Q01279 (EGFR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epidermal growth factor receptor
EC=2.7.10.1

Gene names

Name:

Egfr

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1210 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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; 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 By similarity. Interacts with EPS8; mediates EPS8 phosphorylation. Interacts with ATX2 By similarity. Interacts with GAREM By similarity. 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. Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand 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 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 component	Cell membrane Endoplasmic reticulum Endosome Golgi apparatus Membrane Nucleus
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell morphogenesis Inferred from genetic interaction PubMed 17686994. Source: MGI cell proliferation Inferred from electronic annotation. Source: Compara cell-cell adhesion Inferred from electronic annotation. Source: Compara cerebral cortex cell migration Inferred from mutant phenotype Ref.9. Source: MGI digestive tract morphogenesis Inferred from mutant phenotype Ref.9. Source: MGI embryonic placenta development Inferred from mutant phenotype Ref.9. Source: MGI hair follicle development Inferred from mutant phenotype Ref.9. Source: MGI morphogenesis of an epithelial fold Inferred from mutant phenotype Ref.9. Source: MGI negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of DNA repair Inferred from electronic annotation. Source: Compara positive regulation of DNA replication Inferred from electronic annotation. Source: Compara positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara positive regulation of catenin import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S Inferred from electronic annotation. Source: Compara 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 nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from direct assay PubMed 15314156. Source: MGI regulation of nitric-oxide synthase activity Inferred from electronic annotation. Source: Compara regulation of peptidyl-tyrosine phosphorylation Inferred from mutant phenotype PubMed 11940581. Source: MGI response to UV-A Inferred from electronic annotation. Source: Compara salivary gland morphogenesis Inferred from mutant phenotype PubMed 10521784. Source: MGI signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell basolateral plasma membrane Inferred from direct assay PubMed 7723235. Source: MGI 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from electronic annotation. Source: Compara 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
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW epidermal growth factor-activated receptor activity Inferred from direct assay PubMed 14712229. Source: MGI nitric-oxide synthase regulator activity Inferred from electronic annotation. Source: Compara receptor signaling protein tyrosine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kras	P32883	3	EBI-6296235,EBI-644267

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 1210	1186	Epidermal growth factor receptor		PRO_0000016666
Regions
	Topological domain	25 – 647	623	Extracellular Potential
	Transmembrane	648 – 670	23	Helical; Potential
	Topological domain	671 – 1210	540	Cytoplasmic Potential
	Repeat	75 – 300	226	Approximate
	Repeat	390 – 600	211	Approximate
	Domain	714 – 981	268	Protein kinase
	Nucleotide binding	720 – 728	9	ATP By similarity
	Nucleotide binding	792 – 793	2	ATP By similarity
	Region	690 – 706	17	Important for dimerization, phosphorylation and activation By similarity
	Compositional bias	1028 – 1071	44	Ser-rich
Sites
	Active site	839	1	Proton acceptor By similarity
	Binding site	747	1	ATP By similarity
	Binding site	857	1	ATP By similarity
	Site	1018	1	Important for interaction with PIK3C2B By similarity
Amino acid modifications
	Modified residue	229	1	Phosphoserine By similarity
	Modified residue	680	1	Phosphothreonine; by PKC and PKD/PRKD1 By similarity
	Modified residue	695	1	Phosphothreonine; by PKD/PRKD1 By similarity
	Modified residue	697	1	Phosphoserine By similarity
	Modified residue	993	1	Phosphoserine By similarity
	Modified residue	997	1	Phosphoserine By similarity
	Modified residue	1000	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1018	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1028	1	Phosphoserine By similarity
	Modified residue	1041	1	Phosphoserine By similarity
	Modified residue	1043	1	Phosphothreonine By similarity
	Modified residue	1044	1	Phosphoserine By similarity
	Modified residue	1070	1	Phosphoserine By similarity
	Modified residue	1071	1	Phosphoserine By similarity
	Modified residue	1092	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1110	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1166	1	Phosphoserine By similarity
	Modified residue	1172	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1197	1	Phosphotyrosine; by autocatalysis By similarity
	Modified residue	1199	1	Omega-N-methylated arginine By similarity
	Glycosylation	128	1	N-linked (GlcNAc...) Potential
	Glycosylation	175	1	N-linked (GlcNAc...) Ref.13
	Glycosylation	196	1	N-linked (GlcNAc...) Potential
	Glycosylation	352	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	413	1	N-linked (GlcNAc...) Potential
	Glycosylation	444	1	N-linked (GlcNAc...) Ref.12
	Glycosylation	528	1	N-linked (GlcNAc...) Potential
	Glycosylation	568	1	N-linked (GlcNAc...) Potential
	Glycosylation	603	1	N-linked (GlcNAc...) Potential
	Glycosylation	623	1	N-linked (GlcNAc...) Potential
	Disulfide bond	190 ↔ 199		By similarity
	Disulfide bond	194 ↔ 207		By similarity
	Disulfide bond	215 ↔ 223		By similarity
	Disulfide bond	219 ↔ 231		By similarity
	Disulfide bond	232 ↔ 240		By similarity
	Disulfide bond	236 ↔ 248		By similarity
	Disulfide bond	251 ↔ 260		By similarity
	Disulfide bond	264 ↔ 291		By similarity
	Disulfide bond	295 ↔ 307		By similarity
	Disulfide bond	311 ↔ 326		By similarity
	Disulfide bond	329 ↔ 333		By similarity
	Disulfide bond	506 ↔ 515		By similarity
	Disulfide bond	510 ↔ 523		By similarity
	Disulfide bond	526 ↔ 535		By similarity
	Disulfide bond	539 ↔ 555		By similarity
	Disulfide bond	558 ↔ 571		By similarity
	Disulfide bond	562 ↔ 579		By similarity
	Disulfide bond	582 ↔ 591		By similarity
	Disulfide bond	595 ↔ 617		By similarity
	Disulfide bond	620 ↔ 628		By similarity
	Disulfide bond	624 ↔ 636		By similarity
	Cross-link	718		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	739		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	756		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	869		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	931		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
	Cross-link	972		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Experimental info
	Sequence conflict	539	1	C → W in CAA42219. Ref.5
	Sequence conflict	991	1	L → F in AAA17899. Ref.4
	Sequence conflict	1116 – 1117	2	HP → DR in CAA78249. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q01279 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 690E20D46DF2D2F5	FASTA	1,210	134,853
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Plasma.
+	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.
IPI	IPI00121190.
PIR	A53183.
RefSeq	NP_997538.1. NM_207655.2.
UniGene	Mm.420648. Mm.439882. Mm.8534.
3D structure databases
ProteinModelPortal	Q01279.
SMR	Q01279. Positions 26-1005.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5763N.
IntAct	Q01279. 1 interaction.
MINT	MINT-143143.
PTM databases
PhosphoSite	Q01279.
Proteomic databases
PaxDb	Q01279.
PRIDE	Q01279.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
GeneID	13649.
KEGG	mmu:13649.
Organism-specific databases
CTD	1956.
MGI	MGI:95294. Egfr.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00600000084253.
HOGENOM	HOG000230982.
HOVERGEN	HBG000490.
InParanoid	Q01279.
KO	K04361.
OMA	MRRRHIV.
OrthoDB	EOG44MXR6.
Enzyme and pathway databases
BRENDA	2.7.10.1. 3474.
Gene expression databases
ArrayExpress	Q01279.
Bgee	Q01279.
CleanEx	MM_EGFR.
Genevestigator	Q01279.
GermOnline	ENSMUSG00000020122. Mus musculus.
Family and domain databases
InterPro	IPR000494. EGF_rcpt_L. IPR006211. Furin-like_Cys-rich_dom. IPR006212. Furin_repeat. IPR009030. Growth_fac_rcpt. IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_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]
Pfam	PF00757. Furin-like. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF01030. Recep_L_domain. 2 hits. [Graphical view]
PIRSF	PIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTS	PR00109. TYRKINASE.
SMART	SM00261. FU. 4 hits. SM00219. TyrKc. 1 hit. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 2 hits. SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q01279.
ChEMBL	CHEMBL3608.
ChiTaRS	EGFR. mouse.
NextBio	284374.
SOURCE	Search...

Entry information

Entry name

EGFR_MOUSE

Accession

Primary (citable) accession number: Q01279

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program