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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses (PubMed:8404850). Known ligands include EGF, TGFA/TGF-alpha, AREG, 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 (By similarity). Plays a role in enhancing learning and memory performance (PubMed:20639532).By similarity3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei747ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei839Proton acceptorPROSITE-ProRule annotation1
Binding sitei857ATPPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei1018Important for interaction with PIK3C2BBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi720 – 728ATPPROSITE-ProRule annotation9
Nucleotide bindingi792 – 793ATPPROSITE-ProRule annotation2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 3474

Reactome - a knowledgebase of biological pathways and processes

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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
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Epidermal growth factor receptor (EC:2.7.10.1)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Egfr
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:95294 Egfr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini25 – 647ExtracellularSequence analysisAdd BLAST623
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei648 – 670HelicalSequence analysisAdd BLAST23
Topological domaini671 – 1210CytoplasmicSequence analysisAdd BLAST540

Keywords - Cellular componenti

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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>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

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3608

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24By similarityAdd BLAST24
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001666625 – 1210Epidermal growth factor receptorAdd BLAST1186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi31 ↔ 58By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi128N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi157 ↔ 187By similarity
Glycosylationi175N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi190 ↔ 199By similarity
Disulfide bondi194 ↔ 207By similarity
Glycosylationi196N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi215 ↔ 223By similarity
Disulfide bondi219 ↔ 231By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei229PhosphoserineBy similarity1
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
Disulfide bondi337 ↔ 362By similarity
Glycosylationi352N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi413N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi444N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi470 ↔ 499By similarity
Disulfide bondi506 ↔ 515By similarity
Disulfide bondi510 ↔ 523By similarity
Disulfide bondi526 ↔ 535By similarity
Glycosylationi528N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi539 ↔ 555By similarity
Disulfide bondi558 ↔ 571By similarity
Disulfide bondi562 ↔ 579By similarity
Glycosylationi568N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi582 ↔ 591By similarity
Disulfide bondi595 ↔ 617By similarity
Glycosylationi603N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi620 ↔ 628By similarity
Glycosylationi623N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi624 ↔ 636By similarity
Modified residuei680Phosphothreonine; by PKC and PKD/PRKD1By similarity1
Modified residuei695Phosphothreonine; by PKD/PRKD1By similarity1
Modified residuei697PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki718Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki931Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei993PhosphoserineBy similarity1
Modified residuei997PhosphoserineBy similarity1
Modified residuei1000Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1018Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1028PhosphoserineBy similarity1
Modified residuei1041PhosphoserineBy similarity1
Modified residuei1043PhosphothreonineBy similarity1
Modified residuei1044PhosphoserineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi1051S-palmitoyl cysteineBy similarity1
Modified residuei1069PhosphotyrosineBy similarity1
Modified residuei1070PhosphoserineBy similarity1
Modified residuei1071PhosphoserineBy similarity1
Modified residuei1092Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1110Phosphotyrosine; by autocatalysisBy similarity1
Lipidationi1146S-palmitoyl cysteineBy similarity1
Modified residuei1166PhosphoserineBy similarity1
Modified residuei1172Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1197PhosphotyrosineCombined sources1
Modified residuei1199Omega-N-methylarginine; alternateBy similarity1
Modified residuei1199Omega-N-methylated arginine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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 on Tyr residues in response to EGF. Phosphorylation at 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-1199 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
Palmitoylated on Cys residues by ZDHHC20. Palmitoylation inhibits internalization after ligand binding, and increases the persistence of tyrosine-phosphorylated EGFR at the cell membrane. Palmitoylation increases the amplitude and duration of EGFR signaling.By similarity
Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q01279

PeptideAtlas

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PeptideAtlasi
Q01279

PRoteomics IDEntifications database

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PRIDEi
Q01279

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01279

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q01279

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q01279

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000020122 Expressed in 334 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

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CleanExi
MM_EGFR

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q01279 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q01279 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 autophosphorylation in absence of stimulation by EGF (By similarity). Interacts with LAPTM4B; positively correlates with EGFR activation (By similarity). Interacts with STX19 (PubMed:16420529).By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
199402, 26 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q01279

Database of interacting proteins

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DIPi
DIP-5763N

Protein interaction database and analysis system

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IntActi
Q01279, 14 interactors

Molecular INTeraction database

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MINTi
Q01279

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000020329

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q01279

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q01279

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q01279

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati75 – 300ApproximateAdd BLAST226
Repeati390 – 600ApproximateAdd BLAST211
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini714 – 981Protein kinasePROSITE-ProRule annotationAdd BLAST268

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni690 – 706Important for dimerization, phosphorylation and activationBy similarityAdd BLAST17

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1025 Eukaryota
ENOG410XNSR LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155450

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230982

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000490

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q01279

KEGG Orthology (KO)

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KOi
K04361

Identification of Orthologs from Complete Genome Data

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OMAi
GYYWEYV

Database of Orthologous Groups

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OrthoDBi
EOG091G00NO

Database for complete collections of gene phylogenies

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PhylomeDBi
Q01279

TreeFam database of animal gene trees

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TreeFami
TF106002

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00064 FU, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016245 Tyr_kinase_EGF/ERB/XmrK_rcpt

Pfam protein domain database

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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

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000619 TyrPK_EGF-R, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00261 FU, 4 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i690E20D46DF2D2F5
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q9WVF5Q9WVF5_MOUSE
Epidermal growth factor receptor
Egfr mCG_140518
655Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
Q5SVE7Q5SVE7_MOUSE
Epidermal growth factor receptor
Egfr
136Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti539C → W in CAA42219 (PubMed:2030916).Curated1
Sequence conflicti991L → F in AAA17899 (PubMed:8125255).Curated1
Sequence conflicti1116 – 1117HP → DR in CAA78249 (Ref. 6) Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS24443.1

Protein sequence database of the Protein Information Resource

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PIRi
A53183

NCBI Reference Sequences

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RefSeqi
NP_997538.1, NM_207655.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.420648
Mm.439882
Mm.8534

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122

Database of genes from NCBI RefSeq genomes

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GeneIDi
13649

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:13649

UCSC genome browser

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UCSCi
uc007ibo.1 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199402, 26 interactors
CORUMiQ01279
DIPiDIP-5763N
IntActiQ01279, 14 interactors
MINTiQ01279
STRINGi10090.ENSMUSP00000020329

Chemistry databases

BindingDBiQ01279
ChEMBLiCHEMBL3608

PTM databases

iPTMnetiQ01279
PhosphoSitePlusiQ01279
SwissPalmiQ01279

Proteomic databases

PaxDbiQ01279
PeptideAtlasiQ01279
PRIDEiQ01279

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122
GeneIDi13649
KEGGimmu:13649
UCSCiuc007ibo.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1956
MGIiMGI:95294 Egfr

Phylogenomic databases

eggNOGiKOG1025 Eukaryota
ENOG410XNSR LUCA
GeneTreeiENSGT00940000155450
HOGENOMiHOG000230982
HOVERGENiHBG000490
InParanoidiQ01279
KOiK04361
OMAiGYYWEYV
OrthoDBiEOG091G00NO
PhylomeDBiQ01279
TreeFamiTF106002

Enzyme and pathway databases

BRENDAi2.7.10.1 3474
ReactomeiR-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
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
Egfr mouse

Protein Ontology

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PROi
PR:Q01279

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000020122 Expressed in 334 organ(s), highest expression level in liver
CleanExiMM_EGFR
ExpressionAtlasiQ01279 baseline and differential
GenevisibleiQ01279 MM

Family and domain databases

CDDicd00064 FU, 3 hits
Gene3Di3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR032778 GF_recep_IV
IPR009030 Growth_fac_rcpt_cys_sf
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR016245 Tyr_kinase_EGF/ERB/XmrK_rcpt
PfamiView 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
PIRSFiPIRSF000619 TyrPK_EGF-R, 1 hit
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00261 FU, 4 hits
SM00219 TyrKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 2 hits
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiEGFR_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q01279
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 211 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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