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Reviewed, UniProtKB/Swiss-Prot Q01279 (EGFR_MOUSE)

Last modified June 16, 2009. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Epidermal growth factor receptor
    EC=2.7.10.1
Gene names
Name: Egfr
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

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

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General annotation (Comments)

Function

The EGF receptor mediates the biological signal of EGF, and also of TGF-alpha, amphiregulin, heparin-binding EGF, GP30 and vaccinia virus growth factor By similarity.

Catalytic activity

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

Subunit structure

Binds RIPK1. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. The autophosphorylated form interacts with PIK3C2B, maybe indirectly. Interacts with PELP1 and MUC1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

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 By similarity.

Miscellaneous

Binding of EGF to the receptor leads to dimerization, internalization of the EGF-receptor complex, induction of the tyrosine kinase activity, stimulation of cell DNA synthesis, and cell proliferation.

Sequence similarities

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

Contains 1 protein kinase domain.

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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 – 67023 Potential
Topological domain671 – 1210540Cytoplasmic Potential
Repeat75 – 300226Approximate
Repeat390 – 600211Approximate
Domain714 – 981268Protein kinase
Nucleotide binding720 – 7289ATP By similarity
Compositional bias1028 – 107144Ser-rich

Sites

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

Amino acid modifications

Modified residue6801Phosphothreonine; by PKC By similarity
Modified residue6951Phosphothreonine By similarity
Modified residue6971Phosphoserine By similarity
Modified residue7271Phosphothreonine By similarity
Modified residue8711Phosphotyrosine By similarity
Modified residue9801Phosphotyrosine By similarity
Modified residue9931Phosphoserine Ref.9
Modified residue9951Phosphothreonine By similarity
Modified residue9971Phosphoserine By similarity
Modified residue10001Phosphotyrosine Ref.9
Modified residue10281Phosphoserine By similarity
Modified residue10391Phosphoserine By similarity
Modified residue10411Phosphoserine By similarity
Modified residue10431Phosphothreonine By similarity
Modified residue10441Phosphoserine By similarity
Modified residue10471Phosphoserine By similarity
Modified residue10691Phosphotyrosine By similarity
Modified residue10701Phosphoserine By similarity
Modified residue10711Phosphoserine By similarity
Modified residue10921Phosphotyrosine; by autocatalysis By similarity
Modified residue11101Phosphotyrosine; by autocatalysis By similarity
Modified residue11381Phosphotyrosine By similarity
Modified residue11661Phosphoserine By similarity
Modified residue11721Phosphotyrosine; by autocatalysis By similarity
Modified residue11971Phosphotyrosine; by autocatalysis By similarity
Glycosylation1281N-linked (GlcNAc...) Potential
Glycosylation1751N-linked (GlcNAc...) Ref.8
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Ref.7
Glycosylation4131N-linked (GlcNAc...) Potential
Glycosylation4441N-linked (GlcNAc...) Ref.7
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 conflict191C → S Ref.2
Sequence conflict5391C → W in CAA42219. Ref.5
Sequence conflict9911L → F in AAA17899. Ref.4
Sequence conflict1116 – 11172HP → DR Ref.6

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Sequences

Sequence LengthMass (Da)Tools
Q01279-1 [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

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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: 1408137] [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: 7678348] [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: 8125255] [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: 2030916] [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]"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: 16944957] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444, MASS SPECTROMETRY.
Tissue: Plasma.
[8]"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: 17330941] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175, MASS SPECTROMETRY.
Tissue: Plasma.
[9]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-993 AND TYR-1000, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00121190.
PIRA53183.
RefSeqNP_997538.1.
UniGeneMm.420648
Mm.439882
Mm.8534

3D structure databases

HSSPHSSP built from PDB template 1M17 based on UniProtKB Q9H2C9.
SMRQ01279. Positions 25-525, 26-636, 698-1008.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5763N.

PTM databases

PhosphoSiteQ01279.

Proteomic databases

PRIDEQ01279.

Genome annotation databases

EnsemblENSMUSG00000020122. Mus musculus. [Contig view]
GeneID13649.

Organism-specific databases

MGIMGI:95294. Egfr.

Phylogenomic databases

HOGENOMQ01279.
HOVERGENQ01279.
OMAQ01279. MRRRHIV.

Enzyme and pathway databases

BRENDA2.7.10.1. 244.

Gene expression databases

ArrayExpressQ01279.
BgeeQ01279.
CleanExMM_EGFR.
GermOnlineENSMUSG00000020122. Mus musculus.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like.
IPR006212. Furin_repeat.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR016245. Tyr_kinase_rcpt_EGF/ERB/XmrK.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[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.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio284374.
SOURCESearch...

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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: June 16, 2009
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents