EBI-297353;
CC       Q53FC7:-; NbExp=3; IntAct=EBI-297353, EBI-9356749;
CC       Q96BE0:-; NbExp=2; IntAct=EBI-297353, EBI-9356686;
CC       P00519:ABL1; NbExp=2; IntAct=EBI-297353, EBI-375543;
CC       P42684:ABL2; NbExp=8; IntAct=EBI-297353, EBI-1102694;
CC       Q15109:AGER; NbExp=2; IntAct=EBI-297353, EBI-1646426;
CC       Q9UKV8:AGO2; NbExp=11; IntAct=EBI-297353, EBI-528269;
CC       Q09666:AHNAK; NbExp=3; IntAct=EBI-297353, EBI-2555881;
CC       Q02952:AKAP12; NbExp=2; IntAct=EBI-297353, EBI-2562430;
CC       Q92625:ANKS1A; NbExp=5; IntAct=EBI-297353, EBI-1048612;
CC       Q96CW1:AP2M1; NbExp=4; IntAct=EBI-297353, EBI-297683;
CC       O00213:APBB1; NbExp=4; IntAct=EBI-297353, EBI-81694;
CC       Q92870:APBB2; NbExp=6; IntAct=EBI-297353, EBI-79277;
CC       O95704:APBB3; NbExp=2; IntAct=EBI-297353, EBI-286427;
CC       Q9UKG1:APPL1; NbExp=2; IntAct=EBI-297353, EBI-741243;
CC       O14965:AURKA; NbExp=4; IntAct=EBI-297353, EBI-448680;
CC       P30530:AXL; NbExp=4; IntAct=EBI-297353, EBI-2850927;
CC       Q14457:BECN1; NbExp=7; IntAct=EBI-297353, EBI-949378;
CC       P51451:BLK; NbExp=2; IntAct=EBI-297353, EBI-2105445;
CC       P62158:CALM3; NbExp=4; IntAct=EBI-297353, EBI-397435;
CC       P62161:Calm3 (xeno); NbExp=6; IntAct=EBI-297353, EBI-397530;
CC       P49069:CAMLG; NbExp=2; IntAct=EBI-297353, EBI-1748958;
CC       Q03135:CAV1; NbExp=6; IntAct=EBI-297353, EBI-603614;
CC       P22681:CBL; NbExp=22; IntAct=EBI-297353, EBI-518228;
CC       P22682:Cbl (xeno); NbExp=2; IntAct=EBI-297353, EBI-640919;
CC       Q16543:CDC37; NbExp=9; IntAct=EBI-297353, EBI-295634;
CC       P12830:CDH1; NbExp=3; IntAct=EBI-297353, EBI-727477;
CC       Q9BZP6:CHIA; NbExp=2; IntAct=EBI-297353, EBI-14357960;
CC       Q9NSE2:CISH; NbExp=3; IntAct=EBI-297353, EBI-617866;
CC       Q7Z7G1:CLNK; NbExp=2; IntAct=EBI-297353, EBI-7878194;
CC       P46108:CRK; NbExp=3; IntAct=EBI-297353, EBI-886;
CC       P46108-1:CRK; NbExp=3; IntAct=EBI-297353, EBI-287556;
CC       P46109:CRKL; NbExp=3; IntAct=EBI-297353, EBI-910;
CC       P35221:CTNNA1; NbExp=4; IntAct=EBI-297353, EBI-701918;
CC       O60716:CTNND1; NbExp=4; IntAct=EBI-297353, EBI-701927;
CC       Q14247:CTTN; NbExp=3; IntAct=EBI-297353, EBI-351886;
CC       Q6PKX4:DOK6; NbExp=2; IntAct=EBI-297353, EBI-2880244;
CC       P01133:EGF; NbExp=21; IntAct=EBI-297353, EBI-640857;
CC       Q12929:EPS8; NbExp=2; IntAct=EBI-297353, EBI-375576;
CC       P04626:ERBB2; NbExp=25; IntAct=EBI-297353, EBI-641062;
CC       P21860:ERBB3; NbExp=13; IntAct=EBI-297353, EBI-720706;
CC       Q15303:ERBB4; NbExp=2; IntAct=EBI-297353, EBI-80371;
CC       P07992:ERCC1; NbExp=21; IntAct=EBI-297353, EBI-750962;
CC       Q9UJM3:ERRFI1; NbExp=13; IntAct=EBI-297353, EBI-2941912;
CC       P03372:ESR1; NbExp=2; IntAct=EBI-297353, EBI-78473;
CC       P03372-4:ESR1; NbExp=4; IntAct=EBI-297353, EBI-4309277;
CC       Q92731:ESR2; NbExp=8; IntAct=EBI-297353, EBI-78505;
CC       Q96A65:EXOC4; NbExp=2; IntAct=EBI-297353, EBI-355383;
CC       P09769:FGR; NbExp=2; IntAct=EBI-297353, EBI-1383732;
CC       Q14318:FKBP8; NbExp=3; IntAct=EBI-297353, EBI-724839;
CC       Q13480:GAB1; NbExp=3; IntAct=EBI-297353, EBI-517684;
CC       P60520:GABARAPL2; NbExp=2; IntAct=EBI-297353, EBI-720116;
CC       P04406:GAPDH; NbExp=6; IntAct=EBI-297353, EBI-354056;
CC       Q8NBJ4:GOLM1; NbExp=13; IntAct=EBI-297353, EBI-712073;
CC       Q14956:GPNMB; NbExp=3; IntAct=EBI-297353, EBI-7250369;
CC       Q14956-1:GPNMB; NbExp=2; IntAct=EBI-297353, EBI-16191078;
CC       O75791:GRAP2; NbExp=2; IntAct=EBI-297353, EBI-740418;
CC       P62993:GRB2; NbExp=36; IntAct=EBI-297353, EBI-401755;
CC       P08631:HCK; NbExp=2; IntAct=EBI-297353, EBI-346340;
CC       Q9UBN7:HDAC6; NbExp=11; IntAct=EBI-297353, EBI-301697;
CC       Q8WUI4:HDAC7; NbExp=2; IntAct=EBI-297353, EBI-1048378;
CC       P07900:HSP90AA1; NbExp=5; IntAct=EBI-297353, EBI-296047;
CC       P08238:HSP90AB1; NbExp=8; IntAct=EBI-297353, EBI-352572;
CC       Q6PK50:HSP90AB1; NbExp=2; IntAct=EBI-297353, EBI-9356629;
CC       P08107:HSPA1B; NbExp=6; IntAct=EBI-297353, EBI-629985;
CC       P11142:HSPA8; NbExp=5; IntAct=EBI-297353, EBI-351896;
CC       P38646:HSPA9; NbExp=4; IntAct=EBI-297353, EBI-354932;
CC       P04792:HSPB1; NbExp=3; IntAct=EBI-297353, EBI-352682;
CC       P17936:IGFBP3; NbExp=3; IntAct=EBI-297353, EBI-715709;
CC       P46940:IQGAP1; NbExp=4; IntAct=EBI-297353, EBI-297509;
CC       O14654:IRS4; NbExp=2; IntAct=EBI-297353, EBI-356594;
CC       Q86VI4:LAPTM4B; NbExp=10; IntAct=EBI-297353, EBI-3267258;
CC       O43561:LAT; NbExp=2; IntAct=EBI-297353, EBI-1222766;
CC       Q13094:LCP2; NbExp=2; IntAct=EBI-297353, EBI-346946;
CC       Q96FE5:LINGO1; NbExp=2; IntAct=EBI-297353, EBI-719955;
CC       Q38SD2:LRRK1; NbExp=2; IntAct=EBI-297353, EBI-1050422;
CC       P07948:LYN; NbExp=6; IntAct=EBI-297353, EBI-79452;
CC       P07948-1:LYN; NbExp=2; IntAct=EBI-297353, EBI-6895930;
CC       Q9UQF2:MAPK8IP1; NbExp=3; IntAct=EBI-297353, EBI-78404;
CC       Q13387:MAPK8IP2; NbExp=4; IntAct=EBI-297353, EBI-722813;
CC       Q9Y2H9:MAST1; NbExp=2; IntAct=EBI-297353, EBI-3385920;
CC       P08581:MET; NbExp=8; IntAct=EBI-297353, EBI-1039152;
CC       P14174:MIF; NbExp=3; IntAct=EBI-297353, EBI-372712;
CC       P15941:MUC1; NbExp=3; IntAct=EBI-297353, EBI-2804728;
CC       P16333:NCK1; NbExp=3; IntAct=EBI-297353, EBI-389883;
CC       P46934:NEDD4; NbExp=3; IntAct=EBI-297353, EBI-726944;
CC       P04150:NR3C1; NbExp=2; IntAct=EBI-297353, EBI-493507;
CC       P16234:PDGFRA; NbExp=3; IntAct=EBI-297353, EBI-2861522;
CC       O00750:PIK3C2B; NbExp=9; IntAct=EBI-297353, EBI-641107;
CC       P27986:PIK3R1; NbExp=5; IntAct=EBI-297353, EBI-79464;
CC       O00459:PIK3R2; NbExp=3; IntAct=EBI-297353, EBI-346930;
CC       Q92569:PIK3R3; NbExp=6; IntAct=EBI-297353, EBI-79893;
CC       P19174:PLCG1; NbExp=6; IntAct=EBI-297353, EBI-79387;
CC       P16885:PLCG2; NbExp=5; IntAct=EBI-297353, EBI-617403;
CC       P17252:PRKCA; NbExp=2; IntAct=EBI-297353, EBI-1383528;
CC       P97313:Prkdc (xeno); NbExp=4; IntAct=EBI-297353, EBI-2272005;
CC       Q05397:PTK2; NbExp=3; IntAct=EBI-297353, EBI-702142;
CC       P18031:PTPN1; NbExp=7; IntAct=EBI-297353, EBI-968788;
CC       P20417:Ptpn1 (xeno); NbExp=11; IntAct=EBI-297353, EBI-916819;
CC       Q05209:PTPN12; NbExp=3; IntAct=EBI-297353, EBI-2266035;
CC       Q9Y2R2:PTPN22; NbExp=2; IntAct=EBI-297353, EBI-1211241;
CC       P23470:PTPRG; NbExp=2; IntAct=EBI-297353, EBI-2258115;
CC       Q9UJ41:RABGEF1; NbExp=4; IntAct=EBI-297353, EBI-913954;
CC       Q70E73:RAPH1; NbExp=2; IntAct=EBI-297353, EBI-3940924;
CC       P20936:RASA1; NbExp=7; IntAct=EBI-297353, EBI-1026476;
CC       Q13671:RIN1; NbExp=3; IntAct=EBI-297353, EBI-366017;
CC       Q01973:ROR1; NbExp=8; IntAct=EBI-297353, EBI-6082337;
CC       Q92622:RUBCN; NbExp=3; IntAct=EBI-297353, EBI-2952709;
CC       Q80U62:Rubcn (xeno); NbExp=2; IntAct=EBI-297353, EBI-3506572;
CC       P31947:SFN; NbExp=8; IntAct=EBI-297353, EBI-476295;
CC       Q9NRF2:SH2B1; NbExp=2; IntAct=EBI-297353, EBI-310491;
CC       Q9UQQ2:SH2B3; NbExp=2; IntAct=EBI-297353, EBI-7879749;
CC       Q9BRG2:SH2D3A; NbExp=2; IntAct=EBI-297353, EBI-2339271;
CC       P29353:SHC1; NbExp=28; IntAct=EBI-297353, EBI-78835;
CC       P29353-7:SHC1; NbExp=4; IntAct=EBI-297353, EBI-9691288;
CC       P98077:SHC2; NbExp=3; IntAct=EBI-297353, EBI-7256023;
CC       Q6S5L8:SHC4; NbExp=2; IntAct=EBI-297353, EBI-9453524;
CC       Q13239:SLA; NbExp=2; IntAct=EBI-297353, EBI-726214;
CC       P13866:SLC5A1; NbExp=3; IntAct=EBI-297353, EBI-1772443;
CC       P12931:SRC; NbExp=7; IntAct=EBI-297353, EBI-621482;
CC       P42224:STAT1; NbExp=6; IntAct=EBI-297353, EBI-1057697;
CC       P40763:STAT3; NbExp=14; IntAct=EBI-297353, EBI-518675;
CC       P42229:STAT5A; NbExp=3; IntAct=EBI-297353, EBI-749537;
CC       P31948:STIP1; NbExp=2; IntAct=EBI-297353, EBI-1054052;
CC       Q9UNE7:STUB1; NbExp=3; IntAct=EBI-297353, EBI-357085;
CC       P43405:SYK; NbExp=6; IntAct=EBI-297353, EBI-78302;
CC       P01135:TGFA; NbExp=2; IntAct=EBI-297353, EBI-1034374;
CC       Q9Y490:TLN1; NbExp=2; IntAct=EBI-297353, EBI-2462036;
CC       O60603:TLR2; NbExp=2; IntAct=EBI-297353, EBI-973722;
CC       Q9Y6Q6-2:TNFRSF11A; NbExp=3; IntAct=EBI-297353, EBI-20899422;
CC       Q68CZ2:TNS3; NbExp=4; IntAct=EBI-297353, EBI-1220488;
CC       O75674:TOM1L1; NbExp=6; IntAct=EBI-297353, EBI-712991;
CC       Q12933:TRAF2; NbExp=3; IntAct=EBI-297353, EBI-355744;
CC       Q8K424:Trpv3 (xeno); NbExp=2; IntAct=EBI-297353, EBI-2650739;
CC       Q71U36:TUBA1A; NbExp=3; IntAct=EBI-297353, EBI-302552;
CC       P10599:TXN; NbExp=4; IntAct=EBI-297353, EBI-594644;
CC       P09936:UCHL1; NbExp=2; IntAct=EBI-297353, EBI-714860;
CC       Q9P0L0:VAPA; NbExp=2; IntAct=EBI-297353, EBI-1059156;
CC       P07947:YES1; NbExp=3; IntAct=EBI-297353, EBI-515331;
CC       P27348:YWHAQ; NbExp=6; IntAct=EBI-297353, EBI-359854;
CC       P63104:YWHAZ; NbExp=5; IntAct=EBI-297353, EBI-347088;
CC       P43403:ZAP70; NbExp=2; IntAct=EBI-297353, EBI-1211276;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17182860,
CC       ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:27153536,
CC       ECO:0000269|PubMed:2790960}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:27153536}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:27153536}; Single-pass type I membrane
CC       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,
CC       ECO:0000269|PubMed:27153536}. Endosome membrane. Nucleus
CC       {ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:20551055,
CC       ECO:0000269|PubMed:20674546}. Note=In response to EGF,
CC       translocated from the cell membrane to the nucleus via Golgi and
CC       ER (PubMed:20674546). Endocytosed upon activation by ligand
CC       (PubMed:2790960, PubMed:17182860, PubMed:27153536). Colocalized
CC       with GPER1 in the nucleus of estrogen agonist-induced cancer-
CC       associated fibroblasts (CAF) (PubMed:20551055).
CC       {ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:20674546,
CC       ECO:0000269|PubMed:27153536, 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
CC       expressed in ovarian cancers. {ECO:0000269|PubMed:17671655}.
CC   -!- PTM: Phosphorylated on Tyr residues in response to EGF
CC       (PubMed:27153536). Phosphorylation at Ser-695 is partial and
CC       occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-
CC       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.
CC       Autophosphorylation at Tyr-1197 is stimulated by methylation at
CC       Arg-1199 and enhances interaction with PTPN6. Autophosphorylation
CC       at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by
CC       PTPN1 and PTPN2. {ECO:0000269|PubMed:10523301,
CC       ECO:0000269|PubMed:12873986, ECO:0000269|PubMed:16083266,
CC       ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19836242,
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
CC       capacity but may play a role in lysosomal targeting
CC       (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-
CC       63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also
CC       occurs. Deubiquitination by OTUD7B prevents degradation.
CC       Ubiquitinated by RNF115 and RNF126 (By similarity).
CC       {ECO:0000250|UniProtKB:Q01279, ECO:0000269|PubMed:16543144,
CC       ECO:0000269|PubMed:22179831, ECO:0000269|PubMed:22298428,
CC       ECO:0000269|PubMed:27153536}.
CC   -!- PTM: Palmitoylated on Cys residues by ZDHHC20. Palmitoylation
CC       inhibits internalization after ligand binding, and increases the
CC       persistence of tyrosine-phosphorylated EGFR at the cell membrane.
CC       Palmitoylation increases the amplitude and duration of EGFR
CC       signaling. {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
CC       affecting tissues of the lung. The most common form of lung cancer
CC       is non-small cell lung cancer (NSCLC) that can be divided into 3
CC       major histologic subtypes: squamous cell carcinoma,
CC       adenocarcinoma, and large cell lung cancer. NSCLC is often
CC       diagnosed at an advanced stage and has a poor prognosis.
CC       {ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793,
CC       ECO:0000269|PubMed:16672372}. Note=The gene represented in this
CC       entry is involved in disease pathogenesis.
CC   -!- DISEASE: Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)
CC       [MIM:616069]: A disorder characterized by inflammatory features
CC       with neonatal onset, involving the skin, hair, and gut. The skin
CC       lesions involve perioral and perianal erythema, psoriasiform
CC       erythroderma, with flares of erythema, scaling, and widespread
CC       pustules. Gastrointestinal symptoms include malabsorptive diarrhea
CC       that is exacerbated by intercurrent gastrointestinal infections.
CC       The hair is short or broken, and the eyelashes and eyebrows are
CC       wiry and disorganized. {ECO:0000269|PubMed:24691054}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       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";
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; 1DNQ; Model; -; A=25-336.
DR   PDB; 1DNR; Model; -; A=337-645.
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; 2EXP; Model; -; A=311-326.
DR   PDB; 2EXQ; Model; -; A=27-536.
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   PDBsum; 1DNQ; -.
DR   PDBsum; 1DNR; -.
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; 2EXP; -.
DR   PDBsum; 2EXQ; -.
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   SMR; P00533; -.
DR   BioGrid; 108276; 1255.
DR   CORUM; P00533; -.
DR   DIP; DIP-405N; -.
DR   ELM; P00533; -.
DR   IntAct; P00533; 498.
DR   MINT; P00533; -.
DR   STRING; 9606.ENSP00000275493; -.
DR   BindingDB; P00533; -.
DR   ChEMBL; CHEMBL203; -.
DR   DrugBank; DB08916; Afatinib.
DR   DrugBank; DB00002; Cetuximab.
DR   DrugBank; DB05424; CI-1033.
DR   DrugBank; DB00530; Erlotinib.
DR   DrugBank; DB03496; Flavopiridol.
DR   DrugBank; DB00317; Gefitinib.
DR   DrugBank; DB05324; HuMax-EGFr.
DR   DrugBank; DB11737; Icotinib.
DR   DrugBank; DB04988; IGN311.
DR   DrugBank; DB05774; IMC-11F8.
DR   DrugBank; DB05900; INSM-18.
DR   DrugBank; DB01259; Lapatinib.
DR   DrugBank; DB00281; Lidocaine.
DR   DrugBank; DB05101; Matuzumab.
DR   DrugBank; DB07662; N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE.
DR   DrugBank; DB09559; Necitumumab.
DR   DrugBank; DB13164; Olmutinib.
DR   DrugBank; DB09330; Osimertinib.
DR   DrugBank; DB01269; Panitumumab.
DR   DrugBank; DB05374; Rindopepimut.
DR   DrugBank; DB07602; S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE.
DR   DrugBank; DB00072; Trastuzumab.
DR   DrugBank; DB05294; Vandetanib.
DR   GuidetoPHARMACOLOGY; 1797; -.
DR   MoonDB; P00533; Predicted.
DR   GlyConnect; 137; -.
DR   iPTMnet; P00533; -.
DR   PhosphoSitePlus; P00533; -.
DR   SwissPalm; P00533; -.
DR   UniCarbKB; P00533; -.
DR   BioMuta; EGFR; -.
DR   DMDM; 2811086; -.
DR   SWISS-2DPAGE; P00533; -.
DR   CPTAC; CPTAC-1043; -.
DR   CPTAC; CPTAC-1781; -.
DR   CPTAC; CPTAC-802; -.
DR   EPD; P00533; -.
DR   jPOST; 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; -.
DR   DNASU; 1956; -.
DR   Ensembl; ENST00000275493; ENSP00000275493; ENSG00000146648. [P00533-1]
DR   Ensembl; ENST00000342916; ENSP00000342376; ENSG00000146648. [P00533-4]
DR   Ensembl; ENST00000344576; ENSP00000345973; ENSG00000146648. [P00533-3]
DR   Ensembl; ENST00000420316; ENSP00000413843; ENSG00000146648. [P00533-2]
DR   GeneID; 1956; -.
DR   KEGG; hsa:1956; -.
DR   UCSC; uc003tqh.4; human. [P00533-1]
DR   CTD; 1956; -.
DR   DisGeNET; 1956; -.
DR   GeneCards; EGFR; -.
DR   HGNC; HGNC:3236; EGFR.
DR   HPA; CAB000035; -.
DR   HPA; CAB068186; -.
DR   HPA; CAB073534; -.
DR   HPA; HPA001200; -.
DR   HPA; HPA018530; -.
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   eggNOG; KOG1025; Eukaryota.
DR   eggNOG; ENOG410XNSR; LUCA.
DR   GeneTree; ENSGT00940000155450; -.
DR   InParanoid; P00533; -.
DR   KO; K04361; -.
DR   OMA; GYYWEYV; -.
DR   OrthoDB; 81952at2759; -.
DR   PhylomeDB; P00533; -.
DR   TreeFam; TF106002; -.
DR   BRENDA; 2.7.10.1; 2681.
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; Non-genomic estrogen signaling.
DR   Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR   Reactome; R-HSA-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR   SignaLink; P00533; -.
DR   SIGNOR; P00533; -.
DR   ChiTaRS; EGFR; human.
DR   EvolutionaryTrace; P00533; -.
DR   GeneWiki; Epidermal_growth_factor_receptor; -.
DR   GenomeRNAi; 1956; -.
DR   PMAP-CutDB; P00533; -.
DR   PRO; PR:P00533; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000146648; Expressed in 234 organ(s), highest expression level in placenta.
DR   ExpressionAtlas; P00533; baseline and differential.
DR   Genevisible; P00533; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0030665; C:clathrin-coated 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:0030139; C:endocytic vesicle; IEA:Ensembl.
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: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; IEA:Ensembl.
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:0070435; C:Shc-EGFR complex; ISS:BHF-UCL.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
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-activated receptor activity; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; NAS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
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:0043006; P:activation of phospholipase A2 activity by calcium-mediated signaling; TAS:UniProtKB.
DR   GO; GO:0007202; P:activation of phospholipase C activity; TAS:UniProtKB.
DR   GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
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:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
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:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
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:0007623; P:circadian rhythm; IEA:Ensembl.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0016101; P:diterpenoid metabolic process; 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:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
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:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl.
DR   GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR   GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0061024; P:membrane organization; TAS:Reactome.
DR   GO; GO:0007494; P:midgut development; IEA:Ensembl.
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:1901185; P:negative regulation of ERBB signaling pathway; TAS:Reactome.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0045746; P:negative regulation of Notch signaling pathway; TAS:Reactome.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; NAS:UniProtKB.
DR   GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
DR   GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
DR   GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
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:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
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:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
DR   GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl.
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:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
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:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
DR   GO; GO:0051205; P:protein insertion into membrane; TAS:UniProtKB.
DR   GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
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:0006357; P:regulation of transcription by RNA polymerase II; TAS:Reactome.
DR   GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
DR   GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
DR   GO; GO:0033594; P:response to hydroxyisoflavone; IEA:Ensembl.
DR   GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
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:0043586; P:tongue development; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:Ensembl.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR   CDD; cd00064; FU; 3.
DR   DisProt; DP00309; -.
DR   Gene3D; 3.80.20.20; -; 2.
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; Pkinase_Tyr; 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   Complete proteome; Developmental protein; Direct protein sequencing;
KW   Disease mutation; Disulfide bond; Endoplasmic reticulum; Endosome;
KW   Glycoprotein; Golgi apparatus; Host cell receptor for virus entry;
KW   Isopeptide bond; Kinase; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Polymorphism;
KW   Proto-oncogene; Receptor; Reference proteome; Repeat; Secreted;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL        1     24       {ECO:0000269|PubMed:15340161,
FT                                ECO:0000269|PubMed:6328312,
FT                                ECO:0000269|Ref.16}.
FT   CHAIN        25   1210       Epidermal growth factor receptor.
FT                                /FTId=PRO_0000016665.
FT   TOPO_DOM     25    645       Extracellular. {ECO:0000255}.
FT   TRANSMEM    646    668       Helical. {ECO:0000255}.
FT   TOPO_DOM    669   1210       Cytoplasmic. {ECO:0000255}.
FT   REPEAT       75    300       Approximate.
FT   REPEAT      390    600       Approximate.
FT   DOMAIN      712    979       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     718    726       ATP. {ECO:0000244|PDB:2GS7,
FT                                ECO:0000244|PDB:3GT8,
FT                                ECO:0000244|PDB:4ZSE,
FT                                ECO:0000244|PDB:5CNN,
FT                                ECO:0000244|PDB:5CNO,
FT                                ECO:0000244|PDB:5D41,
FT                                ECO:0000269|PubMed:19563760}.
FT   NP_BIND     790    791       ATP. {ECO:0000244|PDB:2EB3,
FT                                ECO:0000244|PDB:2GS7,
FT                                ECO:0000244|PDB:2ITN,
FT                                ECO:0000244|PDB:2ITV,
FT                                ECO:0000244|PDB:2ITX,
FT                                ECO:0000244|PDB:3GT8,
FT                                ECO:0000244|PDB:3VJN,
FT                                ECO:0000244|PDB:3VJO,
FT                                ECO:0000244|PDB:4RIW,
FT                                ECO:0000244|PDB:4RIX,
FT                                ECO:0000244|PDB:4RIY,
FT                                ECO:0000244|PDB:4ZSE,
FT                                ECO:0000244|PDB:5CNN,
FT                                ECO:0000244|PDB:5CNO,
FT                                ECO:0000244|PDB:5D41,
FT                                ECO:0000269|PubMed:17349580,
FT                                ECO:0000269|PubMed:19563760}.
FT   REGION      688    704       Important for dimerization,
FT                                phosphorylation and activation.
FT   ACT_SITE    837    837       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028}.
FT   BINDING     745    745       ATP. {ECO:0000244|PDB:2EB3,
FT                                ECO:0000244|PDB:2GS7,
FT                                ECO:0000244|PDB:2ITN,
FT                                ECO:0000244|PDB:3GT8,
FT                                ECO:0000244|PDB:3VJN,
FT                                ECO:0000244|PDB:3VJO,
FT                                ECO:0000244|PDB:4RIW,
FT                                ECO:0000244|PDB:4RIY,
FT                                ECO:0000244|PDB:4ZSE,
FT                                ECO:0000244|PDB:5CNN,
FT                                ECO:0000244|PDB:5CNO,
FT                                ECO:0000244|PDB:5D41,
FT                                ECO:0000269|PubMed:17349580,
FT                                ECO:0000269|PubMed:19563760}.
FT   BINDING     855    855       ATP. {ECO:0000244|PDB:2EB3,
FT                                ECO:0000244|PDB:2GS7,
FT                                ECO:0000244|PDB:2ITN,
FT                                ECO:0000244|PDB:2ITV,
FT                                ECO:0000244|PDB:2ITX,
FT                                ECO:0000244|PDB:3GT8,
FT                                ECO:0000244|PDB:3VJN,
FT                                ECO:0000244|PDB:4RIW,
FT                                ECO:0000244|PDB:4RIX,
FT                                ECO:0000244|PDB:4RIY,
FT                                ECO:0000244|PDB:4ZSE,
FT                                ECO:0000244|PDB:5CNN,
FT                                ECO:0000244|PDB:5CNO,
FT                                ECO:0000244|PDB:5D41,
FT                                ECO:0000269|PubMed:17349580,
FT                                ECO:0000269|PubMed:19563760}.
FT   SITE       1016   1016       Important for interaction with PIK3C2B.
FT   MOD_RES     229    229       Phosphoserine.
FT                                {ECO:0000269|PubMed:21487020}.
FT   MOD_RES     678    678       Phosphothreonine; by PKC and PKD/PRKD1.
FT                                {ECO:0000269|PubMed:10523301}.
FT   MOD_RES     693    693       Phosphothreonine; by PKD/PRKD1.
FT                                {ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163,
FT                                ECO:0000244|PubMed:24275569,
FT                                ECO:0000269|PubMed:10523301,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:3138233}.
FT   MOD_RES     695    695       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976,
FT                                ECO:0000269|PubMed:3138233}.
FT   MOD_RES     991    991       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:24275569,
FT                                ECO:0000269|PubMed:16083266}.
FT   MOD_RES     995    995       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES     998    998       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000269|PubMed:19563760}.
FT   MOD_RES    1016   1016       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:19563760}.
FT   MOD_RES    1026   1026       Phosphoserine.
FT                                {ECO:0000244|PubMed:24275569,
FT                                ECO:0000269|PubMed:16083266}.
FT   MOD_RES    1039   1039       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1041   1041       Phosphothreonine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1042   1042       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   MOD_RES    1064   1064       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1069   1069       Phosphotyrosine.
FT                                {ECO:0000305|PubMed:22888118}.
FT   MOD_RES    1070   1070       Phosphoserine.
FT                                {ECO:0000269|PubMed:3138233}.
FT   MOD_RES    1071   1071       Phosphoserine.
FT                                {ECO:0000269|PubMed:3138233}.
FT   MOD_RES    1081   1081       Phosphoserine.
FT                                {ECO:0000244|PubMed:18691976}.
FT   MOD_RES    1092   1092       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:12873986,
FT                                ECO:0000269|PubMed:27153536}.
FT   MOD_RES    1110   1110       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:12873986,
FT                                ECO:0000269|PubMed:2543678}.
FT   MOD_RES    1166   1166       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES    1172   1172       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000269|PubMed:27153536}.
FT   MOD_RES    1197   1197       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000244|PubMed:17081983,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000269|PubMed:19563760,
FT                                ECO:0000269|PubMed:19836242,
FT                                ECO:0000269|PubMed:27153536}.
FT   MOD_RES    1199   1199       Omega-N-methylarginine.
FT                                {ECO:0000269|PubMed:21258366}.
FT   LIPID      1049   1049       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:27153536}.
FT   LIPID      1146   1146       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:27153536}.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (complex)
FT                                asparagine; atypical; partial.
FT                                {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000269|PubMed:10731668,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:20837704}.
FT                                /FTId=CAR_000227.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) asparagine;
FT                                atypical. {ECO:0000244|PDB:3NJP,
FT                                ECO:0000269|PubMed:20837704}.
FT   CARBOHYD    128    128       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:8962717}.
FT   CARBOHYD    175    175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:20837704,
FT                                ECO:0000269|PubMed:8962717}.
FT   CARBOHYD    196    196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:20837704}.
FT   CARBOHYD    352    352       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000269|PubMed:10731668,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:20837704}.
FT   CARBOHYD    361    361       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000269|PubMed:10731668,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:20837704}.
FT   CARBOHYD    413    413       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:19159218,
FT                                ECO:0000269|PubMed:8962717}.
FT   CARBOHYD    444    444       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:20837704,
FT                                ECO:0000269|PubMed:8962717}.
FT   CARBOHYD    528    528       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:20837704,
FT                                ECO:0000269|PubMed:8962717}.
FT   CARBOHYD    568    568       N-linked (GlcNAc...) asparagine; partial.
FT                                {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000269|PubMed:10731668,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266,
FT                                ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    603    603       N-linked (GlcNAc...) asparagine; partial.
FT                                {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000269|PubMed:10731668,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:12731890,
FT                                ECO:0000269|PubMed:16083266}.
FT   CARBOHYD    623    623       N-linked (GlcNAc...) (high mannose)
FT                                asparagine.
FT                                {ECO:0000305|PubMed:12731890}.
FT   DISULFID     31     58       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    157    187       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    190    199       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    194    207       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    215    223       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    219    231       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    232    240       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    236    248       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    251    260       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    264    291       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    295    307       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD}.
FT   DISULFID    311    326       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3G5V,
FT                                ECO:0000244|PDB:3G5Y,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    329    333       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD}.
FT   DISULFID    337    362       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3C09,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5SX4,
FT                                ECO:0000244|PDB:5SX5,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000244|PDB:6B3S,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    470    499       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3C09,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5SX4,
FT                                ECO:0000244|PDB:5SX5,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000244|PDB:6B3S}.
FT   DISULFID    506    515       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5SX4,
FT                                ECO:0000244|PDB:5SX5,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000244|PDB:6B3S,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    510    523       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1MOX,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2U,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3C09,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3P0Y,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5SX4,
FT                                ECO:0000244|PDB:5SX5,
FT                                ECO:0000244|PDB:5WB7,
FT                                ECO:0000244|PDB:5WB8,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000244|PDB:6B3S,
FT                                ECO:0000269|PubMed:12297049,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    526    535       {ECO:0000244|PDB:1IVO,
FT                                ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRL,
FT                                ECO:0000244|PDB:4KRM,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12297050,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    539    555       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    558    571       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    562    579       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    582    591       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    595    617       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    620    628       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRO,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UIP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   DISULFID    624    636       {ECO:0000244|PDB:1NQL,
FT                                ECO:0000244|PDB:1YY9,
FT                                ECO:0000244|PDB:3B2V,
FT                                ECO:0000244|PDB:3NJP,
FT                                ECO:0000244|PDB:3QWQ,
FT                                ECO:0000244|PDB:4KRP,
FT                                ECO:0000244|PDB:4UV7,
FT                                ECO:0000244|PDB:5XWD,
FT                                ECO:0000269|PubMed:12620237,
FT                                ECO:0000269|PubMed:15837620,
FT                                ECO:0000269|PubMed:20837704}.
FT   CROSSLNK    716    716       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   CROSSLNK    737    737       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   CROSSLNK    754    754       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   CROSSLNK    867    867       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   CROSSLNK    929    929       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   CROSSLNK    970    970       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000269|PubMed:16543144}.
FT   VAR_SEQ     404    405       FL -> LS (in isoform 2).
FT                                {ECO:0000303|PubMed:7654368,
FT                                ECO:0000303|PubMed:8918811,
FT                                ECO:0000303|PubMed:9103388,
FT                                ECO:0000303|Ref.6}.
FT                                /FTId=VSP_002887.
FT   VAR_SEQ     406   1210       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7654368,
FT                                ECO:0000303|PubMed:8918811,
FT                                ECO:0000303|PubMed:9103388,
FT                                ECO:0000303|Ref.6}.
FT                                /FTId=VSP_002888.
FT   VAR_SEQ     628    705       CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFM
FT                                RRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR ->
FT                                PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESCL
FT                                GWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:11161793}.
FT                                /FTId=VSP_002889.
FT   VAR_SEQ     628    628       C -> S (in isoform 4).
FT                                {ECO:0000303|PubMed:11161793}.
FT                                /FTId=VSP_002891.
FT   VAR_SEQ     629   1210       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:11161793}.
FT                                /FTId=VSP_002892.
FT   VAR_SEQ     706   1210       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:11161793}.
FT                                /FTId=VSP_002890.
FT   VARIANT      30    297       Missing (variant EGFR vIII; found in a
FT                                lung cancer sample; somatic mutation;
FT                                induces lung cancer when exogenously
FT                                expressed).
FT                                {ECO:0000269|PubMed:16672372}.
FT                                /FTId=VAR_066493.
FT   VARIANT      98     98       R -> Q (in dbSNP:rs17289589).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_019293.
FT   VARIANT     266    266       P -> R (in dbSNP:rs17336639).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_019294.
FT   VARIANT     428    428       G -> D (in NISBD2; loss of function; the
FT                                mutant does not localize to the cell
FT                                membrane; has diffuse cytoplasmic
FT                                localization; dbSNP:rs606231253).
FT                                {ECO:0000269|PubMed:24691054}.
FT                                /FTId=VAR_072435.
FT   VARIANT     521    521       R -> K (in dbSNP:rs2227983).
FT                                {ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_019295.
FT   VARIANT     674    674       V -> I (in dbSNP:rs17337079).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_019296.
FT   VARIANT     709    709       E -> A (found in a lung cancer sample;
FT                                more sensitive to gefitinib than wild-
FT                                type; dbSNP:rs397517085).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628,
FT                                ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026084.
FT   VARIANT     709    709       E -> G (found in a lung cancer sample;
FT                                constitutively activated kinase with
FT                                higher levels of basal
FT                                autophosphorylation; more sensitive to
FT                                gefitinib than wild-type;
FT                                dbSNP:rs397517085).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628}.
FT                                /FTId=VAR_069498.
FT   VARIANT     709    709       E -> K (found in a lung cancer sample;
FT                                dbSNP:rs727504256).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026085.
FT   VARIANT     719    719       G -> A (found in a lung cancer sample;
FT                                dbSNP:rs121913428).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026086.
FT   VARIANT     719    719       G -> C (found in a lung cancer sample;
FT                                dbSNP:rs28929495).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026087.
FT   VARIANT     719    719       G -> D (found in a lung cancer sample;
FT                                dbSNP:rs121913428).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026088.
FT   VARIANT     719    719       G -> S (found in a lung cancer sample;
FT                                somatic mutation; strongly increased
FT                                kinase activity; constitutively activated
FT                                kinase with higher levels of basal
FT                                autophosphorylation; more sensitive to
FT                                gefitinib than wild-type;
FT                                dbSNP:rs28929495).
FT                                {ECO:0000269|PubMed:15118125,
FT                                ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628,
FT                                ECO:0000269|PubMed:16533793,
FT                                ECO:0000269|PubMed:17349580}.
FT                                /FTId=VAR_019297.
FT   VARIANT     724    724       G -> S (found in a lung cancer sample;
FT                                dbSNP:rs1051753269).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026089.
FT   VARIANT     734    734       E -> K (found in a lung cancer sample;
FT                                dbSNP:rs121913420).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026090.
FT   VARIANT     746    752       ELREATS -> D (found in a lung cancer
FT                                sample). {ECO:0000269|PubMed:15623594}.
FT                                /FTId=VAR_069499.
FT   VARIANT     746    751       ELREAT -> A (found in a lung cancer
FT                                sample). {ECO:0000269|PubMed:15623594}.
FT                                /FTId=VAR_069500.
FT   VARIANT     746    750       Missing (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:15623594}.
FT                                /FTId=VAR_026092.
FT   VARIANT     746    746       Missing (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026091.
FT   VARIANT     747    751       Missing (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:15623594}.
FT                                /FTId=VAR_069501.
FT   VARIANT     747    749       Missing (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026094.
FT   VARIANT     747    747       L -> F (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026093.
FT   VARIANT     748    748       R -> P (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026095.
FT   VARIANT     752    759       Missing (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026096.
FT   VARIANT     768    768       S -> I (found in a lung cancer sample;
FT                                constitutively activated kinase with
FT                                higher levels of basal
FT                                autophosphorylation; more sensitive to
FT                                gefitinib than wild-type;
FT                                dbSNP:rs121913465).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628}.
FT                                /FTId=VAR_069502.
FT   VARIANT     769    769       V -> M (found in a lung cancer sample;
FT                                dbSNP:rs147149347).
FT                                {ECO:0000269|PubMed:15623594}.
FT                                /FTId=VAR_069503.
FT   VARIANT     787    787       Q -> R (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026097.
FT   VARIANT     790    790       T -> M (found in a lung cancer sample;
FT                                increased kinase activity;
FT                                dbSNP:rs121434569).
FT                                {ECO:0000269|PubMed:16533793,
FT                                ECO:0000269|PubMed:18227510}.
FT                                /FTId=VAR_026098.
FT   VARIANT     833    833       L -> V (found in a lung cancer sample;
FT                                more sensitive to gefitinib than wild-
FT                                type; dbSNP:rs397517126).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628,
FT                                ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026099.
FT   VARIANT     834    834       V -> L (found in a lung cancer sample;
FT                                dbSNP:rs397517127).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026100.
FT   VARIANT     835    835       H -> L (found in a lung cancer sample;
FT                                more sensitive to gefitinib than wild-
FT                                type; dbSNP:rs397517128).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628}.
FT                                /FTId=VAR_069504.
FT   VARIANT     838    838       L -> V (found in a lung cancer sample;
FT                                more sensitive to gefitinib than wild-
FT                                type; dbSNP:rs864621996).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628}.
FT                                /FTId=VAR_069505.
FT   VARIANT     858    858       L -> M (found in a lung cancer sample;
FT                                dbSNP:rs121913443).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026101.
FT   VARIANT     858    858       L -> R (found in a lung cancer sample;
FT                                somatic mutation; constitutively
FT                                activated enzyme with strongly increased
FT                                kinase activity; more sensitive to
FT                                gefitinib than wild-type;
FT                                dbSNP:rs121434568).
FT                                {ECO:0000269|PubMed:15118125,
FT                                ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628,
FT                                ECO:0000269|PubMed:16533793,
FT                                ECO:0000269|PubMed:17349580}.
FT                                /FTId=VAR_019298.
FT   VARIANT     861    861       L -> Q (found in a lung cancer sample;
FT                                constitutively activated kinase with
FT                                higher levels of basal
FT                                autophosphorylation; more sensitive to
FT                                gefitinib than wild-type;
FT                                dbSNP:rs121913444).
FT                                {ECO:0000269|PubMed:15623594,
FT                                ECO:0000269|PubMed:16205628,
FT                                ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026102.
FT   VARIANT     873    873       G -> E (found in a lung cancer sample).
FT                                {ECO:0000269|PubMed:16533793}.
FT                                /FTId=VAR_026103.
FT   VARIANT     962    962       R -> G (in dbSNP:rs17337451).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_019299.
FT   VARIANT     988    988       H -> P (in dbSNP:rs17290699).
FT                                {ECO:0000269|Ref.7}.
FT                                /FTId=VAR_019300.
FT   VARIANT    1034   1034       L -> R (in dbSNP:rs34352568).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042095.
FT   VARIANT    1210   1210       A -> V (in dbSNP:rs35918369).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042096.
FT   MUTAGEN     275    275       Y->A: Strongly reduced
FT                                autophosphorylation and activation of
FT                                downstream kinases; when associated with
FT                                A-309. {ECO:0000269|PubMed:12297050}.
FT   MUTAGEN     287    287       F->A: Strongly reduced
FT                                autophosphorylation and activation of
FT                                downstream kinases; when associated with
FT                                A-309. {ECO:0000269|PubMed:12297050}.
FT   MUTAGEN     309    309       R->S: Strongly reduced
FT                                autophosphorylation and activation of
FT                                downstream kinases; when associated with
FT                                A-275. Strongly reduced
FT                                autophosphorylation and activation of
FT                                downstream kinases; when associated with
FT                                A-287. {ECO:0000269|PubMed:12297050}.
FT   MUTAGEN     429    429       R->E: Abolishes autophosphorylation and
FT                                activation of downstream kinases.
FT                                {ECO:0000269|PubMed:12297050}.
FT   MUTAGEN     587    590       DGPH->AGPA: Decreases intramolecular
FT                                interactions and facilitates EGF binding.
FT                                {ECO:0000269|PubMed:12620237}.
FT   MUTAGEN     609    609       K->A: Decreases intramolecular
FT                                interactions and facilitates EGF binding.
FT                                {ECO:0000269|PubMed:12620237}.
FT   MUTAGEN     688    688       L->A: Strongly reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19560417,
FT                                ECO:0000269|PubMed:19563760}.
FT   MUTAGEN     689    689       V->A: Reduced autophosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     689    689       V->M: Constitutively activated kinase.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     690    690       E->A: Reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19560417,
FT                                ECO:0000269|PubMed:19563760}.
FT   MUTAGEN     692    692       L->A,P: Strongly reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19560417,
FT                                ECO:0000269|PubMed:19563760}.
FT   MUTAGEN     693    693       T->A: Increased phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     693    693       T->D: Strongly reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     694    694       P->A: Strongly reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     699    699       P->A: Reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     700    700       N->A: Abolishes phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     704    704       L->A: Abolishes phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     705    705       R->A: Abolishes phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     706    706       I->A: Abolishes phosphorylation.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     745    745       K->A,M: Abolishes kinase activity.
FT                                {ECO:0000269|PubMed:19560417}.
FT   MUTAGEN     974    974       D->A: Strongly reduced phosphorylation.
FT   MUTAGEN     977    977       R->A: Reduced phosphorylation.
FT                                {ECO:0000269|PubMed:19563760}.
FT   MUTAGEN    1005   1006       ED->RK: Constitutively activated kinase.
FT                                {ECO:0000269|PubMed:19563760}.
FT   MUTAGEN    1016   1016       Y->F: 50% decrease in interaction with
FT                                PIK3C2B. 65% decrease in interaction with
FT                                PIK3C2B; when associated with F-1197.
FT                                Abolishes interaction with PIK3C2B; when
FT                                associated with F-1197 and F-1092.
FT                                {ECO:0000269|PubMed:10805725}.
FT   MUTAGEN    1048   1210       Missing: Abolishes palmitoylation.
FT                                {ECO:0000269|PubMed:27153536}.
FT   MUTAGEN    1049   1049       C->A: Decreased palmitoylation.
FT                                {ECO:0000269|PubMed:27153536}.
FT   MUTAGEN    1067   1067       Q->G: No effect on interaction with CBLC.
FT                                {ECO:0000269|PubMed:22888118}.
FT   MUTAGEN    1068   1068       R->G: Strongly decreases interaction with
FT                                CBLC. {ECO:0000269|PubMed:22888118}.
FT   MUTAGEN    1069   1069       Y->F: Abolishes interaction with CBLC.
FT                                {ECO:0000269|PubMed:22888118}.
FT   MUTAGEN    1092   1092       Y->F: No change in interaction with
FT                                PIK3C2B. Abolishes interaction with
FT                                PIK3C2B; when associated with F-1197 and
FT                                F-1016. {ECO:0000269|PubMed:10805725}.
FT   MUTAGEN    1110   1110       Y->F: No change in interaction with
FT                                PIK3C2B. {ECO:0000269|PubMed:10805725}.
FT   MUTAGEN    1146   1146       C->A: Decreased palmitoylation.
FT                                {ECO:0000269|PubMed:27153536}.
FT   MUTAGEN    1172   1172       Y->F: No change in interaction with
FT                                PIK3C2B. {ECO:0000269|PubMed:10805725}.
FT   MUTAGEN    1197   1197       Y->F: No change in interaction with
FT                                PIK3C2B. 65% decrease in interaction with
FT                                PIK3C2B; when associated with F-1016.
FT                                Abolishes interaction with PIK3C2B; when
FT                                associated with F-1092 and F-1016.
FT                                {ECO:0000269|PubMed:10805725}.
FT   CONFLICT    540    540       N -> K (in Ref. 1; CAA25240).
FT                                {ECO:0000305}.
FT   STRAND       40     43       {ECO:0000244|PDB:3QWQ}.
FT   HELIX        44     55       {ECO:0000244|PDB:4UV7}.
FT   STRAND       60     69       {ECO:0000244|PDB:4UV7}.
FT   HELIX        77     81       {ECO:0000244|PDB:4UV7}.
FT   STRAND       84     87       {ECO:0000244|PDB:4UV7}.
FT   STRAND       89     93       {ECO:0000244|PDB:4UV7}.
FT   HELIX       101    103       {ECO:0000244|PDB:1IVO}.
FT   TURN        114    116       {ECO:0000244|PDB:4UV7}.
FT   STRAND      117    122       {ECO:0000244|PDB:4UV7}.
FT   STRAND      125    129       {ECO:0000244|PDB:1MOX}.
FT   STRAND      145    152       {ECO:0000244|PDB:4UV7}.
FT   HELIX       159    161       {ECO:0000244|PDB:4UV7}.
FT   HELIX       164    166       {ECO:0000244|PDB:4UV7}.
FT   HELIX       170    173       {ECO:0000244|PDB:1MOX}.
FT   STRAND      183    185       {ECO:0000244|PDB:5XWD}.
FT   HELIX       195    197       {ECO:0000244|PDB:4UV7}.
FT   STRAND      199    204       {ECO:0000244|PDB:4UV7}.
FT   STRAND      211    214       {ECO:0000244|PDB:1MOX}.
FT   STRAND      217    221       {ECO:0000244|PDB:5XWD}.
FT   STRAND      223    227       {ECO:0000244|PDB:4UV7}.
FT   HELIX       228    230       {ECO:0000244|PDB:4UV7}.
FT   STRAND      236    238       {ECO:0000244|PDB:4UV7}.
FT   STRAND      240    244       {ECO:0000244|PDB:4UV7}.
FT   TURN        245    247       {ECO:0000244|PDB:4UV7}.
FT   STRAND      248    256       {ECO:0000244|PDB:4UV7}.
FT   STRAND      259    263       {ECO:0000244|PDB:4UV7}.
FT   STRAND      267    271       {ECO:0000244|PDB:4UV7}.
FT   TURN        272    275       {ECO:0000244|PDB:4UV7}.
FT   STRAND      276    279       {ECO:0000244|PDB:4UV7}.
FT   STRAND      285    287       {ECO:0000244|PDB:4UV7}.
FT   STRAND      290    294       {ECO:0000244|PDB:4UV7}.
FT   TURN        296    298       {ECO:0000244|PDB:3B2V}.
FT   STRAND      299    301       {ECO:0000244|PDB:5WB7}.
FT   STRAND      303    305       {ECO:0000244|PDB:4KRP}.
FT   STRAND      306    310       {ECO:0000244|PDB:4UV7}.
FT   STRAND      313    315       {ECO:0000244|PDB:3B2V}.
FT   STRAND      318    320       {ECO:0000244|PDB:3G5Y}.
FT   STRAND      323    325       {ECO:0000244|PDB:3G5Y}.
FT   STRAND      330    332       {ECO:0000244|PDB:4UV7}.
FT   STRAND      336    338       {ECO:0000244|PDB:3P0Y}.
FT   TURN        340    342       {ECO:0000244|PDB:3QWQ}.
FT   HELIX       343    345       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      349    351       {ECO:0000244|PDB:3P0Y}.
FT   TURN        353    355       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       356    359       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      363    367       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      369    371       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       373    377       {ECO:0000244|PDB:3P0Y}.
FT   TURN        380    383       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       389    397       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      400    403       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      405    407       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       418    420       {ECO:0000244|PDB:3P0Y}.
FT   TURN        433    435       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      436    442       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      458    464       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       472    474       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       477    480       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      481    483       {ECO:0000244|PDB:1YY9}.
FT   STRAND      488    494       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       496    501       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      508    510       {ECO:0000244|PDB:5SX4}.
FT   STRAND      515    519       {ECO:0000244|PDB:3P0Y}.
FT   HELIX       520    522       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      523    526       {ECO:0000244|PDB:3P0Y}.
FT   STRAND      531    533       {ECO:0000244|PDB:4KRL}.
FT   STRAND      535    537       {ECO:0000244|PDB:1YY9}.
FT   STRAND      540    546       {ECO:0000244|PDB:4UV7}.
FT   STRAND      548    551       {ECO:0000244|PDB:4UV7}.
FT   STRAND      554    557       {ECO:0000244|PDB:4UV7}.
FT   STRAND      560    562       {ECO:0000244|PDB:4KRO}.
FT   STRAND      566    568       {ECO:0000244|PDB:1YY9}.
FT   STRAND      570    575       {ECO:0000244|PDB:4UV7}.
FT   STRAND      578    587       {ECO:0000244|PDB:4UV7}.
FT   STRAND      590    594       {ECO:0000244|PDB:4UV7}.
FT   STRAND      597    602       {ECO:0000244|PDB:4UV7}.
FT   STRAND      606    611       {ECO:0000244|PDB:4UV7}.
FT   STRAND      615    619       {ECO:0000244|PDB:4UV7}.
FT   STRAND      629    632       {ECO:0000244|PDB:4UV7}.
FT   HELIX       633    635       {ECO:0000244|PDB:4UV7}.
FT   STRAND      643    646       {ECO:0000244|PDB:2KS1}.
FT   HELIX       648    669       {ECO:0000244|PDB:2KS1}.
FT   STRAND      671    673       {ECO:0000244|PDB:1Z9I}.
FT   HELIX       679    684       {ECO:0000244|PDB:3GOP}.
FT   HELIX       685    687       {ECO:0000244|PDB:3GOP}.
FT   STRAND      688    692       {ECO:0000244|PDB:1Z9I}.
FT   STRAND      694    697       {ECO:0000244|PDB:1Z9I}.
FT   STRAND      703    706       {ECO:0000244|PDB:3POZ}.
FT   HELIX       709    711       {ECO:0000244|PDB:5UG9}.
FT   STRAND      712    721       {ECO:0000244|PDB:5UG9}.
FT   STRAND      724    731       {ECO:0000244|PDB:5UG9}.
FT   TURN        734    736       {ECO:0000244|PDB:5UG9}.
FT   STRAND      740    747       {ECO:0000244|PDB:5UG9}.
FT   STRAND      748    750       {ECO:0000244|PDB:2ITU}.
FT   TURN        753    755       {ECO:0000244|PDB:3W2S}.
FT   HELIX       756    767       {ECO:0000244|PDB:5UG9}.
FT   STRAND      772    774       {ECO:0000244|PDB:4I21}.
FT   STRAND      777    791       {ECO:0000244|PDB:5UG9}.
FT   STRAND      794    797       {ECO:0000244|PDB:5ZWJ}.
FT   HELIX       798    804       {ECO:0000244|PDB:5UG9}.
FT   HELIX       806    808       {ECO:0000244|PDB:5UG9}.
FT   HELIX       811    830       {ECO:0000244|PDB:5UG9}.
FT   HELIX       840    842       {ECO:0000244|PDB:5UG9}.
FT   STRAND      843    847       {ECO:0000244|PDB:5UG9}.
FT   STRAND      850    853       {ECO:0000244|PDB:5UG9}.
FT   HELIX       858    862       {ECO:0000244|PDB:3POZ}.
FT   TURN        863    865       {ECO:0000244|PDB:3POZ}.
FT   STRAND      867    870       {ECO:0000244|PDB:5UG9}.
FT   STRAND      871    875       {ECO:0000244|PDB:5X2A}.
FT   HELIX       878    880       {ECO:0000244|PDB:5UG9}.
FT   HELIX       883    888       {ECO:0000244|PDB:5UG9}.
FT   HELIX       893    908       {ECO:0000244|PDB:5UG9}.
FT   TURN        909    911       {ECO:0000244|PDB:2GS7}.
FT   TURN        914    917       {ECO:0000244|PDB:5UG9}.
FT   HELIX       920    922       {ECO:0000244|PDB:5UG9}.
FT   HELIX       923    928       {ECO:0000244|PDB:5UG9}.
FT   STRAND      937    939       {ECO:0000244|PDB:5ZWJ}.
FT   HELIX       941    950       {ECO:0000244|PDB:5UG9}.
FT   STRAND      951    953       {ECO:0000244|PDB:5JEB}.
FT   HELIX       955    957       {ECO:0000244|PDB:5UG9}.
FT   HELIX       961    972       {ECO:0000244|PDB:5UG9}.
FT   HELIX       975    977       {ECO:0000244|PDB:5UG9}.
FT   HELIX       984    986       {ECO:0000244|PDB:5HG8}.
FT   TURN        992    998       {ECO:0000244|PDB:5HG8}.
FT   STRAND     1004   1010       {ECO:0000244|PDB:3W2S}.
FT   HELIX      1013   1016       {ECO:0000244|PDB:3POZ}.
FT   STRAND     1068   1070       {ECO:0000244|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
//
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