UniProtKB - P00533 (EGFR_HUMAN)
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- BLAST
>sp|P00533|EGFR_HUMAN Epidermal growth factor receptor OS=Homo sapiens OX=9606 GN=EGFR PE=1 SV=2 MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA RNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV APQSSEFIGA
- Align
Protein
Epidermal growth factor receptor
Gene
EGFR
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:2790960, PubMed:10805725, PubMed:27153536). Known ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF (PubMed:2790960, PubMed:7679104, PubMed:8144591, PubMed:9419975, PubMed:15611079, PubMed:12297049, PubMed:27153536, PubMed:20837704). 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 (PubMed:27153536). May also activate the NF-kappa-B signaling cascade (PubMed:11116146). 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 (PubMed:11602604). Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin (PubMed:11483589). Plays a role in enhancing learning and memory performance (By similarity).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
20 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.24"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, LIGAND-BINDING. - Ref.26"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) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION OF AREG AS LIGAND, FUNCTION. - Ref.30"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) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION OF BETACELLULIN/BTC AS LIGAND. - Ref.33"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) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND, FUNCTION. - Ref.38"RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation."
Derrien A., Druey K.M.
J. Biol. Chem. 276:48532-48538(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF RGS16. - Ref.40"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-1092 AND TYR-1110. - Ref.42"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EGFR SIGNALING, IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2, INTERACTION WITH PIK3C2B, MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND TYR-1197. - Ref.43"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, INTERACTION WITH RIPK1. - Ref.44"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF MUC1, INTERACTION WITH MUC1. - Ref.45"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, INTERACTION WITH SOCS5. - Ref.46"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) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION OF EPIGEN/EPGN AS A LIGAND, FUNCTION. - Ref.50"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION. - Ref.70"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199 BY PRMT5, INTERACTION WITH PRMT5 AND PTPN6. - Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146. - Ref.82"Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha."
Garrett T.P., McKern N.M., Lou M., Elleman T.C., Adams T.E., Lovrecz G.O., Zhu H.J., Walker F., Frenkel M.J., Hoyne P.A., Jorissen R.N., Nice E.C., Burgess A.W., Ward C.W.
Cell 110:763-773(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 25-525 IN COMPLEX WITH TGFA, FUNCTION, GLYCOSYLATION AT ASN-56; ASN-196 AND ASN-352, DISULFIDE BONDS. - Ref.83"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-646 IN COMPLEX WITH EGF, FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429, DISULFIDE BONDS, GLYCOSYLATION AT ASN-56; ASN-175; ASN-196; ASN-352; ASN-361 AND ASN-444. - Ref.84"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-642 IN COMPLEX WITH EGF, FUNCTION, SUBUNIT, MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609, DISULFIDE BONDS, GLYCOSYLATION AT ASN-352; ASN-361; ASN-444; ASN-528; ASN-568 AND ASN-603. - Ref.85"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH GW572016, CATALYTIC ACTIVITY, FUNCTION. - Ref.92"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 669-1022 OF MUTANT MET-745, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LEU-688; VAL-689; GLU-690; LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706 AND LYS-745. - Ref.94"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-638 IN COMPLEX WITH EGF, FUNCTION, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-56; ASN-73; ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528.
Isoform 2 may act as an antagonist of EGF action.
(Microbial infection) Acts as a receptor for hepatitis C virus (HCV) in hepatocytes and facilitates its cell entry. Mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes that are essential for HCV entry and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.1 Publication
Manual assertion based on experiment ini
- Ref.71"EGFR and EphA2 are host factors for hepatitis C virus entry and possible targets for antiviral therapy."
Lupberger J., Zeisel M.B., Xiao F., Thumann C., Fofana I., Zona L., Davis C., Mee C.J., Turek M., Gorke S., Royer C., Fischer B., Zahid M.N., Lavillette D., Fresquet J., Cosset F.L., Rothenberg S.M., Pietschmann T. , Patel A.H., Pessaux P., Doffoel M., Raffelsberger W., Poch O., McKeating J.A., Brino L., Baumert T.F.
Nat. Med. 17:589-595(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION (MICROBIAL INFECTION).
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
6 PublicationsManual assertion based on experiment ini
- Ref.85"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH GW572016, CATALYTIC ACTIVITY, FUNCTION. - Ref.88"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 696-1022 OF WILD-TYPE AND VARIANTS SER-719 AND ARG-858 IN COMPLEXES WITH ATP ANALOGS AND SYNTHETIC INHIBITORS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION OF VARIANTS SER-719 AND ARG-858. - Ref.89"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH ERRFI1, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, INTERACTION WITH ERRFI1. - Ref.90"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 695-1022 OF VARIANT MET-790, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT MET-790. - Ref.91"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197, MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006, SUBUNIT. - Ref.92"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 669-1022 OF MUTANT MET-745, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LEU-688; VAL-689; GLU-690; LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706 AND LYS-745.
<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling.4 Publications
Manual assertion based on experiment ini
- Ref.41"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) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, INTERACTION WITH LRIG1. - Ref.45"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, INTERACTION WITH SOCS5. - Ref.60"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) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, INTERACTION WITH CBL AND GRB2. - Ref.89"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH ERRFI1, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, INTERACTION WITH ERRFI1.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 745 | ATPCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 837 | Proton acceptorPROSITE-ProRule annotation Manual assertion according to rulesi | 1 | |
| Binding sitei | 855 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 1016 | Important for interaction with PIK3C2B | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 718 – 726 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 9 | |
| Nucleotide bindingi | 790 – 791 | ATPCombined sources Manual assertion inferred from combination of experimental and computational evidencei 2 PublicationsManual assertion based on experiment ini
| 2 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- actin filament binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- ATP binding Source: UniProtKB-KW
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- calmodulin binding Source: Ensembl
- chromatin binding Source: UniProtKBInferred from direct assayi
- double-stranded DNA binding Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- enzyme binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- epidermal growth factor-activated receptor activity Source: UniProtKBInferred from direct assayi
- epidermal growth factor binding Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestori
- identical protein binding Source: IntActInferred from physical interactioni
- integrin binding Source: Ensembl
- MAP kinase kinase kinase activity Source: UniProtKBNon-traceable author statementi
- phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
- protein heterodimerization activity Source: UniProtKBInferred from direct assayi
- protein kinase binding Source: Ensembl
- protein phosphatase binding Source: UniProtKBInferred from physical interactioni
- protein tyrosine kinase activity Source: UniProtKBInferred from direct assayi
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
- transmembrane receptor protein tyrosine kinase activity Source: GO_CentralInferred from biological aspect of ancestori
- transmembrane signaling receptor activity Source: MGIInferred from direct assayi
- ubiquitin protein ligase binding Source: UniProtKBInferred from physical interactioni
- virus receptor activity Source: UniProtKB-KW
GO - Biological processi
- activation of phospholipase A2 activity by calcium-mediated signaling Source: UniProtKB <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- activation of phospholipase C activity Source: UniProtKBTraceable author statementi
- astrocyte activation Source: Ensembl
- cell-cell adhesion Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cell differentiation Source: GO_CentralInferred from biological aspect of ancestori
- cell proliferation Source: UniProtKBInferred from direct assayi
- cell surface receptor signaling pathway Source: MGIInferred from direct assayi
- cellular response to amino acid stimulus Source: Ensembl
- cellular response to cadmium ion Source: CAFAInferred from mutant phenotypei
- cellular response to dexamethasone stimulus Source: Ensembl
- cellular response to epidermal growth factor stimulus Source: UniProtKB
- cellular response to estradiol stimulus Source: UniProtKBInferred from direct assayi
- cellular response to mechanical stimulus Source: Ensembl
- cellular response to reactive oxygen species Source: CAFAInferred from mutant phenotypei
- cerebral cortex cell migration Source: Ensembl
- circadian rhythm Source: Ensembl
- digestive tract morphogenesis Source: Ensembl
- diterpenoid metabolic process Source: Ensembl
- embryonic placenta development Source: Ensembl
- epidermal growth factor receptor signaling pathway Source: UniProtKBInferred from direct assayi
- ERBB2 signaling pathway Source: Reactome
- eyelid development in camera-type eye Source: Ensembl
- hair follicle development Source: Ensembl
- hydrogen peroxide metabolic process Source: Ensembl
- learning or memory Source: UniProtKB
- liver regeneration Source: Ensembl
- lung development Source: Ensembl
- magnesium ion homeostasis Source: Ensembl
- MAPK cascade Source: Reactome
- membrane organization Source: Reactome
- midgut development Source: Ensembl
- morphogenesis of an epithelial fold Source: Ensembl
- negative regulation of apoptotic process Source: UniProtKBInferred from mutant phenotypei
- negative regulation of cardiocyte differentiation Source: BHF-UCLInferred from mutant phenotypei
- negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
- negative regulation of ERBB signaling pathway Source: Reactome
- negative regulation of mitotic cell cycle Source: Ensembl
- negative regulation of Notch signaling pathway Source: Reactome
- negative regulation of protein catabolic process Source: UniProtKBInferred from direct assayi
- negative regulation of signal transduction Source: GO_CentralInferred from biological aspect of ancestori
- neuron projection morphogenesis Source: Ensembl
- ossification Source: UniProtKBNon-traceable author statementi
- ovulation cycle Source: Ensembl
- peptidyl-tyrosine autophosphorylation Source: UniProtKBInferred from mutant phenotypei
- peptidyl-tyrosine phosphorylation Source: ParkinsonsUK-UCLInferred from direct assayi
- positive regulation of blood vessel diameter Source: Ensembl
- positive regulation of bone resorption Source: Ensembl
- positive regulation of canonical Wnt signaling pathway Source: BHF-UCLInferred from mutant phenotypei
- positive regulation of cell growth Source: UniProtKBInferred from direct assayi
- positive regulation of cell migration Source: UniProtKBInferred from mutant phenotypei
- positive regulation of cell proliferation Source: MGIInferred from direct assayi
- positive regulation of DNA repair Source: UniProtKBInferred from direct assayi
- positive regulation of DNA replication Source: UniProtKBInferred from direct assayi
- positive regulation of epithelial cell proliferation Source: UniProtKBInferred from direct assayi
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKBInferred from direct assayi
- positive regulation of fibroblast proliferation Source: Ensembl
- positive regulation of inflammatory response Source: Ensembl
- positive regulation of MAP kinase activity Source: UniProtKBInferred from direct assayi
- positive regulation of NIK/NF-kappaB signaling Source: CAFAInferred from mutant phenotypei
- positive regulation of nitric oxide mediated signal transduction Source: UniProtKBInferred from direct assayi
- positive regulation of peptidyl-serine phosphorylation Source: UniProtKBInferred from mutant phenotypei
- positive regulation of phosphorylation Source: UniProtKBInferred from direct assayi
- positive regulation of production of miRNAs involved in gene silencing by miRNA Source: BHF-UCLInferred from mutant phenotypei
- positive regulation of prolactin secretion Source: Ensembl
- positive regulation of protein kinase B signaling Source: BHF-UCLInferred from mutant phenotypei
- positive regulation of protein kinase C activity Source: ParkinsonsUK-UCLInferred from direct assayi
- positive regulation of protein localization to plasma membrane Source: ParkinsonsUK-UCLInferred from direct assayi
- positive regulation of protein phosphorylation Source: UniProtKBInferred from direct assayi
- positive regulation of smooth muscle cell proliferation Source: Ensembl
- positive regulation of superoxide anion generation Source: Ensembl
- positive regulation of synaptic transmission, glutamatergic Source: Ensembl
- positive regulation of transcription, DNA-templated Source: CAFAInferred from mutant phenotypei
- positive regulation of transcription by RNA polymerase II Source: UniProtKBInferred from direct assayi
- positive regulation of vasoconstriction Source: Ensembl
- protein autophosphorylation Source: UniProtKBInferred from mutant phenotypei
- protein insertion into membrane Source: UniProtKBTraceable author statementi
- regulation of cell motility Source: Reactome
- regulation of ERK1 and ERK2 cascade Source: CAFAInferred from mutant phenotypei
- regulation of JNK cascade Source: CAFAInferred from mutant phenotypei
- regulation of nitric-oxide synthase activity Source: UniProtKBInferred from direct assayi
- regulation of peptidyl-tyrosine phosphorylation Source: UniProtKBInferred from mutant phenotypei
- regulation of phosphatidylinositol 3-kinase signaling Source: CAFAInferred from mutant phenotypei
- regulation of transcription by RNA polymerase II Source: Reactome
- response to calcium ion Source: Ensembl
- response to cobalamin Source: Ensembl
- response to hydroxyisoflavone Source: Ensembl
- response to osmotic stress Source: Ensembl
- response to UV-A Source: BHF-UCLInferred from direct assayi
- salivary gland morphogenesis Source: Ensembl
- signal transduction Source: UniProtKBInferred from direct assayi
- tongue development Source: Ensembl
- translation Source: Ensembl
- wound healing Source: Ensembl
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Developmental protein, Host cell receptor for virus entry, Kinase, Receptor, Transferase, Tyrosine-protein kinase |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 2.7.10.1 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-1227986 Signaling by ERBB2 R-HSA-1236382 Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants R-HSA-1236394 Signaling by ERBB4 R-HSA-1250196 SHC1 events in ERBB2 signaling R-HSA-1251932 PLCG1 events in ERBB2 signaling R-HSA-1257604 PIP3 activates AKT signaling R-HSA-177929 Signaling by EGFR R-HSA-179812 GRB2 events in EGFR signaling R-HSA-180292 GAB1 signalosome R-HSA-180336 SHC1 events in EGFR signaling R-HSA-182971 EGFR downregulation R-HSA-1963640 GRB2 events in ERBB2 signaling R-HSA-1963642 PI3K events in ERBB2 signaling R-HSA-212718 EGFR interacts with phospholipase C-gamma R-HSA-2179392 EGFR Transactivation by Gastrin R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer R-HSA-445144 Signal transduction by L1 R-HSA-5637810 Constitutive Signaling by EGFRvIII R-HSA-5638303 Inhibition of Signaling by Overexpressed EGFR R-HSA-5673001 RAF/MAP kinase cascade R-HSA-6785631 ERBB2 Regulates Cell Motility R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling R-HSA-8847993 ERBB2 Activates PTK6 Signaling R-HSA-8856825 Cargo recognition for clathrin-mediated endocytosis R-HSA-8856828 Clathrin-mediated endocytosis R-HSA-8857538 PTK6 promotes HIF1A stabilization R-HSA-8863795 Downregulation of ERBB2 signaling R-HSA-8866910 TFAP2 (AP-2) family regulates transcription of growth factors and their receptors R-HSA-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P00533 |
SIGNOR Signaling Network Open Resource More...SIGNORi | P00533 |
Protein family/group databases
MoonDB Database of extreme multifunctional and moonlighting proteins More...MoonDBi | P00533 Predicted |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Epidermal growth factor receptor (EC:2.7.10.1)Alternative name(s): Proto-oncogene c-ErbB-1 Receptor tyrosine-protein kinase erbB-1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:EGFR Synonyms:ERBB, ERBB1, HER1 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000146648.15 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3236 EGFR |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 131550 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P00533 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Golgi apparatus
Nucleus
- Nucleus membrane ; Single-pass type I membrane protein
- Nucleus 3 Publications
Manual assertion based on experiment ini
- Ref.50"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION. - Ref.65"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH COPG1, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.66"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPER1, SUBCELLULAR LOCATION.
Endoplasmic reticulum
- Endoplasmic reticulum membrane 1 Publication
Manual assertion based on experiment ini
- Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
- Endoplasmic reticulum membrane 1 Publication
Endosome
- Endosome 2 Publications
Manual assertion based on experiment ini
- Ref.53"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TNF2, SUBCELLULAR LOCATION. - Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
- Endosome membrane
- Endosome 2 Publications
Plasma membrane
- Cell membrane 3 Publications
Manual assertion based on experiment ini
- Ref.24"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, LIGAND-BINDING. - Ref.53"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TNF2, SUBCELLULAR LOCATION. - Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
Manual assertion based on experiment ini
- Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER (PubMed:20674546). Endocytosed upon activation by ligand (PubMed:2790960, PubMed:17182860, PubMed:27153536). Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) (PubMed:20551055).4 Publications- Cell membrane 3 Publications
- Ref.24"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, LIGAND-BINDING. - Ref.53"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TNF2, SUBCELLULAR LOCATION. - Ref.65"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH COPG1, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
Manual assertion based on experiment ini
Endoplasmic reticulum
- endoplasmic reticulum membrane Source: UniProtKB-SubCell
Endosome
- early endosome membrane Source: UniProtKBInferred from direct assayi
- endosome Source: UniProtKBInferred from direct assayi
- endosome membrane Source: UniProtKBInferred from direct assayi
- multivesicular body, internal vesicle lumen Source: UniProtKBInferred from direct assayi
Extracellular region or secreted
- extracellular space Source: UniProtKBNon-traceable author statementi
Golgi apparatus
- Golgi membrane Source: UniProtKB-SubCell
Nucleus
- nuclear membrane Source: UniProtKB-SubCell
- nucleus Source: UniProtKBInferred from direct assayi
Plasma Membrane
- apical plasma membrane Source: Ensembl
- basal plasma membrane Source: GO_CentralInferred from biological aspect of ancestori
- basolateral plasma membrane Source: BHF-UCLInferred from direct assayi
- integral component of plasma membrane Source: GO_CentralInferred from biological aspect of ancestori
- plasma membrane Source: HGNCInferred from direct assayi
- Shc-EGFR complex Source: BHF-UCL
Other locations
- cell surface Source: UniProtKBInferred from direct assayi
- clathrin-coated vesicle membrane Source: Reactome
- cytoplasm Source: UniProtKBInferred from direct assayi
- endocytic vesicle Source: Ensembl
- focal adhesion Source: UniProtKBInferred from high throughput direct assayi
- membrane Source: UniProtKBInferred from direct assayi
- membrane raft Source: UniProtKBInferred from direct assayi
- perinuclear region of cytoplasm Source: Ensembl
- protein-containing complex Source: UniProtKBInferred from direct assayi
- receptor complex Source: MGIInferred from direct assayi
- synapse Source: Ensembl
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 25 – 645 | ExtracellularSequence analysisAdd BLAST | 621 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 646 – 668 | HelicalSequence analysisAdd BLAST | 23 | |
| Topological domaini | 669 – 1210 | CytoplasmicSequence analysisAdd BLAST | 542 |
Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus, Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Lung cancer (LNCR)3 PublicationsManual assertion based on experiment ini
- Ref.98"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS SER-719 AND ARG-858, POSSIBLE INVOLVEMENT IN LUNG CANCER. - Ref.99"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719; SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748; 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858; ARG-858; GLN-861 AND GLU-873, POSSIBLE INVOLVEMENT IN LUNG CANCER. - Ref.101"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) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT 30-VAL--ARG-297 DEL, POSSIBLE INVOLVEMENT IN LUNG CANCER.
Ref.98
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-719 AND ARG-858, POSSIBLE INVOLVEMENT IN LUNG CANCER.
Ref.99
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719; SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748; 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858; ARG-858; GLN-861 AND GLU-873, POSSIBLE INVOLVEMENT IN LUNG CANCER.
Ref.101
"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) [PubMed] [Europe PMC] [Abstract]
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) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT 30-VAL--ARG-297 DEL, POSSIBLE INVOLVEMENT IN LUNG CANCER.
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.
See also OMIM:211980Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)1 PublicationManual assertion based on experiment ini
- Ref.103"Epithelial inflammation resulting from an inherited loss-of-function mutation in EGFR."
Campbell P., Morton P.E., Takeichi T., Salam A., Roberts N., Proudfoot L.E., Mellerio J.E., Aminu K., Wellington C., Patil S.N., Akiyama M., Liu L., McMillan J.R., Aristodemou S., Ishida-Yamamoto A., Abdul-Wahab A., Petrof G., Fong K. , Harnchoowong S., Stone K.L., Harper J.I., McLean W.H., Simpson M.A., Parsons M., McGrath J.A.
J. Invest. Dermatol. 134:2570-2578(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NISBD2 ASP-428, CHARACTERIZATION OF VARIANT NISBD2 ASP-428, INVOLVEMENT IN NISBD2.
Ref.103
"Epithelial inflammation resulting from an inherited loss-of-function mutation in EGFR."
Campbell P., Morton P.E., Takeichi T., Salam A., Roberts N., Proudfoot L.E., Mellerio J.E., Aminu K., Wellington C., Patil S.N., Akiyama M., Liu L., McMillan J.R., Aristodemou S., Ishida-Yamamoto A., Abdul-Wahab A., Petrof G., Fong K. , Harnchoowong S., Stone K.L., Harper J.I., McLean W.H., Simpson M.A., Parsons M., McGrath J.A.
J. Invest. Dermatol. 134:2570-2578(2014) [PubMed] [Europe PMC] [Abstract]
Campbell P., Morton P.E., Takeichi T., Salam A., Roberts N., Proudfoot L.E., Mellerio J.E., Aminu K., Wellington C., Patil S.N., Akiyama M., Liu L., McMillan J.R., Aristodemou S., Ishida-Yamamoto A., Abdul-Wahab A., Petrof G., Fong K. , Harnchoowong S., Stone K.L., Harper J.I., McLean W.H., Simpson M.A., Parsons M., McGrath J.A.
J. Invest. Dermatol. 134:2570-2578(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT NISBD2 ASP-428, CHARACTERIZATION OF VARIANT NISBD2 ASP-428, INVOLVEMENT IN NISBD2.
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by inflammatory features with neonatal onset, involving the skin, hair, and gut. The skin lesions involve perioral and perianal erythema, psoriasiform erythroderma, with flares of erythema, scaling, and widespread pustules. Gastrointestinal symptoms include malabsorptive diarrhea that is exacerbated by intercurrent gastrointestinal infections. The hair is short or broken, and the eyelashes and eyebrows are wiry and disorganized.
See also OMIM:616069| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_072435 | 428 | G → D in NISBD2; loss of function; the mutant does not localize to the cell membrane; has diffuse cytoplasmic localization. 1 Publication Manual assertion based on experiment ini
| 1 |
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 275 | Y → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 287 | F → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 309 | R → S: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 429 | R → E: Abolishes autophosphorylation and activation of downstream kinases. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 587 – 590 | DGPH → AGPA: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Mutagenesisi | 609 | K → A: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 688 | L → A: Strongly reduced phosphorylation. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 689 | V → A: Reduced autophosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 689 | V → M: Constitutively activated kinase. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 690 | E → A: Reduced phosphorylation. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 692 | L → A or P: Strongly reduced phosphorylation. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 693 | T → A: Increased phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 693 | T → D: Strongly reduced phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 694 | P → A: Strongly reduced phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 699 | P → A: Reduced phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 700 | N → A: Abolishes phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 704 | L → A: Abolishes phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 705 | R → A: Abolishes phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 706 | I → A: Abolishes phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 745 | K → A or M: Abolishes kinase activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 974 | D → A: Strongly reduced phosphorylation. | 1 | |
| Mutagenesisi | 977 | R → A: Reduced phosphorylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1005 – 1006 | ED → RK: Constitutively activated kinase. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Mutagenesisi | 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. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1048 – 1210 | Missing : Abolishes palmitoylation. 1 Publication Manual assertion based on experiment ini
| 163 | |
| Mutagenesisi | 1049 | C → A: Decreased palmitoylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1067 | Q → G: No effect on interaction with CBLC. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1068 | R → G: Strongly decreases interaction with CBLC. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1069 | Y → F: Abolishes interaction with CBLC. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1092 | Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1110 | Y → F: No change in interaction with PIK3C2B. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1146 | C → A: Decreased palmitoylation. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 1172 | Y → F: No change in interaction with PIK3C2B. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 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. 1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease mutation, Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 1956 |
MalaCards human disease database More...MalaCardsi | EGFR |
| MIMi | 211980 phenotype 616069 phenotype |
Open Targets More...OpenTargetsi | ENSG00000146648 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 251579 Giant cell glioblastoma 251576 Gliosarcoma 294023 Neonatal inflammatory skin and bowel disease 357191 Selection of therapeutic option in non-small cell lung carcinoma |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA7360 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL203 |
Drug and drug target database More...DrugBanki | DB08916 Afatinib DB00002 Cetuximab DB05424 CI-1033 DB00530 Erlotinib DB03496 Flavopiridol DB00317 Gefitinib DB05324 HuMax-EGFr DB11737 Icotinib DB04988 IGN311 DB05774 IMC-11F8 DB05900 INSM-18 DB01259 Lapatinib DB00281 Lidocaine DB05101 Matuzumab DB07662 N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE DB09559 Necitumumab DB13164 Olmutinib DB09330 Osimertinib DB01269 Panitumumab DB05374 Rindopepimut DB07602 S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE DB00072 Trastuzumab DB05294 Vandetanib |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 1797 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EGFR |
Domain mapping of disease mutations (DMDM) More...DMDMi | 2811086 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 24 | 3 Publications Manual assertion based on experiment ini
| 24 | |
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000016665 | 25 – 1210 | Epidermal growth factor receptorAdd BLAST | 1186 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 31 ↔ 58 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_000227 | 56 | N-linked (GlcNAc...) (complex) asparagine; atypical; partialCombined sources Manual assertion inferred from combination of experimental and computational evidencei 6 PublicationsManual assertion based on experiment ini
| 1 | |
| Glycosylationi | 73 | N-linked (GlcNAc...) asparagine; atypicalCombined sources Manual assertion inferred from combination of experimental and computational evidencei 1 PublicationManual assertion based on experiment ini
| 1 | |
| Glycosylationi | 128 | N-linked (GlcNAc...) asparagine3 Publications Manual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 157 ↔ 187 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 175 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 190 ↔ 199 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 194 ↔ 207 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 196 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 215 ↔ 223 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 219 ↔ 231 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 229 | Phosphoserine1 Publication Manual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 232 ↔ 240 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 236 ↔ 248 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 251 ↔ 260 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 264 ↔ 291 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 295 ↔ 307 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | ||
| Disulfide bondi | 311 ↔ 326 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 329 ↔ 333 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | ||
| Disulfide bondi | 337 ↔ 362 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 352 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 8 PublicationsManual assertion based on experiment ini
| 1 | |
| Glycosylationi | 361 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 6 PublicationsManual assertion based on experiment ini
| 1 | |
| Glycosylationi | 413 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Glycosylationi | 444 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 6 PublicationsManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 470 ↔ 499 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | ||
| Disulfide bondi | 506 ↔ 515 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 510 ↔ 523 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 526 ↔ 535 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 528 | N-linked (GlcNAc...) asparagineCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 539 ↔ 555 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 558 ↔ 571 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 562 ↔ 579 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 568 | N-linked (GlcNAc...) asparagine; partialCombined sources Manual assertion inferred from combination of experimental and computational evidencei 5 PublicationsManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 582 ↔ 591 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Disulfide bondi | 595 ↔ 617 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 603 | N-linked (GlcNAc...) asparagine; partialCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Disulfide bondi | 620 ↔ 628 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Glycosylationi | 623 | N-linked (GlcNAc...) (high mannose) asparagine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| Disulfide bondi | 624 ↔ 636 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei 3 PublicationsManual assertion based on experiment ini
| ||
| Modified residuei | 678 | Phosphothreonine; by PKC and PKD/PRKD11 Publication Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 693 | Phosphothreonine; by PKD/PRKD1Combined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 695 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 716 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| ||
| Cross-linki | 737 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| ||
| Cross-linki | 754 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| ||
| Cross-linki | 867 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| ||
| Cross-linki | 929 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| ||
| Cross-linki | 970 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication Manual assertion based on experiment ini
| ||
| Modified residuei | 991 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 995 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 998 | Phosphotyrosine; by autocatalysisCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1016 | Phosphotyrosine; by autocatalysis1 Publication Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1026 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1039 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 1041 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 1042 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 1049 | S-palmitoyl cysteine1 Publication Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1064 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 1069 | Phosphotyrosine1 Publication Manual assertion inferred by curator fromi
| 1 | |
| Modified residuei | 1070 | Phosphoserine1 Publication Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1071 | Phosphoserine1 Publication Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1081 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 1092 | Phosphotyrosine; by autocatalysis2 Publications Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1110 | Phosphotyrosine; by autocatalysis2 Publications Manual assertion based on experiment ini
| 1 | |
| Lipidationi | 1146 | S-palmitoyl cysteine1 Publication Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1166 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 1172 | Phosphotyrosine; by autocatalysisCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1197 | Phosphotyrosine; by autocatalysisCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Modified residuei | 1199 | Omega-N-methylarginine1 Publication Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylated on Tyr residues in response to EGF (PubMed:27153536). Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2.9 Publications
Manual assertion based on experiment ini
- Ref.17"Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo."
Heisermann G.J., Gill G.N.
J. Biol. Chem. 263:13152-13158(1988) [PubMed] [Europe PMC] [Abstract] - Ref.25"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) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT TYR-1110. - Ref.29"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) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT THR-678 AND THR-693. - Ref.40"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-1092 AND TYR-1110. - Ref.47"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)."
Wu S.L., Kim J., Hancock W.S., Karger B.
J. Proteome Res. 4:1155-1170(2005) [PubMed] [Europe PMC] [Abstract]Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY. - Ref.60"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) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, INTERACTION WITH CBL AND GRB2. - Ref.70"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199 BY PRMT5, INTERACTION WITH PRMT5 AND PTPN6. - Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146. - Ref.91"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197, MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006, SUBUNIT.
Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting (PubMed:27153536). Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity).By similarity
Manual assertion inferred from sequence similarity toi
4 PublicationsManual assertion based on experiment ini
- Ref.20"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) [PubMed] [Europe PMC] [Abstract] - Ref.73"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ANKRD13A; ANKRD13B AND ALKRD13D, UBIQUITINATION, SUBCELLULAR LOCATION. - Ref.74"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) [PubMed] [Europe PMC] [Abstract]Cited for: UBIQUITINATION, DEUBIQUITINATION BY OTUD7B. - Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling.1 Publication
Manual assertion based on experiment ini
- Ref.80"Inhibition of DHHC20-Mediated EGFR Palmitoylation Creates a Dependence on EGFR Signaling."
Runkle K.B., Kharbanda A., Stypulkowski E., Cao X.J., Wang W., Garcia B.A., Witze E.S.
Mol. Cell 62:385-396(2016) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, PALMITOYLATION AT CYS-1049 AND CYS-1146, IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION, PHOSPHORYLATION AT TYR-1092; TYR-1172 AND TYR-1197, SUBCELLULAR LOCATION, MUTAGENESIS OF 1048-ALA--ALA-1210; CYS-1049 AND CYS-1146.
Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.3 Publications
Manual assertion based on experiment ini
- Ref.60"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) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, INTERACTION WITH CBL AND GRB2. - Ref.70"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199 BY PRMT5, INTERACTION WITH PRMT5 AND PTPN6. - Ref.91"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197, MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006, SUBUNIT.
Keywords - PTMi
Disulfide bond, Glycoprotein, Isopeptide bond, Lipoprotein, Methylation, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P00533 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P00533 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P00533 |
PeptideAtlas More...PeptideAtlasi | P00533 |
PRoteomics IDEntifications database More...PRIDEi | P00533 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 51261 51262 [P00533-2] 51263 [P00533-3] 51264 [P00533-4] |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P00533 |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 137 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P00533 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P00533 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P00533 |
UniCarbKB; an annotated and curated database of glycan structures More...UniCarbKBi | P00533 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | P00533 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.1 Publication
Manual assertion based on experiment ini
- Ref.52"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) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000146648 Expressed in 234 organ(s), highest expression level in placenta |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P00533 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P00533 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB000035 CAB068186 CAB073534 HPA001200 HPA018530 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2 (PubMed:10805725). Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation (PubMed:18046415). Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B (PubMed:10805725). Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through ELOC- and ELOB-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA (PubMed:17115032). Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2 (PubMed:10026169). Interacts with ATX2. Interacts with GAREM1. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126 (PubMed:23418353). Interacts with GPRC5A (via its transmembrane domain) (PubMed:25311788). Interacts with FAM83B; positively regulates EGFR inducing its autophosphorylation in absence of stimulation by EGF (PubMed:23912460). Interacts with LAPTM4B; positively correlates with EGFR activation (PubMed:28479384). Interacts with STX19 (PubMed:16420529).40 Publications
Manual assertion based on experiment ini
- Ref.27"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZPR1. - Ref.28"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ZPR1. - Ref.31"Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation."
Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.
J. Biol. Chem. 270:20242-20245(1995) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL. - Ref.35"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH AP2M1. - Ref.36"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GRB2; NCK1 AND NCK2. - Ref.40"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-1092 AND TYR-1110. - Ref.41"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) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, INTERACTION WITH LRIG1. - Ref.42"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN EGFR SIGNALING, IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2, INTERACTION WITH PIK3C2B, MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND TYR-1197. - Ref.43"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, INTERACTION WITH RIPK1. - Ref.44"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN PHOSPHORYLATION OF MUC1, INTERACTION WITH MUC1. - Ref.45"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, INTERACTION WITH SOCS5. - Ref.48"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PELP1. - Ref.50"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION. - Ref.53"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TNF2, SUBCELLULAR LOCATION. - Ref.54"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ATX2. - Ref.55"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GAB2. - Ref.60"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) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, INTERACTION WITH CBL AND GRB2. - Ref.61"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GAREM1. - Ref.64"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPER1. - Ref.65"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH COPG1, SUBCELLULAR LOCATION, TOPOLOGY. - Ref.66"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPER1, SUBCELLULAR LOCATION. - Ref.70"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) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199 BY PRMT5, INTERACTION WITH PRMT5 AND PTPN6. - Ref.72"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FER, PHOSPHORYLATION. - Ref.73"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ANKRD13A; ANKRD13B AND ALKRD13D, UBIQUITINATION, SUBCELLULAR LOCATION. - Ref.75"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) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RNF115 AND RNF126. - Ref.78"EGFR phosphorylates and inhibits lung tumor suppressor GPRC5A in lung cancer."
Lin X., Zhong S., Ye X., Liao Y., Yao F., Yang X., Sun B., Zhang J., Li Q., Gao Y., Wang Y., Liu J., Han B., Chin Y.E., Zhou B.P., Deng J.
Mol. Cancer 13:233-233(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPRC5A. - Ref.79"Hyperactivation of EGFR and downstream effector phospholipase D1 by oncogenic FAM83B."
Cipriano R., Bryson B.L., Miskimen K.L., Bartel C.A., Hernandez-Sanchez W., Bruntz R.C., Scott S.A., Lindsley C.W., Brown H.A., Jackson M.W.
Oncogene 33:3298-3306(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FAM83B. - Ref.81"Beclin1 antagonizes LAPTM4B-mediated EGFR overactivation in gastric cancer cells."
Tian M., Chen Y., Tian D., Qiao X., Ma Z., Li J.
Gene 626:48-53(2017) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH LAPTM4B. - Ref.83"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-646 IN COMPLEX WITH EGF, FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429, DISULFIDE BONDS, GLYCOSYLATION AT ASN-56; ASN-175; ASN-196; ASN-352; ASN-361 AND ASN-444. - Ref.84"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-642 IN COMPLEX WITH EGF, FUNCTION, SUBUNIT, MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609, DISULFIDE BONDS, GLYCOSYLATION AT ASN-352; ASN-361; ASN-444; ASN-528; ASN-568 AND ASN-603. - Ref.85"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH GW572016, CATALYTIC ACTIVITY, FUNCTION. - Ref.86"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-642 IN COMPLEX WITH CETUXIMAB. - Ref.89"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH ERRFI1, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, INTERACTION WITH ERRFI1. - Ref.91"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197, MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006, SUBUNIT. - Ref.92"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 669-1022 OF MUTANT MET-745, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LEU-688; VAL-689; GLU-690; LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706 AND LYS-745. - Ref.93"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) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 634-677 IN COMPLEX WITH ERBB2, SUBUNIT. - Ref.94"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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-638 IN COMPLEX WITH EGF, FUNCTION, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-56; ASN-73; ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528. - Ref.95"Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide."
Structural genomics consortium
Submitted (OCT-2010) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1066-1076 IN COMPLEX WITH CBLB, INTERACTION WITH CBLB. - Ref.96"Structural 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) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1062-1074 IN COMPLEX WITH CBLC, PHOSPHORYLATION AT TYR-1069, INTERACTION WITH CBLC, MUTAGENESIS OF GLN-1067; ARG-1068 AND TYR-1069.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
GO - Molecular functioni
- actin filament binding Source: UniProtKBInferred from direct assayi
- cadherin binding Source: BHF-UCLInferred from high throughput direct assayi
- calmodulin binding Source: Ensembl
- enzyme binding Source: UniProtKBInferred from physical interactioni
- epidermal growth factor binding Source: GO_CentralInferred from biological aspect of ancestori
- identical protein binding Source: IntActInferred from physical interactioni