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P04412

- EGFR_DROME

UniProt

P04412 - EGFR_DROME

Protein

Epidermal growth factor receptor

Gene

Egfr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 3 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Binds to four ligands: Spitz, Gurken, Vein and Argos, which is an antagonist. Transduces the signal through the ras-raf-MAPK pathway. Involved in a myriad of developmental decisions. Critical for the proliferation of imaginal tissues, and for the determination of both the antero-posterior and dorso-ventral polarities of the oocyte. In the embryo, plays a role in the establishment of ventral cell fates, maintenance of amnioserosa and ventral neuroectodermal cells, germ band retraction, cell fate specification in the central nervous system and production of cuticle. Required for embryonic epithelial tissue repair.1 Publication

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei971 – 9711ATPPROSITE-ProRule annotation
    Active sitei1063 – 10631Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi944 – 9529ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. epidermal growth factor-activated receptor activity Source: FlyBase
    3. protein binding Source: IntAct
    4. protein tyrosine kinase activity Source: FlyBase
    5. transmembrane signaling receptor activity Source: FlyBase

    GO - Biological processi

    1. antennal development Source: FlyBase
    2. anterior/posterior pattern specification Source: FlyBase
    3. behavioral response to ethanol Source: FlyBase
    4. blastoderm segmentation Source: FlyBase
    5. border follicle cell migration Source: FlyBase
    6. brain development Source: FlyBase
    7. branched duct epithelial cell fate determination, open tracheal system Source: FlyBase
    8. cell fate determination Source: FlyBase
    9. cell projection assembly Source: FlyBase
    10. chorion-containing eggshell pattern formation Source: FlyBase
    11. compound eye cone cell fate commitment Source: FlyBase
    12. compound eye development Source: FlyBase
    13. compound eye morphogenesis Source: FlyBase
    14. compound eye photoreceptor cell differentiation Source: FlyBase
    15. compound eye photoreceptor fate commitment Source: FlyBase
    16. determination of genital disc primordium Source: FlyBase
    17. digestive tract morphogenesis Source: FlyBase
    18. dorsal/ventral pattern formation Source: FlyBase
    19. dorsal appendage formation Source: FlyBase
    20. dorsal closure Source: FlyBase
    21. embryonic pattern specification Source: FlyBase
    22. epidermal growth factor receptor signaling pathway Source: FlyBase
    23. epithelial cell proliferation involved in Malpighian tubule morphogenesis Source: FlyBase
    24. establishment or maintenance of apical/basal cell polarity Source: FlyBase
    25. eye-antennal disc morphogenesis Source: FlyBase
    26. eye development Source: FlyBase
    27. female germ-line cyst encapsulation Source: FlyBase
    28. G2/M transition of mitotic cell cycle Source: FlyBase
    29. gastrulation Source: FlyBase
    30. germ-band shortening Source: FlyBase
    31. germ-line stem cell maintenance Source: FlyBase
    32. gonad development Source: FlyBase
    33. haltere development Source: FlyBase
    34. heart process Source: FlyBase
    35. imaginal disc-derived wing morphogenesis Source: FlyBase
    36. imaginal disc-derived wing vein morphogenesis Source: FlyBase
    37. imaginal disc-derived wing vein specification Source: FlyBase
    38. imaginal disc development Source: FlyBase
    39. leg disc proximal/distal pattern formation Source: FlyBase
    40. maintenance of epithelial integrity, open tracheal system Source: FlyBase
    41. male germ-line cyst encapsulation Source: FlyBase
    42. Malpighian tubule morphogenesis Source: FlyBase
    43. maternal determination of dorsal/ventral axis, ovarian follicular epithelium, soma encoded Source: FlyBase
    44. morphogenesis of an epithelium Source: FlyBase
    45. morphogenesis of follicular epithelium Source: FlyBase
    46. muscle attachment Source: FlyBase
    47. muscle cell fate specification Source: FlyBase
    48. negative regulation of apoptotic process Source: FlyBase
    49. negative regulation of apoptotic signaling pathway Source: FlyBase
    50. negative regulation of compound eye retinal cell programmed cell death Source: FlyBase
    51. negative regulation of G1/S transition of mitotic cell cycle Source: FlyBase
    52. neurogenesis Source: FlyBase
    53. notum cell fate specification Source: FlyBase
    54. notum development Source: FlyBase
    55. oenocyte differentiation Source: FlyBase
    56. olfactory learning Source: FlyBase
    57. ommatidial rotation Source: FlyBase
    58. oocyte anterior/posterior axis specification Source: FlyBase
    59. oocyte axis specification Source: FlyBase
    60. oocyte dorsal/ventral axis specification Source: FlyBase
    61. open tracheal system development Source: FlyBase
    62. peptidyl-tyrosine phosphorylation Source: GOC
    63. peripheral nervous system development Source: FlyBase
    64. positive regulation of cell proliferation Source: FlyBase
    65. positive regulation of wound healing Source: FlyBase
    66. progression of morphogenetic furrow involved in compound eye morphogenesis Source: FlyBase
    67. protein phosphorylation Source: FlyBase
    68. R7 cell differentiation Source: FlyBase
    69. regulation of hemocyte differentiation Source: FlyBase
    70. regulation of mitotic cell cycle Source: FlyBase
    71. regulation of R8 cell spacing in compound eye Source: FlyBase
    72. salivary gland development Source: FlyBase
    73. second mitotic wave involved in compound eye morphogenesis Source: FlyBase
    74. segment polarity determination Source: FlyBase
    75. single organismal cell-cell adhesion Source: FlyBase
    76. spiracle morphogenesis, open tracheal system Source: FlyBase
    77. stem cell fate commitment Source: FlyBase
    78. stomatogastric nervous system development Source: FlyBase
    79. tracheal pit formation in open tracheal system Source: FlyBase
    80. wing and notum subfield formation Source: FlyBase
    81. wing disc morphogenesis Source: FlyBase
    82. wing disc proximal/distal pattern formation Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 1994.
    SignaLinkiP04412.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epidermal growth factor receptor (EC:2.7.10.1)
    Short name:
    Egfr
    Alternative name(s):
    Drosophila relative of ERBB
    Gurken receptor
    Protein torpedo
    Gene namesi
    Name:Egfr
    Synonyms:c-erbB, DER, top
    ORF Names:CG10079
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0003731. Egfr.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: FlyBase

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Embryonic wound healing defects.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi793 – 7931C → R in EGFR-ELP-1.
    Mutagenesisi936 – 9361A → T in EGFR-ELP-B1 and EGFR-ELP-B1RB1.
    Mutagenesisi1058 – 10581R → Q in EGFR-ELP-B1RB1.
    Mutagenesisi1135 – 11351T → I in EGFR-2W74.
    Mutagenesisi1156 – 11561G → S in EGFR-2C82.
    Mutagenesisi1162 – 11621P → L in EGFR-1F26.
    Mutagenesisi1166 – 11661S → L in EGFR-2L65.
    Mutagenesisi1210 – 12167DKFTRLP → EKVHPAA in EGFR-2X51.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 14261396Epidermal growth factor receptorPRO_0000016676Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi419 – 4191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi482 – 4821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi569 – 5691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi599 – 5991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi617 – 6171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi816 – 8161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi823 – 8231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence Analysis
    Modified residuei902 – 9021Phosphothreonine; by PKCBy similarity
    Modified residuei1310 – 13101Phosphotyrosine; by autocatalysisBy similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP04412.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed in embryos. In larvae, uniform expression is seen in wing disks, genital disk, anlagen of testis and ovary, and brain cortex. In eye-antenna disk, highest expression is anterior to morphogenetic furrow, levels remain high in photoreceptor precursor cells. This pattern is reversed in posterior eye disk. In adults expression is high in brain cortex and thoracic and abdominal ganglia.1 Publication

    Gene expression databases

    BgeeiP04412.

    Interactioni

    Subunit structurei

    Interacts (when phosphorylated on tyrosine residues) with Vav (via SH2 domain).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    kek1P916432EBI-197863,EBI-6896313
    spiQ010834EBI-197863,EBI-91342

    Protein-protein interaction databases

    BioGridi63083. 72 interactions.
    DIPiDIP-17316N.
    IntActiP04412. 5 interactions.
    MINTiMINT-806082.

    Structurei

    Secondary structure

    1
    1426
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi101 – 1033
    Helixi115 – 12612
    Beta strandi131 – 1344
    Beta strandi136 – 1416
    Helixi149 – 1513
    Beta strandi156 – 1594
    Beta strandi161 – 1666
    Beta strandi169 – 1724
    Beta strandi194 – 2007
    Beta strandi204 – 2074
    Beta strandi216 – 2238
    Turni230 – 2323
    Helixi235 – 2373
    Beta strandi239 – 2413
    Beta strandi246 – 2483
    Beta strandi269 – 2735
    Helixi274 – 2763
    Beta strandi281 – 2855
    Beta strandi287 – 2893
    Beta strandi290 – 2923
    Beta strandi295 – 3006
    Beta strandi305 – 31612
    Beta strandi319 – 3279
    Beta strandi330 – 3345
    Beta strandi338 – 3425
    Turni343 – 3464
    Beta strandi347 – 3504
    Beta strandi356 – 3583
    Beta strandi361 – 3655
    Beta strandi370 – 3734
    Beta strandi376 – 3805
    Beta strandi385 – 39410
    Beta strandi396 – 3983
    Beta strandi402 – 4043
    Turni411 – 4133
    Helixi414 – 4174
    Beta strandi421 – 4255
    Beta strandi427 – 4293
    Helixi431 – 4355
    Beta strandi438 – 4403
    Turni442 – 4443
    Beta strandi446 – 4494
    Helixi455 – 4639
    Beta strandi466 – 4694
    Beta strandi471 – 4733
    Helixi484 – 4863
    Beta strandi491 – 4933
    Turni499 – 5024
    Beta strandi503 – 5097
    Beta strandi525 – 5317
    Turni539 – 5413
    Helixi544 – 5474
    Beta strandi555 – 5617
    Helixi563 – 5675
    Turni568 – 5703
    Beta strandi575 – 5773
    Beta strandi582 – 5865
    Beta strandi590 – 5989
    Beta strandi601 – 6044
    Beta strandi608 – 6103
    Beta strandi616 – 6183
    Beta strandi628 – 6303
    Beta strandi638 – 6403

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3I2TX-ray2.70A100-644[»]
    3LTFX-ray3.20A/C100-688[»]
    3LTGX-ray3.40A/C100-688[»]
    ProteinModelPortaliP04412.
    SMRiP04412. Positions 100-804, 884-1248.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04412.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 868838ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini890 – 1426537CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei869 – 88921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini938 – 1198261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    InParanoidiP04412.
    KOiK04361.
    OrthoDBiEOG7SV0TH.
    PhylomeDBiP04412.

    Family and domain databases

    Gene3Di3.80.20.20. 4 hits.
    InterProiIPR000494. EGF_rcpt_L.
    IPR006211. Furin-like_Cys-rich_dom.
    IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view]
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00261. FU. 7 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 3 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Type I (identifier: P04412-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLLRRRNGPC PFPLLLLLLA HCICIWPASA ARDRYARQNN RQRHQDIDRD     50
    RDRDRFLYRS SSAQNRQRGG ANFALGLGAN GVTIPTSLED KNKNEFVKGK 100
    ICIGTKSRLS VPSNKEHHYR NLRDRYTNCT YVDGNLKLTW LPNENLDLSF 150
    LDNIREVTGY ILISHVDVKK VVFPKLQIIR GRTLFSLSVE EEKYALFVTY 200
    SKMYTLEIPD LRDVLNGQVG FHNNYNLCHM RTIQWSEIVS NGTDAYYNYD 250
    FTAPERECPK CHESCTHGCW GEGPKNCQKF SKLTCSPQCA GGRCYGPKPR 300
    ECCHLFCAGG CTGPTQKDCI ACKNFFDEAV SKEECPPMRK YNPTTYVLET 350
    NPEGKYAYGA TCVKECPGHL LRDNGACVRS CPQDKMDKGG ECVPCNGPCP 400
    KTCPGVTVLH AGNIDSFRNC TVIDGNIRIL DQTFSGFQDV YANYTMGPRY 450
    IPLDPERREV FSTVKEITGY LNIEGTHPQF RNLSYFRNLE TIHGRQLMES 500
    MFAALAIVKS SLYSLEMRNL KQISSGSVVI QHNRDLCYVS NIRWPAIQKE 550
    PEQKVWVNEN LRADLCEKNG TICSDQCNED GCWGAGTDQC LTCKNFNFNG 600
    TCIADCGYIS NAYKFDNRTC KICHPECRTC NGAGADHCQE CVHVRDGQHC 650
    VSECPKNKYN DRGVCRECHA TCDGCTGPKD TIGIGACTTC NLAIINNDAT 700
    VKRCLLKDDK CPDGYFWEYV HPQEQGSLKP LAGRAVCRKC HPLCELCTNY 750
    GYHEQVCSKC THYKRREQCE TECPADHYTD EEQRECFQRH PECNGCTGPG 800
    ADDCKSCRNF KLFDANETGP YVNSTMFNCT SKCPLEMRHV NYQYTAIGPY 850
    CAASPPRSSK ITANLDVNMI FIITGAVLVP TICILCVVTY ICRQKQKAKK 900
    ETVKMTMALS GCEDSEPLRP SNIGANLCKL RIVKDAELRK GGVLGMGAFG 950
    RVYKGVWVPE GENVKIPVAI KELLKSTGAE SSEEFLREAY IMASEEHVNL 1000
    LKLLAVCMSS QMMLITQLMP LGCLLDYVRN NRDKIGSKAL LNWSTQIAKG 1050
    MSYLEEKRLV HRDLAARNVL VQTPSLVKIT DFGLAKLLSS DSNEYKAAGG 1100
    KMPIKWLALE CIRNRVFTSK SDVWAFGVTI WELLTFGQRP HENIPAKDIP 1150
    DLIEVGLKLE QPEICSLDIY CTLLSCWHLD AAMRPTFKQL TTVFAEFARD 1200
    PGRYLAIPGD KFTRLPAYTS QDEKDLIRKL APTTDGSEAI AKPDDYLQPK 1250
    AAPGPSHRTD CTDEMPKLNR YCKDPSNKNS STGDDERDSS AREVGVGNLR 1300
    LDLPVDEDDY LMPTCQPGPN NNNNMNNPNQ NNMAAVGVAA GYMDLIGVPV 1350
    SVDNPEYLLN AQTLGVGESP IPTQTIGIPV MGGPGTMEVK VPMPGSEPTS 1400
    SDHEYYNDTQ RELQPLHRNR NTETRV 1426
    Length:1,426
    Mass (Da):159,718
    Last modified:December 15, 1998 - v3
    Checksum:i4D424C3C99DA4AF4
    GO
    Isoform Type II (identifier: P04412-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-101: MLLRRRNGPC...NKNEFVKGKI → MMIISMWMSI...GYVDNGNMKV

    Show »
    Length:1,377
    Mass (Da):153,700
    Checksum:iAEA869BD7849A0D5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371K → E(PubMed:9882502)Curated
    Sequence conflicti137 – 1371K → E(PubMed:10731132)Curated
    Sequence conflicti329 – 3313AVS → GVC(PubMed:9882502)Curated
    Sequence conflicti329 – 3313AVS → GVC(PubMed:10731132)Curated
    Sequence conflicti458 – 4581R → L(PubMed:9882502)Curated
    Sequence conflicti458 – 4581R → L(PubMed:10731132)Curated
    Sequence conflicti789 – 7891R → C(PubMed:9882502)Curated
    Sequence conflicti789 – 7891R → C(PubMed:10731132)Curated
    Sequence conflicti959 – 9591P → A in CAA26157. (PubMed:2983232)Curated
    Sequence conflicti995 – 9951E → V(PubMed:9882502)Curated
    Sequence conflicti995 – 9951E → V(PubMed:10731132)Curated
    Sequence conflicti1072 – 10809QTPSLVKIT → RLLAGEDH(PubMed:2982499)Curated
    Sequence conflicti1072 – 10809QTPSLVKIT → RLLAGEDH(PubMed:3093080)Curated
    Sequence conflicti1072 – 10809QTPSLVKIT → RLLAGEDH(PubMed:9731193)Curated
    Sequence conflicti1097 – 10982AA → I in CAA05747. (PubMed:9731193)Curated
    Sequence conflicti1118 – 11181T → R in CAA05747. (PubMed:9731193)Curated
    Sequence conflicti1242 – 12421K → E(PubMed:9882502)Curated
    Sequence conflicti1242 – 12421K → E(PubMed:10731132)Curated
    Sequence conflicti1265 – 12651M → I(PubMed:9882502)Curated
    Sequence conflicti1265 – 12651M → I(PubMed:10731132)Curated
    Sequence conflicti1287 – 12871R → T(PubMed:9882502)Curated
    Sequence conflicti1287 – 12871R → T(PubMed:10731132)Curated
    Sequence conflicti1325 – 13251M → I in AAF46732. (PubMed:10731132)Curated
    Sequence conflicti1383 – 13831G → V(PubMed:9882502)Curated
    Sequence conflicti1383 – 13831G → V(PubMed:10731132)Curated
    Sequence conflicti1412 – 142615ELQPL…TETRV → SCSHASKPQHGDEGVGSSRV GAIANEEGESCQVPLEAMRY AFAGCYLR(PubMed:2982499)CuratedAdd
    BLAST
    Sequence conflicti1412 – 142615ELQPL…TETRV → SCSHASKPQHGDEGVGSSRV GAIANEEGESCQVPLEAMRY AFAGCYLR(PubMed:3093080)CuratedAdd
    BLAST

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 101101MLLRR…VKGKI → MMIISMWMSISRGLWDSSSI LSVLLILACMASITTSSSVS NAGYVDNGNMKV in isoform Type II. CuratedVSP_002897Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052754, AF052753 Genomic DNA. Translation: AAC08536.1.
    AF052754, AF052752 Genomic DNA. Translation: AAC08535.1.
    K03054 Genomic DNA. Translation: AAA51462.1.
    K03417 mRNA. Translation: AAA51460.1.
    K03416 mRNA. Translation: AAA50965.1.
    AF109077 Genomic DNA. Translation: AAD26134.1.
    AF109078, AF109082 Genomic DNA. Translation: AAD26132.1.
    AF109078, AF109084 Genomic DNA. Translation: AAD26133.1.
    AF109079, AF109081 Genomic DNA. Translation: AAD26130.1.
    AF109079, AF109083 Genomic DNA. Translation: AAD26131.1.
    AF109080 Genomic DNA. Translation: AAD26135.1.
    AE013599 Genomic DNA. Translation: AAF46732.1.
    X02293 Genomic DNA. Translation: CAA26157.1.
    AJ002912 Genomic DNA. Translation: CAA05747.1.
    X78920 Genomic DNA. Translation: CAA55523.1.
    X78918 Genomic DNA. Translation: CAA55521.1.
    X78919 Genomic DNA. Translation: CAA55522.1.
    PIRiA00640. GQFFE.
    RefSeqiNP_476759.1. NM_057411.3.
    UniGeneiDm.20748.

    Genome annotation databases

    GeneIDi37455.
    KEGGidme:Dmel_CG10079.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF052754 , AF052753 Genomic DNA. Translation: AAC08536.1 .
    AF052754 , AF052752 Genomic DNA. Translation: AAC08535.1 .
    K03054 Genomic DNA. Translation: AAA51462.1 .
    K03417 mRNA. Translation: AAA51460.1 .
    K03416 mRNA. Translation: AAA50965.1 .
    AF109077 Genomic DNA. Translation: AAD26134.1 .
    AF109078 , AF109082 Genomic DNA. Translation: AAD26132.1 .
    AF109078 , AF109084 Genomic DNA. Translation: AAD26133.1 .
    AF109079 , AF109081 Genomic DNA. Translation: AAD26130.1 .
    AF109079 , AF109083 Genomic DNA. Translation: AAD26131.1 .
    AF109080 Genomic DNA. Translation: AAD26135.1 .
    AE013599 Genomic DNA. Translation: AAF46732.1 .
    X02293 Genomic DNA. Translation: CAA26157.1 .
    AJ002912 Genomic DNA. Translation: CAA05747.1 .
    X78920 Genomic DNA. Translation: CAA55523.1 .
    X78918 Genomic DNA. Translation: CAA55521.1 .
    X78919 Genomic DNA. Translation: CAA55522.1 .
    PIRi A00640. GQFFE.
    RefSeqi NP_476759.1. NM_057411.3.
    UniGenei Dm.20748.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3I2T X-ray 2.70 A 100-644 [» ]
    3LTF X-ray 3.20 A/C 100-688 [» ]
    3LTG X-ray 3.40 A/C 100-688 [» ]
    ProteinModelPortali P04412.
    SMRi P04412. Positions 100-804, 884-1248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63083. 72 interactions.
    DIPi DIP-17316N.
    IntActi P04412. 5 interactions.
    MINTi MINT-806082.

    Proteomic databases

    PaxDbi P04412.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 37455.
    KEGGi dme:Dmel_CG10079.

    Organism-specific databases

    CTDi 1956.
    FlyBasei FBgn0003731. Egfr.

    Phylogenomic databases

    eggNOGi COG0515.
    InParanoidi P04412.
    KOi K04361.
    OrthoDBi EOG7SV0TH.
    PhylomeDBi P04412.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 1994.
    SignaLinki P04412.

    Miscellaneous databases

    ChiTaRSi EGFR. drosophila.
    EvolutionaryTracei P04412.
    GenomeRNAii 37455.
    NextBioi 803734.

    Gene expression databases

    Bgeei P04412.

    Family and domain databases

    Gene3Di 3.80.20.20. 4 hits.
    InterProi IPR000494. EGF_rcpt_L.
    IPR006211. Furin-like_Cys-rich_dom.
    IPR006212. Furin_repeat.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view ]
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00261. FU. 7 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 3 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular analysis of the Drosophila EGF receptor homolog reveals that several genetically defined classes of alleles cluster in subdomains of the receptor protein."
      Clifford R., Schuepbach T.
      Genetics 137:531-550(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TYPE I AND TYPE II).
    2. Clifford R., Schuepbach T.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "The Drosophila EGF receptor gene homolog: conservation of both hormone binding and kinase domains."
      Livneh E., Glazer L., Segal D., Schlessinger J., Shilo B.-Z.
      Cell 40:599-607(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    4. "Alternative 5' exons and tissue-specific expression of the Drosophila EGF receptor homolog transcripts."
      Schejter E.D., Segal D., Glazer L., Shilo B.-Z.
      Cell 46:1091-1101(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, ALTERNATIVE SPLICING.
      Strain: Oregon-R.
      Tissue: Embryo.
    5. "Several levels of EGF receptor signaling during photoreceptor specification in wild-type, Ellipse, and null mutant Drosophila."
      Lesokhin A.M., Yu S.-Y., Katz J., Baker N.E.
      Dev. Biol. 205:129-144(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS TYPE I AND TYPE II), TISSUE SPECIFICITY, MUTANTS.
    6. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM TYPE I).
      Strain: Berkeley.
    7. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    8. "A Drosophila genomic sequence with homology to human epidermal growth factor receptor."
      Wadsworth S.C., Vincent W.S. III, Bilodeau-Wentworth D.
      Nature 314:178-180(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 959-1078.
      Strain: Daekwanryeong.
    9. "Sampling the genomic pool of protein tyrosine kinase genes using the polymerase chain reaction with genomic DNA."
      Oates A.C., Wollberg P., Achen M.G., Wilks A.F.
      Biochem. Biophys. Res. Commun. 249:660-667(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1069-1121.
      Tissue: Embryo.
    10. "Interallelic complementation among DER/flb alleles: implications for the mechanism of signal transduction by receptor-tyrosine kinases."
      Raz E., Schejter E.D., Shilo B.Z.
      Genetics 129:191-201(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1133-1137; 1155-1167 AND 1209-1216, MUTANTS.
    11. "There must be 50 ways to rule the signal: the case of the Drosophila EGF receptor."
      Perrimon N., Perkins L.A.
      Cell 89:13-16(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    12. "Identification of the Drosophila melanogaster homologue of the mammalian signal transducer protein, Vav."
      Dekel I., Russek N., Jones T., Mortin M.A., Katzav S.
      FEBS Lett. 472:99-104(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VAV.
    13. "Hole-in-one mutant phenotypes link EGFR/ERK signaling to epithelial tissue repair in Drosophila."
      Geiger J.A., Carvalho L., Campos I., Santos A.C., Jacinto A.
      PLoS ONE 6:E28349-E28349(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiEGFR_DROME
    AccessioniPrimary (citable) accession number: P04412
    Secondary accession number(s): O18370
    , O61601, P81868, Q9W2G0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 170 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3