UniProtKB - Q01279 (EGFR_MOUSE)
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Protein
Epidermal growth factor receptor
Gene
Egfr
Organism
Mus musculus (Mouse)
Status
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. Plays a role in enhancing learning and memory performance (PubMed:20639532).3 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Binding sitei | 747 | ATPPROSITE-ProRule annotation | 1 | |
| Active sitei | 839 | Proton acceptorPROSITE-ProRule annotation | 1 | |
| Binding sitei | 857 | ATPPROSITE-ProRule annotation | 1 | |
| Sitei | 1018 | Important for interaction with PIK3C2BBy similarity | 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 720 – 728 | ATPPROSITE-ProRule annotation | 9 | |
| Nucleotide bindingi | 792 – 793 | ATPPROSITE-ProRule annotation | 2 |
GO - Molecular functioni
- actin filament binding Source: MGI
- ATP binding Source: UniProtKB-KW
- cadherin binding Source: MGI
- calmodulin binding Source: Ensembl
- chromatin binding Source: UniProtKB
- enzyme binding Source: MGI
- epidermal growth factor-activated receptor activity Source: MGI
- epidermal growth factor binding Source: MGI
- glycoprotein binding Source: Ensembl
- identical protein binding Source: MGI
- integrin binding Source: Ensembl
- kinase activity Source: MGI
- nitric-oxide synthase regulator activity Source: Ensembl
- protein heterodimerization activity Source: MGI
- protein kinase binding Source: Ensembl
- protein phosphatase binding Source: MGI
- protein tyrosine kinase activity Source: UniProtKB
- signal transducer, downstream of receptor, with protein tyrosine kinase activity Source: InterPro
- signal transducer activity Source: MGI
- transmembrane signaling receptor activity Source: MGI
- ubiquitin protein ligase binding Source: MGI
GO - Biological processi
- activation of MAPKK activity Source: Ensembl
- astrocyte activation Source: Ensembl
- 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 cadmium ion Source: MGI
- cellular response to dexamethasone stimulus Source: Ensembl
- cellular response to drug Source: Ensembl
- cellular response to epidermal growth factor stimulus Source: Ensembl
- cellular response to estradiol stimulus Source: UniProtKB
- cellular response to growth factor stimulus Source: MGI
- cellular response to mechanical stimulus Source: Ensembl
- cellular response to reactive oxygen species Source: MGI
- cerebral cortex cell migration Source: MGI
- circadian rhythm Source: Ensembl
- digestive tract morphogenesis Source: MGI
- diterpenoid metabolic process Source: Ensembl
- embryonic placenta development Source: MGI
- epidermal growth factor receptor signaling pathway Source: MGI
- epidermis development Source: MGI
- eyelid development in camera-type eye Source: MGI
- hair follicle development Source: MGI
- hydrogen peroxide metabolic process Source: Ensembl
- learning or memory Source: Ensembl
- liver regeneration Source: Ensembl
- lung development Source: Ensembl
- magnesium ion homeostasis Source: Ensembl
- midgut development Source: Ensembl
- morphogenesis of an epithelial fold Source: MGI
- negative regulation of apoptotic process Source: MGI
- negative regulation of cardiocyte differentiation Source: MGI
- negative regulation of mitotic cell cycle Source: Ensembl
- negative regulation of protein catabolic process Source: MGI
- neuron projection morphogenesis Source: Ensembl
- ovulation cycle Source: Ensembl
- peptidyl-tyrosine phosphorylation Source: MGI
- positive regulation of blood vessel diameter Source: Ensembl
- positive regulation of bone resorption Source: Ensembl
- positive regulation of catenin import into nucleus Source: MGI
- positive regulation of cell growth Source: UniProtKB
- 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 inflammatory response Source: Ensembl
- positive regulation of MAP kinase activity Source: MGI
- positive regulation of NIK/NF-kappaB signaling Source: MGI
- positive regulation of nitric oxide biosynthetic process Source: MGI
- positive regulation of phosphorylation Source: MGI
- positive regulation of production of miRNAs involved in gene silencing by miRNA Source: MGI
- positive regulation of prolactin secretion Source: Ensembl
- positive regulation of protein kinase B signaling Source: MGI
- positive regulation of protein kinase C activity Source: MGI
- positive regulation of protein localization to plasma membrane Source: MGI
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of smooth muscle cell proliferation Source: Ensembl
- positive regulation of superoxide anion generation Source: Ensembl
- positive regulation of synaptic transmission, glutamatergic Source: Ensembl
- positive regulation of transcription, DNA-templated Source: MGI
- positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
- positive regulation of vasoconstriction Source: Ensembl
- protein autophosphorylation Source: MGI
- receptor-mediated endocytosis Source: MGI
- regulation of cell proliferation Source: MGI
- regulation of ERK1 and ERK2 cascade Source: MGI
- regulation of JNK cascade Source: MGI
- regulation of nitric-oxide synthase activity Source: MGI
- regulation of peptidyl-tyrosine phosphorylation Source: MGI
- regulation of phosphatidylinositol 3-kinase signaling Source: MGI
- response to calcium ion Source: Ensembl
- response to cobalamin Source: Ensembl
- response to hydroxyisoflavone Source: Ensembl
- response to osmotic stress Source: Ensembl
- response to UV-A Source: MGI
- salivary gland morphogenesis Source: MGI
- signal transduction Source: MGI
- single organismal cell-cell adhesion Source: MGI
- tongue development Source: Ensembl
- translation Source: Ensembl
- wound healing Source: Ensembl
Keywordsi
| Molecular function | Developmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
| BRENDAi | 2.7.10.1. 3474. |
| Reactomei | R-MMU-1227986. Signaling by ERBB2. R-MMU-1236394. Signaling by ERBB4. R-MMU-1250196. SHC1 events in ERBB2 signaling. R-MMU-1257604. PIP3 activates AKT signaling. R-MMU-177929. Signaling by EGFR. R-MMU-179812. GRB2 events in EGFR signaling. R-MMU-180292. GAB1 signalosome. R-MMU-180336. SHC1 events in EGFR signaling. R-MMU-182971. EGFR downregulation. R-MMU-1963642. PI3K events in ERBB2 signaling. R-MMU-212718. EGFR interacts with phospholipase C-gamma. R-MMU-2179392. EGFR Transactivation by Gastrin. R-MMU-445144. Signal transduction by L1. R-MMU-5673001. RAF/MAP kinase cascade. R-MMU-6785631. ERBB2 Regulates Cell Motility. R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. R-MMU-8847993. ERBB2 Activates PTK6 Signaling. R-MMU-8856825. Cargo recognition for clathrin-mediated endocytosis. R-MMU-8856828. Clathrin-mediated endocytosis. R-MMU-8857538. PTK6 promotes HIF1A stabilization. R-MMU-8863795. Downregulation of ERBB2 signaling. |
Names & Taxonomyi
| Protein namesi | |
| Gene namesi | Name:Egfr |
| Organismi | Mus musculus (Mouse) |
| Taxonomic identifieri | 10090 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
| Proteomesi |
|
Organism-specific databases
| MGIi | MGI:95294. Egfr. |
Subcellular locationi
- Cell membrane; Single-pass type I membrane protein
- Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity
- Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity
- Nucleus membrane By similarity; 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).By similarity
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Topological domaini | 25 – 647 | ExtracellularSequence analysisAdd BLAST | 623 | |
| Transmembranei | 648 – 670 | HelicalSequence analysisAdd BLAST | 23 | |
| Topological domaini | 671 – 1210 | CytoplasmicSequence analysisAdd BLAST | 540 |
GO - Cellular componenti
- apical plasma membrane Source: Ensembl
- 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
- synapse Source: Ensembl
Keywords - Cellular componenti
Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane, NucleusPathology & 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
Chemistry databases
| ChEMBLi | CHEMBL3608. |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Signal peptidei | 1 – 24 | Sequence analysisAdd BLAST | 24 | |
| ChainiPRO_0000016666 | 25 – 1210 | Epidermal growth factor receptorAdd BLAST | 1186 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Glycosylationi | 128 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 175 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Disulfide bondi | 190 ↔ 199 | By similarity | ||
| Disulfide bondi | 194 ↔ 207 | By similarity | ||
| Glycosylationi | 196 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 215 ↔ 223 | By similarity | ||
| Disulfide bondi | 219 ↔ 231 | By similarity | ||
| Modified residuei | 229 | PhosphoserineBy similarity | 1 | |
| Disulfide bondi | 232 ↔ 240 | By similarity | ||
| Disulfide bondi | 236 ↔ 248 | By similarity | ||
| Disulfide bondi | 251 ↔ 260 | By similarity | ||
| Disulfide bondi | 264 ↔ 291 | By similarity | ||
| Disulfide bondi | 295 ↔ 307 | By similarity | ||
| Disulfide bondi | 311 ↔ 326 | By similarity | ||
| Disulfide bondi | 329 ↔ 333 | By similarity | ||
| Glycosylationi | 352 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Glycosylationi | 413 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Glycosylationi | 444 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
| Disulfide bondi | 506 ↔ 515 | By similarity | ||
| Disulfide bondi | 510 ↔ 523 | By similarity | ||
| Disulfide bondi | 526 ↔ 535 | By similarity | ||
| Glycosylationi | 528 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 539 ↔ 555 | By similarity | ||
| Disulfide bondi | 558 ↔ 571 | By similarity | ||
| Disulfide bondi | 562 ↔ 579 | By similarity | ||
| Glycosylationi | 568 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 582 ↔ 591 | By similarity | ||
| Disulfide bondi | 595 ↔ 617 | By similarity | ||
| Glycosylationi | 603 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 620 ↔ 628 | By similarity | ||
| Glycosylationi | 623 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 624 ↔ 636 | By similarity | ||
| Modified residuei | 680 | Phosphothreonine; by PKC and PKD/PRKD1By similarity | 1 | |
| Modified residuei | 695 | Phosphothreonine; by PKD/PRKD1By similarity | 1 | |
| Modified residuei | 697 | PhosphoserineBy similarity | 1 | |
| Cross-linki | 718 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
| Cross-linki | 739 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
| Cross-linki | 756 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
| Cross-linki | 869 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
| Cross-linki | 931 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
| Cross-linki | 972 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity | ||
| Modified residuei | 993 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 997 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1000 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 1018 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 1028 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1041 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1043 | PhosphothreonineBy similarity | 1 | |
| Modified residuei | 1044 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1070 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1071 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1092 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 1110 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 1166 | PhosphoserineBy similarity | 1 | |
| Modified residuei | 1172 | Phosphotyrosine; by autocatalysisBy similarity | 1 | |
| Modified residuei | 1197 | PhosphotyrosineCombined sources | 1 | |
| Modified residuei | 1199 | Omega-N-methylarginine; alternateBy similarity | 1 | |
| Modified residuei | 1199 | Omega-N-methylated arginine; alternateBy similarity | 1 |
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 conjugationProteomic databases
| PaxDbi | Q01279. |
| PeptideAtlasi | Q01279. |
| PRIDEi | Q01279. |
PTM databases
| iPTMneti | Q01279. |
| PhosphoSitePlusi | Q01279. |
| SwissPalmi | Q01279. |
Expressioni
Gene expression databases
| Bgeei | ENSMUSG00000020122. |
| CleanExi | MM_EGFR. |
| ExpressionAtlasi | Q01279. baseline and differential. |
| Genevisiblei | Q01279. 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 ELOC- and ELOB-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 GAREM1. 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. Interacts with GPRC5A (via its transmembrane domain) (PubMed:25744720). Interacts with FAM83B; positively regulates EGFR inducing its autophospharylation in absence of stimulation by EGF (By similarity).By similarity3 Publications
Binary interactionsi
GO - Molecular functioni
- actin filament binding Source: MGI
- cadherin binding Source: MGI
- calmodulin binding Source: Ensembl
- enzyme binding Source: MGI
- epidermal growth factor binding Source: MGI
- glycoprotein binding Source: Ensembl
- identical protein binding Source: MGI
- integrin binding Source: Ensembl
- protein heterodimerization activity Source: MGI
- protein kinase binding Source: Ensembl
- protein phosphatase binding Source: MGI
- ubiquitin protein ligase binding Source: MGI
Protein-protein interaction databases
| BioGridi | 199402. 22 interactors. |
| DIPi | DIP-5763N. |
| IntActi | Q01279. 9 interactors. |
| MINTi | MINT-143143. |
| STRINGi | 10090.ENSMUSP00000020329. |
Chemistry databases
| BindingDBi | Q01279. |
Structurei
3D structure databases
| ProteinModelPortali | Q01279. |
| SMRi | Q01279. |
| ModBasei | Search... |
| MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Repeati | 75 – 300 | ApproximateAdd BLAST | 226 | |
| Repeati | 390 – 600 | ApproximateAdd BLAST | 211 | |
| Domaini | 714 – 981 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 268 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Regioni | 690 – 706 | Important for dimerization, phosphorylation and activationBy similarityAdd BLAST | 17 |
Sequence similaritiesi
Belongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.PROSITE-ProRule annotation
Keywords - Domaini
Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
| eggNOGi | KOG1025. Eukaryota. ENOG410XNSR. LUCA. |
| GeneTreei | ENSGT00760000118799. |
| HOGENOMi | HOG000230982. |
| HOVERGENi | HBG000490. |
| InParanoidi | Q01279. |
| KOi | K04361. |
| OMAi | VCRKCHP. |
| OrthoDBi | EOG091G00NO. |
| PhylomeDBi | Q01279. |
| TreeFami | TF106002. |
Family and domain databases
| Gene3Di | 3.80.20.20. 4 hits. |
| InterProi | View protein in InterPro IPR006211. Furin-like_Cys-rich_dom. IPR006212. Furin_repeat. IPR032778. GF_recep_IV. IPR009030. Growth_fac_rcpt_. IPR011009. Kinase-like_dom. IPR032675. L_dom-like. 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. |
| Pfami | View protein in Pfam PF00757. Furin-like. 1 hit. PF14843. GF_recep_IV. 1 hit. PF07714. Pkinase_Tyr. 1 hit. PF01030. Recep_L_domain. 2 hits. |
| PIRSFi | PIRSF000619. TyrPK_EGF-R. 2 hits. |
| PRINTSi | PR00109. TYRKINASE. |
| SMARTi | View protein in SMART SM00261. FU. 4 hits. SM00219. TyrKc. 1 hit. |
| SUPFAMi | SSF52058. SSF52058. 2 hits. SSF56112. SSF56112. 1 hit. SSF57184. SSF57184. 2 hits. |
| PROSITEi | View protein in PROSITE PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00109. PROTEIN_KINASE_TYR. 1 hit. |
Sequencei
Sequence statusi: Complete.
Sequence processingi: The displayed sequence is further processed into a mature form.
Q01279-1 [UniParc]FASTAAdd to basket
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
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 539 | C → W in CAA42219 (PubMed:2030916).Curated | 1 | |
| Sequence conflicti | 991 | L → F in AAA17899 (PubMed:8125255).Curated | 1 | |
| Sequence conflicti | 1116 – 1117 | HP → DR in CAA78249 (Ref. 6) Curated | 2 |
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. |
| CCDSi | CCDS24443.1. |
| PIRi | A53183. |
| RefSeqi | NP_997538.1. NM_207655.2. |
| UniGenei | Mm.420648. Mm.439882. Mm.8534. |
Genome annotation databases
| Ensembli | ENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122. |
| GeneIDi | 13649. |
| KEGGi | mmu:13649. |
| UCSCi | uc007ibo.1. mouse. |
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 one 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. |
Entry informationi
| Entry namei | EGFR_MOUSE | |
| Accessioni | Q01279Primary (citable) accession number: Q01279 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1996 |
| Last sequence update: | February 1, 1996 | |
| Last modified: | July 5, 2017 | |
| This is version 197 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
Miscellaneousi
Keywords - Technical termi
Complete proteome, Reference proteomeDocuments
- 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
