产品简要
公司名称 :
MyBioSource
产品类型 :
蛋白
产品名称 :
重组人类表皮生长因子受体
目录 :
MBS717309
规格 :
0.05毫克(大肠杆菌)
价格 :
180美元
更多信息或购买 :
产品信息
目录号 :
MBS717309
产品类型 :
重组蛋白
产品全称 :
重组人类表皮生长因子受体
产品简称 :
表皮生长因子受体
产品名称同义词 :
Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1
其他名称 :
epidermal growth factor receptor isoform a; Epidermal growth factor receptor; epidermal growth factor receptor; epidermal growth factor receptor; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1
产品基因名称 :
表皮生长因子受体
其他基因名称 :
表皮生长因子受体;表皮生长因子受体;ERBB;HER1;mENA;ERBB1;PIG61;NISBD2;ERBB;ERBB1;HER1
UniProt数据库进入名 :
EGFR_HUMAN
宿主 :
大肠杆菌
序列位置 :
26-645
序列长度 :
1210
序列 :
EEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGN
LEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLEN
LQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQE
ILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQ
NHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCS
GRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEAT
CKDTCPPLMLYNPTTYQMDVN
LEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLEN
LQIIRGNMYYENSYALAVLSNYDANKTGLKELPMRNLQE
ILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDFQ
NHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCS
GRCRGKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEAT
CKDTCPPLMLYNPTTYQMDVN
纯度 :
Greater than 90% as determined by SDS-PAGE.
储存稳定性 :
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
产品种类 :
信号转导
产品描述 :
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. Isoform 2 may act as an antagonist of EGF action.
产品引用 :
Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells.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.Nature 309:418-425(1984)
Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta.Ilekis J.V., Stark B.C., Scoccia B.Mol. Reprod. Dev. 41:149-156(1995)
A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor.Reiter J.L., Maihle N.J.Nucleic Acids Res. 24:4050-4056(1996)
Expression of a truncated epidermal growth factor receptor-like protein (TEGFR)
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Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms.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.Genomics 71:1-20(2001)
Cloning of the cDNA for a short EGF receptor from human placenta.Xu L., Hong A., He X.NIEHS SNPs programHuman and mouse alternative EGFR transcripts encoding only the extracellular domain of the receptor.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.Expression cloning of human EGF receptor complementary DNA
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Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells.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.Nature 309:806-810(1984)
Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells.Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G., O'Malley B.W.Biochem. Biophys. Res. Commun. 124:125-132(1984)
The human EGF receptor gene
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Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis.Haley J.D., Waterfield M.D.J. Biol. Chem. 266:1746-1753(1991)
Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene.Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985)
Production of an epidermal growth factor receptor-related protein.Weber W., Gill G.N., Spiess J.Science 224:294-297(1984)
Kohda D.Submitted (SEP-1997)
to UniProtKBEpidermal growth factor receptor threonine and serine residues phosphorylated in vivo.Heisermann G.J., Gill G.N.J. Biol. Chem. 263:13152-13158(1988)
Signal peptide prediction based on analysis of experimentally verified cleavage sites.Zhang Z., Henzel W.J.Protein Sci. 13:2819-2824(2004)
Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase.Russo M.W., Lukas T.J., Cohen S., Staros J.V.J. Biol. Chem. 260:5205-5208(1985)
Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain.Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.Mol. Cell 21:737-748(2006)
Disulfide bond structure of human epidermal growth factor receptor.Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.J. Biol. Chem. 273:11150-11157(1998)
ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA.Mroczkowski B., Mosig G., Cohen S.Nature 309:270-273(1984)
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Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation.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.Cell 59:33-43(1989)
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.Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M., Howk R., Givol D., Ullrich A., Schlessinger J.J. Biol. Chem. 264:10667-10671(1989)
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.Johnson G.R., Kannan B., Shoyab M., Stromberg K.J. Biol. Chem. 268:2924-2931(1993)
Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor.Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T., Davis R.J.Science 272:1797-1802(1996)
Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells.Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.J. Cell Biol. 143:1471-1484(1998)
Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor.Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.EMBO J. 18:5567-5576(1999)
Recombinant human betacellulin. Molecular structure, biological activities, and receptor interaction.Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J., Igarashi K., Sasada R.J. Biol. Chem. 269:9966-9973(1994)
Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF)
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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.Komurasaki T., Toyoda H., Uchida D., Morimoto S.Oncogene 15:2841-2848(1997)
Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase.Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.Mol. Cell. Biol. 18:1622-1634(1998)
Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis.Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.EMBO J. 18:2489-2499(1999)
Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck.Braverman L.E., Quilliam L.A.J. Biol. Chem. 274:5542-5549(1999)
Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor.Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.J. Biochem. 127:65-72(2000)
RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation.Derrien A., Druey K.M.J. Biol. Chem. 276:48532-48538(2001)
Characterization of glycosylation sites of the epidermal growth factor receptor.Zhen Y., Caprioli R.M., Staros J.V.Biochemistry 42:5478-5492(2003)
Identification and characterization of signal transducer and activator of transcription 3 recruitment sites within the epidermal growth factor receptor.Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.Cancer Res. 63:3923-3930(2003)
LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation.Gur G., Rubin C., Katz M., Amit I., Citri A., Nilsson J., Amariglio N., Henriksson R., Rechavi G., Hedman H., Wides R., Yarden Y.EMBO J. 23:3270-3281(2004)
Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors.Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.Mol. Cell. Biol. 20:3817-3830(2000)
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.Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S., Vartanian T.J. Biol. Chem. 276:8865-8874(2001)
The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin.Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III, Kufe D.J. Biol. Chem. 276:35239-35242(2001)
Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling.Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y.J. Biol. Chem. 280:7038-7048(2005)
Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity.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.J. Biol. Chem. 280:8503-8512(2005)
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)
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Functional implications of altered subcellular localization of PELP1 in breast cancer cells.Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z., Sahin A.A., Kumar R.Cancer Res. 65:7724-7732(2005)
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006)
Tyrosine phosphorylation controls PCNA function through protein stability.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.Nat. Cell Biol. 8:1359-1368(2006)
Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia.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.J. Clin. Invest. 117:2260-2267(2007)
Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation.Shen F., Lin Q., Gu Y., Childress C., Yang W.Mol. Biol. Cell 18:732-742(2007)
Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking.Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.Cell. Signal. 20:1725-1739(2008)
Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein.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.EMBO J. 27:2305-2316(2008)
Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. IIIJ. Proteome Res. 7:1346-1351(2008)
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008)
A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008)
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009)
An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis.Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.Curr. Biol. 19:1788-1798(2009)
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.Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E., Taniguchi H., Konishi H.J. Biol. Chem. 284:20206-20214(2009)
Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009)
Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009)
G protein-coupled receptor 30 expression is up-regulated by EGF and TGF alpha in estrogen receptor alpha-positive cancer cells.Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F., Fuqua S.A., Ando S., Maggiolini M.Mol. Endocrinol. 23:1815-1826(2009)
COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport.Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.Biochem. Biophys. Res. Commun. 399:498-504(2010)
Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts.Madeo A., Maggiolini M.Cancer Res. 70:6036-6046(2010)
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.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.Sci. Signal. 3:RA3-RA3(2010)
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011)
Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells.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.J. Biol. Chem. 286:20558-20568(2011)
Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation.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.Nat. Cell Biol. 13:174-181(2011)
FER tyrosine kinase (FER)
overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB.Guo C., Stark G.R.Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011)
The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane.Tanno H., Yamaguchi T., Goto E., Ishido S., Komada M.Mol. Biol. Cell 23:1343-1353(2012)
Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression.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.Oncogene 31:4599-4608(2012)
The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor.Smith C.J., Berry D.M., McGlade C.J.J. Cell Sci. 126:1366-1380(2013)
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014)
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H., Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.Cell 110:775-787(2002)
EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A.Mol. Cell 11:507-517(2003)
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.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.Cancer Res. 64:6652-6659(2004)
Structural basis for inhibition of the epidermal growth factor receptor by cetuximab.Li S., Schmitz K.R., Jeffrey P.D., Wiltzius J.J., Kussie P., Ferguson K.M.Cancer Cell 7:301-311(2005)
A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor.Choowongkomon K., Carlin C.R., Sonnichsen F.D.J. Biol. Chem. 280:24043-24052(2005)
Structures of lung cancer-derived EGFR mutants and inhibitor complexes
mechanism of activation and insights into differential inhibitor sensitivity.Yun C.H., Boggon T.J., Li Y., Woo M.S., Greulich H., Meyerson M., Eck M.J.Cancer Cell 11:217-227(2007)
Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface.Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.Nature 450:741-744(2007)
The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP.Yun C.H., Mengwasser K.E., Toms A.V., Woo M.S., Greulich H., Wong K.K., Meyerson M., Eck M.J.Proc. Natl. Acad. Sci. U.S.A. 105:2070-2075(2008)
Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment.Jura N., Endres N.F., Engel K., Deindl S., Das R., Lamers M.H., Wemmer D.E., Zhang X., Kuriyan J.Cell 137:1293-1307(2009)
The juxtamembrane region of the EGF receptor functions as an activation domain.Red Brewer M., Choi S.H., Alvarado D., Moravcevic K., Pozzi A., Lemmon M.A., Carpenter G.Mol. Cell 34:641-651(2009)
Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases.Mineev K.S., Bocharov E.V., Pustovalova Y.E., Bocharova O.V., Chupin V.V., Arseniev A.S.J. Mol. Biol. 400:231-243(2010)
Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Springer T.A.Mol. Cell. Biol. 30:5432-5443(2010)
Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide.Structural genomics consortiumSubmitted (OCT-2010)
to the PDB data bankStructural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c.Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., Yamanashi Y., Yamamoto T., Nakagawa A.J. Biochem. 152:487-495(2012)
High frequency of epidermal growth factor receptor mutations with complex patterns in non-small cell lung cancers related to gefitinib responsiveness in Taiwan.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.Clin. Cancer Res. 10:8195-8203(2004)
EGFR mutations in lung cancer
correlation with clinical response to gefitinib therapy.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.Science 304:1497-1500(2004)
Distinct epidermal growth factor receptor and KRAS mutation patterns in non-small cell lung cancer patients with different tobacco exposure and clinicopathologic features.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.Clin. Cancer Res. 12:1647-1653(2006)
Distinctive activation patterns in constitutively active and gefitinib-sensitive EGFR mutants.Chen Y.R., Fu Y.N., Lin C.H., Yang S.T., Hu S.F., Chen Y.T., Tsai S.F., Huang S.F.Oncogene 25:1205-1215(2006)
Epidermal growth factor receptor variant III mutations in lung tumorigenesis and sensitivity to tyrosine kinase inhibitors.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.Proc. Natl. Acad. Sci. U.S.A. 103:7817-7822(2006)
Patterns of somatic mutation in human cancer genomes.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.Nature 446:153-158(2007)
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+Additional computationally mapped references. p>Provides general information on the entry.
NCBI GI登录号 :
29725609
NCBI登录号 :
NP_005219.2
NCBI基因登录号 :
NM_005228.3
UniProt数据库登录号 :
P00533
NCBI分子量 :
72.5kD
NCBI信号通路 :
AGE/RAGE Pathway (698754); ARMS-mediated Activation Pathway (1269471); Adaptive Immune System Pathway (1269171); Adherens Junction Pathway (83070); Adherens Junction Pathway (481); AhR Pathway (755436); Alpha6-Beta4 Integrin Signaling Pathway (198807); Androgen Receptor Signaling Pathway (198806); Arf6 Signaling Events Pathway (138034); Axon Guidance Pathway (1270303)
NCBI总结 :
The protein encoded by this gene is a transmembrane glycoprotein that is a member of the protein kinase superfamily. This protein is a receptor for members of the epidermal growth factor family. EGFR is a cell surface protein that binds to epidermal growth factor. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. Mutations in this gene are associated with lung cancer. Multiple alternatively spliced transcript variants that encode different protein isoforms have been found for this gene. [provided by RefSeq, Jul 2010]
UniProt数据库总结 :
EGFR: a receptor tyrosine kinase. This is a receptor for epidermal growth factor (EGF) and related growth factors including TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30, and vaccinia virus growth factor. EGFR is involved in the control of cell growth and differentiation. It is a single-pass transmembrane tyrosine kinase. Ligand binding to this receptor results in receptor dimerization, autophosphorylation (in trans), activation of various downstream signaling molecules and lysosomal degradation. It can be phosphorylated and activated by Src. Activated EGFR binds the SH2 domain of phospholipase C-gamma (PLC-gamma), activating PLC-gamma-mediated downstream signaling. Phosphorylated EGFR binds Cbl, leading to its ubiquitination and degradation. Grb2 and SHC bind to phospho-EGFR and are involved in the activation of MAP kinase signaling pathways. Phosphorylation on Ser and Thr residues is thought to represent a mechanism for attenuation of EGFR kinase activity. EGFR is overexpressed in breast, head and neck cancers, correlating with poor survival. Activating somatic mutations are seen in lung cancer, corresponding to the minority of patients with strong responses to the EGFR inhibitor Iressa (gefitinib). Mutations and amplifications are also seen in glioblastoma, and upregulation is seen in colon cancer and neoplasms. In xenografts, inhibitors synergize with cytotoxic drugs in the inhibition of many tumor types. Inhibitors include: Iressa/ZD1839, Erbitux, Tarceva, and lapatinib. Four alternatively spliced isoforms have been described. Protein type: Membrane protein, integral; EC 2.7.10.1; Protein kinase, TK; Protein kinase, tyrosine (receptor); Kinase, protein; Tumor suppressor; TK group; EGFR family. Chromosomal Location of Human Ortholog: 7p12. Cellular Component: AP-2 adaptor complex; basolateral plasma membrane; cell surface; cytoplasm; early endosome membrane; endoplasmic reticulum membrane; endosome; endosome membrane; extracellular space; focal adhesion; Golgi membrane; integral to membrane; lipid raft; membrane; nuclear membrane; nucleus; perinuclear region of cytoplasm; plasma membrane; receptor complex. Molecular Function: actin filament binding; ATP binding; chromatin binding; double-stranded DNA binding; enzyme binding; epidermal growth factor receptor activity; identical protein binding; MAP kinase kinase kinase activity; nitric-oxide synthase regulator activity; protein binding; protein heterodimerization activity; protein phosphatase binding; protein-tyrosine kinase activity; receptor signaling protein tyrosine kinase activity; transmembrane receptor activity; transmembrane receptor protein tyrosine kinase activity; ubiquitin protein ligase binding. Biological Process: activation of MAPKK activity; axon guidance; calcium-dependent phospholipase A2 activation; cell proliferation; cell surface receptor linked signal transduction; cell-cell adhesion; cerebral cortex cell migration; digestive tract morphogenesis; embryonic placenta development; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; G1/S-specific positive regulation of cyclin-dependent protein kinase activity; hair follicle development; innate immune response; insulin receptor signaling pathway; learning and/or memory; MAPKKK cascade; negative regulation of apoptosis; negative regulation of epidermal growth factor receptor signaling pathway; negative regulation of protein catabolic process; nerve growth factor receptor signaling pathway; ossification; peptidyl-tyrosine phosphorylation; phosphoinositide-mediated signaling; phospholipase C activation; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of DNA repair; positive regulation of DNA replication; positive regulation of epithelial cell proliferation; positive regulation of fibroblast proliferation; positive regulation of MAP kinase activity; positive regulation of nitric oxide biosynthetic process; positive regulation of phosphorylation; positive regulation of protein amino acid phosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of transcription from RNA polymerase II promoter; protein amino acid autophosphorylation; protein insertion into membrane; Ras protein signal transduction; regulation of nitric-oxide synthase activity; regulation of peptidyl-tyrosine phosphorylation; response to stress; salivary gland morphogenesis; signal transduction; small GTPase mediated signal transduction; vascular endothelial growth factor receptor signaling pathway. Disease: Lung Cancer
尺寸1 :
0.05毫克(大肠杆菌)
价格1 :
180美元
尺寸2 :
0.2毫克(大肠杆菌)
价格2 :
410
size3 :
0.5毫克(大肠杆菌)
价格3 :
665
size4 :
1毫克(大肠杆菌)
price4 :
1050
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