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Protein

Epidermal growth factor receptor

Gene

Egfr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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

Enzyme regulationi

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei747 – 7471ATPPROSITE-ProRule annotation
Active sitei839 – 8391Proton acceptorPROSITE-ProRule annotation
Binding sitei857 – 8571ATPPROSITE-ProRule annotation
Sitei1018 – 10181Important for interaction with PIK3C2BBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi720 – 7289ATPPROSITE-ProRule annotation
Nucleotide bindingi792 – 7932ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cell morphogenesis Source: MGI
  • cell proliferation Source: MGI
  • cell surface receptor signaling pathway Source: MGI
  • cellular response to amino acid stimulus Source: UniProtKB
  • cellular response to epidermal growth factor stimulus Source: Ensembl
  • cellular response to estradiol stimulus Source: UniProtKB
  • cerebral cortex cell migration Source: MGI
  • digestive tract morphogenesis Source: MGI
  • embryonic placenta development Source: MGI
  • epidermal growth factor receptor signaling pathway Source: MGI
  • epidermis development Source: MGI
  • hair follicle development Source: MGI
  • learning or memory Source: Ensembl
  • morphogenesis of an epithelial fold Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of protein catabolic process Source: MGI
  • peptidyl-tyrosine phosphorylation Source: MGI
  • positive regulation of catenin import into nucleus Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of cell proliferation Source: MGI
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: MGI
  • positive regulation of DNA repair Source: MGI
  • positive regulation of DNA replication Source: MGI
  • positive regulation of epithelial cell proliferation Source: MGI
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of fibroblast proliferation Source: BHF-UCL
  • positive regulation of MAP kinase activity Source: MGI
  • positive regulation of nitric oxide biosynthetic process Source: MGI
  • positive regulation of phosphorylation Source: MGI
  • positive regulation of protein kinase B signaling Source: MGI
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein autophosphorylation Source: MGI
  • regulation of cell proliferation Source: MGI
  • regulation of nitric-oxide synthase activity Source: MGI
  • regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • response to UV-A Source: MGI
  • salivary gland morphogenesis Source: MGI
  • signal transduction Source: MGI
  • single organismal cell-cell adhesion Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_284350. Signaling by EGFR.
REACT_285497. GRB2 events in EGFR signaling.
REACT_286571. SHC1 events in EGFR signaling.
REACT_306499. GAB1 signalosome.
REACT_309124. EGFR interacts with phospholipase C-gamma.
REACT_321592. SHC1 events in ERBB2 signaling.
REACT_325060. EGFR Transactivation by Gastrin.
REACT_327089. GRB2 events in ERBB2 signaling.
REACT_333474. PIP3 activates AKT signaling.
REACT_336938. PLCG1 events in ERBB2 signaling.
REACT_346893. PI3K events in ERBB2 signaling.
REACT_348099. Signaling by ERBB2.
REACT_348853. Signaling by ERBB4.
REACT_350802. EGFR downregulation.
REACT_353319. Signal transduction by L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor (EC:2.7.10.1)
Gene namesi
Name:Egfr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95294. Egfr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 647623ExtracellularSequence AnalysisAdd
BLAST
Transmembranei648 – 67023HelicalSequence AnalysisAdd
BLAST
Topological domaini671 – 1210540CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: MGI
  • cell surface Source: MGI
  • cytoplasm Source: MGI
  • early endosome membrane Source: MGI
  • endocytic vesicle Source: MGI
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • endosome Source: UniProtKB
  • endosome membrane Source: MGI
  • focal adhesion Source: MGI
  • Golgi membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: MGI
  • membrane Source: MGI
  • membrane raft Source: MGI
  • multivesicular body, internal vesicle lumen Source: MGI
  • nuclear membrane Source: UniProtKB-SubCell
  • nucleus Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
  • plasma membrane Source: MGI
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 12101186Epidermal growth factor receptorPRO_0000016666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi175 – 1751N-linked (GlcNAc...)1 Publication
Disulfide bondi190 ↔ 199By similarity
Disulfide bondi194 ↔ 207By similarity
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi215 ↔ 223By similarity
Disulfide bondi219 ↔ 231By similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Disulfide bondi232 ↔ 240By similarity
Disulfide bondi236 ↔ 248By similarity
Disulfide bondi251 ↔ 260By similarity
Disulfide bondi264 ↔ 291By similarity
Disulfide bondi295 ↔ 307By similarity
Disulfide bondi311 ↔ 326By similarity
Disulfide bondi329 ↔ 333By similarity
Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi444 – 4441N-linked (GlcNAc...)1 Publication
Disulfide bondi506 ↔ 515By similarity
Disulfide bondi510 ↔ 523By similarity
Disulfide bondi526 ↔ 535By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi539 ↔ 555By similarity
Disulfide bondi558 ↔ 571By similarity
Disulfide bondi562 ↔ 579By similarity
Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi582 ↔ 591By similarity
Disulfide bondi595 ↔ 617By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi620 ↔ 628By similarity
Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi624 ↔ 636By similarity
Modified residuei680 – 6801Phosphothreonine; by PKC and PKD/PRKD1By similarity
Modified residuei695 – 6951Phosphothreonine; by PKD/PRKD1By similarity
Modified residuei697 – 6971PhosphoserineBy similarity
Cross-linki718 – 718Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki739 – 739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki756 – 756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki869 – 869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki931 – 931Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki972 – 972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei993 – 9931PhosphoserineBy similarity
Modified residuei997 – 9971PhosphoserineBy similarity
Modified residuei1000 – 10001Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1018 – 10181Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1028 – 10281PhosphoserineBy similarity
Modified residuei1041 – 10411PhosphoserineBy similarity
Modified residuei1043 – 10431PhosphothreonineBy similarity
Modified residuei1044 – 10441PhosphoserineBy similarity
Modified residuei1070 – 10701PhosphoserineBy similarity
Modified residuei1071 – 10711PhosphoserineBy similarity
Modified residuei1092 – 10921Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1110 – 11101Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1166 – 11661PhosphoserineBy similarity
Modified residuei1172 – 11721Phosphotyrosine; by autocatalysisBy similarity
Modified residuei1197 – 11971Phosphotyrosine; alternate1 Publication
Modified residuei1197 – 11971Phosphotyrosine; by autocatalysis; alternateBy similarity
Modified residuei1199 – 11991Omega-N-methylarginine; alternateBy similarity
Modified residuei1199 – 11991Omega-N-methylated arginine; alternateBy similarity

Post-translational modificationi

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 occurs. Deubiquitinated by OTUD7B, preventing degradation (By similarity). Ubiquitinated by RNF115 and RNF126.By similarity1 Publication
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).By similarity
Methylated. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ01279.
PaxDbiQ01279.
PRIDEiQ01279.

PTM databases

PhosphoSiteiQ01279.

Expressioni

Gene expression databases

BgeeiQ01279.
CleanExiMM_EGFR.
ExpressionAtlasiQ01279. baseline and differential.
GenevisibleiQ01279. MM.

Interactioni

Subunit structurei

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. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Interacts with RNF115 and RNF126.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CblP226822EBI-6296235,EBI-640919
EGFP011333EBI-6296235,EBI-640857From a different organism.
KrasP328833EBI-6296235,EBI-644267

Protein-protein interaction databases

BioGridi199402. 20 interactions.
DIPiDIP-5763N.
IntActiQ01279. 9 interactions.
MINTiMINT-143143.
STRINGi10090.ENSMUSP00000020329.

Structurei

3D structure databases

ProteinModelPortaliQ01279.
SMRiQ01279. Positions 26-636, 644-1020.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati75 – 300226ApproximateAdd
BLAST
Repeati390 – 600211ApproximateAdd
BLAST
Domaini714 – 981268Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni690 – 70617Important for dimerization, phosphorylation and activationBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiQ01279.
OMAiFYRTLME.
PhylomeDBiQ01279.
TreeFamiTF106002.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q01279-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS
60 70 80 90 100
LQRMYNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP
110 120 130 140 150
LENLQIIRGN ALYENTYALA ILSNYGTNRT GLRELPMRNL QEILIGAVRF
160 170 180 190 200
SNNPILCNMD TIQWRDIVQN VFMSNMSMDL QSHPSSCPKC DPSCPNGSCW
210 220 230 240 250
GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC TGPRESDCLV
260 270 280 290 300
CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
310 320 330 340 350
VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS
360 370 380 390 400
INATNIKHFK YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE
410 420 430 440 450
ITGFLLIQAW PDNWTDLHAF ENLEIIRGRT KQHGQFSLAV VGLNITSLGL
460 470 480 490 500
RSLKEISDGD VIISGNRNLC YANTINWKKL FGTPNQKTKI MNNRAEKDCK
510 520 530 540 550
AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN ILEGEPREFV
560 570 580 590 600
ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM
610 620 630 640 650
GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT
660 670 680 690 700
GIVGGLLFIV VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA
710 720 730 740 750
PNQAHLRILK ETEFKKIKVL GSGAFGTVYK GLWIPEGEKV KIPVAIKELR
760 770 780 790 800
EATSPKANKE ILDEAYVMAS VDNPHVCRLL GICLTSTVQL ITQLMPYGCL
810 820 830 840 850
LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL AARNVLVKTP
860 870 880 890 900
QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW
910 920 930 940 950
SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV
960 970 980 990 1000
KCWMIDADSR PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY
1010 1020 1030 1040 1050
RALMDEEDME DVVDADEYLI PQQGFFNSPS TSRTPLLSSL SATSNNSTVA
1060 1070 1080 1090 1100
CINRNGSCRV KEDAFLQRYS SDPTGAVTED NIDDAFLPVP EYVNQSVPKR
1110 1120 1130 1140 1150
PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN TAQPTCLSSG
1160 1170 1180 1190 1200
FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV
1210
APPSSEFIGA
Length:1,210
Mass (Da):134,853
Last modified:February 1, 1996 - v1
Checksum:i690E20D46DF2D2F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti539 – 5391C → W in CAA42219 (PubMed:2030916).Curated
Sequence conflicti991 – 9911L → F in AAA17899 (PubMed:8125255).Curated
Sequence conflicti1116 – 11172HP → DR in CAA78249 (Ref. 6) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24443.1.
PIRiA53183.
RefSeqiNP_997538.1. NM_207655.2.
UniGeneiMm.420648.
Mm.439882.
Mm.8534.

Genome annotation databases

EnsembliENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
GeneIDi13649.
UCSCiuc007ibo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS24443.1.
PIRiA53183.
RefSeqiNP_997538.1. NM_207655.2.
UniGeneiMm.420648.
Mm.439882.
Mm.8534.

3D structure databases

ProteinModelPortaliQ01279.
SMRiQ01279. Positions 26-636, 644-1020.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199402. 20 interactions.
DIPiDIP-5763N.
IntActiQ01279. 9 interactions.
MINTiMINT-143143.
STRINGi10090.ENSMUSP00000020329.

Chemistry

BindingDBiQ01279.
ChEMBLiCHEMBL3608.

PTM databases

PhosphoSiteiQ01279.

Proteomic databases

MaxQBiQ01279.
PaxDbiQ01279.
PRIDEiQ01279.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
GeneIDi13649.
UCSCiuc007ibo.1. mouse.

Organism-specific databases

CTDi1956.
MGIiMGI:95294. Egfr.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118799.
HOGENOMiHOG000230982.
HOVERGENiHBG000490.
InParanoidiQ01279.
OMAiFYRTLME.
PhylomeDBiQ01279.
TreeFamiTF106002.

Enzyme and pathway databases

BRENDAi2.7.10.1. 3474.
ReactomeiREACT_284350. Signaling by EGFR.
REACT_285497. GRB2 events in EGFR signaling.
REACT_286571. SHC1 events in EGFR signaling.
REACT_306499. GAB1 signalosome.
REACT_309124. EGFR interacts with phospholipase C-gamma.
REACT_321592. SHC1 events in ERBB2 signaling.
REACT_325060. EGFR Transactivation by Gastrin.
REACT_327089. GRB2 events in ERBB2 signaling.
REACT_333474. PIP3 activates AKT signaling.
REACT_336938. PLCG1 events in ERBB2 signaling.
REACT_346893. PI3K events in ERBB2 signaling.
REACT_348099. Signaling by ERBB2.
REACT_348853. Signaling by ERBB4.
REACT_350802. EGFR downregulation.
REACT_353319. Signal transduction by L1.

Miscellaneous databases

ChiTaRSiEgfr. mouse.
NextBioi284374.
PROiQ01279.
SOURCEiSearch...

Gene expression databases

BgeeiQ01279.
CleanExiMM_EGFR.
ExpressionAtlasiQ01279. baseline and differential.
GenevisibleiQ01279. MM.

Family and domain databases

Gene3Di3.80.20.20. 2 hits.
InterProiIPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000494. Rcpt_L-dom.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
PfamiPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00261. FU. 4 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBQUITINATION BY RNF115 AND RNF126, INTERACTION WITH RNF115 AND RNF126.

Entry informationi

Entry nameiEGFR_MOUSE
AccessioniPrimary (citable) accession number: Q01279
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 22, 2015
This is version 175 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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