Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04412 (EGFR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor

Short name=Egfr
EC=2.7.10.1
Alternative name(s):
Drosophila relative of ERBB
Gurken receptor
Protein torpedo
Gene names
Name:Egfr
Synonyms:c-erbB, DER, top
ORF Names:CG10079
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Catalytic activity

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

Subunit structure

Interacts (when phosphorylated on tyrosine residues) with Vav (via SH2 domain). Ref.12

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

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. Ref.5

Disruption phenotype

Embryonic wound healing defects. Ref.13

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement PubMed 14616073. Source: FlyBase

Malpighian tubule morphogenesis

Inferred from mutant phenotype PubMed 9927461. Source: FlyBase

R7 cell differentiation

Traceable author statement PubMed 14505358. Source: FlyBase

antennal development

Non-traceable author statement PubMed 11875444. Source: FlyBase

anterior/posterior pattern specification

Traceable author statement PubMed 9988212. Source: FlyBase

behavioral response to ethanol

Inferred from mutant phenotype PubMed 19464045. Source: FlyBase

blastoderm segmentation

Traceable author statement PubMed 12648473. Source: FlyBase

border follicle cell migration

Inferred from mutant phenotype PubMed 11141565. Source: FlyBase

brain development

Traceable author statement PubMed 12648473. Source: FlyBase

branched duct epithelial cell fate determination, open tracheal system

Traceable author statement PubMed 10684581PubMed 11063940. Source: FlyBase

cell fate determination

Traceable author statement PubMed 12648473PubMed 14616073PubMed 9631645. Source: FlyBase

cell projection assembly

Inferred from mutant phenotype PubMed 12198500. Source: FlyBase

chorion-containing eggshell pattern formation

Inferred from genetic interaction PubMed 11606538. Source: FlyBase

compound eye cone cell fate commitment

Traceable author statement PubMed 12419199PubMed 12648473. Source: FlyBase

compound eye development

Inferred from mutant phenotype PubMed 11301250PubMed 1634999. Source: FlyBase

compound eye morphogenesis

Traceable author statement PubMed 14616073. Source: FlyBase

compound eye photoreceptor cell differentiation

Inferred from mutant phenotype PubMed 16377567. Source: FlyBase

compound eye photoreceptor fate commitment

Traceable author statement PubMed 9631645. Source: FlyBase

determination of genital disc primordium

Inferred from mutant phenotype PubMed 15893978. Source: FlyBase

digestive tract morphogenesis

Inferred from mutant phenotype PubMed 21176204. Source: FlyBase

dorsal appendage formation

Inferred from mutant phenotype PubMed 17008069. Source: FlyBase

dorsal closure

Inferred from mutant phenotype PubMed 23579691PubMed 9927461. Source: FlyBase

dorsal/ventral pattern formation

Traceable author statement PubMed 12648473. Source: FlyBase

embryonic pattern specification

Inferred from genetic interaction PubMed 17898168. Source: FlyBase

epidermal growth factor receptor signaling pathway

Traceable author statement PubMed 9154002. Source: FlyBase

epithelial cell proliferation involved in Malpighian tubule morphogenesis

Inferred from mutant phenotype PubMed 11861476PubMed 9637680. Source: FlyBase

establishment or maintenance of apical/basal cell polarity

Inferred from mutant phenotype PubMed 16908845. Source: FlyBase

eye development

Inferred from mutant phenotype PubMed 14536058. Source: FlyBase

eye-antennal disc morphogenesis

Inferred from mutant phenotype PubMed 16963016. Source: FlyBase

female germ-line cyst encapsulation

Traceable author statement PubMed 12648473. Source: FlyBase

gastrulation

Traceable author statement PubMed 12648473. Source: FlyBase

germ-band shortening

Inferred from mutant phenotype PubMed 8946251PubMed 9927461. Source: FlyBase

germ-line stem cell maintenance

Inferred from genetic interaction PubMed 16399083. Source: FlyBase

gonad development

Inferred from mutant phenotype PubMed 21377458. Source: FlyBase

haltere development

Inferred from mutant phenotype PubMed 16815386. Source: FlyBase

heart process

Inferred from mutant phenotype PubMed 20523889. Source: FlyBase

imaginal disc development

Inferred from mutant phenotype PubMed 10934021. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 10995384PubMed 12930782PubMed 14536058PubMed 16648592. Source: FlyBase

imaginal disc-derived wing vein morphogenesis

Inferred from mutant phenotype PubMed 15766758PubMed 23549788. Source: FlyBase

imaginal disc-derived wing vein specification

Traceable author statement PubMed 12648473. Source: FlyBase

leg disc proximal/distal pattern formation

Inferred from mutant phenotype PubMed 12181568. Source: FlyBase

maintenance of epithelial integrity, open tracheal system

Inferred from mutant phenotype PubMed 16831830. Source: FlyBase

male germ-line cyst encapsulation

Traceable author statement PubMed 12648473. Source: FlyBase

maternal determination of dorsal/ventral axis, ovarian follicular epithelium, soma encoded

Inferred from mutant phenotype PubMed 3107840. Source: FlyBase

morphogenesis of an epithelium

Inferred from mutant phenotype PubMed 9927461. Source: FlyBase

morphogenesis of follicular epithelium

Inferred from mutant phenotype PubMed 9504923. Source: FlyBase

muscle attachment

Traceable author statement PubMed 12648473. Source: FlyBase

muscle cell fate specification

Traceable author statement PubMed 12648473. Source: FlyBase

negative regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 15809036. Source: FlyBase

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 17055987PubMed 23579691. Source: FlyBase

negative regulation of apoptotic signaling pathway

Inferred from genetic interaction PubMed 9814703. Source: FlyBase

negative regulation of compound eye retinal cell programmed cell death

Inferred from mutant phenotype PubMed 15511643. Source: FlyBase

neurogenesis

Inferred from genetic interaction PubMed 17898168. Source: FlyBase

notum cell fate specification

Inferred from mutant phenotype PubMed 10995384. Source: FlyBase

notum development

Inferred from mutant phenotype PubMed 10995384. Source: FlyBase

oenocyte differentiation

Traceable author statement PubMed 12648473. Source: FlyBase

olfactory learning

Inferred from mutant phenotype PubMed 23512935. Source: FlyBase

ommatidial rotation

Inferred from mutant phenotype PubMed 14507782PubMed 14507785. Source: FlyBase

oocyte anterior/posterior axis specification

Non-traceable author statement PubMed 10878576PubMed 9642168. Source: FlyBase

oocyte axis specification

Inferred from mutant phenotype PubMed 16908845. Source: FlyBase

oocyte dorsal/ventral axis specification

Non-traceable author statement PubMed 9642168. Source: FlyBase

open tracheal system development

Traceable author statement PubMed 10684581PubMed 11063940PubMed 12648473PubMed 12791296. Source: FlyBase

peptidyl-tyrosine phosphorylation

Non-traceable author statement PubMed 10908587. Source: GOC

peripheral nervous system development

Inferred from mutant phenotype PubMed 12967983. Source: FlyBase

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 19141677PubMed 21176204. Source: FlyBase

positive regulation of wound healing

Inferred from mutant phenotype Ref.13. Source: FlyBase

progression of morphogenetic furrow involved in compound eye morphogenesis

Traceable author statement PubMed 14616073. Source: FlyBase

protein phosphorylation

Non-traceable author statement PubMed 10908587. Source: FlyBase

regulation of R8 cell spacing in compound eye

Non-traceable author statement PubMed 11880339. Source: FlyBase

regulation of hemocyte differentiation

Inferred from mutant phenotype PubMed 15381778. Source: FlyBase

regulation of mitotic cell cycle

Traceable author statement PubMed 14616073. Source: FlyBase

salivary gland development

Inferred from mutant phenotype PubMed 9927461. Source: FlyBase

second mitotic wave involved in compound eye morphogenesis

Inferred from mutant phenotype PubMed 11257224. Source: FlyBase

segment polarity determination

Inferred from mutant phenotype PubMed 15930099. Source: FlyBase

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 16831830. Source: FlyBase

spiracle morphogenesis, open tracheal system

Inferred from mutant phenotype PubMed 15930099. Source: FlyBase

stem cell fate commitment

Inferred from mutant phenotype PubMed 20463031. Source: FlyBase

stomatogastric nervous system development

Traceable author statement PubMed 12648473. Source: FlyBase

tracheal pit formation in open tracheal system

Traceable author statement PubMed 12791296. Source: FlyBase

wing and notum subfield formation

Inferred from mutant phenotype PubMed 10860999. Source: FlyBase

wing disc morphogenesis

Inferred from mutant phenotype PubMed 12930782. Source: FlyBase

wing disc proximal/distal pattern formation

Traceable author statement PubMed 12717815. Source: FlyBase

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 16054027. Source: FlyBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

epidermal growth factor-activated receptor activity

Inferred from sequence or structural similarity Ref.3. Source: FlyBase

protein binding

Inferred from physical interaction PubMed 20723758PubMed 23827685. Source: IntAct

protein tyrosine kinase activity

Non-traceable author statement PubMed 10908587. Source: FlyBase

transmembrane signaling receptor activity

Traceable author statement PubMed 12879448. Source: FlyBase

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Type I (identifier: P04412-1)

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.
Isoform Type II (identifier: P04412-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 14261396Epidermal growth factor receptor
PRO_0000016676

Regions

Topological domain31 – 868838Extracellular Potential
Transmembrane869 – 88921Helical; Potential
Topological domain890 – 1426537Cytoplasmic Potential
Domain938 – 1198261Protein kinase
Nucleotide binding944 – 9529ATP By similarity

Sites

Active site10631Proton acceptor By similarity
Binding site9711ATP By similarity

Amino acid modifications

Modified residue9021Phosphothreonine; by PKC By similarity
Modified residue13101Phosphotyrosine; by autocatalysis By similarity
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation4821N-linked (GlcNAc...) Potential
Glycosylation5691N-linked (GlcNAc...) Potential
Glycosylation5991N-linked (GlcNAc...) Potential
Glycosylation6171N-linked (GlcNAc...) Potential
Glycosylation8161N-linked (GlcNAc...) Potential
Glycosylation8231N-linked (GlcNAc...) Potential
Glycosylation8281N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 101101MLLRR…VKGKI → MMIISMWMSISRGLWDSSSI LSVLLILACMASITTSSSVS NAGYVDNGNMKV in isoform Type II.
VSP_002897

Experimental info

Mutagenesis7931C → R in EGFR-ELP-1.
Mutagenesis9361A → T in EGFR-ELP-B1 and EGFR-ELP-B1RB1.
Mutagenesis10581R → Q in EGFR-ELP-B1RB1.
Mutagenesis11351T → I in EGFR-2W74.
Mutagenesis11561G → S in EGFR-2C82.
Mutagenesis11621P → L in EGFR-1F26.
Mutagenesis11661S → L in EGFR-2L65.
Mutagenesis1210 – 12167DKFTRLP → EKVHPAA in EGFR-2X51.
Sequence conflict1371K → E Ref.5
Sequence conflict1371K → E Ref.6
Sequence conflict329 – 3313AVS → GVC Ref.5
Sequence conflict329 – 3313AVS → GVC Ref.6
Sequence conflict4581R → L Ref.5
Sequence conflict4581R → L Ref.6
Sequence conflict7891R → C Ref.5
Sequence conflict7891R → C Ref.6
Sequence conflict9591P → A in CAA26157. Ref.8
Sequence conflict9951E → V Ref.5
Sequence conflict9951E → V Ref.6
Sequence conflict1072 – 10809QTPSLVKIT → RLLAGEDH Ref.3
Sequence conflict1072 – 10809QTPSLVKIT → RLLAGEDH Ref.4
Sequence conflict1072 – 10809QTPSLVKIT → RLLAGEDH Ref.9
Sequence conflict1097 – 10982AA → I in CAA05747. Ref.9
Sequence conflict11181T → R in CAA05747. Ref.9
Sequence conflict12421K → E Ref.5
Sequence conflict12421K → E Ref.6
Sequence conflict12651M → I Ref.5
Sequence conflict12651M → I Ref.6
Sequence conflict12871R → T Ref.5
Sequence conflict12871R → T Ref.6
Sequence conflict13251M → I in AAF46732. Ref.6
Sequence conflict13831G → V Ref.5
Sequence conflict13831G → V Ref.6
Sequence conflict1412 – 142615ELQPL…TETRV → SCSHASKPQHGDEGVGSSRV GAIANEEGESCQVPLEAMRY AFAGCYLR Ref.3
Sequence conflict1412 – 142615ELQPL…TETRV → SCSHASKPQHGDEGVGSSRV GAIANEEGESCQVPLEAMRY AFAGCYLR Ref.4

Secondary structure

........................................................................................................................ 1426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Type I [UniParc].

Last modified December 15, 1998. Version 3.
Checksum: 4D424C3C99DA4AF4

FASTA1,426159,718
        10         20         30         40         50         60 
MLLRRRNGPC PFPLLLLLLA HCICIWPASA ARDRYARQNN RQRHQDIDRD RDRDRFLYRS 

        70         80         90        100        110        120 
SSAQNRQRGG ANFALGLGAN GVTIPTSLED KNKNEFVKGK ICIGTKSRLS VPSNKEHHYR 

       130        140        150        160        170        180 
NLRDRYTNCT YVDGNLKLTW LPNENLDLSF LDNIREVTGY ILISHVDVKK VVFPKLQIIR 

       190        200        210        220        230        240 
GRTLFSLSVE EEKYALFVTY SKMYTLEIPD LRDVLNGQVG FHNNYNLCHM RTIQWSEIVS 

       250        260        270        280        290        300 
NGTDAYYNYD FTAPERECPK CHESCTHGCW GEGPKNCQKF SKLTCSPQCA GGRCYGPKPR 

       310        320        330        340        350        360 
ECCHLFCAGG CTGPTQKDCI ACKNFFDEAV SKEECPPMRK YNPTTYVLET NPEGKYAYGA 

       370        380        390        400        410        420 
TCVKECPGHL LRDNGACVRS CPQDKMDKGG ECVPCNGPCP KTCPGVTVLH AGNIDSFRNC 

       430        440        450        460        470        480 
TVIDGNIRIL DQTFSGFQDV YANYTMGPRY IPLDPERREV FSTVKEITGY LNIEGTHPQF 

       490        500        510        520        530        540 
RNLSYFRNLE TIHGRQLMES MFAALAIVKS SLYSLEMRNL KQISSGSVVI QHNRDLCYVS 

       550        560        570        580        590        600 
NIRWPAIQKE PEQKVWVNEN LRADLCEKNG TICSDQCNED GCWGAGTDQC LTCKNFNFNG 

       610        620        630        640        650        660 
TCIADCGYIS NAYKFDNRTC KICHPECRTC NGAGADHCQE CVHVRDGQHC VSECPKNKYN 

       670        680        690        700        710        720 
DRGVCRECHA TCDGCTGPKD TIGIGACTTC NLAIINNDAT VKRCLLKDDK CPDGYFWEYV 

       730        740        750        760        770        780 
HPQEQGSLKP LAGRAVCRKC HPLCELCTNY GYHEQVCSKC THYKRREQCE TECPADHYTD 

       790        800        810        820        830        840 
EEQRECFQRH PECNGCTGPG ADDCKSCRNF KLFDANETGP YVNSTMFNCT SKCPLEMRHV 

       850        860        870        880        890        900 
NYQYTAIGPY CAASPPRSSK ITANLDVNMI FIITGAVLVP TICILCVVTY ICRQKQKAKK 

       910        920        930        940        950        960 
ETVKMTMALS GCEDSEPLRP SNIGANLCKL RIVKDAELRK GGVLGMGAFG RVYKGVWVPE 

       970        980        990       1000       1010       1020 
GENVKIPVAI KELLKSTGAE SSEEFLREAY IMASEEHVNL LKLLAVCMSS QMMLITQLMP 

      1030       1040       1050       1060       1070       1080 
LGCLLDYVRN NRDKIGSKAL LNWSTQIAKG MSYLEEKRLV HRDLAARNVL VQTPSLVKIT 

      1090       1100       1110       1120       1130       1140 
DFGLAKLLSS DSNEYKAAGG KMPIKWLALE CIRNRVFTSK SDVWAFGVTI WELLTFGQRP 

      1150       1160       1170       1180       1190       1200 
HENIPAKDIP DLIEVGLKLE QPEICSLDIY CTLLSCWHLD AAMRPTFKQL TTVFAEFARD 

      1210       1220       1230       1240       1250       1260 
PGRYLAIPGD KFTRLPAYTS QDEKDLIRKL APTTDGSEAI AKPDDYLQPK AAPGPSHRTD 

      1270       1280       1290       1300       1310       1320 
CTDEMPKLNR YCKDPSNKNS STGDDERDSS AREVGVGNLR LDLPVDEDDY LMPTCQPGPN 

      1330       1340       1350       1360       1370       1380 
NNNNMNNPNQ NNMAAVGVAA GYMDLIGVPV SVDNPEYLLN AQTLGVGESP IPTQTIGIPV 

      1390       1400       1410       1420 
MGGPGTMEVK VPMPGSEPTS SDHEYYNDTQ RELQPLHRNR NTETRV 

« Hide

Isoform Type II [UniParc].

Checksum: AEA869BD7849A0D5
Show »

FASTA1,377153,700

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRGQFFE. A00640.
RefSeqNP_476759.1. NM_057411.3.
UniGeneDm.20748.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3I2TX-ray2.70A100-644[»]
3LTFX-ray3.20A/C100-688[»]
3LTGX-ray3.40A/C100-688[»]
ProteinModelPortalP04412.
SMRP04412. Positions 100-804, 884-1248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid63083. 72 interactions.
DIPDIP-17316N.
IntActP04412. 5 interactions.
MINTMINT-806082.

Proteomic databases

PaxDbP04412.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID37455.
KEGGdme:Dmel_CG10079.

Organism-specific databases

CTD1956.
FlyBaseFBgn0003731. Egfr.

Phylogenomic databases

eggNOGCOG0515.
InParanoidP04412.
KOK04361.
OrthoDBEOG7SV0TH.
PhylomeDBP04412.

Enzyme and pathway databases

BRENDA2.7.10.1. 1994.
SignaLinkP04412.

Gene expression databases

BgeeP04412.

Family and domain databases

Gene3D3.80.20.20. 4 hits.
InterProIPR000494. 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]
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 7 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 3 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEGFR. drosophila.
EvolutionaryTraceP04412.
GenomeRNAi37455.
NextBio803734.

Entry information

Entry nameEGFR_DROME
AccessionPrimary (citable) accession number: P04412
Secondary accession number(s): O18370 expand/collapse secondary AC list , O61601, P81868, Q9W2G0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase