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Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)

 EGFR_HUMAN              Reviewed;        1210 AA.
P00533; O00688; O00732; P06268; Q14225; Q68GS5; Q92795; Q9BZS2;
Q9GZX1; Q9H2C9; Q9H3C9; Q9UMD7; Q9UMD8; Q9UMG5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 246.
RecName: Full=Epidermal growth factor receptor;
EC=2.7.10.1;
AltName: Full=Proto-oncogene c-ErbB-1;
AltName: Full=Receptor tyrosine-protein kinase erbB-1;
Flags: Precursor;
Name=EGFR; Synonyms=ERBB, ERBB1, HER1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=6328312; DOI=10.1038/309418a0;
Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W.,
Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J.,
Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.;
"Human epidermal growth factor receptor cDNA sequence and aberrant
expression of the amplified gene in A431 epidermoid carcinoma cells.";
Nature 309:418-425(1984).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=7654368; DOI=10.1002/mrd.1080410205;
Ilekis J.V., Stark B.C., Scoccia B.;
"Possible role of variant RNA transcripts in the regulation of
epidermal growth factor receptor expression in human placenta.";
Mol. Reprod. Dev. 41:149-156(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=8918811; DOI=10.1093/nar/24.20.4050;
Reiter J.L., Maihle N.J.;
"A 1.8 kb alternative transcript from the human epidermal growth
factor receptor gene encodes a truncated form of the receptor.";
Nucleic Acids Res. 24:4050-4056(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=9103388; DOI=10.1006/gyno.1996.4526;
Ilekis J.V., Gariti J., Niederberger C., Scoccia B.;
"Expression of a truncated epidermal growth factor receptor-like
protein (TEGFR) in ovarian cancer.";
Gynecol. Oncol. 65:36-41(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4).
TISSUE=Placenta;
PubMed=11161793; DOI=10.1006/geno.2000.6341;
Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J.,
Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L.,
Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D.,
Maihle N.J.;
"Comparative genomic sequence analysis and isolation of human and
mouse alternative EGFR transcripts encoding truncated receptor
isoforms.";
Genomics 71:1-20(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Xu L., Hong A., He X.;
"Cloning of the cDNA for a short EGF receptor from human placenta.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-98; ARG-266;
LYS-521; ILE-674; GLY-962 AND PRO-988.
NIEHS SNPs program;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-687.
Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M.,
Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R.,
Maihle N.J.;
"Human and mouse alternative EGFR transcripts encoding only the
extracellular domain of the receptor.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 713-924.
PubMed=6326261; DOI=10.1126/science.6326261;
Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M.,
Verma I.M., Gill G.N., Rosenfeld M.G.;
"Expression cloning of human EGF receptor complementary DNA: gene
amplification and three related messenger RNA products in A431
cells.";
Science 224:843-848(1984).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 150-962.
PubMed=6330563; DOI=10.1038/309806a0;
Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P.,
Roe B.A., Merlino G.T., Pastan I.;
"Human epidermal growth factor receptor cDNA is homologous to a
variety of RNAs overproduced in A431 carcinoma cells.";
Nature 309:806-810(1984).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1210.
PubMed=6093780; DOI=10.1016/0006-291X(84)90926-4;
Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G.,
O'Malley B.W.;
"Isolation of an evolutionarily conserved epidermal growth factor
receptor cDNA from human A431 carcinoma cells.";
Biochem. Biophys. Res. Commun. 124:125-132(1984).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
PubMed=3329716;
Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A.,
Waterfield M.D.;
"The human EGF receptor gene: structure of the 110 kb locus and
identification of sequences regulating its transcription.";
Oncogene Res. 1:375-396(1987).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
PubMed=1988448;
Haley J.D., Waterfield M.D.;
"Contributory effects of de novo transcription and premature
transcript termination in the regulation of human epidermal growth
factor receptor proto-oncogene RNA synthesis.";
J. Biol. Chem. 266:1746-1753(1991).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
PubMed=2991899; DOI=10.1073/pnas.82.15.4920;
Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.;
"Characterization and sequence of the promoter region of the human
epidermal growth factor receptor gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-49.
PubMed=6324343; DOI=10.1126/science.6324343;
Weber W., Gill G.N., Spiess J.;
"Production of an epidermal growth factor receptor-related protein.";
Science 224:294-297(1984).
[16]
PROTEIN SEQUENCE OF 540.
Kohda D.;
Submitted (SEP-1997) to UniProtKB.
[17]
PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND
1068-1077, AND PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND
SER-1071.
PubMed=3138233;
Heisermann G.J., Gill G.N.;
"Epidermal growth factor receptor threonine and serine residues
phosphorylated in vivo.";
J. Biol. Chem. 263:13152-13158(1988).
[18]
PROTEIN SEQUENCE OF 25-39.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[19]
PROTEIN SEQUENCE OF 740-744 AND 746-747.
PubMed=2985580;
Russo M.W., Lukas T.J., Cohen S., Staros J.V.;
"Identification of residues in the nucleotide binding site of the
epidermal growth factor receptor/kinase.";
J. Biol. Chem. 260:5205-5208(1985).
[20]
PROTEIN SEQUENCE OF 861-875 AND 914-932, UBIQUITINATION AT LYS-716;
LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
"Differential regulation of EGF receptor internalization and
degradation by multiubiquitination within the kinase domain.";
Mol. Cell 21:737-748(2006).
[21]
PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
PubMed=9556602; DOI=10.1074/jbc.273.18.11150;
Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.;
"Disulfide bond structure of human epidermal growth factor receptor.";
J. Biol. Chem. 273:11150-11157(1998).
[22]
RECEPTOR ACTIVITY.
PubMed=6325948; DOI=10.1038/309270a0;
Mroczkowski B., Mosig G., Cohen S.;
"ATP-stimulated interaction between epidermal growth factor receptor
and supercoiled DNA.";
Nature 309:270-273(1984).
[23]
REVIEW.
PubMed=3039909; DOI=10.1146/annurev.bi.56.070187.004313;
Carpenter G.;
"Receptors for epidermal growth factor and other polypeptide
mitogens.";
Annu. Rev. Biochem. 56:881-914(1987).
[24]
LIGAND-BINDING.
PubMed=2790960; DOI=10.1016/0092-8674(89)90867-2;
Chen W.S., Lazar C.S., Lund K.A., Welsh J.B., Chang C.P., Walton G.M.,
Der C.J., Wiley H.S., Gill G.N., Rosenfeld M.G.;
"Functional independence of the epidermal growth factor receptor from
a domain required for ligand-induced internalization and calcium
regulation.";
Cell 59:33-43(1989).
[25]
PHOSPHORYLATION AT TYR-1110.
PubMed=2543678;
Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M.,
Howk R., Givol D., Ullrich A., Schlessinger J.;
"All autophosphorylation sites of epidermal growth factor (EGF)
receptor and HER2/neu are located in their carboxyl-terminal tails.
Identification of a novel site in EGF receptor.";
J. Biol. Chem. 264:10667-10671(1989).
[26]
IDENTIFICATION OF AMPHIREGULIN AS LIGAND.
PubMed=7679104;
Johnson G.R., Kannan B., Shoyab M., Stromberg K.;
"Amphiregulin induces tyrosine phosphorylation of the epidermal growth
factor receptor and p185erbB2. Evidence that amphiregulin acts
exclusively through the epidermal growth factor receptor at the
surface of human epithelial cells.";
J. Biol. Chem. 268:2924-2931(1993).
[27]
INTERACTION WITH ZPR1.
PubMed=8650580; DOI=10.1126/science.272.5269.1797;
Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G.,
Barrett T., Davis R.J.;
"Binding of zinc finger protein ZPR1 to the epidermal growth factor
receptor.";
Science 272:1797-1802(1996).
[28]
INTERACTION WITH ZPR1.
PubMed=9852145; DOI=10.1083/jcb.143.6.1471;
Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.;
"Interaction of ZPR1 with translation elongation factor-1alpha in
proliferating cells.";
J. Cell Biol. 143:1471-1484(1998).
[29]
PHOSPHORYLATION AT THR-678 AND THR-693.
PubMed=10523301; DOI=10.1093/emboj/18.20.5567;
Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.;
"Cell-type specific phosphorylation of threonines T654 and T669 by PKD
defines the signal capacity of the EGF receptor.";
EMBO J. 18:5567-5576(1999).
[30]
IDENTIFICATION OF BETACELLULIN/BTC AS LIGAND.
PubMed=8144591;
Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J.,
Igarashi K., Sasada R.;
"Recombinant human betacellulin. Molecular structure, biological
activities, and receptor interaction.";
J. Biol. Chem. 269:9966-9973(1994).
[31]
FUNCTION IN PHOSPHORYLATION OF CBL, AND INTERACTION WITH CBL.
PubMed=7657591; DOI=10.1074/jbc.270.35.20242;
Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.;
"Tyrosine phosphorylation of the c-cbl proto-oncogene protein product
and association with epidermal growth factor (EGF) receptor upon EGF
stimulation.";
J. Biol. Chem. 270:20242-20245(1995).
[32]
GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
PubMed=8962717; DOI=10.3109/08977199609034572;
Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.;
"Analysis of the glycosylation patterns of the extracellular domain of
the epidermal growth factor receptor expressed in Chinese hamster
ovary fibroblasts.";
Growth Factors 13:121-132(1996).
[33]
IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND.
PubMed=9419975; DOI=10.1038/sj.onc.1201458;
Komurasaki T., Toyoda H., Uchida D., Morimoto S.;
"Epiregulin binds to epidermal growth factor receptor and ErbB-4 and
induces tyrosine phosphorylation of epidermal growth factor receptor,
ErbB-2, ErbB-3 and ErbB-4.";
Oncogene 15:2841-2848(1997).
[34]
PHOSPHORYLATION, AND DEPHOSPHORYLATION BY PTPN1 AND PTPN2.
PubMed=9488479; DOI=10.1128/MCB.18.3.1622;
Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.;
"Epidermal growth factor receptor and the adaptor protein p52Shc are
specific substrates of T-cell protein tyrosine phosphatase.";
Mol. Cell. Biol. 18:1622-1634(1998).
[35]
INTERACTION WITH AP2M1.
PubMed=10228163; DOI=10.1093/emboj/18.9.2489;
Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.;
"Inhibition of the receptor-binding function of clathrin adaptor
protein AP-2 by dominant-negative mutant mu2 subunit and its effects
on endocytosis.";
EMBO J. 18:2489-2499(1999).
[36]
INTERACTION WITH GRB2; NCK1 AND NCK2.
PubMed=10026169; DOI=10.1074/jbc.274.9.5542;
Braverman L.E., Quilliam L.A.;
"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-
containing adapter protein having similar binding and biological
properties to Nck.";
J. Biol. Chem. 274:5542-5549(1999).
[37]
GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
PubMed=10731668; DOI=10.1093/oxfordjournals.jbchem.a022585;
Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.;
"Characterization of the N-oligosaccharides attached to the atypical
Asn-X-Cys sequence of recombinant human epidermal growth factor
receptor.";
J. Biochem. 127:65-72(2000).
[38]
FUNCTION IN PHOSPHORYLATION OF RGS16.
PubMed=11602604; DOI=10.1074/jbc.M108862200;
Derrien A., Druey K.M.;
"RGS16 function is regulated by epidermal growth factor receptor-
mediated tyrosine phosphorylation.";
J. Biol. Chem. 276:48532-48538(2001).
[39]
GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;
ASN-413; ASN-444; ASN-528; ASN-568; ASN-603 AND ASN-623.
PubMed=12731890; DOI=10.1021/bi027101p;
Zhen Y., Caprioli R.M., Staros J.V.;
"Characterization of glycosylation sites of the epidermal growth
factor receptor.";
Biochemistry 42:5478-5492(2003).
[40]
FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, AND
PHOSPHORYLATION AT TYR-1092 AND TYR-1110.
PubMed=12873986;
Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.;
"Identification and characterization of signal transducer and
activator of transcription 3 recruitment sites within the epidermal
growth factor receptor.";
Cancer Res. 63:3923-3930(2003).
[41]
ENZYME REGULATION, AND INTERACTION WITH LRIG1.
PubMed=15282549; DOI=10.1038/sj.emboj.7600342;
Gur G., Rubin C., Katz M., Amit I., Citri A., Nilsson J.,
Amariglio N., Henriksson R., Rechavi G., Hedman H., Wides R.,
Yarden Y.;
"LRIG1 restricts growth factor signaling by enhancing receptor
ubiquitylation and degradation.";
EMBO J. 23:3270-3281(2004).
[42]
FUNCTION IN EGFR SIGNALING, IDENTIFICATION IN A COMPLEX WITH PIK3C2A
AND ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2,
INTERACTION WITH PIK3C2B, AND MUTAGENESIS OF TYR-1016; TYR-1092;
TYR-1110; TYR-1172 AND TYR-1197.
PubMed=10805725; DOI=10.1128/MCB.20.11.3817-3830.2000;
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D.,
Domin J.;
"Class II phosphoinositide 3-kinases are downstream targets of
activated polypeptide growth factor receptors.";
Mol. Cell. Biol. 20:3817-3830(2000).
[43]
FUNCTION IN NF-KAPPA-B ACTIVATION, AND INTERACTION WITH RIPK1.
PubMed=11116146; DOI=10.1074/jbc.M008458200;
Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S.,
Vartanian T.;
"The epidermal growth factor receptor engages receptor interacting
protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to
activate NF-kappa B. Identification of a novel receptor-tyrosine
kinase signalosome.";
J. Biol. Chem. 276:8865-8874(2001).
[44]
FUNCTION IN PHOSPHORYLATION OF MUC1, AND INTERACTION WITH MUC1.
PubMed=11483589; DOI=10.1074/jbc.C100359200;
Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III,
Kufe D.;
"The epidermal growth factor receptor regulates interaction of the
human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin.";
J. Biol. Chem. 276:35239-35242(2001).
[45]
ENZYME REGULATION, AND INTERACTION WITH SOCS5.
PubMed=15590694; DOI=10.1074/jbc.M408575200;
Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N.,
Rechavi G., Yarden Y.;
"Suppressors of cytokine signaling 4 and 5 regulate epidermal growth
factor receptor signaling.";
J. Biol. Chem. 280:7038-7048(2005).
[46]
IDENTIFICATION OF EPIGEN/EPGN AS A LIGAND.
PubMed=15611079; DOI=10.1074/jbc.M413919200;
Kochupurakkal B.S., Harari D., Di-Segni A., Maik-Rachline G.,
Lyass L., Gur G., Kerber G., Citri A., Lavi S., Eilam R.,
Chalifa-Caspi V., Eshhar Z., Pikarsky E., Pinkas-Kramarski R.,
Bacus S.S., Yarden Y.;
"Epigen, the last ligand of ErbB receptors, reveals intricate
relationships between affinity and mitogenicity.";
J. Biol. Chem. 280:8503-8512(2005).
[47]
GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361;
ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION AT
THR-693; SER-991 AND SER-1026, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16083266; DOI=10.1021/pr050113n;
Wu S.L., Kim J., Hancock W.S., Karger B.;
"Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS
platform for high sequence coverage of complex proteins with extensive
post-translational modifications-comprehensive analysis of beta-casein
and epidermal growth factor receptor (EGFR).";
J. Proteome Res. 4:1155-1170(2005).
[48]
INTERACTION WITH PELP1.
PubMed=16140940; DOI=10.1158/0008-5472.CAN-05-0614;
Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z.,
Sahin A.A., Kumar R.;
"Functional implications of altered subcellular localization of PELP1
in breast cancer cells.";
Cancer Res. 65:7724-7732(2005).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1172 AND TYR-1197, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[50]
FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION,
INTERACTION WITH PCNA, AND SUBCELLULAR LOCATION.
PubMed=17115032; DOI=10.1038/ncb1501;
Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C.,
McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.;
"Tyrosine phosphorylation controls PCNA function through protein
stability.";
Nat. Cell Biol. 8:1359-1368(2006).
[51]
TISSUE SPECIFICITY.
PubMed=17671655; DOI=10.1172/JCI31680;
Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D.,
Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E.,
Hoenderop J.G., Knoers N.V., Bindels R.J.;
"Impaired basolateral sorting of pro-EGF causes isolated recessive
renal hypomagnesemia.";
J. Clin. Invest. 117:2260-2267(2007).
[52]
INTERACTION WITH TNF2, AND SUBCELLULAR LOCATION.
PubMed=17182860; DOI=10.1091/mbc.E06-02-0142;
Shen F., Lin Q., Gu Y., Childress C., Yang W.;
"Activated Cdc42-associated kinase 1 is a component of EGF receptor
signaling complex and regulates EGF receptor degradation.";
Mol. Biol. Cell 18:732-742(2007).
[53]
INTERACTION WITH ATX2.
PubMed=18602463; DOI=10.1016/j.cellsig.2008.05.018;
Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J.,
Auburger G.;
"Ataxin-2 associates with the endocytosis complex and affects EGF
receptor trafficking.";
Cell. Signal. 20:1725-1739(2008).
[54]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[55]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[56]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-1064;
SER-1081; SER-1166 AND TYR-1197, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[57]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; SER-995; TYR-998;
SER-1039; THR-1041; SER-1042; SER-1064 AND SER-1166, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[58]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[59]
ENZYME REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197,
DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, AND INTERACTION WITH
CBL AND GRB2.
PubMed=19836242; DOI=10.1016/j.cub.2009.09.048;
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F.,
Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.;
"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase
controlling EGFR endocytosis.";
Curr. Biol. 19:1788-1798(2009).
[60]
INTERACTION WITH GAREM1.
PubMed=19509291; DOI=10.1074/jbc.M109.021139;
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E.,
Taniguchi H., Konishi H.;
"GAREM, a novel adaptor protein for growth factor receptor-bound
protein 2, contributes to cellular transformation through the
activation of extracellular signal-regulated kinase signaling.";
J. Biol. Chem. 284:20206-20214(2009).
[61]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[63]
INTERACTION WITH GPER1.
PubMed=19749156; DOI=10.1210/me.2009-0120;
Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S.,
De Amicis F., Fuqua S.A., Ando S., Maggiolini M.;
"G protein-coupled receptor 30 expression is up-regulated by EGF and
TGF alpha in estrogen receptor alpha-positive cancer cells.";
Mol. Endocrinol. 23:1815-1826(2009).
[64]
INTERACTION WITH COPG1, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=20674546; DOI=10.1016/j.bbrc.2010.07.096;
Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.;
"COPI-mediated retrograde trafficking from the Golgi to the ER
regulates EGFR nuclear transport.";
Biochem. Biophys. Res. Commun. 399:498-504(2010).
[65]
INTERACTION WITH GPER1, AND SUBCELLULAR LOCATION.
PubMed=20551055; DOI=10.1158/0008-5472.CAN-10-0408;
Madeo A., Maggiolini M.;
"Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-
induced gene expression and migration in breast cancer-associated
fibroblasts.";
Cancer Res. 70:6036-6046(2010).
[66]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1064
AND TYR-1197, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[67]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[68]
PHOSPHORYLATION AT SER-229.
PubMed=21487020; DOI=10.1074/jbc.M111.240796;
Huang W.C., Chen Y.J., Li L.Y., Wei Y.L., Hsu S.C., Tsai S.L.,
Chiu P.C., Huang W.P., Wang Y.N., Chen C.H., Chang W.C., Chang W.C.,
Chen A.J., Tsai C.H., Hung M.C.;
"Nuclear translocation of epidermal growth factor receptor by Akt-
dependent phosphorylation enhances breast cancer-resistant protein
expression in gefitinib-resistant cells.";
J. Biol. Chem. 286:20558-20568(2011).
[69]
FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT
ARG-1199 BY PRMT5, AND INTERACTION WITH PRMT5 AND PTPN6.
PubMed=21258366; DOI=10.1038/ncb2158;
Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J.,
Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T.,
Tsai C.H., Hung M.C.;
"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation
negatively modulates EGFR-mediated ERK activation.";
Nat. Cell Biol. 13:174-181(2011).
[70]
FUNCTION (MICROBIAL INFECTION).
PubMed=21516087; DOI=10.1038/nm.2341;
Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L.,
Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B.,
Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M.,
Pietschmann T., Patel A.H., Pessaux P., Doffoel M., Raffelsberger W.,
Poch O., McKeating J.A., Brino L., Baumert T.F.;
"EGFR and EphA2 are host factors for hepatitis C virus entry and
possible targets for antiviral therapy.";
Nat. Med. 17:589-595(2011).
[71]
INTERACTION WITH FER, AND PHOSPHORYLATION.
PubMed=21518868; DOI=10.1073/pnas.1105369108;
Guo C., Stark G.R.;
"FER tyrosine kinase (FER) overexpression mediates resistance to
quinacrine through EGF-dependent activation of NF-kappaB.";
Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011).
[72]
INTERACTION WITH ANKRD13A; ANKRD13B AND ALKRD13D, UBIQUITINATION, AND
SUBCELLULAR LOCATION.
PubMed=22298428; DOI=10.1091/mbc.E11-09-0817;
Tanno H., Yamaguchi T., Goto E., Ishido S., Komada M.;
"The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor
endocytosis from the plasma membrane.";
Mol. Biol. Cell 23:1343-1353(2012).
[73]
UBIQUITINATION, AND DEUBIQUITINATION BY OTUD7B.
PubMed=22179831; DOI=10.1038/onc.2011.587;
Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F.,
Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N.,
Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z.,
Sinn P., Mills G.B., Yarden Y.;
"Deubiquitination of EGFR by Cezanne-1 contributes to cancer
progression.";
Oncogene 31:4599-4608(2012).
[74]
INTERACTION WITH RNF115 AND RNF126.
PubMed=23418353; DOI=10.1242/jcs.116129;
Smith C.J., Berry D.M., McGlade C.J.;
"The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal
sorting of the epidermal growth factor receptor.";
J. Cell Sci. 126:1366-1380(2013).
[75]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-1064, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[76]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1026
AND SER-1166, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[77]
INTERACTION WITH GPRC5A.
PubMed=25311788; DOI=10.1186/1476-4598-13-233;
Lin X., Zhong S., Ye X., Liao Y., Yao F., Yang X., Sun B., Zhang J.,
Li Q., Gao Y., Wang Y., Liu J., Han B., Chin Y.E., Zhou B.P., Deng J.;
"EGFR phosphorylates and inhibits lung tumor suppressor GPRC5A in lung
cancer.";
Mol. Cancer 13:233-233(2014).
[78]
INTERACTION WITH FAM83B.
PubMed=23912460; DOI=10.1038/onc.2013.293;
Cipriano R., Bryson B.L., Miskimen K.L., Bartel C.A.,
Hernandez-Sanchez W., Bruntz R.C., Scott S.A., Lindsley C.W.,
Brown H.A., Jackson M.W.;
"Hyperactivation of EGFR and downstream effector phospholipase D1 by
oncogenic FAM83B.";
Oncogene 33:3298-3306(2014).
[79]
INTERACTION WITH LAPTM4B.
PubMed=28479384; DOI=10.1016/j.gene.2017.05.006;
Tian M., Chen Y., Tian D., Qiao X., Ma Z., Li J.;
"Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric
cancer cells.";
Gene 626:48-53(2017).
[80]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-646 IN COMPLEX WITH EGF,
FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION, SUBUNIT, SUBCELLULAR
LOCATION, MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429,
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-56; ASN-175; ASN-196;
ASN-352; ASN-361 AND ASN-444.
PubMed=12297050; DOI=10.1016/S0092-8674(02)00963-7;
Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H.,
Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.;
"Crystal structure of the complex of human epidermal growth factor and
receptor extracellular domains.";
Cell 110:775-787(2002).
[81]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-642 IN COMPLEX WITH EGF,
FUNCTION, SUBUNIT, MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609,
DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-352; ASN-361; ASN-444;
ASN-528; ASN-568 AND ASN-603.
PubMed=12620237; DOI=10.1016/S1097-2765(03)00047-9;
Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J.,
Lemmon M.A.;
"EGF activates its receptor by removing interactions that autoinhibit
ectodomain dimerization.";
Mol. Cell 11:507-517(2003).
[82]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH
GW572016, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=15374980; DOI=10.1158/0008-5472.CAN-04-1168;
Wood E.R., Truesdale A.T., McDonald O.B., Yuan D., Hassell A.,
Dickerson S.H., Ellis B., Pennisi C., Horne E., Lackey K.,
Alligood K.J., Rusnak D.W., Gilmer T.M., Shewchuk L.;
"A unique structure for epidermal growth factor receptor bound to
GW572016 (Lapatinib): relationships among protein conformation,
inhibitor off-rate, and receptor activity in tumor cells.";
Cancer Res. 64:6652-6659(2004).
[83]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-642 IN COMPLEX WITH
CETUXIMAB.
PubMed=15837620; DOI=10.1016/j.ccr.2005.03.003;
Li S., Schmitz K.R., Jeffrey P.D., Wiltzius J.J., Kussie P.,
Ferguson K.M.;
"Structural basis for inhibition of the epidermal growth factor
receptor by cetuximab.";
Cancer Cell 7:301-311(2005).
[84]
STRUCTURE BY NMR OF 669-721.
PubMed=15840573; DOI=10.1074/jbc.M502698200;
Choowongkomon K., Carlin C.R., Sonnichsen F.D.;
"A structural model for the membrane-bound form of the juxtamembrane
domain of the epidermal growth factor receptor.";
J. Biol. Chem. 280:24043-24052(2005).
[85]
X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 696-1022 OF WILD-TYPE AND
VARIANTS SER-719 AND ARG-858 IN COMPLEXES WITH ATP ANALOGS AND
SYNTHETIC INHIBITORS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND
CHARACTERIZATION OF VARIANTS SER-719 AND ARG-858.
PubMed=17349580; DOI=10.1016/j.ccr.2006.12.017;
Yun C.H., Boggon T.J., Li Y., Woo M.S., Greulich H., Meyerson M.,
Eck M.J.;
"Structures of lung cancer-derived EGFR mutants and inhibitor
complexes: mechanism of activation and insights into differential
inhibitor sensitivity.";
Cancer Cell 11:217-227(2007).
[86]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH
ERRFI1, ENZYME REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
SUBUNIT, AND INTERACTION WITH ERRFI1.
PubMed=18046415; DOI=10.1038/nature05998;
Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.;
"Inhibition of the EGF receptor by binding of MIG6 to an activating
kinase domain interface.";
Nature 450:741-744(2007).
[87]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 695-1022 OF VARIANT MET-790,
CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANT MET-790.
PubMed=18227510; DOI=10.1073/pnas.0709662105;
Yun C.H., Mengwasser K.E., Toms A.V., Woo M.S., Greulich H.,
Wong K.K., Meyerson M., Eck M.J.;
"The T790M mutation in EGFR kinase causes drug resistance by
increasing the affinity for ATP.";
Proc. Natl. Acad. Sci. U.S.A. 105:2070-2075(2008).
[88]
X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC
ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197,
MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND
1005-GLU-ASP-1006, AND SUBUNIT.
PubMed=19563760; DOI=10.1016/j.cell.2009.04.025;
Jura N., Endres N.F., Engel K., Deindl S., Das R., Lamers M.H.,
Wemmer D.E., Zhang X., Kuriyan J.;
"Mechanism for activation of the EGF receptor catalytic domain by the
juxtamembrane segment.";
Cell 137:1293-1307(2009).
[89]
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 669-1022 OF MUTANT MET-745,
CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LEU-688; VAL-689; GLU-690;
LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706
AND LYS-745.
PubMed=19560417; DOI=10.1016/j.molcel.2009.04.034;
Red Brewer M., Choi S.H., Alvarado D., Moravcevic K., Pozzi A.,
Lemmon M.A., Carpenter G.;
"The juxtamembrane region of the EGF receptor functions as an
activation domain.";
Mol. Cell 34:641-651(2009).
[90]
STRUCTURE BY NMR OF 634-677 IN COMPLEX WITH ERBB2, AND SUBUNIT.
PubMed=20471394; DOI=10.1016/j.jmb.2010.05.016;
Mineev K.S., Bocharov E.V., Pustovalova Y.E., Bocharova O.V.,
Chupin V.V., Arseniev A.S.;
"Spatial structure of the transmembrane domain heterodimer of ErbB1
and ErbB2 receptor tyrosine kinases.";
J. Mol. Biol. 400:231-243(2010).
[91]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-638 IN COMPLEX WITH EGF,
FUNCTION, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-56;
ASN-73; ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528.
PubMed=20837704; DOI=10.1128/MCB.00742-10;
Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S.,
Springer T.A.;
"Structural evidence for loose linkage between ligand binding and
kinase activation in the epidermal growth factor receptor.";
Mol. Cell. Biol. 30:5432-5443(2010).
[92]
X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1066-1076 IN COMPLEX WITH
CBLB, AND INTERACTION WITH CBLB.
Structural genomics consortium;
"Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069
peptide.";
Submitted (OCT-2010) to the PDB data bank.
[93]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1062-1074 IN COMPLEX WITH
CBLC, PHOSPHORYLATION AT TYR-1069, INTERACTION WITH CBLC, AND
MUTAGENESIS OF GLN-1067; ARG-1068 AND TYR-1069.
PubMed=22888118; DOI=10.1093/jb/mvs085;
Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M.,
Yamanashi Y., Yamamoto T., Nakagawa A.;
"Structural flexibility regulates phosphopeptide-binding activity of
the tyrosine kinase binding domain of Cbl-c.";
J. Biochem. 152:487-495(2012).
[94]
VARIANTS ALA-709; GLY-709; CYS-719; SER-719; 746-GLU--ALA-750 DEL;
746-GLU--THR-751 DELINS ALA; 746-GLU--SER-752 DELINS ASP;
747-LEU--THR-751 DEL; ILE-768; MET-769; VAL-833; LEU-835; VAL-838;
ARG-858 AND GLN-861.
PubMed=15623594; DOI=10.1158/1078-0432.CCR-04-1245;
Huang S.F., Liu H.P., Li L.H., Ku Y.C., Fu Y.N., Tsai H.Y., Chen Y.T.,
Lin Y.F., Chang W.C., Kuo H.P., Wu Y.C., Chen Y.R., Tsai S.F.;
"High frequency of epidermal growth factor receptor mutations with
complex patterns in non-small cell lung cancers related to gefitinib
responsiveness in Taiwan.";
Clin. Cancer Res. 10:8195-8203(2004).
[95]
VARIANTS SER-719 AND ARG-858, AND POSSIBLE INVOLVEMENT IN LUNG CANCER.
PubMed=15118125; DOI=10.1126/science.1099314;
Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S.,
Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H.,
Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.;
"EGFR mutations in lung cancer: correlation with clinical response to
gefitinib therapy.";
Science 304:1497-1500(2004).
[96]
VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719;
SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748;
752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858;
ARG-858; GLN-861 AND GLU-873, AND POSSIBLE INVOLVEMENT IN LUNG CANCER.
PubMed=16533793; DOI=10.1158/1078-0432.CCR-05-1981;
Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K.,
Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.;
"Distinct epidermal growth factor receptor and KRAS mutation patterns
in non-small cell lung cancer patients with different tobacco exposure
and clinicopathologic features.";
Clin. Cancer Res. 12:1647-1653(2006).
[97]
CHARACTERIZATION OF VARIANTS ALA-709; GLY-709; SER-719; ILE-768;
VAL-833; LEU-835; VAL-838; ARG-858 AND GLN-861.
PubMed=16205628; DOI=10.1038/sj.onc.1209159;
Chen Y.R., Fu Y.N., Lin C.H., Yang S.T., Hu S.F., Chen Y.T.,
Tsai S.F., Huang S.F.;
"Distinctive activation patterns in constitutively active and
gefitinib-sensitive EGFR mutants.";
Oncogene 25:1205-1215(2006).
[98]
VARIANT 30-VAL--ARG-297 DEL, AND POSSIBLE INVOLVEMENT IN LUNG CANCER.
PubMed=16672372; DOI=10.1073/pnas.0510284103;
Ji H., Zhao X., Yuza Y., Shimamura T., Li D., Protopopov A.,
Jung B.L., McNamara K., Xia H., Glatt K.A., Thomas R.K., Sasaki H.,
Horner J.W., Eck M., Mitchell A., Sun Y., Al-Hashem R., Bronson R.T.,
Rabindran S.K., Discafani C.M., Maher E., Shapiro G.I., Meyerson M.,
Wong K.K.;
"Epidermal growth factor receptor variant III mutations in lung
tumorigenesis and sensitivity to tyrosine kinase inhibitors.";
Proc. Natl. Acad. Sci. U.S.A. 103:7817-7822(2006).
[99]
VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[100]
VARIANT NISBD2 ASP-428, CHARACTERIZATION OF VARIANT NISBD2 ASP-428,
AND INVOLVEMENT IN NISBD2.
PubMed=24691054; DOI=10.1038/jid.2014.164;
Campbell P., Morton P.E., Takeichi T., Salam A., Roberts N.,
Proudfoot L.E., Mellerio J.E., Aminu K., Wellington C., Patil S.N.,
Akiyama M., Liu L., McMillan J.R., Aristodemou S., Ishida-Yamamoto A.,
Abdul-Wahab A., Petrof G., Fong K., Harnchoowong S., Stone K.L.,
Harper J.I., McLean W.H., Simpson M.A., Parsons M., McGrath J.A.;
"Epithelial inflammation resulting from an inherited loss-of-function
mutation in EGFR.";
J. Invest. Dermatol. 134:2570-2578(2014).
-!- FUNCTION: Receptor tyrosine kinase binding ligands of the EGF
family and activating several signaling cascades to convert
extracellular cues into appropriate cellular responses. Known
ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN,
BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF.
Ligand binding triggers receptor homo- and/or heterodimerization
and autophosphorylation on key cytoplasmic residues. The
phosphorylated receptor recruits adapter proteins like GRB2 which
in turn activates complex downstream signaling cascades. Activates
at least 4 major downstream signaling cascades including the RAS-
RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May
also activate the NF-kappa-B signaling cascade. Also directly
phosphorylates other proteins like RGS16, activating its GTPase
activity and probably coupling the EGF receptor signaling to the G
protein-coupled receptor signaling. Also phosphorylates MUC1 and
increases its interaction with SRC and CTNNB1/beta-catenin. Plays
a role in enhancing learning and memory performance (By
similarity). {ECO:0000250|UniProtKB:Q01279}.
-!- FUNCTION: Isoform 2 may act as an antagonist of EGF action.
-!- FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C
virus (HCV) in hepatocytes and facilitates its cell entry.
Mediates HCV entry by promoting the formation of the CD81-CLDN1
receptor complexes that are essential for HCV entry and by
enhancing membrane fusion of cells expressing HCV envelope
glycoproteins. {ECO:0000269|PubMed:21516087}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:15374980,
ECO:0000269|PubMed:17349580, ECO:0000269|PubMed:18046415,
ECO:0000269|PubMed:18227510, ECO:0000269|PubMed:19560417,
ECO:0000269|PubMed:19563760}.
-!- ENZYME REGULATION: Endocytosis and inhibition of the activated
EGFR by phosphatases like PTPRJ and PTPRK constitute immediate
regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that
regulates EGFR endocytosis and activity. Moreover, inducible
feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1
constitute alternative regulatory mechanisms for the EGFR
signaling. {ECO:0000269|PubMed:15282549,
ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:18046415,
ECO:0000269|PubMed:19836242}.
-!- SUBUNIT: Binding of the ligand triggers homo- and/or
heterodimerization of the receptor triggering its
autophosphorylation. Heterodimer with ERBB2. Interacts with
ERRFI1; inhibits dimerization of the kinase domain and
autophosphorylation. Part of a complex with ERBB2 and either
PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein
coupling the receptor to downstream signaling pathways. Interacts
with GAB2; involved in signaling downstream of EGFR. Interacts
with STAT3; mediates EGFR downstream signaling in cell
proliferation. Interacts with RIPK1; involved in NF-kappa-B
activation. Interacts (autophosphorylated) with CBL, CBLB and
CBLC; involved in EGFR ubiquitination and regulation. Interacts
with SOCS5; regulates EGFR degradation through ELOC- and ELOB-
mediated ubiquitination and proteasomal degradation. Interacts
with PRMT5; methylates EGFR and enhances interaction with PTPN6.
Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent
activation of MAPK/ERK. Interacts with COPG1; essential for
regulation of EGF-dependent nuclear transport of EGFR by
retrograde trafficking from the Golgi to the ER. Interacts with
TNK2; this interaction is dependent on EGF stimulation and kinase
activity of EGFR. Interacts with PCNA; positively regulates PCNA.
Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1.
Interacts with FER. May interact with EPS8; mediates EPS8
phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and
NCK2. Interacts with ATX2. Interacts with GAREM1. Interacts
(ubiquitinated) with ANKRD13A/B/D; the interaction is direct and
may regulate EGFR internalization after EGF stimulation. Interacts
with GPER1; the interaction occurs in an estrogen-dependent
manner. Interacts (via C-terminal cytoplasmic kinase domain) with
ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126.
Interacts with GPRC5A (via its transmembrane
domain)(PubMed:25311788). Interacts with FAM83B; positively
regulates EGFR inducing its autophospharylation in absence of
stimulation by EGF (PubMed:23912460). Interacts with LAPTM4B;
positively correlates with EGFR activation (PubMed:28479384).
{ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:10228163,
ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11116146,
ECO:0000269|PubMed:11483589, ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12620237, ECO:0000269|PubMed:12873986,
ECO:0000269|PubMed:15282549, ECO:0000269|PubMed:15374980,
ECO:0000269|PubMed:15590694, ECO:0000269|PubMed:15837620,
ECO:0000269|PubMed:16140940, ECO:0000269|PubMed:17115032,
ECO:0000269|PubMed:17182860, ECO:0000269|PubMed:18046415,
ECO:0000269|PubMed:18602463, ECO:0000269|PubMed:19172738,
ECO:0000269|PubMed:19509291, ECO:0000269|PubMed:19560417,
ECO:0000269|PubMed:19563760, ECO:0000269|PubMed:19749156,
ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:20471394,
ECO:0000269|PubMed:20551055, ECO:0000269|PubMed:20674546,
ECO:0000269|PubMed:20837704, ECO:0000269|PubMed:21258366,
ECO:0000269|PubMed:21518868, ECO:0000269|PubMed:22298428,
ECO:0000269|PubMed:22888118, ECO:0000269|PubMed:23418353,
ECO:0000269|PubMed:23912460, ECO:0000269|PubMed:25311788,
ECO:0000269|PubMed:28479384, ECO:0000269|PubMed:7657591,
ECO:0000269|PubMed:8650580, ECO:0000269|PubMed:9852145,
ECO:0000269|Ref.92}.
-!- INTERACTION:
Self; NbExp=30; IntAct=EBI-297353, EBI-297353;
Q53FC7:-; NbExp=3; IntAct=EBI-297353, EBI-9356749;
Q96BE0:-; NbExp=2; IntAct=EBI-297353, EBI-9356686;
P00519:ABL1; NbExp=2; IntAct=EBI-297353, EBI-375543;
P42684:ABL2; NbExp=8; IntAct=EBI-297353, EBI-1102694;
Q15109:AGER; NbExp=2; IntAct=EBI-297353, EBI-1646426;
Q9UKV8:AGO2; NbExp=11; IntAct=EBI-297353, EBI-528269;
Q09666:AHNAK; NbExp=3; IntAct=EBI-297353, EBI-2555881;
Q02952:AKAP12; NbExp=2; IntAct=EBI-297353, EBI-2562430;
Q92625:ANKS1A; NbExp=5; IntAct=EBI-297353, EBI-1048612;
Q96CW1:AP2M1; NbExp=4; IntAct=EBI-297353, EBI-297683;
O00213:APBB1; NbExp=4; IntAct=EBI-297353, EBI-81694;
Q92870:APBB2; NbExp=6; IntAct=EBI-297353, EBI-79277;
O95704:APBB3; NbExp=2; IntAct=EBI-297353, EBI-286427;
Q9UKG1:APPL1; NbExp=2; IntAct=EBI-297353, EBI-741243;
O14965:AURKA; NbExp=4; IntAct=EBI-297353, EBI-448680;
P30530:AXL; NbExp=4; IntAct=EBI-297353, EBI-2850927;
Q14457:BECN1; NbExp=7; IntAct=EBI-297353, EBI-949378;
P51451:BLK; NbExp=2; IntAct=EBI-297353, EBI-2105445;
P62158:CALM3; NbExp=4; IntAct=EBI-297353, EBI-397435;
P62161:Calm3 (xeno); NbExp=6; IntAct=EBI-297353, EBI-397530;
P49069:CAMLG; NbExp=2; IntAct=EBI-297353, EBI-1748958;
Q03135:CAV1; NbExp=6; IntAct=EBI-297353, EBI-603614;
P22681:CBL; NbExp=22; IntAct=EBI-297353, EBI-518228;
P22682:Cbl (xeno); NbExp=2; IntAct=EBI-297353, EBI-640919;
Q16543:CDC37; NbExp=9; IntAct=EBI-297353, EBI-295634;
P12830:CDH1; NbExp=3; IntAct=EBI-297353, EBI-727477;
Q9NSE2:CISH; NbExp=3; IntAct=EBI-297353, EBI-617866;
Q7Z7G1:CLNK; NbExp=2; IntAct=EBI-297353, EBI-7878194;
P46108:CRK; NbExp=3; IntAct=EBI-297353, EBI-886;
P46108-1:CRK; NbExp=3; IntAct=EBI-297353, EBI-287556;
P46109:CRKL; NbExp=3; IntAct=EBI-297353, EBI-910;
P35221:CTNNA1; NbExp=4; IntAct=EBI-297353, EBI-701918;
O60716:CTNND1; NbExp=4; IntAct=EBI-297353, EBI-701927;
Q14247:CTTN; NbExp=3; IntAct=EBI-297353, EBI-351886;
Q99418:CYTH2; NbExp=5; IntAct=EBI-297353, EBI-448974;
Q6PKX4:DOK6; NbExp=2; IntAct=EBI-297353, EBI-2880244;
P01133:EGF; NbExp=22; IntAct=EBI-297353, EBI-640857;
Q12929:EPS8; NbExp=2; IntAct=EBI-297353, EBI-375576;
P04626:ERBB2; NbExp=25; IntAct=EBI-297353, EBI-641062;
P21860:ERBB3; NbExp=13; IntAct=EBI-297353, EBI-720706;
Q15303:ERBB4; NbExp=2; IntAct=EBI-297353, EBI-80371;
P07992:ERCC1; NbExp=21; IntAct=EBI-297353, EBI-750962;
Q9UJM3:ERRFI1; NbExp=15; IntAct=EBI-297353, EBI-2941912;
P03372:ESR1; NbExp=2; IntAct=EBI-297353, EBI-78473;
P03372-4:ESR1; NbExp=4; IntAct=EBI-297353, EBI-4309277;
Q96A65:EXOC4; NbExp=2; IntAct=EBI-297353, EBI-355383;
P09769:FGR; NbExp=2; IntAct=EBI-297353, EBI-1383732;
Q14318:FKBP8; NbExp=3; IntAct=EBI-297353, EBI-724839;
Q13480:GAB1; NbExp=3; IntAct=EBI-297353, EBI-517684;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-297353, EBI-720116;
P04406:GAPDH; NbExp=6; IntAct=EBI-297353, EBI-354056;
Q14956:GPNMB; NbExp=3; IntAct=EBI-297353, EBI-7250369;
Q14956-1:GPNMB; NbExp=2; IntAct=EBI-297353, EBI-16191078;
O75791:GRAP2; NbExp=2; IntAct=EBI-297353, EBI-740418;
P62993:GRB2; NbExp=36; IntAct=EBI-297353, EBI-401755;
P08631:HCK; NbExp=2; IntAct=EBI-297353, EBI-346340;
Q9UBN7:HDAC6; NbExp=11; IntAct=EBI-297353, EBI-301697;
Q8WUI4:HDAC7; NbExp=2; IntAct=EBI-297353, EBI-1048378;
P07900:HSP90AA1; NbExp=5; IntAct=EBI-297353, EBI-296047;
P08238:HSP90AB1; NbExp=8; IntAct=EBI-297353, EBI-352572;
Q6PK50:HSP90AB1; NbExp=2; IntAct=EBI-297353, EBI-9356629;
P08107:HSPA1B; NbExp=6; IntAct=EBI-297353, EBI-629985;
P11142:HSPA8; NbExp=5; IntAct=EBI-297353, EBI-351896;
P38646:HSPA9; NbExp=4; IntAct=EBI-297353, EBI-354932;
P04792:HSPB1; NbExp=3; IntAct=EBI-297353, EBI-352682;
P17936:IGFBP3; NbExp=3; IntAct=EBI-297353, EBI-715709;
P46940:IQGAP1; NbExp=4; IntAct=EBI-297353, EBI-297509;
O14654:IRS4; NbExp=2; IntAct=EBI-297353, EBI-356594;
Q86VI4:LAPTM4B; NbExp=10; IntAct=EBI-297353, EBI-3267258;
O43561:LAT; NbExp=2; IntAct=EBI-297353, EBI-1222766;
Q13094:LCP2; NbExp=2; IntAct=EBI-297353, EBI-346946;
Q96FE5:LINGO1; NbExp=2; IntAct=EBI-297353, EBI-719955;
Q38SD2:LRRK1; NbExp=2; IntAct=EBI-297353, EBI-1050422;
P07948:LYN; NbExp=6; IntAct=EBI-297353, EBI-79452;
P07948-1:LYN; NbExp=2; IntAct=EBI-297353, EBI-6895930;
Q9UQF2:MAPK8IP1; NbExp=3; IntAct=EBI-297353, EBI-78404;
Q13387:MAPK8IP2; NbExp=4; IntAct=EBI-297353, EBI-722813;
Q9Y2H9:MAST1; NbExp=2; IntAct=EBI-297353, EBI-3385920;
P08581:MET; NbExp=8; IntAct=EBI-297353, EBI-1039152;
P14174:MIF; NbExp=3; IntAct=EBI-297353, EBI-372712;
P15941:MUC1; NbExp=3; IntAct=EBI-297353, EBI-2804728;
P16333:NCK1; NbExp=3; IntAct=EBI-297353, EBI-389883;
P04150:NR3C1; NbExp=2; IntAct=EBI-297353, EBI-493507;
P16234:PDGFRA; NbExp=3; IntAct=EBI-297353, EBI-2861522;
O00750:PIK3C2B; NbExp=9; IntAct=EBI-297353, EBI-641107;
P27986:PIK3R1; NbExp=5; IntAct=EBI-297353, EBI-79464;
O00459:PIK3R2; NbExp=3; IntAct=EBI-297353, EBI-346930;
Q92569:PIK3R3; NbExp=6; IntAct=EBI-297353, EBI-79893;
P19174:PLCG1; NbExp=6; IntAct=EBI-297353, EBI-79387;
P16885:PLCG2; NbExp=5; IntAct=EBI-297353, EBI-617403;
P17252:PRKCA; NbExp=2; IntAct=EBI-297353, EBI-1383528;
P97313:Prkdc (xeno); NbExp=4; IntAct=EBI-297353, EBI-2272005;
Q05397:PTK2; NbExp=3; IntAct=EBI-297353, EBI-702142;
P18031:PTPN1; NbExp=7; IntAct=EBI-297353, EBI-968788;
P20417:Ptpn1 (xeno); NbExp=11; IntAct=EBI-297353, EBI-916819;
Q05209:PTPN12; NbExp=3; IntAct=EBI-297353, EBI-2266035;
Q9Y2R2:PTPN22; NbExp=2; IntAct=EBI-297353, EBI-1211241;
Q9UJ41:RABGEF1; NbExp=4; IntAct=EBI-297353, EBI-913954;
Q70E73:RAPH1; NbExp=2; IntAct=EBI-297353, EBI-3940924;
P20936:RASA1; NbExp=7; IntAct=EBI-297353, EBI-1026476;
Q13671:RIN1; NbExp=3; IntAct=EBI-297353, EBI-366017;
Q01973:ROR1; NbExp=8; IntAct=EBI-297353, EBI-6082337;
Q92622:RUBCN; NbExp=3; IntAct=EBI-297353, EBI-2952709;
Q80U62:Rubcn (xeno); NbExp=2; IntAct=EBI-297353, EBI-3506572;
P31947:SFN; NbExp=8; IntAct=EBI-297353, EBI-476295;
Q9NRF2:SH2B1; NbExp=2; IntAct=EBI-297353, EBI-310491;
Q9UQQ2:SH2B3; NbExp=2; IntAct=EBI-297353, EBI-7879749;
Q9BRG2:SH2D3A; NbExp=2; IntAct=EBI-297353, EBI-2339271;
P29353:SHC1; NbExp=28; IntAct=EBI-297353, EBI-78835;
P29353-7:SHC1; NbExp=4; IntAct=EBI-297353, EBI-9691288;
P98077:SHC2; NbExp=3; IntAct=EBI-297353, EBI-7256023;
Q6S5L8:SHC4; NbExp=2; IntAct=EBI-297353, EBI-9453524;
Q13239:SLA; NbExp=2; IntAct=EBI-297353, EBI-726214;
P13866:SLC5A1; NbExp=3; IntAct=EBI-297353, EBI-1772443;
P12931:SRC; NbExp=7; IntAct=EBI-297353, EBI-621482;
P42224:STAT1; NbExp=6; IntAct=EBI-297353, EBI-1057697;
P40763:STAT3; NbExp=14; IntAct=EBI-297353, EBI-518675;
P42229:STAT5A; NbExp=3; IntAct=EBI-297353, EBI-749537;
P31948:STIP1; NbExp=2; IntAct=EBI-297353, EBI-1054052;
Q9UNE7:STUB1; NbExp=3; IntAct=EBI-297353, EBI-357085;
P43405:SYK; NbExp=6; IntAct=EBI-297353, EBI-78302;
P01135:TGFA; NbExp=2; IntAct=EBI-297353, EBI-1034374;
Q9Y490:TLN1; NbExp=2; IntAct=EBI-297353, EBI-2462036;
O60603:TLR2; NbExp=2; IntAct=EBI-297353, EBI-973722;
Q68CZ2:TNS3; NbExp=4; IntAct=EBI-297353, EBI-1220488;
O75674:TOM1L1; NbExp=6; IntAct=EBI-297353, EBI-712991;
Q12933:TRAF2; NbExp=3; IntAct=EBI-297353, EBI-355744;
Q8K424:Trpv3 (xeno); NbExp=2; IntAct=EBI-297353, EBI-2650739;
Q71U36:TUBA1A; NbExp=3; IntAct=EBI-297353, EBI-302552;
P10599:TXN; NbExp=4; IntAct=EBI-297353, EBI-594644;
P09936:UCHL1; NbExp=2; IntAct=EBI-297353, EBI-714860;
Q9P0L0:VAPA; NbExp=2; IntAct=EBI-297353, EBI-1059156;
P07947:YES1; NbExp=3; IntAct=EBI-297353, EBI-515331;
P27348:YWHAQ; NbExp=6; IntAct=EBI-297353, EBI-359854;
P63104:YWHAZ; NbExp=5; IntAct=EBI-297353, EBI-347088;
P43403:ZAP70; NbExp=2; IntAct=EBI-297353, EBI-1211276;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Endoplasmic reticulum membrane; Single-pass type I
membrane protein. Golgi apparatus membrane; Single-pass type I
membrane protein. Nucleus membrane; Single-pass type I membrane
protein. Endosome. Endosome membrane. Nucleus. Note=In response to
EGF, translocated from the cell membrane to the nucleus via Golgi
and ER. Endocytosed upon activation by ligand. Colocalized with
GPER1 in the nucleus of estrogen agonist-induced cancer-associated
fibroblasts (CAF).
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=p170;
IsoId=P00533-1; Sequence=Displayed;
Name=2; Synonyms=p60, Truncated, TEGFR;
IsoId=P00533-2; Sequence=VSP_002887, VSP_002888;
Name=3; Synonyms=p110;
IsoId=P00533-3; Sequence=VSP_002889, VSP_002890;
Name=4;
IsoId=P00533-4; Sequence=VSP_002891, VSP_002892;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 2 is also
expressed in ovarian cancers. {ECO:0000269|PubMed:17671655}.
-!- PTM: Phosphorylation at Ser-695 is partial and occurs only if Thr-
693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by
PRKD1 inhibits EGF-induced MAPK8/JNK1 activation.
Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the
receptor at the plasma membrane. Autophosphorylation at Tyr-1197
is stimulated by methylation at Arg-1199 and enhances interaction
with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110
recruits STAT3. Dephosphorylated by PTPN1 and PTPN2.
{ECO:0000269|PubMed:10523301, ECO:0000269|PubMed:12873986,
ECO:0000269|PubMed:16083266, ECO:0000269|PubMed:19563760,
ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:21258366,
ECO:0000269|PubMed:2543678, ECO:0000269|PubMed:3138233}.
-!- PTM: Monoubiquitinated and polyubiquitinated upon EGF stimulation;
which does not affect tyrosine kinase activity or signaling
capacity but may play a role in lysosomal targeting. Polyubiquitin
linkage is mainly through 'Lys-63', but linkage through 'Lys-48',
'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B
prevents degradation. Ubiquitinated by RNF115 and RNF126 (By
similarity). {ECO:0000250|UniProtKB:Q01279,
ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:22179831,
ECO:0000269|PubMed:22298428}.
-!- PTM: Methylated. Methylation at Arg-1199 by PRMT5 stimulates
phosphorylation at Tyr-1197. {ECO:0000269|PubMed:19563760,
ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:21258366}.
-!- DISEASE: Lung cancer (LNCR) [MIM:211980]: A common malignancy
affecting tissues of the lung. The most common form of lung cancer
is non-small cell lung cancer (NSCLC) that can be divided into 3
major histologic subtypes: squamous cell carcinoma,
adenocarcinoma, and large cell lung cancer. NSCLC is often
diagnosed at an advanced stage and has a poor prognosis.
{ECO:0000269|PubMed:15118125, ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:16672372}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)
[MIM:616069]: A disorder characterized by inflammatory features
with neonatal onset, involving the skin, hair, and gut. The skin
lesions involve perioral and perianal erythema, psoriasiform
erythroderma, with flares of erythema, scaling, and widespread
pustules. Gastrointestinal symptoms include malabsorptive diarrhea
that is exacerbated by intercurrent gastrointestinal infections.
The hair is short or broken, and the eyelashes and eyebrows are
wiry and disorganized. {ECO:0000269|PubMed:24691054}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/egfr/";
-!- WEB RESOURCE: Name=Wikipedia; Note=EGFR entry;
URL="https://en.wikipedia.org/wiki/Epidermal_growth_factor_receptor";
-----------------------------------------------------------------------
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EMBL; X00588; CAA25240.1; -; mRNA.
EMBL; U95089; AAB53063.1; -; mRNA.
EMBL; U48722; AAC50802.1; -; mRNA.
EMBL; U48723; AAC50804.1; -; Genomic_DNA.
EMBL; U48724; AAC50796.1; -; Genomic_DNA.
EMBL; U48725; AAC50797.1; -; Genomic_DNA.
EMBL; U48726; AAC50798.1; -; Genomic_DNA.
EMBL; U48727; AAC50799.1; -; Genomic_DNA.
EMBL; U48728; AAC50800.1; -; Genomic_DNA.
EMBL; U48729; AAC50801.1; -; Genomic_DNA.
EMBL; AF288738; AAG35786.1; -; Genomic_DNA.
EMBL; AF288738; AAG35787.1; -; Genomic_DNA.
EMBL; AF288738; AAG35788.1; -; Genomic_DNA.
EMBL; AF288738; AAG35789.1; -; Genomic_DNA.
EMBL; AF288738; AAG35790.1; -; Genomic_DNA.
EMBL; AY698024; AAT97979.1; -; mRNA.
EMBL; AY588246; AAS83109.1; -; Genomic_DNA.
EMBL; AF277897; AAK01080.1; -; mRNA.
EMBL; AF125253; AAG43240.1; -; mRNA.
EMBL; AF125539; AAG43243.1; -; Genomic_DNA.
EMBL; AF125538; AAG43243.1; JOINED; Genomic_DNA.
EMBL; X06370; CAA29668.1; -; Genomic_DNA.
EMBL; X00663; CAA25282.1; -; mRNA.
EMBL; M38425; AAA63171.1; -; Genomic_DNA.
EMBL; M11234; AAA52370.1; -; Genomic_DNA.
CCDS; CCDS47587.1; -. [P00533-2]
CCDS; CCDS5514.1; -. [P00533-1]
CCDS; CCDS5515.1; -. [P00533-3]
CCDS; CCDS5516.1; -. [P00533-4]
PIR; A00641; GQHUE.
RefSeq; NP_005219.2; NM_005228.4. [P00533-1]
RefSeq; NP_958439.1; NM_201282.1. [P00533-4]
RefSeq; NP_958440.1; NM_201283.1. [P00533-2]
RefSeq; NP_958441.1; NM_201284.1. [P00533-3]
UniGene; Hs.488293; -.
UniGene; Hs.605083; -.
UniGene; Hs.731652; -.
PDB; 1DNQ; Model; -; A=25-336.
PDB; 1DNR; Model; -; A=337-645.
PDB; 1IVO; X-ray; 3.30 A; A/B=25-646.
PDB; 1M14; X-ray; 2.60 A; A=695-1022.
PDB; 1M17; X-ray; 2.60 A; A=695-1022.
PDB; 1MOX; X-ray; 2.50 A; A/B=25-525.
PDB; 1NQL; X-ray; 2.80 A; A=25-642.
PDB; 1XKK; X-ray; 2.40 A; A=695-1022.
PDB; 1YY9; X-ray; 2.60 A; A=25-642.
PDB; 1Z9I; NMR; -; A=669-721.
PDB; 2EB2; X-ray; 2.50 A; A=695-1022.
PDB; 2EB3; X-ray; 2.84 A; A=695-1022.
PDB; 2EXP; Model; -; A=311-326.
PDB; 2EXQ; Model; -; A=27-536.
PDB; 2GS2; X-ray; 2.80 A; A=696-1022.
PDB; 2GS6; X-ray; 2.60 A; A=696-1022.
PDB; 2GS7; X-ray; 2.60 A; A/B=696-1022.
PDB; 2ITN; X-ray; 2.47 A; A=696-1019.
PDB; 2ITO; X-ray; 3.25 A; A=696-1022.
PDB; 2ITP; X-ray; 2.74 A; A=696-1022.
PDB; 2ITQ; X-ray; 2.68 A; A=696-1022.
PDB; 2ITT; X-ray; 2.73 A; A=696-1022.
PDB; 2ITU; X-ray; 2.80 A; A=696-1022.
PDB; 2ITV; X-ray; 2.47 A; A=696-1022.
PDB; 2ITW; X-ray; 2.88 A; A=696-1022.
PDB; 2ITX; X-ray; 2.98 A; A=696-1022.
PDB; 2ITY; X-ray; 3.42 A; A=696-1022.
PDB; 2ITZ; X-ray; 2.72 A; A=696-1022.
PDB; 2J5E; X-ray; 3.10 A; A=696-1022.
PDB; 2J5F; X-ray; 3.00 A; A=696-1022.
PDB; 2J6M; X-ray; 3.10 A; A=696-1022.
PDB; 2JIT; X-ray; 3.10 A; A/B=696-1022.
PDB; 2JIU; X-ray; 3.05 A; A/B=695-1022.
PDB; 2JIV; X-ray; 3.50 A; A/B=695-1022.
PDB; 2KS1; NMR; -; B=634-677.
PDB; 2M0B; NMR; -; A/B=634-677.
PDB; 2M20; NMR; -; A/B=642-697.
PDB; 2N5S; NMR; -; A=642-690.
PDB; 2RF9; X-ray; 3.50 A; A/B=696-1022.
PDB; 2RFD; X-ray; 3.60 A; A/B=702-1022.
PDB; 2RFE; X-ray; 2.90 A; A/B/C/D=702-1022.
PDB; 2RGP; X-ray; 2.00 A; A=702-1016.
PDB; 3B2U; X-ray; 2.58 A; A/B/E/I/M/P/S/V=335-538.
PDB; 3B2V; X-ray; 3.30 A; A=25-642.
PDB; 3BEL; X-ray; 2.30 A; A=702-1016.
PDB; 3BUO; X-ray; 2.60 A; A/C=1063-1075.
PDB; 3C09; X-ray; 3.20 A; A/D=336-538.
PDB; 3G5V; X-ray; 2.00 A; C=311-326.
PDB; 3G5Y; X-ray; 1.59 A; E=311-326.
PDB; 3GOP; X-ray; 2.80 A; A=669-1022.
PDB; 3GT8; X-ray; 2.96 A; A/B/C/D=696-1022.
PDB; 3IKA; X-ray; 2.90 A; A/B=694-1022.
PDB; 3LZB; X-ray; 2.70 A; A/B/C/D/E/F/G/H=696-983.
PDB; 3NJP; X-ray; 3.30 A; A/B=25-638.
PDB; 3OB2; X-ray; 2.10 A; A=1063-1074.
PDB; 3OP0; X-ray; 2.52 A; C/D=1066-1076.
PDB; 3P0Y; X-ray; 1.80 A; A=334-538.
PDB; 3PFV; X-ray; 2.27 A; C/D=1066-1076.
PDB; 3POZ; X-ray; 1.50 A; A=696-1022.
PDB; 3QWQ; X-ray; 2.75 A; A=1-642.
PDB; 3UG1; X-ray; 2.75 A; A=695-1022.
PDB; 3UG2; X-ray; 2.50 A; A=695-1022.
PDB; 3VJN; X-ray; 2.34 A; A=695-1022.
PDB; 3VJO; X-ray; 2.64 A; A=695-1022.
PDB; 3VRP; X-ray; 1.52 A; B=1062-1074.
PDB; 3VRR; X-ray; 2.00 A; C=1062-1074.
PDB; 3W2O; X-ray; 2.35 A; A=698-1022.
PDB; 3W2P; X-ray; 2.05 A; A=698-1022.
PDB; 3W2Q; X-ray; 2.20 A; A=698-1022.
PDB; 3W2R; X-ray; 2.05 A; A=698-1022.
PDB; 3W2S; X-ray; 1.90 A; A=696-1022.
PDB; 3W32; X-ray; 1.80 A; A=696-1022.
PDB; 3W33; X-ray; 1.70 A; A=696-1022.
PDB; 4G5J; X-ray; 2.80 A; A=696-1022.
PDB; 4G5P; X-ray; 3.17 A; A/B=696-1022.
PDB; 4HJO; X-ray; 2.75 A; A=696-1022.
PDB; 4I1Z; X-ray; 3.00 A; A=695-1022.
PDB; 4I20; X-ray; 3.34 A; A=695-1022.
PDB; 4I21; X-ray; 3.37 A; A/B=695-1022.
PDB; 4I22; X-ray; 1.71 A; A=695-1022.
PDB; 4I23; X-ray; 2.80 A; A=695-1022.
PDB; 4I24; X-ray; 1.80 A; A/B=695-1022.
PDB; 4JQ7; X-ray; 2.73 A; A=696-1021.
PDB; 4JQ8; X-ray; 2.83 A; A=696-1021.
PDB; 4JR3; X-ray; 2.70 A; A=696-1021.
PDB; 4JRV; X-ray; 2.80 A; A=696-1021.
PDB; 4KRL; X-ray; 2.85 A; A=335-538.
PDB; 4KRM; X-ray; 2.66 A; A/C/E/G/I/K=335-538.
PDB; 4KRO; X-ray; 3.05 A; A=25-642.
PDB; 4KRP; X-ray; 2.82 A; A=25-642.
PDB; 4LI5; X-ray; 2.64 A; A=696-1020.
PDB; 4LL0; X-ray; 4.00 A; A/B=694-1022.
PDB; 4LQM; X-ray; 2.50 A; A=694-1022.
PDB; 4LRM; X-ray; 3.53 A; A/B/C/D/E=694-1022.
PDB; 4R3P; X-ray; 2.90 A; A=696-1018.
PDB; 4R3R; X-ray; 3.25 A; A=696-1018.
PDB; 4R5S; X-ray; 3.00 A; A=696-1022.
PDB; 4RIW; X-ray; 3.10 A; B/D=682-1022.
PDB; 4RIX; X-ray; 3.10 A; B/D=682-1022.
PDB; 4RIY; X-ray; 2.98 A; B/D=682-1022.
PDB; 4RJ4; X-ray; 2.78 A; A=695-1022.
PDB; 4RJ5; X-ray; 3.10 A; A=695-1022.
PDB; 4RJ6; X-ray; 2.70 A; A=695-1022.
PDB; 4RJ7; X-ray; 2.55 A; A=695-1022.
PDB; 4RJ8; X-ray; 2.50 A; A=695-1022.
PDB; 4TKS; X-ray; 3.20 A; A=695-1022.
PDB; 4UIP; X-ray; 2.95 A; A=26-637.
PDB; 4UV7; X-ray; 2.10 A; A=25-645.
PDB; 4WD5; X-ray; 3.30 A; A/B=694-1022.
PDB; 4WKQ; X-ray; 1.85 A; A=696-1022.
PDB; 4WRG; X-ray; 1.90 A; A=696-1022.
PDB; 4ZAU; X-ray; 2.80 A; A=696-1022.
PDB; 4ZJV; X-ray; 2.70 A; A/B=695-1022.
PDB; 4ZSE; X-ray; 1.97 A; A/B/C/D=695-1022.
PDB; 5C8K; X-ray; 3.00 A; A=695-1022.
PDB; 5C8M; X-ray; 2.90 A; A=695-1022.
PDB; 5C8N; X-ray; 2.40 A; A=695-1022.
PDB; 5CAL; X-ray; 2.70 A; A=695-1022.
PDB; 5CAN; X-ray; 2.80 A; A=695-1022.
PDB; 5CAO; X-ray; 2.60 A; A=695-1022.
PDB; 5CAP; X-ray; 2.40 A; A=695-1022.
PDB; 5CAQ; X-ray; 2.50 A; A=695-1022.
PDB; 5CAS; X-ray; 2.10 A; A=695-1022.
PDB; 5CAU; X-ray; 2.25 A; A=695-1022.
PDB; 5CAV; X-ray; 2.73 A; A=695-1022.
PDB; 5CNN; X-ray; 1.90 A; A/B=696-1042.
PDB; 5CNO; X-ray; 1.55 A; A/B/X=696-1022.
PDB; 5CZH; X-ray; 2.80 A; A=694-1022.
PDB; 5CZI; X-ray; 2.60 A; A=694-1022.
PDB; 5D41; X-ray; 2.31 A; A/B=695-1022.
PDB; 5EDP; X-ray; 2.90 A; A=695-1022.
PDB; 5EDQ; X-ray; 2.80 A; A=695-1022.
PDB; 5EDR; X-ray; 2.60 A; A=695-1022.
PDB; 5EM5; X-ray; 2.65 A; A=695-1022.
PDB; 5EM6; X-ray; 2.78 A; A=695-1022.
PDB; 5EM7; X-ray; 2.81 A; A=695-1022.
PDB; 5EM8; X-ray; 2.80 A; A=695-1022.
PDB; 5FED; X-ray; 2.65 A; A=696-1022.
PDB; 5FEE; X-ray; 2.70 A; A=696-1022.
PDB; 5FEQ; X-ray; 3.40 A; A=696-1022.
PDB; 5GMP; X-ray; 2.80 A; A=696-1022.
PDB; 5GNK; X-ray; 1.80 A; A=696-988.
PDB; 5GTY; X-ray; 3.14 A; A/B/C/D/E/F/G/H=696-1022.
PDB; 5GTZ; X-ray; 3.00 A; A=696-1022.
PDB; 5HCX; X-ray; 2.60 A; A=696-1022.
PDB; 5HCY; X-ray; 2.46 A; A=696-1022.
PDB; 5HCZ; X-ray; 2.62 A; A=696-1022.
PDB; 5HG5; X-ray; 1.52 A; A=695-1022.
PDB; 5HG7; X-ray; 1.85 A; A=695-1022.
PDB; 5HG8; X-ray; 1.42 A; A=695-1022.
PDB; 5HG9; X-ray; 2.15 A; A=695-1022.
PDB; 5HIB; X-ray; 2.85 A; A=695-1022.
PDB; 5HIC; X-ray; 2.60 A; A=695-1022.
PDB; 5J9Y; X-ray; 2.80 A; A=697-1019.
PDB; 5J9Z; X-ray; 2.50 A; A=696-1020.
PDB; 5JEB; X-ray; 3.30 A; A=696-1022.
PDB; 5LV6; NMR; -; A/B=634-677.
PDB; 5SX4; X-ray; 2.80 A; M/N=335-525.
PDB; 5SX5; X-ray; 2.50 A; M/N=335-525.
PDB; 5U8L; X-ray; 1.60 A; A=695-1022.
PDB; 5UG8; X-ray; 1.46 A; A=695-1022.
PDB; 5UG9; X-ray; 1.33 A; A=695-1022.
PDB; 5UGA; X-ray; 1.82 A; A=695-1022.
PDB; 5UGB; X-ray; 2.53 A; A=695-1022.
PDB; 5UGC; X-ray; 1.58 A; A=695-1022.
PDB; 5XGM; X-ray; 2.95 A; A=696-1022.
PDB; 5XGN; X-ray; 3.00 A; A/B=696-1022.
PDBsum; 1DNQ; -.
PDBsum; 1DNR; -.
PDBsum; 1IVO; -.
PDBsum; 1M14; -.
PDBsum; 1M17; -.
PDBsum; 1MOX; -.
PDBsum; 1NQL; -.
PDBsum; 1XKK; -.
PDBsum; 1YY9; -.
PDBsum; 1Z9I; -.
PDBsum; 2EB2; -.
PDBsum; 2EB3; -.
PDBsum; 2EXP; -.
PDBsum; 2EXQ; -.
PDBsum; 2GS2; -.
PDBsum; 2GS6; -.
PDBsum; 2GS7; -.
PDBsum; 2ITN; -.
PDBsum; 2ITO; -.
PDBsum; 2ITP; -.
PDBsum; 2ITQ; -.
PDBsum; 2ITT; -.
PDBsum; 2ITU; -.
PDBsum; 2ITV; -.
PDBsum; 2ITW; -.
PDBsum; 2ITX; -.
PDBsum; 2ITY; -.
PDBsum; 2ITZ; -.
PDBsum; 2J5E; -.
PDBsum; 2J5F; -.
PDBsum; 2J6M; -.
PDBsum; 2JIT; -.
PDBsum; 2JIU; -.
PDBsum; 2JIV; -.
PDBsum; 2KS1; -.
PDBsum; 2M0B; -.
PDBsum; 2M20; -.
PDBsum; 2N5S; -.
PDBsum; 2RF9; -.
PDBsum; 2RFD; -.
PDBsum; 2RFE; -.
PDBsum; 2RGP; -.
PDBsum; 3B2U; -.
PDBsum; 3B2V; -.
PDBsum; 3BEL; -.
PDBsum; 3BUO; -.
PDBsum; 3C09; -.
PDBsum; 3G5V; -.
PDBsum; 3G5Y; -.
PDBsum; 3GOP; -.
PDBsum; 3GT8; -.
PDBsum; 3IKA; -.
PDBsum; 3LZB; -.
PDBsum; 3NJP; -.
PDBsum; 3OB2; -.
PDBsum; 3OP0; -.
PDBsum; 3P0Y; -.
PDBsum; 3PFV; -.
PDBsum; 3POZ; -.
PDBsum; 3QWQ; -.
PDBsum; 3UG1; -.
PDBsum; 3UG2; -.
PDBsum; 3VJN; -.
PDBsum; 3VJO; -.
PDBsum; 3VRP; -.
PDBsum; 3VRR; -.
PDBsum; 3W2O; -.
PDBsum; 3W2P; -.
PDBsum; 3W2Q; -.
PDBsum; 3W2R; -.
PDBsum; 3W2S; -.
PDBsum; 3W32; -.
PDBsum; 3W33; -.
PDBsum; 4G5J; -.
PDBsum; 4G5P; -.
PDBsum; 4HJO; -.
PDBsum; 4I1Z; -.
PDBsum; 4I20; -.
PDBsum; 4I21; -.
PDBsum; 4I22; -.
PDBsum; 4I23; -.
PDBsum; 4I24; -.
PDBsum; 4JQ7; -.
PDBsum; 4JQ8; -.
PDBsum; 4JR3; -.
PDBsum; 4JRV; -.
PDBsum; 4KRL; -.
PDBsum; 4KRM; -.
PDBsum; 4KRO; -.
PDBsum; 4KRP; -.
PDBsum; 4LI5; -.
PDBsum; 4LL0; -.
PDBsum; 4LQM; -.
PDBsum; 4LRM; -.
PDBsum; 4R3P; -.
PDBsum; 4R3R; -.
PDBsum; 4R5S; -.
PDBsum; 4RIW; -.
PDBsum; 4RIX; -.
PDBsum; 4RIY; -.
PDBsum; 4RJ4; -.
PDBsum; 4RJ5; -.
PDBsum; 4RJ6; -.
PDBsum; 4RJ7; -.
PDBsum; 4RJ8; -.
PDBsum; 4TKS; -.
PDBsum; 4UIP; -.
PDBsum; 4UV7; -.
PDBsum; 4WD5; -.
PDBsum; 4WKQ; -.
PDBsum; 4WRG; -.
PDBsum; 4ZAU; -.
PDBsum; 4ZJV; -.
PDBsum; 4ZSE; -.
PDBsum; 5C8K; -.
PDBsum; 5C8M; -.
PDBsum; 5C8N; -.
PDBsum; 5CAL; -.
PDBsum; 5CAN; -.
PDBsum; 5CAO; -.
PDBsum; 5CAP; -.
PDBsum; 5CAQ; -.
PDBsum; 5CAS; -.
PDBsum; 5CAU; -.
PDBsum; 5CAV; -.
PDBsum; 5CNN; -.
PDBsum; 5CNO; -.
PDBsum; 5CZH; -.
PDBsum; 5CZI; -.
PDBsum; 5D41; -.
PDBsum; 5EDP; -.
PDBsum; 5EDQ; -.
PDBsum; 5EDR; -.
PDBsum; 5EM5; -.
PDBsum; 5EM6; -.
PDBsum; 5EM7; -.
PDBsum; 5EM8; -.
PDBsum; 5FED; -.
PDBsum; 5FEE; -.
PDBsum; 5FEQ; -.
PDBsum; 5GMP; -.
PDBsum; 5GNK; -.
PDBsum; 5GTY; -.
PDBsum; 5GTZ; -.
PDBsum; 5HCX; -.
PDBsum; 5HCY; -.
PDBsum; 5HCZ; -.
PDBsum; 5HG5; -.
PDBsum; 5HG7; -.
PDBsum; 5HG8; -.
PDBsum; 5HG9; -.
PDBsum; 5HIB; -.
PDBsum; 5HIC; -.
PDBsum; 5J9Y; -.
PDBsum; 5J9Z; -.
PDBsum; 5JEB; -.
PDBsum; 5LV6; -.
PDBsum; 5SX4; -.
PDBsum; 5SX5; -.
PDBsum; 5U8L; -.
PDBsum; 5UG8; -.
PDBsum; 5UG9; -.
PDBsum; 5UGA; -.
PDBsum; 5UGB; -.
PDBsum; 5UGC; -.
PDBsum; 5XGM; -.
PDBsum; 5XGN; -.
DisProt; DP00309; -.
ProteinModelPortal; P00533; -.
SMR; P00533; -.
BioGrid; 108276; 1199.
CORUM; P00533; -.
DIP; DIP-405N; -.
ELM; P00533; -.
IntAct; P00533; 492.
MINT; MINT-206389; -.
STRING; 9606.ENSP00000275493; -.
BindingDB; P00533; -.
ChEMBL; CHEMBL203; -.
DrugBank; DB08916; Afatinib.
DrugBank; DB00002; Cetuximab.
DrugBank; DB05424; CI-1033.
DrugBank; DB00530; Erlotinib.
DrugBank; DB03496; Flavopiridol.
DrugBank; DB00317; Gefitinib.
DrugBank; DB05324; HuMax-EGFr.
DrugBank; DB11737; Icotinib.
DrugBank; DB04988; IGN311.
DrugBank; DB05774; IMC-11F8.
DrugBank; DB05900; INSM-18.
DrugBank; DB01259; Lapatinib.
DrugBank; DB00281; Lidocaine.
DrugBank; DB05101; Matuzumab.
DrugBank; DB07662; N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE.
DrugBank; DB09559; Necitumumab.
DrugBank; DB13164; Olmutinib.
DrugBank; DB09330; Osimertinib.
DrugBank; DB01269; Panitumumab.
DrugBank; DB05374; Rindopepimut.
DrugBank; DB07602; S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE.
DrugBank; DB00072; Trastuzumab.
DrugBank; DB05294; Vandetanib.
GuidetoPHARMACOLOGY; 1797; -.
iPTMnet; P00533; -.
PhosphoSitePlus; P00533; -.
SwissPalm; P00533; -.
UniCarbKB; P00533; -.
BioMuta; EGFR; -.
DMDM; 2811086; -.
SWISS-2DPAGE; P00533; -.
EPD; P00533; -.
MaxQB; P00533; -.
PaxDb; P00533; -.
PeptideAtlas; P00533; -.
PRIDE; P00533; -.
DNASU; 1956; -.
Ensembl; ENST00000275493; ENSP00000275493; ENSG00000146648. [P00533-1]
Ensembl; ENST00000342916; ENSP00000342376; ENSG00000146648. [P00533-4]
Ensembl; ENST00000344576; ENSP00000345973; ENSG00000146648. [P00533-3]
Ensembl; ENST00000420316; ENSP00000413843; ENSG00000146648. [P00533-2]
GeneID; 1956; -.
KEGG; hsa:1956; -.
UCSC; uc003tqh.4; human. [P00533-1]
CTD; 1956; -.
DisGeNET; 1956; -.
EuPathDB; HostDB:ENSG00000146648.15; -.
GeneCards; EGFR; -.
HGNC; HGNC:3236; EGFR.
HPA; CAB000035; -.
HPA; CAB068186; -.
HPA; CAB073534; -.
HPA; HPA001200; -.
HPA; HPA018530; -.
MalaCards; EGFR; -.
MIM; 131550; gene.
MIM; 211980; phenotype.
MIM; 616069; phenotype.
neXtProt; NX_P00533; -.
OpenTargets; ENSG00000146648; -.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
Orphanet; 294023; Neonatal inflammatory skin and bowel disease.
Orphanet; 357191; Selection of therapeutic option in non-small cell lung carcinoma.
PharmGKB; PA7360; -.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
GeneTree; ENSGT00760000118799; -.
HOVERGEN; HBG000490; -.
InParanoid; P00533; -.
KO; K04361; -.
OMA; VCRKCHP; -.
OrthoDB; EOG091G00NO; -.
PhylomeDB; P00533; -.
TreeFam; TF106002; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1236394; Signaling by ERBB4.
Reactome; R-HSA-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-HSA-1251932; PLCG1 events in ERBB2 signaling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-177929; Signaling by EGFR.
Reactome; R-HSA-179812; GRB2 events in EGFR signaling.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-180336; SHC1 events in EGFR signaling.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-HSA-1963642; PI3K events in ERBB2 signaling.
Reactome; R-HSA-212718; EGFR interacts with phospholipase C-gamma.
Reactome; R-HSA-2179392; EGFR Transactivation by Gastrin.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
Reactome; R-HSA-5638303; Inhibition of Signaling by Overexpressed EGFR.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8857538; PTK6 promotes HIF1A stabilization.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
Reactome; R-HSA-8866910; TFAP2 (AP-2) family regulates transcription of growth factors and their receptors.
SignaLink; P00533; -.
SIGNOR; P00533; -.
ChiTaRS; EGFR; human.
EvolutionaryTrace; P00533; -.
GeneWiki; Epidermal_growth_factor_receptor; -.
GenomeRNAi; 1956; -.
PMAP-CutDB; P00533; -.
PRO; PR:P00533; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000146648; -.
ExpressionAtlas; P00533; baseline and differential.
Genevisible; P00533; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0030665; C:clathrin-coated vesicle membrane; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
GO; GO:0030139; C:endocytic vesicle; IEA:Ensembl.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; NAS:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0097489; C:multivesicular body, internal vesicle lumen; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:HGNC.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0070435; C:Shc-EGFR complex; ISS:BHF-UCL.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; NAS:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0048408; F:epidermal growth factor binding; IEA:Ensembl.
GO; GO:0005006; F:epidermal growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0004709; F:MAP kinase kinase kinase activity; NAS:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; IEA:InterPro.
GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0004888; F:transmembrane signaling receptor activity; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
GO; GO:0043006; P:activation of phospholipase A2 activity by calcium-mediated signaling; TAS:UniProtKB.
GO; GO:0007202; P:activation of phospholipase C activity; TAS:UniProtKB.
GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0098609; P:cell-cell adhesion; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071276; P:cellular response to cadmium ion; IMP:CAFA.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IMP:CAFA.
GO; GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0048546; P:digestive tract morphogenesis; IEA:Ensembl.
GO; GO:0016101; P:diterpenoid metabolic process; IEA:Ensembl.
GO; GO:0001892; P:embryonic placenta development; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0061029; P:eyelid development in camera-type eye; IEA:Ensembl.
GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0010960; P:magnesium ion homeostasis; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007494; P:midgut development; IEA:Ensembl.
GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:1905208; P:negative regulation of cardiocyte differentiation; IMP:BHF-UCL.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:1901185; P:negative regulation of ERBB signaling pathway; TAS:Reactome.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:0001503; P:ossification; NAS:UniProtKB.
GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IMP:UniProtKB.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:ParkinsonsUK-UCL.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
GO; GO:0035413; P:positive regulation of catenin import into nucleus; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0031659; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0045739; P:positive regulation of DNA repair; IDA:UniProtKB.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IMP:CAFA.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0042327; P:positive regulation of phosphorylation; IDA:UniProtKB.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IMP:BHF-UCL.
GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:BHF-UCL.
GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:ParkinsonsUK-UCL.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CAFA.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
GO; GO:0051205; P:protein insertion into membrane; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:Reactome.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:CAFA.
GO; GO:0046328; P:regulation of JNK cascade; IMP:CAFA.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IDA:UniProtKB.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IMP:CAFA.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
GO; GO:0033594; P:response to hydroxyisoflavone; IEA:Ensembl.
GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
GO; GO:0006950; P:response to stress; NAS:UniProtKB.
GO; GO:0070141; P:response to UV-A; IDA:BHF-UCL.
GO; GO:0007435; P:salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
GO; GO:0043586; P:tongue development; IEA:Ensembl.
GO; GO:0006412; P:translation; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 3.80.20.20; -; 4.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00261; FU; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Developmental protein; Direct protein sequencing;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Endosome;
Glycoprotein; Golgi apparatus; Host cell receptor for virus entry;
Isopeptide bond; Kinase; Membrane; Methylation; Nucleotide-binding;
Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 24 {ECO:0000269|PubMed:15340161,
ECO:0000269|Ref.16}.
CHAIN 25 1210 Epidermal growth factor receptor.
/FTId=PRO_0000016665.
TOPO_DOM 25 645 Extracellular. {ECO:0000255}.
TRANSMEM 646 668 Helical. {ECO:0000255}.
TOPO_DOM 669 1210 Cytoplasmic. {ECO:0000255}.
REPEAT 75 300 Approximate.
REPEAT 390 600 Approximate.
DOMAIN 712 979 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 718 726 ATP.
NP_BIND 790 791 ATP.
REGION 688 704 Important for dimerization,
phosphorylation and activation.
ACT_SITE 837 837 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 745 745 ATP.
BINDING 855 855 ATP.
SITE 1016 1016 Important for interaction with PIK3C2B.
MOD_RES 229 229 Phosphoserine.
{ECO:0000269|PubMed:21487020}.
MOD_RES 678 678 Phosphothreonine; by PKC and PKD/PRKD1.
{ECO:0000269|PubMed:10523301}.
MOD_RES 693 693 Phosphothreonine; by PKD/PRKD1.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:10523301,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:3138233}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:3138233}.
MOD_RES 991 991 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16083266}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 998 998 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:19563760}.
MOD_RES 1016 1016 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:19563760}.
MOD_RES 1026 1026 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16083266}.
MOD_RES 1039 1039 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1041 1041 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1042 1042 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1064 1064 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1069 1069 Phosphotyrosine.
{ECO:0000305|PubMed:22888118}.
MOD_RES 1070 1070 Phosphoserine.
{ECO:0000269|PubMed:3138233}.
MOD_RES 1071 1071 Phosphoserine.
{ECO:0000269|PubMed:3138233}.
MOD_RES 1081 1081 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 1092 1092 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12873986}.
MOD_RES 1110 1110 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:12873986,
ECO:0000269|PubMed:2543678}.
MOD_RES 1166 1166 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:24275569}.
MOD_RES 1172 1172 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:17081983}.
MOD_RES 1197 1197 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:19563760,
ECO:0000269|PubMed:19836242}.
MOD_RES 1199 1199 Omega-N-methylarginine.
{ECO:0000269|PubMed:21258366}.
CARBOHYD 56 56 N-linked (GlcNAc...) (complex)
asparagine; atypical; partial.
{ECO:0000269|PubMed:10731668,
ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:20837704}.
/FTId=CAR_000227.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:20837704}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:8962717}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:20837704,
ECO:0000269|PubMed:8962717}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:20837704}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10731668,
ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12620237,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:20837704}.
CARBOHYD 361 361 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10731668,
ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12620237,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:20837704}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:8962717}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12297050,
ECO:0000269|PubMed:12620237,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:20837704,
ECO:0000269|PubMed:8962717}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12620237,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:20837704,
ECO:0000269|PubMed:8962717}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:10731668,
ECO:0000269|PubMed:12620237,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266,
ECO:0000269|PubMed:19159218}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:10731668,
ECO:0000269|PubMed:12620237,
ECO:0000269|PubMed:12731890,
ECO:0000269|PubMed:16083266}.
CARBOHYD 623 623 N-linked (GlcNAc...) (high mannose)
asparagine.
{ECO:0000305|PubMed:12731890}.
DISULFID 31 58
DISULFID 157 187
DISULFID 190 199
DISULFID 194 207
DISULFID 215 223
DISULFID 219 231
DISULFID 232 240
DISULFID 236 248
DISULFID 251 260
DISULFID 264 291
DISULFID 295 307
DISULFID 311 326
DISULFID 329 333
DISULFID 337 362
DISULFID 470 499
DISULFID 506 515
DISULFID 510 523
DISULFID 526 535
DISULFID 539 555
DISULFID 558 571
DISULFID 562 579
DISULFID 582 591
DISULFID 595 617
DISULFID 620 628
DISULFID 624 636
CROSSLNK 716 716 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 737 737 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 754 754 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 867 867 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 929 929 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 970 970 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
VAR_SEQ 404 405 FL -> LS (in isoform 2).
{ECO:0000303|PubMed:7654368,
ECO:0000303|PubMed:8918811,
ECO:0000303|PubMed:9103388,
ECO:0000303|Ref.6}.
/FTId=VSP_002887.
VAR_SEQ 406 1210 Missing (in isoform 2).
{ECO:0000303|PubMed:7654368,
ECO:0000303|PubMed:8918811,
ECO:0000303|PubMed:9103388,
ECO:0000303|Ref.6}.
/FTId=VSP_002888.
VAR_SEQ 628 705 CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLFM
RRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR ->
PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESCL
GWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH (in
isoform 3).
{ECO:0000303|PubMed:11161793}.
/FTId=VSP_002889.
VAR_SEQ 628 628 C -> S (in isoform 4).
{ECO:0000303|PubMed:11161793}.
/FTId=VSP_002891.
VAR_SEQ 629 1210 Missing (in isoform 4).
{ECO:0000303|PubMed:11161793}.
/FTId=VSP_002892.
VAR_SEQ 706 1210 Missing (in isoform 3).
{ECO:0000303|PubMed:11161793}.
/FTId=VSP_002890.
VARIANT 30 297 Missing (variant EGFR vIII; found in a
lung cancer sample; somatic mutation;
induces lung cancer when exogenously
expressed).
{ECO:0000269|PubMed:16672372}.
/FTId=VAR_066493.
VARIANT 98 98 R -> Q (in dbSNP:rs17289589).
{ECO:0000269|Ref.7}.
/FTId=VAR_019293.
VARIANT 266 266 P -> R (in dbSNP:rs17336639).
{ECO:0000269|Ref.7}.
/FTId=VAR_019294.
VARIANT 428 428 G -> D (in NISBD2; loss of function; the
mutant does not localize to the cell
membrane; has diffuse cytoplasmic
localization; dbSNP:rs606231253).
{ECO:0000269|PubMed:24691054}.
/FTId=VAR_072435.
VARIANT 521 521 R -> K (in dbSNP:rs2227983).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.7}.
/FTId=VAR_019295.
VARIANT 674 674 V -> I (in dbSNP:rs17337079).
{ECO:0000269|Ref.7}.
/FTId=VAR_019296.
VARIANT 709 709 E -> A (found in a lung cancer sample;
more sensitive to gefitinib than wild-
type; dbSNP:rs397517085).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628,
ECO:0000269|PubMed:16533793}.
/FTId=VAR_026084.
VARIANT 709 709 E -> G (found in a lung cancer sample;
constitutively activated kinase with
higher levels of basal
autophosphorylation; more sensitive to
gefitinib than wild-type;
dbSNP:rs397517085).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628}.
/FTId=VAR_069498.
VARIANT 709 709 E -> K (found in a lung cancer sample;
dbSNP:rs727504256).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026085.
VARIANT 719 719 G -> A (found in a lung cancer sample;
dbSNP:rs121913428).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026086.
VARIANT 719 719 G -> C (found in a lung cancer sample;
dbSNP:rs28929495).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16533793}.
/FTId=VAR_026087.
VARIANT 719 719 G -> D (found in a lung cancer sample;
dbSNP:rs121913428).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026088.
VARIANT 719 719 G -> S (found in a lung cancer sample;
somatic mutation; strongly increased
kinase activity; constitutively activated
kinase with higher levels of basal
autophosphorylation; more sensitive to
gefitinib than wild-type;
dbSNP:rs28929495).
{ECO:0000269|PubMed:15118125,
ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628,
ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:17349580}.
/FTId=VAR_019297.
VARIANT 724 724 G -> S (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026089.
VARIANT 734 734 E -> K (found in a lung cancer sample;
dbSNP:rs121913420).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026090.
VARIANT 746 752 ELREATS -> D (found in a lung cancer
sample). {ECO:0000269|PubMed:15623594}.
/FTId=VAR_069499.
VARIANT 746 751 ELREAT -> A (found in a lung cancer
sample). {ECO:0000269|PubMed:15623594}.
/FTId=VAR_069500.
VARIANT 746 750 Missing (found in a lung cancer sample).
{ECO:0000269|PubMed:15623594}.
/FTId=VAR_026092.
VARIANT 746 746 Missing (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026091.
VARIANT 747 751 Missing (found in a lung cancer sample).
{ECO:0000269|PubMed:15623594}.
/FTId=VAR_069501.
VARIANT 747 749 Missing (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026094.
VARIANT 747 747 L -> F (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026093.
VARIANT 748 748 R -> P (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026095.
VARIANT 752 759 Missing (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026096.
VARIANT 768 768 S -> I (found in a lung cancer sample;
constitutively activated kinase with
higher levels of basal
autophosphorylation; more sensitive to
gefitinib than wild-type;
dbSNP:rs121913465).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628}.
/FTId=VAR_069502.
VARIANT 769 769 V -> M (found in a lung cancer sample;
dbSNP:rs147149347).
{ECO:0000269|PubMed:15623594}.
/FTId=VAR_069503.
VARIANT 787 787 Q -> R (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026097.
VARIANT 790 790 T -> M (found in a lung cancer sample;
increased kinase activity;
dbSNP:rs121434569).
{ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:18227510}.
/FTId=VAR_026098.
VARIANT 833 833 L -> V (found in a lung cancer sample;
more sensitive to gefitinib than wild-
type; dbSNP:rs397517126).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628,
ECO:0000269|PubMed:16533793}.
/FTId=VAR_026099.
VARIANT 834 834 V -> L (found in a lung cancer sample;
dbSNP:rs397517127).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026100.
VARIANT 835 835 H -> L (found in a lung cancer sample;
more sensitive to gefitinib than wild-
type; dbSNP:rs397517128).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628}.
/FTId=VAR_069504.
VARIANT 838 838 L -> V (found in a lung cancer sample;
more sensitive to gefitinib than wild-
type; dbSNP:rs864621996).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628}.
/FTId=VAR_069505.
VARIANT 858 858 L -> M (found in a lung cancer sample;
dbSNP:rs121913443).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026101.
VARIANT 858 858 L -> R (found in a lung cancer sample;
somatic mutation; constitutively
activated enzyme with strongly increased
kinase activity; more sensitive to
gefitinib than wild-type;
dbSNP:rs121434568).
{ECO:0000269|PubMed:15118125,
ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628,
ECO:0000269|PubMed:16533793,
ECO:0000269|PubMed:17349580}.
/FTId=VAR_019298.
VARIANT 861 861 L -> Q (found in a lung cancer sample;
constitutively activated kinase with
higher levels of basal
autophosphorylation; more sensitive to
gefitinib than wild-type;
dbSNP:rs121913444).
{ECO:0000269|PubMed:15623594,
ECO:0000269|PubMed:16205628,
ECO:0000269|PubMed:16533793}.
/FTId=VAR_026102.
VARIANT 873 873 G -> E (found in a lung cancer sample).
{ECO:0000269|PubMed:16533793}.
/FTId=VAR_026103.
VARIANT 962 962 R -> G (in dbSNP:rs17337451).
{ECO:0000269|Ref.7}.
/FTId=VAR_019299.
VARIANT 988 988 H -> P (in dbSNP:rs17290699).
{ECO:0000269|Ref.7}.
/FTId=VAR_019300.
VARIANT 1034 1034 L -> R (in dbSNP:rs34352568).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042095.
VARIANT 1210 1210 A -> V (in dbSNP:rs35918369).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042096.
MUTAGEN 275 275 Y->A: Strongly reduced
autophosphorylation and activation of
downstream kinases; when associated with
A-309. {ECO:0000269|PubMed:12297050}.
MUTAGEN 287 287 F->A: Strongly reduced
autophosphorylation and activation of
downstream kinases; when associated with
A-309. {ECO:0000269|PubMed:12297050}.
MUTAGEN 309 309 R->S: Strongly reduced
autophosphorylation and activation of
downstream kinases; when associated with
A-275. Strongly reduced
autophosphorylation and activation of
downstream kinases; when associated with
A-287. {ECO:0000269|PubMed:12297050}.
MUTAGEN 429 429 R->E: Abolishes autophosphorylation and
activation of downstream kinases.
{ECO:0000269|PubMed:12297050}.
MUTAGEN 587 590 DGPH->AGPA: Decreases intramolecular
interactions and facilitates EGF binding.
{ECO:0000269|PubMed:12620237}.
MUTAGEN 609 609 K->A: Decreases intramolecular
interactions and facilitates EGF binding.
{ECO:0000269|PubMed:12620237}.
MUTAGEN 688 688 L->A: Strongly reduced phosphorylation.
{ECO:0000269|PubMed:19560417,
ECO:0000269|PubMed:19563760}.
MUTAGEN 689 689 V->A: Reduced autophosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 689 689 V->M: Constitutively activated kinase.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 690 690 E->A: Reduced phosphorylation.
{ECO:0000269|PubMed:19560417,
ECO:0000269|PubMed:19563760}.
MUTAGEN 692 692 L->A,P: Strongly reduced phosphorylation.
{ECO:0000269|PubMed:19560417,
ECO:0000269|PubMed:19563760}.
MUTAGEN 693 693 T->A: Increased phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 693 693 T->D: Strongly reduced phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 694 694 P->A: Strongly reduced phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 699 699 P->A: Reduced phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 700 700 N->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 704 704 L->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 705 705 R->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 706 706 I->A: Abolishes phosphorylation.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 745 745 K->A,M: Abolishes kinase activity.
{ECO:0000269|PubMed:19560417}.
MUTAGEN 974 974 D->A: Strongly reduced phosphorylation.
MUTAGEN 977 977 R->A: Reduced phosphorylation.
{ECO:0000269|PubMed:19563760}.
MUTAGEN 1005 1006 ED->RK: Constitutively activated kinase.
{ECO:0000269|PubMed:19563760}.
MUTAGEN 1016 1016 Y->F: 50% decrease in interaction with
PIK3C2B. 65% decrease in interaction with
PIK3C2B; when associated with F-1197.
Abolishes interaction with PIK3C2B; when
associated with F-1197 and F-1092.
{ECO:0000269|PubMed:10805725}.
MUTAGEN 1067 1067 Q->G: No effect on interaction with CBLC.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 1068 1068 R->G: Strongly decreases interaction with
CBLC. {ECO:0000269|PubMed:22888118}.
MUTAGEN 1069 1069 Y->F: Abolishes interaction with CBLC.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 1092 1092 Y->F: No change in interaction with
PIK3C2B. Abolishes interaction with
PIK3C2B; when associated with F-1197 and
F-1016. {ECO:0000269|PubMed:10805725}.
MUTAGEN 1110 1110 Y->F: No change in interaction with
PIK3C2B. {ECO:0000269|PubMed:10805725}.
MUTAGEN 1172 1172 Y->F: No change in interaction with
PIK3C2B. {ECO:0000269|PubMed:10805725}.
MUTAGEN 1197 1197 Y->F: No change in interaction with
PIK3C2B. 65% decrease in interaction with
PIK3C2B; when associated with F-1016.
Abolishes interaction with PIK3C2B; when
associated with F-1092 and F-1016.
{ECO:0000269|PubMed:10805725}.
CONFLICT 540 540 N -> K (in Ref. 1; CAA25240).
{ECO:0000305}.
STRAND 40 43 {ECO:0000244|PDB:3QWQ}.
HELIX 44 55 {ECO:0000244|PDB:4UV7}.
STRAND 60 69 {ECO:0000244|PDB:4UV7}.
HELIX 77 81 {ECO:0000244|PDB:4UV7}.
STRAND 84 87 {ECO:0000244|PDB:4UV7}.
STRAND 89 93 {ECO:0000244|PDB:4UV7}.
HELIX 101 103 {ECO:0000244|PDB:1IVO}.
TURN 114 116 {ECO:0000244|PDB:4UV7}.
STRAND 117 122 {ECO:0000244|PDB:4UV7}.
STRAND 125 129 {ECO:0000244|PDB:1MOX}.
STRAND 145 152 {ECO:0000244|PDB:4UV7}.
HELIX 159 161 {ECO:0000244|PDB:4UV7}.
HELIX 164 166 {ECO:0000244|PDB:4UV7}.
HELIX 170 173 {ECO:0000244|PDB:1MOX}.
HELIX 195 197 {ECO:0000244|PDB:4UV7}.
STRAND 199 204 {ECO:0000244|PDB:4UV7}.
STRAND 211 214 {ECO:0000244|PDB:1MOX}.
STRAND 223 227 {ECO:0000244|PDB:4UV7}.
HELIX 228 230 {ECO:0000244|PDB:4UV7}.
STRAND 236 238 {ECO:0000244|PDB:4UV7}.
STRAND 240 244 {ECO:0000244|PDB:4UV7}.
TURN 245 247 {ECO:0000244|PDB:4UV7}.
STRAND 248 256 {ECO:0000244|PDB:4UV7}.
STRAND 259 263 {ECO:0000244|PDB:4UV7}.
STRAND 267 271 {ECO:0000244|PDB:4UV7}.
TURN 272 275 {ECO:0000244|PDB:4UV7}.
STRAND 276 279 {ECO:0000244|PDB:4UV7}.
STRAND 285 287 {ECO:0000244|PDB:4UV7}.
STRAND 290 294 {ECO:0000244|PDB:4UV7}.
TURN 296 298 {ECO:0000244|PDB:3B2V}.
STRAND 299 301 {ECO:0000244|PDB:4KRO}.
STRAND 303 305 {ECO:0000244|PDB:4KRP}.
STRAND 306 310 {ECO:0000244|PDB:4UV7}.
STRAND 313 315 {ECO:0000244|PDB:3B2V}.
STRAND 318 320 {ECO:0000244|PDB:3G5Y}.
STRAND 323 325 {ECO:0000244|PDB:3G5Y}.
STRAND 330 332 {ECO:0000244|PDB:4UV7}.
STRAND 336 338 {ECO:0000244|PDB:3P0Y}.
TURN 340 342 {ECO:0000244|PDB:3QWQ}.
HELIX 343 345 {ECO:0000244|PDB:3P0Y}.
STRAND 349 351 {ECO:0000244|PDB:3P0Y}.
TURN 353 355 {ECO:0000244|PDB:3P0Y}.
HELIX 356 359 {ECO:0000244|PDB:3P0Y}.
STRAND 363 367 {ECO:0000244|PDB:3P0Y}.
STRAND 369 371 {ECO:0000244|PDB:3P0Y}.
HELIX 373 377 {ECO:0000244|PDB:3P0Y}.
TURN 380 383 {ECO:0000244|PDB:3P0Y}.
HELIX 389 397 {ECO:0000244|PDB:3P0Y}.
STRAND 400 403 {ECO:0000244|PDB:3P0Y}.
STRAND 405 407 {ECO:0000244|PDB:3P0Y}.
HELIX 418 420 {ECO:0000244|PDB:3P0Y}.
TURN 433 435 {ECO:0000244|PDB:3P0Y}.
STRAND 436 442 {ECO:0000244|PDB:3P0Y}.
STRAND 458 464 {ECO:0000244|PDB:3P0Y}.
HELIX 472 474 {ECO:0000244|PDB:3P0Y}.
HELIX 477 480 {ECO:0000244|PDB:3P0Y}.
STRAND 481 483 {ECO:0000244|PDB:1YY9}.
STRAND 488 494 {ECO:0000244|PDB:3P0Y}.
HELIX 496 501 {ECO:0000244|PDB:3P0Y}.
STRAND 508 510 {ECO:0000244|PDB:5SX4}.
STRAND 515 519 {ECO:0000244|PDB:3P0Y}.
HELIX 520 522 {ECO:0000244|PDB:3P0Y}.
STRAND 523 526 {ECO:0000244|PDB:3P0Y}.
STRAND 531 533 {ECO:0000244|PDB:4KRL}.
STRAND 535 537 {ECO:0000244|PDB:1YY9}.
STRAND 540 546 {ECO:0000244|PDB:4UV7}.
STRAND 548 551 {ECO:0000244|PDB:4UV7}.
STRAND 554 557 {ECO:0000244|PDB:4UV7}.
STRAND 560 562 {ECO:0000244|PDB:4KRO}.
STRAND 566 568 {ECO:0000244|PDB:1YY9}.
STRAND 570 575 {ECO:0000244|PDB:4UV7}.
STRAND 578 587 {ECO:0000244|PDB:4UV7}.
STRAND 590 594 {ECO:0000244|PDB:4UV7}.
STRAND 597 602 {ECO:0000244|PDB:4UV7}.
STRAND 606 611 {ECO:0000244|PDB:4UV7}.
STRAND 615 619 {ECO:0000244|PDB:4UV7}.
STRAND 629 632 {ECO:0000244|PDB:4UV7}.
HELIX 633 635 {ECO:0000244|PDB:4UV7}.
STRAND 643 646 {ECO:0000244|PDB:2KS1}.
HELIX 648 669 {ECO:0000244|PDB:2KS1}.
STRAND 671 673 {ECO:0000244|PDB:1Z9I}.
HELIX 679 684 {ECO:0000244|PDB:3GOP}.
HELIX 685 687 {ECO:0000244|PDB:3GOP}.
STRAND 688 692 {ECO:0000244|PDB:1Z9I}.
STRAND 694 697 {ECO:0000244|PDB:1Z9I}.
STRAND 703 706 {ECO:0000244|PDB:3POZ}.
HELIX 709 711 {ECO:0000244|PDB:5UG9}.
STRAND 712 721 {ECO:0000244|PDB:5UG9}.
STRAND 724 731 {ECO:0000244|PDB:5UG9}.
TURN 734 736 {ECO:0000244|PDB:5UG9}.
STRAND 740 747 {ECO:0000244|PDB:5UG9}.
STRAND 748 750 {ECO:0000244|PDB:2ITU}.
TURN 753 755 {ECO:0000244|PDB:3W2S}.
HELIX 756 767 {ECO:0000244|PDB:5UG9}.
STRAND 772 774 {ECO:0000244|PDB:4I21}.
STRAND 777 791 {ECO:0000244|PDB:5UG9}.
STRAND 794 797 {ECO:0000244|PDB:4G5P}.
HELIX 798 804 {ECO:0000244|PDB:5UG9}.
HELIX 806 808 {ECO:0000244|PDB:5UG9}.
HELIX 811 830 {ECO:0000244|PDB:5UG9}.
HELIX 840 842 {ECO:0000244|PDB:5UG9}.
STRAND 843 847 {ECO:0000244|PDB:5UG9}.
STRAND 850 853 {ECO:0000244|PDB:5UG9}.
HELIX 858 862 {ECO:0000244|PDB:3POZ}.
TURN 863 865 {ECO:0000244|PDB:3POZ}.
STRAND 867 870 {ECO:0000244|PDB:5UG9}.
STRAND 873 876 {ECO:0000244|PDB:5CZI}.
HELIX 878 880 {ECO:0000244|PDB:5UG9}.
HELIX 883 888 {ECO:0000244|PDB:5UG9}.
HELIX 893 908 {ECO:0000244|PDB:5UG9}.
TURN 909 911 {ECO:0000244|PDB:2GS7}.
TURN 914 917 {ECO:0000244|PDB:5UG9}.
HELIX 920 922 {ECO:0000244|PDB:5UG9}.
HELIX 923 928 {ECO:0000244|PDB:5UG9}.
STRAND 937 939 {ECO:0000244|PDB:5JEB}.
HELIX 941 950 {ECO:0000244|PDB:5UG9}.
STRAND 951 953 {ECO:0000244|PDB:5JEB}.
HELIX 955 957 {ECO:0000244|PDB:5UG9}.
HELIX 961 972 {ECO:0000244|PDB:5UG9}.
HELIX 975 977 {ECO:0000244|PDB:5UG9}.
HELIX 984 986 {ECO:0000244|PDB:5HG8}.
TURN 992 998 {ECO:0000244|PDB:5HG8}.
STRAND 1004 1010 {ECO:0000244|PDB:3W2S}.
HELIX 1013 1016 {ECO:0000244|PDB:3POZ}.
STRAND 1068 1070 {ECO:0000244|PDB:3PFV}.
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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U0978m CLIA Erbb2,Kiaa3023,Mouse,Mus musculus,Neu,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2 96T
E0978h ELISA ERBB2,HER2,Homo sapiens,Human,Metastatic lymph node gene 19 protein,MLN 19,MLN19,NEU,NGL,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2,Tyrosine kin 96T
U0978h CLIA ERBB2,HER2,Homo sapiens,Human,Metastatic lymph node gene 19 protein,MLN 19,MLN19,NEU,NGL,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2,Tyrosine kina 96T
15-288-22631 Receptor tyrosine-protein kinase erbB-2 - EC 2.7.10.1; p185erbB2; C-erbB-2; NEU proto-oncogene; Tyrosine kinase-type cell surface receptor HER2; MLN 19 Polyclonal 0.1 mg
15-288-22631 Receptor tyrosine-protein kinase erbB-2 - EC 2.7.10.1; p185erbB2; C-erbB-2; NEU proto-oncogene; Tyrosine kinase-type cell surface receptor HER2; MLN 19 Polyclonal 0.05 mg
E0978h ELISA kit ERBB2,HER2,Homo sapiens,Human,Metastatic lymph node gene 19 protein,MLN 19,MLN19,NEU,NGL,p185erbB2,Proto-oncogene c-ErbB-2,Proto-oncogene Neu,Receptor tyrosine-protein kinase erbB-2,Tyrosin 96T
EIAAB13165 ERBB4,HER4,Homo sapiens,Human,p180erbB4,Proto-oncogene-like protein c-ErbB-4,Receptor tyrosine-protein kinase erbB-4,Tyrosine kinase-type cell surface receptor HER4
EIAAB13162 ERBB3,HER3,Homo sapiens,Human,Proto-oncogene-like protein c-ErbB-3,Receptor tyrosine-protein kinase erbB-3,Tyrosine kinase-type cell surface receptor HER3
EIAAB13164 Erbb3,Proto-oncogene-like protein c-ErbB-3,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-3
EIAAB13166 Erbb4,Proto-oncogene-like protein c-ErbB-4,Rat,Rattus norvegicus,Receptor tyrosine-protein kinase erbB-4,Tyro-2
EIAAB13167 Erbb4,Mer4,Mouse,Mus musculus,Proto-oncogene-like protein c-ErbB-4,Receptor tyrosine-protein kinase erbB-4
18-783-75623 RABBIT ANTI HUMAN EGF RECEPTOR - EPIDERMAL GROWTH FACTOR RECEPTOR; EC 2.7.10.1; Receptor tyrosine-protein kinase ErbB-1 Polyclonal 0.05 mg
15-288-21146 Epidermal growth factor receptor - EC 2.7.10.1; Receptor tyrosine-protein kinase ErbB-1 Polyclonal 0.05 mg
15-288-21146 Epidermal growth factor receptor - EC 2.7.10.1; Receptor tyrosine-protein kinase ErbB-1 Polyclonal 0.1 mg
E0978c ELISA kit Canis familiaris,Canis lupus familiaris,Dog,ERBB2,p185erbB2,Proto-oncogene c-ErbB-2,Receptor tyrosine-protein kinase erbB-2 96T
U0978c CLIA Canis familiaris,Canis lupus familiaris,Dog,ERBB2,p185erbB2,Proto-oncogene c-ErbB-2,Receptor tyrosine-protein kinase erbB-2 96T


 

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