ID EGFR_HUMAN AC P00533; P06268; DT 21-JUL-1986 (REL. 01, CREATED) DT 21-JUL-1986 (REL. 01

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ID EGFR_HUMAN AC P00533; P06268; DT 21-JUL-1986 (REL. 01, CREATED) DT 21-JUL-1986 (REL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1991 (REL. 20, LAST ANNOTATION UPDATE) DE EPIDERMAL GROWTH FACTOR RECEPTOR PRECURSOR (EC 2.7.1.112). GN ERBB1 OR EGFR. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RM 84219729 RA ULLRICH A., COUSSENS L., HAYFLICK J.S., DULL T.J., GRAY A., TAM A.W., RA LEE J., YARDEN Y., LIBERMANN T.A., SCHLESSINGER J., DOWNWARD J., RA MAYES E.L.V., WHITTLE N., WATERFIELD M.D., SEEBURG P.H.; RL NATURE 309:418-425(1984). RN [2] RP SEQUENCE OF 713-924 FROM N.A. RM 84196372 RA LIN C.R., CHEN W.S., KRUIGER W., STOLARSKY L.S., WEBER W., RA EVANS R.M., VERMA I.M., GILL G.N., ROSENFELD M.G.; RL SCIENCE 224:843-848(1984). RN [3] RP SEQUENCE OF 150-962 FROM N.A. RM 84245835 RA XU Y., ISHII S., CLARK A.J.L., SULLIVAN M., WILSON R.K., MA D.P., RA ROE B.A., MERLINO G.T., PASTAN I.; RL NATURE 309:806-810(1984). RN [4] RP SEQUENCE OF 1028-1210 FROM N.A. RM 85046483 RA SIMMEN F.A., GOPE M.L., SCHULZ T.Z., WRIGHT D.A., CARPENTER G., RA O'MALLEY B.W.; RL BIOCHEM. BIOPHYS. RES. COMMUN. 124:125-132(1984). RN [5] RP SEQUENCE OF 1-29 FROM N.A. RM 88217333 RA HALEY J., WHITTLE N., BENNETT P., KINCHINGTON D., ULLRICH A., RA WATERFIELD M.; RL ONCOGENE RES. 1:375-396(1987). RN [6] RP SEQUENCE OF 1-29 FROM N.A. RA HALEY J.D., WATERFIELD M.D.; RL SUBMITTED (SEP-1990) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [7] RP RECEPTOR ACTIVITY. RM 84191554 RA MROCZKOWSKI B., MOSIG G., COHEN S.; RL NATURE 309:270-273(1984). RN [8] RP PHOSPHORYLATION. RM 89278137 RA MARGOLIS B.L., LAX I., KRIS R., DOMBALAGIAN M., HONEGGER A.M., RA HOWK R., GIVOL D., ULLRICH A., SCHLESSINGER J.; RL J. BIOL. CHEM. 264:10667-10671(1989). RN [9] RP REVIEW. RM 87297456 RA CARPENTER G.; RL ANNU. REV. BIOCHEM. 56:881-914(1987). CC -!- FUNCTION: THE EGF RECEPTOR MEDIATES THE BIOLOGICAL SIGNAL OF EGF CC AND ALSO OF TRANSFORMING GROWTH FACTOR ALPHA AND VACCINIA VIRUS CC GROWTH FACTOR. CC -!- BINDING OF EGF TO THE RECEPTOR LEADS TO INTERNALIZATION OF THE CC EGF-RECEPTOR COMPLEX, INDUCTION OF THE TYROSINE KINASE ACTIVITY, CC STIMULATION OF CELL DNA SYNTHESIS, AND CELL PROLIFERATION. CC -!- SIMILARITY: TO THE EGF RECEPTOR FAMILY. CC -!- CAUTION: REF. 3 SEQUENCE WAS INCORRECT DUE TO FRAMESHIFTS. DR EMBL; X00588; HSEGFPRE. DR EMBL; K02047; HSEGFR. DR EMBL; K01885; HSEGFRCP. DR EMBL; X06370; HSEGFR1. DR EMBL; M38425; HSEGFR01. DR PIR; A00641; GQHUE. DR PIR; A00642; GQHUE2. DR PIR; A23062; A23062. DR MIM; 131550; NINTH EDITION. DR PROSITE; PS00107; PROTEIN_KINASE_ATP. DR PROSITE; PS00109; PROTEIN_KINASE_TYR. KW TRANSMEMBRANE; GLYCOPROTEIN; DUPLICATION; RECEPTOR; SIGNAL; KW TRANSFERASE; TYROSINE-PROTEIN KINASE; ATP-BINDING; PHOSPHORYLATION. FT SIGNAL 1 24 FT CHAIN 25 1210 EGF RECEPTOR. FT DOMAIN 25 645 EXTRACELLULAR. FT TRANSMEM 646 668 FT DOMAIN 669 1210 CYTOPLASMIC (TYROSINE-SPECIFIC PROTEIN FT KINASE ACTIVITY). FT REPEAT 75 300 APPROXIMATE. FT REPEAT 390 600 APPROXIMATE. FT NP_BIND 718 726 ATP (BY SIMILARITY). FT BINDING 745 745 ATP (BY SIMILARITY). FT MOD_RES 678 678 PHOSPHORYLATION (BY PKC). FT MOD_RES 1092 1092 PHOSPHORYLATION (AUTO-). FT MOD_RES 1110 1110 PHOSPHORYLATION (AUTO-). FT MOD_RES 1172 1172 PHOSPHORYLATION (AUTO-). FT MOD_RES 1197 1197 PHOSPHORYLATION (AUTO-, MAJOR SITE). FT CARBOHYD 128 128 POTENTIAL. FT CARBOHYD 175 175 POTENTIAL. FT CARBOHYD 196 196 POTENTIAL. FT CARBOHYD 352 352 POTENTIAL. FT CARBOHYD 361 361 POTENTIAL. FT CARBOHYD 413 413 POTENTIAL. FT CARBOHYD 444 444 POTENTIAL. FT CARBOHYD 528 528 POTENTIAL. FT CARBOHYD 568 568 POTENTIAL. FT CARBOHYD 603 603 POTENTIAL. FT CARBOHYD 623 623 POTENTIAL. SQ SEQUENCE 1210 AA; 134291 MW; 7507159 CN; MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCK LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV APQSSEFIGA //

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