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Q01279 (EGFR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor

EC=2.7.10.1
Gene names
Name:Egfr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1210 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Ref.7 Ref.11

Catalytic activity

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

Enzyme regulation

Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling. Ref.11

Subunit structure

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through TCEB1- and TCEB2-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Interacts with EPS8; mediates EPS8 phosphorylation. Interacts with ATX2. Interacts with GAREM. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Ref.7

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein By similarity. Golgi apparatus membrane; Single-pass type I membrane protein By similarity. Nucleus membrane; Single-pass type I membrane protein By similarity. Endosome. Endosome membrane. Nucleus By similarity. Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF) By similarity.

Post-translational modification

Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occur. Deubiquitinated by OTUD7B, preventing degradation By similarity.

Phosphorylated. Phosphorylation of Ser-697 is partial and occurs only if Thr-695 is phosphorylated. Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2 By similarity.

Methylated. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197 By similarity.

Disruption phenotype

Mice are growth retarded and die at different stages of development depending on their genetic background. Embryonic death is due to placental defects. Mice surviving until birth or later display brain, bone, heart and various epithelial development defects in several organs, including skin, lung and gastrointestinal tract. Ref.8 Ref.9 Ref.10

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
Nucleus
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of MAPKK activity

Inferred from electronic annotation. Source: Ensembl

alkanesulfonate metabolic process

Inferred from electronic annotation. Source: Ensembl

astrocyte activation

Inferred from electronic annotation. Source: Ensembl

cell morphogenesis

Inferred from genetic interaction PubMed 17686994. Source: MGI

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from direct assay PubMed 22711986. Source: UniProtKB

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to estradiol stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cerebral cortex cell migration

Inferred from mutant phenotype Ref.9. Source: MGI

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

digestive tract morphogenesis

Inferred from mutant phenotype Ref.9. Source: MGI

diterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from mutant phenotype Ref.9. Source: MGI

epidermal growth factor receptor signaling pathway

Inferred from direct assay PubMed 14712229PubMed 15695332. Source: MGI

epidermis development

Inferred from mutant phenotype Ref.9. Source: MGI

hair follicle development

Inferred from mutant phenotype Ref.9. Source: MGI

hydrogen peroxide metabolic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

magnesium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial fold

Inferred from mutant phenotype Ref.9. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

neuron projection morphogenesis

Inferred from electronic annotation. Source: Ensembl

ovulation cycle

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: GOC

polysaccharide metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of catenin import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 14712229. Source: MGI

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype Ref.9. Source: MGI

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 20208556. Source: BHF-UCL

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from direct assay PubMed 15314156. Source: MGI

regulation of cell proliferation

Inferred from genetic interaction PubMed 11818567. Source: MGI

regulation of nitric-oxide synthase activity

Inferred from electronic annotation. Source: Ensembl

regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 11940581. Source: MGI

response to UV-A

Inferred from electronic annotation. Source: Ensembl

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to cobalamin

Inferred from electronic annotation. Source: Ensembl

response to hydroxyisoflavone

Inferred from electronic annotation. Source: Ensembl

response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

salivary gland morphogenesis

Inferred from mutant phenotype PubMed 10521784. Source: MGI

signal transduction

Inferred from direct assay PubMed 11940581. Source: MGI

tongue development

Inferred from electronic annotation. Source: Ensembl

translation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from direct assay PubMed 7723235. Source: MGI

cell surface

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from direct assay PubMed 10534613. Source: MGI

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from sequence or structural similarity. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular

Inferred from direct assay PubMed 10534613. Source: MGI

membrane raft

Inferred from electronic annotation. Source: Ensembl

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 20208556. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20208556. Source: BHF-UCL

plasma membrane

Inferred from direct assay PubMed 7641815. Source: MGI

receptor complex

Inferred from sequence orthology PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor-activated receptor activity

Inferred from direct assay PubMed 14712229. Source: MGI

kinase activity

Inferred from direct assay PubMed 12808090. Source: MGI

nitric-oxide synthase regulator activity

Inferred from electronic annotation. Source: Ensembl

protein tyrosine kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

signal transducer activity

Inferred from direct assay PubMed 11940581. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGFP011333EBI-6296235,EBI-640857From a different organism.
KrasP328833EBI-6296235,EBI-644267

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 12101186Epidermal growth factor receptor
PRO_0000016666

Regions

Topological domain25 – 647623Extracellular Potential
Transmembrane648 – 67023Helical; Potential
Topological domain671 – 1210540Cytoplasmic Potential
Repeat75 – 300226Approximate
Repeat390 – 600211Approximate
Domain714 – 981268Protein kinase
Nucleotide binding720 – 7289ATP By similarity
Nucleotide binding792 – 7932ATP By similarity
Region690 – 70617Important for dimerization, phosphorylation and activation By similarity

Sites

Active site8391Proton acceptor By similarity
Binding site7471ATP By similarity
Binding site8571ATP By similarity
Site10181Important for interaction with PIK3C2B By similarity

Amino acid modifications

Modified residue2291Phosphoserine By similarity
Modified residue6801Phosphothreonine; by PKC and PKD/PRKD1 By similarity
Modified residue6951Phosphothreonine; by PKD/PRKD1 By similarity
Modified residue6971Phosphoserine By similarity
Modified residue9931Phosphoserine By similarity
Modified residue9971Phosphoserine By similarity
Modified residue10001Phosphotyrosine; by autocatalysis By similarity
Modified residue10181Phosphotyrosine; by autocatalysis By similarity
Modified residue10281Phosphoserine By similarity
Modified residue10411Phosphoserine By similarity
Modified residue10431Phosphothreonine By similarity
Modified residue10441Phosphoserine By similarity
Modified residue10701Phosphoserine By similarity
Modified residue10711Phosphoserine By similarity
Modified residue10921Phosphotyrosine; by autocatalysis By similarity
Modified residue11101Phosphotyrosine; by autocatalysis By similarity
Modified residue11661Phosphoserine By similarity
Modified residue11721Phosphotyrosine; by autocatalysis By similarity
Modified residue11971Phosphotyrosine; alternate Ref.14
Modified residue11971Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residue11991Omega-N-methylated arginine By similarity
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation1751N-linked (GlcNAc...) Ref.13
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Ref.12
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Ref.12
Glycosylation5281N-linked (GlcNAc...) Potential
Glycosylation5681N-linked (GlcNAc...) Potential
Glycosylation6031N-linked (GlcNAc...) Potential
Glycosylation6231N-linked (GlcNAc...) Potential
Disulfide bond190 ↔ 199 By similarity
Disulfide bond194 ↔ 207 By similarity
Disulfide bond215 ↔ 223 By similarity
Disulfide bond219 ↔ 231 By similarity
Disulfide bond232 ↔ 240 By similarity
Disulfide bond236 ↔ 248 By similarity
Disulfide bond251 ↔ 260 By similarity
Disulfide bond264 ↔ 291 By similarity
Disulfide bond295 ↔ 307 By similarity
Disulfide bond311 ↔ 326 By similarity
Disulfide bond329 ↔ 333 By similarity
Disulfide bond506 ↔ 515 By similarity
Disulfide bond510 ↔ 523 By similarity
Disulfide bond526 ↔ 535 By similarity
Disulfide bond539 ↔ 555 By similarity
Disulfide bond558 ↔ 571 By similarity
Disulfide bond562 ↔ 579 By similarity
Disulfide bond582 ↔ 591 By similarity
Disulfide bond595 ↔ 617 By similarity
Disulfide bond620 ↔ 628 By similarity
Disulfide bond624 ↔ 636 By similarity
Cross-link718Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link931Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict5391C → W in CAA42219. Ref.5
Sequence conflict9911L → F in AAA17899. Ref.4
Sequence conflict1116 – 11172HP → DR in CAA78249. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q01279 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 690E20D46DF2D2F5

FASTA1,210134,853
        10         20         30         40         50         60 
MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS LQRMYNNCEV 

        70         80         90        100        110        120 
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN ALYENTYALA 

       130        140        150        160        170        180 
ILSNYGTNRT GLRELPMRNL QEILIGAVRF SNNPILCNMD TIQWRDIVQN VFMSNMSMDL 

       190        200        210        220        230        240 
QSHPSSCPKC DPSCPNGSCW GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC 

       250        260        270        280        290        300 
TGPRESDCLV CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 

       310        320        330        340        350        360 
VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS INATNIKHFK 

       370        380        390        400        410        420 
YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE ITGFLLIQAW PDNWTDLHAF 

       430        440        450        460        470        480 
ENLEIIRGRT KQHGQFSLAV VGLNITSLGL RSLKEISDGD VIISGNRNLC YANTINWKKL 

       490        500        510        520        530        540 
FGTPNQKTKI MNNRAEKDCK AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN 

       550        560        570        580        590        600 
ILEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM 

       610        620        630        640        650        660 
GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT GIVGGLLFIV 

       670        680        690        700        710        720 
VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA PNQAHLRILK ETEFKKIKVL 

       730        740        750        760        770        780 
GSGAFGTVYK GLWIPEGEKV KIPVAIKELR EATSPKANKE ILDEAYVMAS VDNPHVCRLL 

       790        800        810        820        830        840 
GICLTSTVQL ITQLMPYGCL LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL 

       850        860        870        880        890        900 
AARNVLVKTP QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW 

       910        920        930        940        950        960 
SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV KCWMIDADSR 

       970        980        990       1000       1010       1020 
PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY RALMDEEDME DVVDADEYLI 

      1030       1040       1050       1060       1070       1080 
PQQGFFNSPS TSRTPLLSSL SATSNNSTVA CINRNGSCRV KEDAFLQRYS SDPTGAVTED 

      1090       1100       1110       1120       1130       1140 
NIDDAFLPVP EYVNQSVPKR PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN 

      1150       1160       1170       1180       1190       1200 
TAQPTCLSSG FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV 

      1210 
APPSSEFIGA 

« Hide

References

« Hide 'large scale' references
[1]"Promoter region of the murine fibroblast growth factor receptor 2 (bek/KGFR) gene."
Avivi A., Skorecki K., Yayon A., Givol D.
Oncogene 7:1957-1962(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"Expression of the epidermal growth factor receptor gene is regulated in mouse blastocysts during delayed implantation."
Paria B.C., Das S.K., Andrews G.K., Dey S.K.
Proc. Natl. Acad. Sci. U.S.A. 90:55-59(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c and CD-1.
Tissue: Decidua and Liver.
[3]Hibbs M.L.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[4]"The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase."
Luetteke N.C., Phillips H.K., Qiu T.H., Copeland N.G., Earp H.S., Jenkins N.A., Lee D.C.
Genes Dev. 8:399-413(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: B6/C3.
Tissue: Liver.
[5]"Comparison of EGF receptor sequences as a guide to study the ligand binding site."
Avivi A., Lax I., Ullrich A., Schlessinger J., Givol D., Morse B.
Oncogene 6:673-676(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-714.
Tissue: Brain.
[6]Eisinger D.P., Serrero G.
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 969-1117.
Strain: C3H.
[7]"Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals."
Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T., Wong W.T., di Fiore P.P.
EMBO J. 12:3799-3808(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL GROWTH, FUNCTION IN PHOSPHORYLATION OF EPS8, INTERACTION WITH EPS8.
[8]"Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor."
Miettinen P.J., Berger J.E., Meneses J., Phung Y., Pedersen R.A., Werb Z., Derynck R.
Nature 376:337-341(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"Targeted disruption of mouse EGF receptor: effect of genetic background on mutant phenotype."
Threadgill D.W., Dlugosz A.A., Hansen L.A., Tennenbaum T., Lichti U., Yee D., LaMantia C., Mourton T., Herrup K., Harris R.C.
Science 269:230-234(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[10]"Strain-dependent epithelial defects in mice lacking the EGF receptor."
Sibilia M., Wagner E.F.
Science 269:234-238(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[11]"Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis."
Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.
J. Cell Biol. 150:905-912(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF EPS15, ENZYME REGULATION, ENDOCYTOSIS.
[12]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444.
Strain: C57BL/6.
Tissue: Plasma.
[13]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175.
Strain: C57BL/6.
Tissue: Plasma.
[14]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78987 mRNA. Translation: CAA55587.1.
U03425 mRNA. Translation: AAA17899.1.
X59698 mRNA. Translation: CAA42219.1.
L06864 mRNA. Translation: AAA53029.1.
Z12608 mRNA. Translation: CAA78249.1.
PIRA53183.
RefSeqNP_997538.1. NM_207655.2.
UniGeneMm.420648.
Mm.439882.
Mm.8534.

3D structure databases

ProteinModelPortalQ01279.
SMRQ01279. Positions 26-636, 644-1020.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199402. 20 interactions.
DIPDIP-5763N.
IntActQ01279. 9 interactions.
MINTMINT-143143.

Chemistry

BindingDBQ01279.
ChEMBLCHEMBL3608.

PTM databases

PhosphoSiteQ01279.

Proteomic databases

PaxDbQ01279.
PRIDEQ01279.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
GeneID13649.
KEGGmmu:13649.
UCSCuc007ibo.1. mouse.

Organism-specific databases

CTD1956.
MGIMGI:95294. Egfr.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00600000084253.
HOGENOMHOG000230982.
HOVERGENHBG000490.
InParanoidQ01279.
KOK04361.
OMAMRRRHIV.
PhylomeDBQ01279.
TreeFamTF106002.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

ArrayExpressQ01279.
BgeeQ01279.
CleanExMM_EGFR.
GenevestigatorQ01279.

Family and domain databases

Gene3D3.80.20.20. 2 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.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEGFR. mouse.
NextBio284374.
PROQ01279.
SOURCESearch...

Entry information

Entry nameEGFR_MOUSE
AccessionPrimary (citable) accession number: Q01279
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot