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Protein

Epidermal growth factor receptor

Gene

Egfr

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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.
ReactomeiREACT_284157. SHC1 events in ERBB2 signaling.
REACT_285422. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
REACT_288369. Nuclear signaling by ERBB4.
REACT_293394. Downregulation of ERBB4 signaling.
REACT_294512. Signaling by ERBB2.
REACT_295632. PI3K events in ERBB2 signaling.
REACT_299068. GAB1 signalosome.
REACT_300032. EGFR interacts with phospholipase C-gamma.
REACT_307287. GRB2 events in EGFR signaling.
REACT_308878. Constitutive PI3K/AKT Signaling in Cancer.
REACT_313058. SHC1 events in EGFR signaling.
REACT_318317. Signal transduction by L1.
REACT_323404. Inhibition of Signaling by Overexpressed EGFR.
REACT_325528. PLCG1 events in ERBB2 signaling.
REACT_326060. Sema4D induced cell migration and growth-cone collapse.
REACT_338876. EGFR downregulation.
REACT_339689. PIP3 activates AKT signaling.
REACT_342034. GRB2 events in ERBB2 signaling.
REACT_343362. Constitutive Signaling by EGFRvIII.
REACT_343793. Signaling by EGFR.
REACT_348404. Downregulation of ERBB2:ERBB3 signaling.
REACT_352911. EGFR Transactivation by Gastrin.
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 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003731. Egfr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 868838ExtracellularSequence AnalysisAdd
BLAST
Transmembranei869 – 88921HelicalSequence AnalysisAdd
BLAST
Topological domaini890 – 1426537CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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.
ExpressionAtlasiP04412. differential.

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
InterProiIPR006211. 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.
IPR000494. Rcpt_L-dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MLLRRRNGPC PFPLLLLLLA HCICIWPASA ARDRYARQNN RQRHQDIDRD
60 70 80 90 100
RDRDRFLYRS SSAQNRQRGG ANFALGLGAN GVTIPTSLED KNKNEFVKGK
110 120 130 140 150
ICIGTKSRLS VPSNKEHHYR NLRDRYTNCT YVDGNLKLTW LPNENLDLSF
160 170 180 190 200
LDNIREVTGY ILISHVDVKK VVFPKLQIIR GRTLFSLSVE EEKYALFVTY
210 220 230 240 250
SKMYTLEIPD LRDVLNGQVG FHNNYNLCHM RTIQWSEIVS NGTDAYYNYD
260 270 280 290 300
FTAPERECPK CHESCTHGCW GEGPKNCQKF SKLTCSPQCA GGRCYGPKPR
310 320 330 340 350
ECCHLFCAGG CTGPTQKDCI ACKNFFDEAV SKEECPPMRK YNPTTYVLET
360 370 380 390 400
NPEGKYAYGA TCVKECPGHL LRDNGACVRS CPQDKMDKGG ECVPCNGPCP
410 420 430 440 450
KTCPGVTVLH AGNIDSFRNC TVIDGNIRIL DQTFSGFQDV YANYTMGPRY
460 470 480 490 500
IPLDPERREV FSTVKEITGY LNIEGTHPQF RNLSYFRNLE TIHGRQLMES
510 520 530 540 550
MFAALAIVKS SLYSLEMRNL KQISSGSVVI QHNRDLCYVS NIRWPAIQKE
560 570 580 590 600
PEQKVWVNEN LRADLCEKNG TICSDQCNED GCWGAGTDQC LTCKNFNFNG
610 620 630 640 650
TCIADCGYIS NAYKFDNRTC KICHPECRTC NGAGADHCQE CVHVRDGQHC
660 670 680 690 700
VSECPKNKYN DRGVCRECHA TCDGCTGPKD TIGIGACTTC NLAIINNDAT
710 720 730 740 750
VKRCLLKDDK CPDGYFWEYV HPQEQGSLKP LAGRAVCRKC HPLCELCTNY
760 770 780 790 800
GYHEQVCSKC THYKRREQCE TECPADHYTD EEQRECFQRH PECNGCTGPG
810 820 830 840 850
ADDCKSCRNF KLFDANETGP YVNSTMFNCT SKCPLEMRHV NYQYTAIGPY
860 870 880 890 900
CAASPPRSSK ITANLDVNMI FIITGAVLVP TICILCVVTY ICRQKQKAKK
910 920 930 940 950
ETVKMTMALS GCEDSEPLRP SNIGANLCKL RIVKDAELRK GGVLGMGAFG
960 970 980 990 1000
RVYKGVWVPE GENVKIPVAI KELLKSTGAE SSEEFLREAY IMASEEHVNL
1010 1020 1030 1040 1050
LKLLAVCMSS QMMLITQLMP LGCLLDYVRN NRDKIGSKAL LNWSTQIAKG
1060 1070 1080 1090 1100
MSYLEEKRLV HRDLAARNVL VQTPSLVKIT DFGLAKLLSS DSNEYKAAGG
1110 1120 1130 1140 1150
KMPIKWLALE CIRNRVFTSK SDVWAFGVTI WELLTFGQRP HENIPAKDIP
1160 1170 1180 1190 1200
DLIEVGLKLE QPEICSLDIY CTLLSCWHLD AAMRPTFKQL TTVFAEFARD
1210 1220 1230 1240 1250
PGRYLAIPGD KFTRLPAYTS QDEKDLIRKL APTTDGSEAI AKPDDYLQPK
1260 1270 1280 1290 1300
AAPGPSHRTD CTDEMPKLNR YCKDPSNKNS STGDDERDSS AREVGVGNLR
1310 1320 1330 1340 1350
LDLPVDEDDY LMPTCQPGPN NNNNMNNPNQ NNMAAVGVAA GYMDLIGVPV
1360 1370 1380 1390 1400
SVDNPEYLLN AQTLGVGESP IPTQTIGIPV MGGPGTMEVK VPMPGSEPTS
1410 1420
SDHEYYNDTQ RELQPLHRNR NTETRV
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:
EMBLi
GenBanki
DDBJi
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_057411.4.

Genome annotation databases

GeneIDi37455.
KEGGidme:Dmel_CG10079.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_057411.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP04412.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi37455.
KEGGidme:Dmel_CG10079.

Organism-specific databases

CTDi1956.
FlyBaseiFBgn0003731. Egfr.

Phylogenomic databases

eggNOGiCOG0515.
InParanoidiP04412.
KOiK04361.
OrthoDBiEOG7SV0TH.
PhylomeDBiP04412.

Enzyme and pathway databases

BRENDAi2.7.10.1. 1994.
ReactomeiREACT_284157. SHC1 events in ERBB2 signaling.
REACT_285422. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
REACT_288369. Nuclear signaling by ERBB4.
REACT_293394. Downregulation of ERBB4 signaling.
REACT_294512. Signaling by ERBB2.
REACT_295632. PI3K events in ERBB2 signaling.
REACT_299068. GAB1 signalosome.
REACT_300032. EGFR interacts with phospholipase C-gamma.
REACT_307287. GRB2 events in EGFR signaling.
REACT_308878. Constitutive PI3K/AKT Signaling in Cancer.
REACT_313058. SHC1 events in EGFR signaling.
REACT_318317. Signal transduction by L1.
REACT_323404. Inhibition of Signaling by Overexpressed EGFR.
REACT_325528. PLCG1 events in ERBB2 signaling.
REACT_326060. Sema4D induced cell migration and growth-cone collapse.
REACT_338876. EGFR downregulation.
REACT_339689. PIP3 activates AKT signaling.
REACT_342034. GRB2 events in ERBB2 signaling.
REACT_343362. Constitutive Signaling by EGFRvIII.
REACT_343793. Signaling by EGFR.
REACT_348404. Downregulation of ERBB2:ERBB3 signaling.
REACT_352911. EGFR Transactivation by Gastrin.
SignaLinkiP04412.

Miscellaneous databases

ChiTaRSiEgfr. fly.
EvolutionaryTraceiP04412.
GenomeRNAii37455.
NextBioi803734.
PROiP04412.

Gene expression databases

BgeeiP04412.
ExpressionAtlasiP04412. differential.

Family and domain databases

Gene3Di3.80.20.20. 4 hits.
InterProiIPR006211. 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.
IPR000494. Rcpt_L-dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 175 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.