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UniProtKB/Swiss-Prot entry P00533

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EGFR_HUMAN
Primary accession number P00533
Secondary accession numbers O00688 O00732 P06268 Q14225 Q68GS5 Q92795 Q9BZS2 Q9GZX1 Q9H2C9 Q9H3C9 Q9UMD7 Q9UMD8 Q9UMG5
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on November 1, 1997 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 148)
Name and origin of the protein
Protein name Epidermal growth factor receptor [Precursor]
Synonyms EC 2.7.10.1
Receptor tyrosine-protein kinase ErbB-1
Gene name
Name: EGFR
Synonyms: ERBB1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1038/309418a0; PubMed=6328312 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1002/mrd.1080410205; PubMed=7654368 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1093/nar/24.20.4050; PubMed=8918811 [NCBI, ExPASy, EBI, Israel, Japan]
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 (ISOFORM 2).
TISSUE=Placenta;
DOI=10.1006/gyno.1996.4526; PubMed=9103388 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1006/geno.2000.6341; PubMed=11161793 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1126/science.6326261; PubMed=6326261 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1038/309806a0; PubMed=6330563 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1073/pnas.82.15.4920; PubMed=2991899 [NCBI, ExPASy, EBI, Israel, Japan]
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 OF 25-49.
DOI=10.1126/science.6324343; PubMed=6324343 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1110/ps.04682504; PubMed=15340161 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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 MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2006.02.018; PubMed=16543144 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1074/jbc.273.18.11150; PubMed=9556602 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1038/309270a0; PubMed=6325948 [NCBI, ExPASy, EBI, Israel, Japan]
Mroczkowski B., Mosig G., Cohen S.;
"ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA.";
Nature 309:270-273(1984).
[23]
 REVIEW.
DOI=10.1146/annurev.bi.56.070187.004313; PubMed=3039909 [NCBI, ExPASy, EBI, Israel, Japan]
Carpenter G.;
"Receptors for epidermal growth factor and other polypeptide mitogens.";
Annu. Rev. Biochem. 56:881-914(1987).
[24]
 LIGAND-BINDING.
DOI=10.1016/0092-8674(89)90867-2; PubMed=2790960 [NCBI, ExPASy, EBI, Israel, Japan]
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.
PubMed=2543678 [NCBI, ExPASy, EBI, Israel, Japan]
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]
 INTERACTION WITH CBL.
DOI=10.1074/jbc.270.35.20242; PubMed=7657591 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[27]
 GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
PubMed=8962717 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[28]
 GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
PubMed=10731668 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[29]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[30]
 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.
DOI=10.1128/MCB.20.11.3817-3830.2000; PubMed=10805725 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[31]
 INTERACTION WITH RIPK1.
DOI=10.1074/jbc.M008458200; PubMed=11116146 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[32]
 INTERACTION WITH MUC1, AND FUNCTION.
DOI=10.1074/jbc.C100359200; PubMed=11483589 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[33]
 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 MASS SPECTROMETRY.
DOI=10.1021/pr050113n; PubMed=16083266 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[34]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1069; TYR-1092; SER-1166 AND TYR-1172, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1074/mcp.M500089-MCP200; PubMed=15951569 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.;
"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.";
Mol. Cell. Proteomics 4:1240-1250(2005).
[35]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-978, AND MASS SPECTROMETRY.
TISSUE=Hepatocyte;
DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.;
"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.";
Proteomics 5:3589-3599(2005).
[36]
 INTERACTION WITH PELP1.
DOI=10.1158/0008-5472.CAN-05-0614; PubMed=16140940 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[37]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-995; TYR-998; SER-1064; TYR-1069; TYR-1092; TYR-1110; TYR-1138; TYR-1172 AND TYR-1197, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[38]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-869; TYR-1092; TYR-1172 AND TYR-1197, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[39]
 TISSUE SPECIFICITY.
DOI=10.1172/JCI31680; PubMed=17671655 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[40]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[41]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-991, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[42]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; THR-725; SER-991; SER-1025; SER-1026; SER-1037; SER-1039; SER-1042; SER-1064; SER-1081; SER-1166 AND TYR-1197, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[43]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-991; THR-993; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1045; SER-1064 AND SER-1166, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[44]
 IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[45]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[46]
 VARIANTS LUNG CANCER SER-719 AND ARG-858.
DOI=10.1126/science.1099314; PubMed=15118125 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[47]
 VARIANTS LUNG CANCER 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.
DOI=10.1158/1078-0432.CCR-05-1981; PubMed=16533793 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[48]
 VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X00588; CAA25240.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U95089; AAB53063.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48722; AAC50802.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48723; AAC50804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48724; AAC50796.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48725; AAC50797.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48726; AAC50798.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48727; AAC50799.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48728; AAC50800.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U48729; AAC50801.1; -; Genomic_RNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF288738; AAG35786.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF288738; AAG35787.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF288738; AAG35788.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF288738; AAG35789.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF288738; AAG35790.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY698024; AAT97979.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY588246; AAS83109.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF277897; AAK01080.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125253; AAG43240.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125539; AAG43243.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF125538; AAG43243.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X06370; CAA29668.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00663; CAA25282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M38425; AAA63171.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11234; AAA52370.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00018274; -.
IPI00221346; -.
IPI00221347; -.
IPI00221348; -.
PIR A00641; GQHUE.
RefSeq NP_005219.2; -.
NP_958439.1; -.
NP_958440.1; -.
NP_958441.1; -.
UniGene Hs.488293
3D structure databases
PDB
1DNQ; Model; -; A=25-336.[ExPASy / RCSB / EBI]
1DNR; Model; -; A=337-645.[ExPASy / RCSB / EBI]
1IVO; X-ray; 3.30 A; A/B=25-646.[ExPASy / RCSB / EBI]
1M14; X-ray; 2.60 A; A=695-1022.[ExPASy / RCSB / EBI]
1M17; X-ray; 2.60 A; A=695-1022.[ExPASy / RCSB / EBI]
1MOX; X-ray; 2.50 A; A/B=25-525.[ExPASy / RCSB / EBI]
1NQL; X-ray; 2.80 A; A=25-642.[ExPASy / RCSB / EBI]
1XKK; X-ray; 2.40 A; A=695-1022.[ExPASy / RCSB / EBI]
1YY9; X-ray; 2.60 A; A=25-642.[ExPASy / RCSB / EBI]
1Z9I; NMR; -; A=669-721.[ExPASy / RCSB / EBI]
2EB2; X-ray; 2.50 A; A=695-1022.[ExPASy / RCSB / EBI]
2EB3; X-ray; 2.84 A; A=695-1022.[ExPASy / RCSB / EBI]
2EXP; Model; -; A=311-326.[ExPASy / RCSB / EBI]
2EXQ; Model; -; A=27-536.[ExPASy / RCSB / EBI]
2GS2; X-ray; 2.80 A; A=696-1022.[ExPASy / RCSB / EBI]
2GS6; X-ray; 2.60 A; A=696-1022.[ExPASy / RCSB / EBI]
2GS7; X-ray; 2.60 A; A/B=696-1022.[ExPASy / RCSB / EBI]
2ITN; X-ray; 2.47 A; A=696-1019.[ExPASy / RCSB / EBI]
2ITO; X-ray; 3.25 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITP; X-ray; 2.74 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITQ; X-ray; 2.68 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITT; X-ray; 2.73 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITU; X-ray; 2.80 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITV; X-ray; 2.47 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITW; X-ray; 2.88 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITX; X-ray; 2.98 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITY; X-ray; 3.42 A; A=696-1022.[ExPASy / RCSB / EBI]
2ITZ; X-ray; 2.72 A; A=696-1022.[ExPASy / RCSB / EBI]
2J5E; X-ray; 3.10 A; A=696-1022.[ExPASy / RCSB / EBI]
2J5F; X-ray; 3.00 A; A=696-1022.[ExPASy / RCSB / EBI]
2J6M; X-ray; 3.10 A; A=696-1022.[ExPASy / RCSB / EBI]
2JIT; X-ray; 3.10 A; A/B=696-1022.[ExPASy / RCSB / EBI]
2JIU; X-ray; 3.05 A; A/B=695-1022.[ExPASy / RCSB / EBI]
2JIV; X-ray; 3.50 A; A/B=695-1022.[ExPASy / RCSB / EBI]
2RF9; X-ray; 3.50 A; A/B=696-1022.[ExPASy / RCSB / EBI]
2RFD; X-ray; 3.60 A; A/B=702-1022.[ExPASy / RCSB / EBI]
2RFE; X-ray; 2.90 A; A/B/C/D=702-1022.[ExPASy / RCSB / EBI]
2RGP; X-ray; 2.00 A; A=702-1016.[ExPASy / RCSB / EBI]
3B2U; X-ray; 2.58 A; A/B/E/I/M/P/S/V=335-538.[ExPASy / RCSB / EBI]
3B2V; X-ray; 3.30 A; A=25-642.[ExPASy / RCSB / EBI]
3BEL; X-ray; 2.30 A; A=702-1016.[ExPASy / RCSB / EBI]
3BUO; X-ray; 2.60 A; A/C=1063-1075.[ExPASy / RCSB / EBI]
3C09; X-ray; 3.20 A; A/D=335-538.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1DNQ; -.
1DNR; -.
1IVO; -.
1M14; -.
1M17; -.
1MOX; -.
1NQL; -.
1XKK; -.
1YY9; -.
1Z9I; -.
2EB2; -.
2EB3; -.
2EXP; -.
2EXQ; -.
2GS2; -.
2GS6; -.
2GS7; -.
2ITN; -.
2ITO; -.
2ITP; -.
2ITQ; -.
2ITT; -.
2ITU; -.
2ITV; -.
2ITW; -.
2ITX; -.
2ITY; -.
2ITZ; -.
2J5E; -.
2J5F; -.
2J6M; -.
2JIT; -.
2JIU; -.
2JIV; -.
2RF9; -.
2RFD; -.
2RFE; -.
2RGP; -.
3B2U; -.
3B2V; -.
3BEL; -.
3BUO; -.
3C09; -.
DisProt DP00309; -.
ModBase P00533.
Protein-protein interaction databases
DIP DIP:405N; -.
IntAct P00533; 112.
PTM databases
GlycoSuiteDB P00533; -.
PhosphoSite P00533; -.
Enzyme and pathway databases
BRENDA 2.7.10.1; 247.
Pathway_Interaction_DB a6b1_a6b4_integrin_pathway; a6b1 and a6b4 Integrin signaling.
arf6cyclingpathway; Arf6 signaling events.
endothelinpathway; Endothelins.
lysophospholipid_pathway; LPA receptor mediated events.
telomerasepathway; Regulation of Telomerase.
ptp1bpathway; Signaling events mediated by PTP1B.
syndecan_3_pathway; Syndecan-3-mediated signaling events.
txa2pathway; Thromboxane A2 receptor signaling.
Reactome REACT_9417; Signaling by EGFR.
2D gel databases
SWISS-2DPAGE P00533; -.
Organism-specific databases
GeneCards GC07P055054; -.
H-InvDB HIX0025274; -.
HIX0025338; -.
HGNC HGNC:3236; EGFR.
GenAtlas EGFR.
HPA CAB000035; -.
HPA001200; -.
HPA018530; -.
MIM 131550; gene. [NCBI / EBI]
211980; phenotype. [NCBI / EBI]
Orphanet 360; Glioblastoma.
PharmGKB PA7360; -.
Gene expression databases
ArrayExpress P00533; -.
Bgee P00533; -.
GermOnline ENSG00000146648; Homo sapiens.
Ontologies
GO
GO:0016323; Cellular component: basolateral plasma membrane (inferred from direct assay from UniProtKB).
GO:0005783; Cellular component: endoplasmic reticulum (inferred from direct assay from HPA).
GO:0005768; Cellular component: endosome (inferred from direct assay from UniProtKB).
GO:0005615; Cellular component: extracellular space (non-traceable author statement from UniProtKB).
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0070435; Cellular component: Shc-EGFR complex (inferred from sequence or structural similarity from UniProtKB).
GO:0051015; Molecular function: actin filament binding (inferred from direct assay from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003690; Molecular function: double-stranded DNA binding (non-traceable author statement from UniProtKB).
GO:0005006; Molecular function: epidermal growth factor receptor activity (inferred from direct assay from UniProtKB).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004710; Molecular function: MAP/ERK kinase kinase activity (non-traceable author statement from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from direct assay from UniProtKB).
GO:0019903; Molecular function: protein phosphatase binding (inferred from physical interaction from UniProtKB).
GO:0043006; Biological process: activation of phospholipase A2 activity by calcium-mediated signaling (traceable author statement from UniProtKB).
GO:0007202; Biological process: activation of phospholipase C activity (traceable author statement from UniProtKB).
GO:0008283; Biological process: cell proliferation (traceable author statement from ProtInc).
GO:0016337; Biological process: cell-cell adhesion (inferred from mutant phenotype from UniProtKB).
GO:0007173; Biological process: epidermal growth factor receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0045786; Biological process: negative regulation of cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0001503; Biological process: ossification (non-traceable author statement from UniProtKB).
GO:0030335; Biological process: positive regulation of cell migration (inferred from mutant phenotype from UniProtKB).
GO:0031659; Biological process: positive regulation of cyclin-dependent protein kinase activity during G1/S (inferred from direct assay from UniProtKB).
GO:0050679; Biological process: positive regulation of epithelial cell proliferation (inferred from direct assay from UniProtKB).
GO:0043406; Biological process: positive regulation of MAP kinase activity (inferred from direct assay from UniProtKB).
GO:0045429; Biological process: positive regulation of nitric oxide biosynthetic process (inferred from direct assay from UniProtKB).
GO:0042327; Biological process: positive regulation of phosphorylation (inferred from direct assay from UniProtKB).
GO:0051205; Biological process: protein insertion into membrane (traceable author statement from UniProtKB).
GO:0050999; Biological process: regulation of nitric-oxide synthase activity (inferred from direct assay from UniProtKB).
GO:0050730; Biological process: regulation of peptidyl-tyrosine phosphorylation (inferred from mutant phenotype from UniProtKB).
GO:0006950; Biological process: response to stress (non-traceable author statement from UniProtKB).
GO:0070141; Biological process: response to UV-A (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000494; EGF_rcpt_L.
IPR006211; Furin-like.
IPR006212; Furin_repeat.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR016245; Tyr_kinase_rcpt_EGF/ERB/XmrK.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Pfam PF00757; Furin-like; 2.
PF07714; Pkinase_Tyr; 1.
PF01030; Recep_L_domain; 2.
Pfam graphical view of domain structure.
PIRSF PIRSF000619; TyrPK_EGF-R; 1.
PRINTS PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00261; FU; 3.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas P00533; -.
PRIDE P00533; -.
Genome annotation databases
Ensembl ENSG00000146648; Homo sapiens. [Contig view]
GeneID 1956; -.
KEGG hsa:1956; -.
Phylogenomic databases
HOVERGEN P00533; -.
OMA P00533; ESCLGWI.
Other
DrugBank DB00002; Cetuximab.
DB00530; Erlotinib.
DB00317; Gefitinib.
DB01259; Lapatinib.
DB00281; Lidocaine.
DB01269; Panitumumab.
DB00072; Trastuzumab.
NextBio 7931; -.
PMAP-CutDB P00533; -.
SOURCE EGFR; Homo sapiens.
ProtoNet P00533.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Anti-oncogene; ATP-binding; Cell cycle; Cell membrane; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Isopeptide bond; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Repeat; Secreted; Signal; Transferase; Transmembrane; Tyrosine-protein kinase; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     24  24      
CHAIN   25   1210  1186     Epidermal growth factor receptor. PRO_0000016665
TOPO_DOM   25    645  621     Extracellular (Potential). 
TRANSMEM   646    668  23     Potential. 
TOPO_DOM   669   1210  542     Cytoplasmic (Potential). 
REPEAT   75    300  226     Approximate. 
REPEAT   390    600  211     Approximate. 
DOMAIN   712    979  268     Protein kinase. 
NP_BIND   718    726  9     ATP (By similarity). 
COMPBIAS   1025   1071  47     Ser-rich. 
ACT_SITE   837    837        Proton acceptor (By similarity). 
BINDING   745    745        ATP (By similarity). 
SITE   1016   1016  1     Important for interaction with PIK3C2B. 
MOD_RES   678    678        Phosphothreonine; by PKC. 
MOD_RES   693    693        Phosphothreonine. 
MOD_RES   695    695        Phosphoserine. 
MOD_RES   725    725        Phosphothreonine. 
MOD_RES   869    869        Phosphotyrosine. 
MOD_RES   978    978        Phosphotyrosine. 
MOD_RES   991    991        Phosphoserine. 
MOD_RES   993    993        Phosphothreonine. 
MOD_RES   995    995        Phosphoserine. 
MOD_RES   998    998        Phosphotyrosine. 
MOD_RES   1025   1025        Phosphoserine. 
MOD_RES   1026   1026        Phosphoserine. 
MOD_RES   1037   1037        Phosphoserine. 
MOD_RES   1039   1039        Phosphoserine. 
MOD_RES   1041   1041        Phosphothreonine. 
MOD_RES   1042   1042        Phosphoserine. 
MOD_RES   1045   1045        Phosphoserine. 
MOD_RES   1064   1064        Phosphoserine. 
MOD_RES   1069   1069        Phosphotyrosine. 
MOD_RES   1070   1070        Phosphoserine. 
MOD_RES   1071   1071        Phosphoserine. 
MOD_RES   1081   1081        Phosphoserine. 
MOD_RES   1092   1092        Phosphotyrosine; by autocatalysis. 
MOD_RES   1110   1110        Phosphotyrosine; by autocatalysis. 
MOD_RES   1138   1138        Phosphotyrosine. 
MOD_RES   1166   1166        Phosphoserine. 
MOD_RES   1172   1172        Phosphotyrosine; by autocatalysis. 
MOD_RES   1197   1197        Phosphotyrosine; by autocatalysis. 
CARBOHYD   56     56        N-linked (GlcNAc...) (complex); atypical; partial [GlycoSuiteDB]. CAR_000227
CARBOHYD   128    128        N-linked (GlcNAc...). 
CARBOHYD   175    175        N-linked (GlcNAc...). 
CARBOHYD   196    196        N-linked (GlcNAc...). 
CARBOHYD   352    352        N-linked (GlcNAc...). 
CARBOHYD   361    361        N-linked (GlcNAc...). 
CARBOHYD   413    413        N-linked (GlcNAc...). 
CARBOHYD   444    444        N-linked (GlcNAc...). 
CARBOHYD   528    528        N-linked (GlcNAc...). 
CARBOHYD   568    568        N-linked (GlcNAc...); partial. 
CARBOHYD   603    603        N-linked (GlcNAc...); partial. 
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). 
CROSSLNK   737    737        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   754    754        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   867    867        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   929    929        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
CROSSLNK   970    970        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin). 
VAR_SEQ   404    405        FL -> LS (in isoform 2). VSP_002887
VAR_SEQ   406   1210        Missing (in isoform 2). VSP_002888
VAR_SEQ   628    705        CTGPGLEGCPTNGPKIPSIATGMVGALLLLLVVALGIGLF MRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLR -> PGNESLKAMLFCLFKLSSCNQSNDGSVSHQSGSPAAQESC LGWIPSLLPSEFQLGWGGCSHLHAWPSASVIITASSCH (in isoform 3). VSP_002889
VAR_SEQ   628    628        C -> S (in isoform 4). VSP_002891
VAR_SEQ   629   1210        Missing (in isoform 4). VSP_002892
VAR_SEQ   706   1210        Missing (in isoform 3). VSP_002890
VARIANT   98     98  1     R -> Q (in dbSNP:rs17289589 [NCBI]). VAR_019293 
VARIANT   266    266  1     P -> R (in dbSNP:rs17336639 [NCBI]). VAR_019294 
VARIANT   521    521  1     R -> K (in dbSNP:rs2227983 [NCBI]). VAR_019295 
VARIANT   674    674  1     V -> I (in dbSNP:rs17337079 [NCBI]). VAR_019296 
VARIANT   709    709  1     E -> A (in lung cancer). VAR_026084 [3D]
VARIANT   709    709  1     E -> K (in lung cancer). VAR_026085 [3D]
VARIANT   719    719  1     G -> A (in lung cancer). VAR_026086 [3D]
VARIANT   719    719  1     G -> C (in lung cancer; dbSNP:rs28929495 [NCBI]). VAR_026087 [3D]
VARIANT   719    719  1     G -> D (in lung cancer). VAR_026088 [3D]
VARIANT   719    719  1     G -> S (in lung cancer; somatic mutation). VAR_019297 [3D]
VARIANT   724    724  1     G -> S (in lung cancer). VAR_026089 [3D]
VARIANT   734    734  1     E -> K (in lung cancer). VAR_026090 [3D]
VARIANT   746    750  5     Missing (in lung cancer). VAR_026092
VARIANT   746    746  1     Missing (in lung cancer). VAR_026091
VARIANT   747    749  3     Missing (in lung cancer). VAR_026094
VARIANT   747    747  1     L -> F (in lung cancer). VAR_026093 [3D]
VARIANT   748    748  1     R -> P (in lung cancer). VAR_026095 [3D]
VARIANT   752    759  8     Missing (in lung cancer). VAR_026096
VARIANT   787    787  1     Q -> R (in lung cancer). VAR_026097 [3D]
VARIANT   790    790  1     T -> M (in lung cancer). VAR_026098 [3D]
VARIANT   833    833  1     L -> V (in lung cancer). VAR_026099 [3D]
VARIANT   834    834  1     V -> L (in lung cancer). VAR_026100 [3D]
VARIANT   858    858  1     L -> M (in lung cancer). VAR_026101 [3D]
VARIANT   858    858  1     L -> R (in lung cancer; somatic mutation). VAR_019298 [3D]
VARIANT   861    861  1     L -> Q (in lung cancer). VAR_026102 [3D]
VARIANT   873    873  1     G -> E (in lung cancer). VAR_026103 [3D]
VARIANT   962    962  1     R -> G (in dbSNP:rs17337451 [NCBI]). VAR_019299 [3D]
VARIANT   988    988  1     H -> P (in dbSNP:rs17290699 [NCBI]). VAR_019300 [3D]
VARIANT   1034   1034  1     L -> R. VAR_042095 
VARIANT   1210   1210  1     A -> V. VAR_042096 
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. 
MUTAGEN   1092   1092        Y->F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. 
MUTAGEN   1110   1110        Y->F: No change in interaction with PIK3C2B. 
MUTAGEN   1172   1172        Y->F: No change in interaction with PIK3C2B. 
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. 
CONFLICT   540    540        N -> K (in Ref. 1; CAA25240). 
STRAND   40     43  4      
HELIX   44     55  12      
STRAND   59     63  5      
STRAND   65     67  3      
HELIX   77     81  5      
STRAND   84     87  4      
STRAND   89     93  5      
HELIX   101    103  3      
TURN   114    116  3      
STRAND   117    122  6      
STRAND   145    152  8      
HELIX   159    161  3      
TURN   164    167  4      
TURN   173    175  3      
STRAND   195    197  3      
STRAND   200    202  3      
TURN   203    205  3      
STRAND   211    215  5      
STRAND   224    229  6      
STRAND   236    238  3      
STRAND   241    247  7      
STRAND   249    256  8      
STRAND   259    263  5      
STRAND   267    271  5      
TURN   272    275  4      
STRAND   276    279  4      
STRAND   285    287  3      
STRAND   290    294  5      
STRAND   299    301  3      
STRAND   305    309  5      
STRAND   321    323  3      
STRAND   330    332  3      
STRAND   340    342  3      
HELIX   343    345  3      
HELIX   353    355  3      
HELIX   357    359  3      
STRAND   363    367  5      
STRAND   369    371  3      
HELIX   373    377  5      
TURN   380    383  4      
HELIX   389    397  9      
STRAND   400    403  4      
STRAND   405    408  4      
HELIX   418    420  3      
TURN   433    435  3      
STRAND   436    442  7      
STRAND   458    464  7      
HELIX   472    474  3      
HELIX   477    480  4      
STRAND   492    494  3      
HELIX   496    498  3      
TURN   499    503  5      
TURN   507    509  3      
STRAND   515    519  5      
STRAND   522    525  4      
STRAND   540    543  4      
STRAND   548    557  10      
STRAND   571    575  5      
STRAND   579    587  9      
STRAND   590    594  5      
STRAND   597    600  4      
STRAND   602    611  10      
STRAND   616    619  4      
STRAND   629    632  4      
TURN   633    635  3      
STRAND   704    706  3      
TURN   709    711  3      
STRAND   712    720  9      
STRAND   722    731  10      
STRAND   740    747  8      
HELIX   756    768  13      
STRAND   777    791  15      
HELIX   798    804  7      
STRAND   806    808  3      
HELIX   811    830  20      
HELIX   840    842  3      
STRAND   843    847  5      
STRAND   850    853  4      
HELIX   858    861  4      
TURN   862    865  4      
TURN   878    880  3      
HELIX   883    888  6      
HELIX   893    908  16      
TURN   914    917  4      
HELIX   920    922  3      
HELIX   923    929  7      
HELIX   941    950  10      
HELIX   955    957  3      
HELIX   961    973  13      
HELIX   975    978  4      
TURN   982    986  5      
HELIX   996   1002  7      
HELIX   1013   1016  4      
Sequence information
Length: 1210 AA [This is the length of the unprocessed precursor] Molecular weight: 134277 Da [This is the MW of the unprocessed precursor] CRC64: D8A2A50B4EFB6ED2 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV 

        70         80         90        100        110        120 
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA 

       130        140        150        160        170        180 
VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF 

       190        200        210        220        230        240 
QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC 

       250        260        270        280        290        300 
TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 

       310        320        330        340        350        360 
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK 

       370        380        390        400        410        420 
NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF 

       430        440        450        460        470        480 
ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL 

       490        500        510        520        530        540 
FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN 

       550        560        570        580        590        600 
LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 

       610        620        630        640        650        660 
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV 

       670        680        690        700        710        720 
ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS 

       730        740        750        760        770        780 
GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI 

       790        800        810        820        830        840 
CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA 

       850        860        870        880        890        900 
RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY 

       910        920        930        940        950        960 
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK 

       970        980        990       1000       1010       1020 
FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ 

      1030       1040       1050       1060       1070       1080 
QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED 

      1090       1100       1110       1120       1130       1140 
SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN 

      1150       1160       1170       1180       1190       1200 
TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV 

      1210 
APQSSEFIGA
P00533 in FASTA format

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