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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 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    November 4, 2008 (Entry version 138)
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 [GENOMIC DNA], AND VARIANTS GLN-98; ARG-266; LYS-521; ILE-674; GLY-962 AND PRO-988.
Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.;
"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu).";
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 713-924.
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
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).
[14]
NUCLEOTIDE SEQUENCE OF 25-49.
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).
[15]
PROTEIN SEQUENCE OF 540.
Kohda D.;
Submitted (SEP-1997) to UniProtKB.
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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]
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]
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=696-1022.[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]
3B2U; X-ray; 2.58 A; A/B/E/I/M/P/S/V=334-538.[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=334-538.[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; -.
3B2U; -.
3B2V; -.
3BEL; -.
3BUO; -.
3C09; -.
DisProt DP00309; -.
ModBase P00533.
Protein-protein interaction databases
DIP DIP:405N; -.
IntAct P00533; -.
PTM databases
GlycoSuiteDB P00533; -.
PhosphoSite P00533; -.
Enzyme and pathway databases
Reactome REACT_9417; Signaling by EGFR.
Polymorphism databases
NIEHS-SNPs EGFR.
2D gel databases
SWISS-2DPAGE P00533; -.
Organism-specific databases
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; -.
GeneCards P00533.
Gene expression databases
ArrayExpress 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:0005634; Cellular component: nucleus (inferred from direct assay from UniProtKB).
GO:0051015; Molecular function: actin filament binding (inferred from direct assay from UniProtKB).
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:0007202; Biological process: activation of phospholipase C activity (traceable author statement from UniProtKB).