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P00533 (EGFR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 179. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor

EC=2.7.10.1
Alternative name(s):
Proto-oncogene c-ErbB-1
Receptor tyrosine-protein kinase erbB-1
Gene names
Name:EGFR
Synonyms:ERBB, ERBB1, HER1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Ref.29 Ref.35 Ref.36 Ref.39 Ref.40 Ref.41 Ref.49 Ref.66 Ref.68 Ref.69 Ref.70 Ref.77 Ref.79

Isoform 2 may act as an antagonist of EGF action. Ref.29 Ref.35 Ref.36 Ref.39 Ref.40 Ref.41 Ref.49 Ref.66 Ref.68 Ref.69 Ref.70 Ref.77 Ref.79

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.70 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77

Enzyme regulation

Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling. Ref.37 Ref.42 Ref.60 Ref.74

Subunit structure

Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through TCEB1- and TCEB2-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG; 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. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Ref.29 Ref.32 Ref.33 Ref.36 Ref.37 Ref.39 Ref.40 Ref.41 Ref.42 Ref.47 Ref.49 Ref.52 Ref.55 Ref.60 Ref.64 Ref.66 Ref.67 Ref.68 Ref.69 Ref.74 Ref.76 Ref.77 Ref.78 Ref.79

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome. Endosome membrane. Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Ref.49 Ref.52 Ref.60 Ref.64 Ref.68 Ref.77

Isoform 2: Secreted Ref.49 Ref.52 Ref.60 Ref.64 Ref.68 Ref.77.

Tissue specificity

Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers. Ref.51

Post-translational modification

Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 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.

Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occur.

Methylated. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197. Ref.66

Involvement in disease

Defects in EGFR are associated with lung cancer (LNCR) [MIM:211980]. LNCR is a common malignancy affecting tissues of the lung. The most common form of lung cancer is non-small cell lung cancer (NSCLC) that can be divided into 3 major histologic subtypes: squamous cell carcinoma, adenocarcinoma, and large cell lung cancer. NSCLC is often diagnosed at an advanced stage and has a poor prognosis.

Sequence similarities

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

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Golgi apparatus
Membrane
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Kinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processactivation of phospholipase A2 activity by calcium-mediated signaling

Traceable author statement. Source: UniProtKB

activation of phospholipase C activity

Traceable author statement. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

cell proliferation

Inferred from direct assay Ref.49. Source: UniProtKB

cell-cell adhesion

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of protein catabolic process

Inferred from direct assay Ref.49. Source: UniProtKB

ossification

Non-traceable author statement. Source: UniProtKB

positive regulation of DNA repair

Inferred from direct assay Ref.49. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay Ref.49. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay. Source: UniProtKB

positive regulation of catenin import into nucleus

Inferred from mutant phenotype. Source: BHF-UCL

positive regulation of cell migration

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of cyclin-dependent protein kinase activity involved in G1/S

Inferred from direct assay. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from direct assay. Source: UniProtKB

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay. Source: UniProtKB

positive regulation of phosphorylation

Inferred from direct assay. Source: UniProtKB

positive regulation of protein kinase B signaling cascade

Inferred from mutant phenotype. Source: BHF-UCL

protein autophosphorylation

Inferred from mutant phenotype. Source: UniProtKB

protein insertion into membrane

Traceable author statement. Source: UniProtKB

regulation of nitric-oxide synthase activity

Inferred from direct assay. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype. Source: UniProtKB

response to UV-A

Inferred from direct assay. Source: BHF-UCL

response to stress

Non-traceable author statement. Source: UniProtKB

   Cellular componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Shc-EGFR complex

Inferred from sequence or structural similarity. Source: BHF-UCL

basolateral plasma membrane

Inferred from direct assay. Source: BHF-UCL

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay Ref.52. Source: UniProtKB

extracellular space

Non-traceable author statement Ref.4. Source: UniProtKB

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane raft

Inferred from direct assay. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP/ERK kinase kinase activity

Non-traceable author statement. Source: UniProtKB

actin filament binding

Inferred from direct assay. Source: UniProtKB

double-stranded DNA binding

Non-traceable author statement Ref.22. Source: UniProtKB

epidermal growth factor-activated receptor activity

Inferred from direct assay Ref.49. Source: UniProtKB

identical protein binding

Inferred from physical interaction. Source: IntAct

protein heterodimerization activity

Inferred from direct assay. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P00533-1)

Also known as: p170;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P00533-2)

Also known as: p60; Truncated; TEGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     404-405: FL → LS
     406-1210: Missing.
Isoform 3 (identifier: P00533-3)

Also known as: p110;

The sequence of this isoform differs from the canonical sequence as follows:
     628-705: CTGPGLEGCP...GEAPNQALLR → PGNESLKAML...SVIITASSCH
     706-1210: Missing.
Isoform 4 (identifier: P00533-4)

The sequence of this isoform differs from the canonical sequence as follows:
     628-628: C → S
     629-1210: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.18
Chain25 – 12101186Epidermal growth factor receptor
PRO_0000016665

Regions

Topological domain25 – 645621Extracellular Potential
Transmembrane646 – 66823Helical; Potential
Topological domain669 – 1210542Cytoplasmic Potential
Repeat75 – 300226Approximate
Repeat390 – 600211Approximate
Domain712 – 979268Protein kinase
Nucleotide binding718 – 7269ATP
Nucleotide binding790 – 7912ATP
Region688 – 70417Important for dimerization, phosphorylation and activation
Compositional bias1025 – 107147Ser-rich

Sites

Active site8371Proton acceptor By similarity
Binding site7451ATP
Binding site8551ATP
Site10161Important for interaction with PIK3C2B

Amino acid modifications

Modified residue6781Phosphothreonine; by PKC and PKD/PRKD1
Modified residue6931Phosphothreonine; by PKD/PRKD1
Modified residue6951Phosphoserine Ref.17 Ref.57 Ref.58
Modified residue7251Phosphothreonine Ref.57
Modified residue8691Phosphotyrosine Ref.50
Modified residue9781Phosphotyrosine Ref.46
Modified residue9911Phosphoserine Ref.44 Ref.48 Ref.54 Ref.56 Ref.57 Ref.58
Modified residue9931Phosphothreonine Ref.58
Modified residue9951Phosphoserine Ref.48 Ref.58
Modified residue9981Phosphotyrosine; by autocatalysis Ref.45 Ref.48 Ref.54 Ref.58 Ref.62 Ref.76
Modified residue10161Phosphotyrosine; by autocatalysis Ref.62 Ref.76
Modified residue10251Phosphoserine Ref.57
Modified residue10261Phosphoserine Ref.44 Ref.57
Modified residue10371Phosphoserine Ref.57
Modified residue10391Phosphoserine Ref.57 Ref.58
Modified residue10411Phosphothreonine Ref.58
Modified residue10421Phosphoserine Ref.57 Ref.58
Modified residue10451Phosphoserine Ref.58
Modified residue10641Phosphoserine Ref.48 Ref.57 Ref.58
Modified residue10691Phosphotyrosine Ref.45 Ref.48 Ref.54
Modified residue10701Phosphoserine Ref.17
Modified residue10711Phosphoserine Ref.17
Modified residue10811Phosphoserine Ref.57
Modified residue10921Phosphotyrosine; by autocatalysis Ref.36 Ref.45 Ref.48 Ref.50 Ref.62
Modified residue11101Phosphotyrosine; by autocatalysis Ref.25 Ref.36 Ref.48 Ref.62
Modified residue11381Phosphotyrosine Ref.48 Ref.62
Modified residue11661Phosphoserine Ref.45 Ref.54 Ref.57 Ref.58
Modified residue11721Phosphotyrosine; by autocatalysis Ref.45 Ref.48 Ref.50 Ref.54 Ref.62
Modified residue11971Phosphotyrosine; by autocatalysis Ref.48 Ref.50 Ref.54 Ref.57 Ref.62 Ref.76
Modified residue11991Omega-N-methylated arginine Ref.66
Glycosylation561N-linked (GlcNAc...) (complex); atypical; partial Ref.34 Ref.44 Ref.68 Ref.79
CAR_000227
Glycosylation731N-linked (GlcNAc...) Ref.79
Glycosylation1281N-linked (GlcNAc...) Ref.30 Ref.44
Glycosylation1751N-linked (GlcNAc...) Ref.30 Ref.44 Ref.68 Ref.79
Glycosylation1961N-linked (GlcNAc...) Ref.44 Ref.68 Ref.79
Glycosylation3521N-linked (GlcNAc...) Ref.34 Ref.44 Ref.61 Ref.68 Ref.69 Ref.79
Glycosylation3611N-linked (GlcNAc...) Ref.34 Ref.44 Ref.68 Ref.69 Ref.79
Glycosylation4131N-linked (GlcNAc...) Ref.30 Ref.44 Ref.61
Glycosylation4441N-linked (GlcNAc...) Ref.30 Ref.44 Ref.68 Ref.69 Ref.79
Glycosylation5281N-linked (GlcNAc...) Ref.30 Ref.44 Ref.69 Ref.79
Glycosylation5681N-linked (GlcNAc...); partial Ref.34 Ref.44 Ref.61 Ref.69
Glycosylation6031N-linked (GlcNAc...); partial Ref.34 Ref.44 Ref.69
Disulfide bond31 ↔ 58 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond157 ↔ 187 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond190 ↔ 199 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond194 ↔ 207 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond215 ↔ 223 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond219 ↔ 231 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond232 ↔ 240 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond236 ↔ 248 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond251 ↔ 260 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond264 ↔ 291 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond295 ↔ 307 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond311 ↔ 326 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond329 ↔ 333 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond337 ↔ 362 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond470 ↔ 499 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond506 ↔ 515 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond510 ↔ 523 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond526 ↔ 535 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond539 ↔ 555 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond558 ↔ 571 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond562 ↔ 579 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond582 ↔ 591 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond595 ↔ 617 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond620 ↔ 628 Ref.21 Ref.68 Ref.69 Ref.79
Disulfide bond624 ↔ 636 Ref.21 Ref.68 Ref.69 Ref.79
Cross-link716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20
Cross-link970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.20

Natural variations

Alternative sequence404 – 4052FL → LS in isoform 2.
VSP_002887
Alternative sequence406 – 1210805Missing in isoform 2.
VSP_002888
Alternative sequence628 – 70578CTGPG…QALLR → PGNESLKAMLFCLFKLSSCN QSNDGSVSHQSGSPAAQESC LGWIPSLLPSEFQLGWGGCS HLHAWPSASVIITASSCH in isoform 3.
VSP_002889
Alternative sequence6281C → S in isoform 4.
VSP_002891
Alternative sequence629 – 1210582Missing in isoform 4.
VSP_002892
Alternative sequence706 – 1210505Missing in isoform 3.
VSP_002890
Natural variant30 – 297268Missing Variant EGFR vIII; found in a lung cancer sample; somatic mutation; induces lung cancer when exogenously expressed.
VAR_066493
Natural variant981R → Q. Ref.7
Corresponds to variant rs17289589 [ dbSNP | Ensembl ].
VAR_019293
Natural variant2661P → R. Ref.7
Corresponds to variant rs17336639 [ dbSNP | Ensembl ].
VAR_019294
Natural variant5211R → K. Ref.7 Ref.83
Corresponds to variant rs2227983 [ dbSNP | Ensembl ].
VAR_019295
Natural variant6741V → I Slightly increased autophosphorylation. Ref.7
Corresponds to variant rs17337079 [ dbSNP | Ensembl ].
VAR_019296
Natural variant7091E → A Found in a lung cancer sample. Ref.81
VAR_026084
Natural variant7091E → K Found in a lung cancer sample. Ref.81
VAR_026085
Natural variant7191G → A Found in a lung cancer sample. Ref.81
VAR_026086
Natural variant7191G → C Found in a lung cancer sample. Ref.81
Corresponds to variant rs28929495 [ dbSNP | Ensembl ].
VAR_026087
Natural variant7191G → D Found in a lung cancer sample. Ref.81
VAR_026088
Natural variant7191G → S Found in a lung cancer sample; somatic mutation; strongly increased kinase activity. Ref.73 Ref.80 Ref.81
VAR_019297
Natural variant7241G → S Found in a lung cancer sample. Ref.81
VAR_026089
Natural variant7341E → K Found in a lung cancer sample. Ref.81
VAR_026090
Natural variant746 – 7505Missing Found in a lung cancer sample.
VAR_026092
Natural variant7461Missing Found in a lung cancer sample.
VAR_026091
Natural variant747 – 7493Missing Found in a lung cancer sample.
VAR_026094
Natural variant7471L → F Found in a lung cancer sample. Ref.81
VAR_026093
Natural variant7481R → P Found in a lung cancer sample. Ref.81
VAR_026095
Natural variant752 – 7598Missing Found in a lung cancer sample.
VAR_026096
Natural variant7871Q → R Found in a lung cancer sample. Ref.81
VAR_026097
Natural variant7901T → M Found in a lung cancer sample; increased kinase activity. Ref.75 Ref.81
VAR_026098
Natural variant8331L → V Found in a lung cancer sample. Ref.81
VAR_026099
Natural variant8341V → L Found in a lung cancer sample. Ref.81
VAR_026100
Natural variant8581L → M Found in a lung cancer sample. Ref.81
VAR_026101
Natural variant8581L → R Found in a lung cancer sample; somatic mutation; constitutively activated enzyme with strongly increased kinase activity. Ref.73 Ref.80 Ref.81
VAR_019298
Natural variant8611L → Q Found in a lung cancer sample. Ref.81
VAR_026102
Natural variant8731G → E Found in a lung cancer sample. Ref.81
VAR_026103
Natural variant9621R → G. Ref.7
Corresponds to variant rs17337451 [ dbSNP | Ensembl ].
VAR_019299
Natural variant9881H → P. Ref.7
Corresponds to variant rs17290699 [ dbSNP | Ensembl ].
VAR_019300
Natural variant10341L → R. Ref.83
Corresponds to variant rs34352568 [ dbSNP | Ensembl ].
VAR_042095
Natural variant12101A → V. Ref.83
Corresponds to variant rs35918369 [ dbSNP | Ensembl ].
VAR_042096

Experimental info

Mutagenesis2751Y → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. Ref.68
Mutagenesis2871F → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. Ref.68
Mutagenesis3091R → S: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-275. Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-287. Ref.68
Mutagenesis4291R → E: Abolishes autophosphorylation and activation of downstream kinases. Ref.68
Mutagenesis587 – 5904DGPH → AGPA: Decreases intramolecular interactions and facilitates EGF binding. Ref.69
Mutagenesis6091K → A: Decreases intramolecular interactions and facilitates EGF binding. Ref.69
Mutagenesis6881L → A: Strongly reduced phosphorylation. Ref.76 Ref.77
Mutagenesis6891V → A: Reduced autophosphorylation. Ref.77
Mutagenesis6891V → M: Constitutively activated kinase. Ref.77
Mutagenesis6901E → A: Reduced phosphorylation. Ref.76 Ref.77
Mutagenesis6921L → A or P: Strongly reduced phosphorylation. Ref.76 Ref.77
Mutagenesis6931T → A: Increased phosphorylation. Ref.77
Mutagenesis6931T → D: Strongly reduced phosphorylation. Ref.77
Mutagenesis6941P → A: Strongly reduced phosphorylation. Ref.77
Mutagenesis6991P → A: Reduced phosphorylation. Ref.77
Mutagenesis7001N → A: Abolishes phosphorylation. Ref.77
Mutagenesis7041L → A: Abolishes phosphorylation. Ref.77
Mutagenesis7051R → A: Abolishes phosphorylation. Ref.77
Mutagenesis7061I → A: Abolishes phosphorylation. Ref.77
Mutagenesis7451K → A or M: Abolishes kinase activity. Ref.77
Mutagenesis9741D → A: Strongly reduced phosphorylation.
Mutagenesis9771R → A: Reduced phosphorylation. Ref.76
Mutagenesis1005 – 10062ED → RK: Constitutively activated kinase.
Mutagenesis10161Y → F: 50% decrease in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1197. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1092. Ref.39
Mutagenesis10921Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. Ref.39
Mutagenesis11101Y → F: No change in interaction with PIK3C2B. Ref.39
Mutagenesis11721Y → F: No change in interaction with PIK3C2B. Ref.39
Mutagenesis11971Y → F: No change in interaction with PIK3C2B. 65% decrease in interaction with PIK3C2B; when associated with F-1016. Abolishes interaction with PIK3C2B; when associated with F-1092 and F-1016. Ref.39
Sequence conflict5401N → K in CAA25240. Ref.1

Secondary structure

.............................................................................................................................................................................. 1210
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (p170) [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: D8A2A50B4EFB6ED2

FASTA1,210134,277
        10         20         30         40         50         60 
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS LQRMFNNCEV 

        70         80         90        100        110        120 
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN MYYENSYALA 

       130        140        150        160        170        180 
VLSNYDANKT GLKELPMRNL QEILHGAVRF SNNPALCNVE SIQWRDIVSS DFLSNMSMDF 

       190        200        210        220        230        240 
QNHLGSCQKC DPSCPNGSCW GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC 

       250        260        270        280        290        300 
TGPRESDCLV CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 

       310        320        330        340        350        360 
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS INATNIKHFK 

       370        380        390        400        410        420 
NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE ITGFLLIQAW PENRTDLHAF 

       430        440        450        460        470        480 
ENLEIIRGRT KQHGQFSLAV VSLNITSLGL RSLKEISDGD VIISGNKNLC YANTINWKKL 

       490        500        510        520        530        540 
FGTSGQKTKI ISNRGENSCK ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN 

       550        560        570        580        590        600 
LLEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 

       610        620        630        640        650        660 
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM VGALLLLLVV 

       670        680        690        700        710        720 
ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN QALLRILKET EFKKIKVLGS 

       730        740        750        760        770        780 
GAFGTVYKGL WIPEGEKVKI PVAIKELREA TSPKANKEIL DEAYVMASVD NPHVCRLLGI 

       790        800        810        820        830        840 
CLTSTVQLIT QLMPFGCLLD YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA 

       850        860        870        880        890        900 
RNVLVKTPQH VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY 

       910        920        930        940        950        960 
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC WMIDADSRPK 

       970        980        990       1000       1010       1020 
FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA LMDEEDMDDV VDADEYLIPQ 

      1030       1040       1050       1060       1070       1080 
QGFFSSPSTS RTPLLSSLSA TSNNSTVACI DRNGLQSCPI KEDSFLQRYS SDPTGALTED 

      1090       1100       1110       1120       1130       1140 
SIDDTFLPVP EYINQSVPKR PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN 

      1150       1160       1170       1180       1190       1200 
TVQPTCVNST FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV 

      1210 
APQSSEFIGA 

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Isoform 2 (p60) (Truncated) (TEGFR) [UniParc].

Checksum: F5DEB31787EF1822
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FASTA40544,664
Isoform 3 (p110) [UniParc].

Checksum: 4CF149492FF1650C
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FASTA70577,312
Isoform 4 [UniParc].

Checksum: 3A00A5511A3B6AE2
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FASTA62869,228

References

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[1]"Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells."
Ullrich A., Coussens L., Hayflick J.S., Dull T.J., Gray A., Tam A.W., Lee J., Yarden Y., Libermann T.A., Schlessinger J., Downward J., Mayes E.L.V., Whittle N., Waterfield M.D., Seeburg P.H.
Nature 309:418-425(1984) [PubMed: 6328312] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta."
Ilekis J.V., Stark B.C., Scoccia B.
Mol. Reprod. Dev. 41:149-156(1995) [PubMed: 7654368] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[3]"A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor."
Reiter J.L., Maihle N.J.
Nucleic Acids Res. 24:4050-4056(1996) [PubMed: 8918811] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
Tissue: Placenta.
[4]"Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer."
Ilekis J.V., Gariti J., Niederberger C., Scoccia B.
Gynecol. Oncol. 65:36-41(1997) [PubMed: 9103388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Placenta.
[5]"Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms."
Reiter J.L., Threadgill D.W., Eley G.D., Strunk K.E., Danielsen A.J., Schehl Sinclair C., Pearsall R.S., Green P.J., Yee D., Lampland A.L., Balasubramaniam S., Crossley T.D., Magnuson T.R., James C.D., Maihle N.J.
Genomics 71:1-20(2001) [PubMed: 11161793] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3 AND 4).
Tissue: Placenta.
[6]"Cloning of the cDNA for a short EGF receptor from human placenta."
Xu L., Hong A., He X.
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[7]NIEHS SNPs program
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-98; ARG-266; LYS-521; ILE-674; GLY-962 AND PRO-988.
[8]"Human and mouse alternative EGFR transcripts encoding only the extracellular domain of the receptor."
Reiter J.L., Threadgill D.W., Danielsen A.J., Schehl C.M., Lampland A.L., Balasubramaniam S., Crossley T.O., Magnuson T.R., Maihle N.J.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 575-687.
[9]"Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells."
Lin C.R., Chen W.S., Kruiger W., Stolarsky L.S., Weber W., Evans R.M., Verma I.M., Gill G.N., Rosenfeld M.G.
Science 224:843-848(1984) [PubMed: 6326261] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 713-924.
[10]"Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells."
Xu Y.H., Ishii S., Clark A.J.L., Sullivan M., Wilson R.K., Ma D.P., Roe B.A., Merlino G.T., Pastan I.
Nature 309:806-810(1984) [PubMed: 6330563] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-962.
[11]"Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells."
Simmen F.A., Gope M.L., Schulz T.Z., Wright D.A., Carpenter G., O'Malley B.W.
Biochem. Biophys. Res. Commun. 124:125-132(1984) [PubMed: 6093780] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1028-1210.
[12]"The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription."
Haley J.D., Whittle N., Bennett P., Kinchington D., Ullrich A., Waterfield M.D.
Oncogene Res. 1:375-396(1987) [PubMed: 3329716] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[13]"Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis."
Haley J.D., Waterfield M.D.
J. Biol. Chem. 266:1746-1753(1991) [PubMed: 1988448] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[14]"Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene."
Ishii S., Xu Y.H., Stratton R.H., Roe B.A., Merlino G.T., Pastan I.
Proc. Natl. Acad. Sci. U.S.A. 82:4920-4924(1985) [PubMed: 2991899] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
[15]"Production of an epidermal growth factor receptor-related protein."
Weber W., Gill G.N., Spiess J.
Science 224:294-297(1984) [PubMed: 6324343] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-49.
[16]Kohda D.
Submitted (SEP-1997) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 540.
[17]"Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo."
Heisermann G.J., Gill G.N.
J. Biol. Chem. 263:13152-13158(1988) [PubMed: 3138233] [Abstract]
Cited for: PROTEIN SEQUENCE OF 687-705; 986-998; 1000-1023; 1026-1030 AND 1068-1077, PHOSPHORYLATION AT THR-693; SER-695; SER-1070 AND SER-1071.
[18]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-39.
[19]"Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase."
Russo M.W., Lukas T.J., Cohen S., Staros J.V.
J. Biol. Chem. 260:5205-5208(1985) [PubMed: 2985580] [Abstract]
Cited for: PROTEIN SEQUENCE OF 740-744 AND 746-747.
[20]"Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain."
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.
Mol. Cell 21:737-748(2006) [PubMed: 16543144] [Abstract]
Cited for: PROTEIN SEQUENCE OF 861-875 AND 914-932, UBIQUITINATION AT LYS-716; LYS-737; LYS-754; LYS-867; LYS-929 AND LYS-970, MASS SPECTROMETRY.
[21]"Disulfide bond structure of human epidermal growth factor receptor."
Abe Y., Odaka M., Inagaki F., Lax I., Schlessinger J., Kohda D.
J. Biol. Chem. 273:11150-11157(1998) [PubMed: 9556602] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
[22]"ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA."
Mroczkowski B., Mosig G., Cohen S.
Nature 309:270-273(1984) [PubMed: 6325948] [Abstract]
Cited for: RECEPTOR ACTIVITY.
[23]"Receptors for epidermal growth factor and other polypeptide mitogens."
Carpenter G.
Annu. Rev. Biochem. 56:881-914(1987) [PubMed: 3039909] [Abstract]
Cited for: REVIEW.
[24]"Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation."
Chen W.S., Lazar C.S., Lund K.A., Welsh J.B., Chang C.P., Walton G.M., Der C.J., Wiley H.S., Gill G.N., Rosenfeld M.G.
Cell 59:33-43(1989) [PubMed: 2790960] [Abstract]
Cited for: LIGAND-BINDING.
[25]"All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor."
Margolis B.L., Lax I., Kris R., Dombalagian M., Honegger A.M., Howk R., Givol D., Ullrich A., Schlessinger J.
J. Biol. Chem. 264:10667-10671(1989) [PubMed: 2543678] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT TYR-1110.
[26]"Amphiregulin induces tyrosine phosphorylation of the epidermal growth factor receptor and p185erbB2. Evidence that amphiregulin acts exclusively through the epidermal growth factor receptor at the surface of human epithelial cells."
Johnson G.R., Kannan B., Shoyab M., Stromberg K.
J. Biol. Chem. 268:2924-2931(1993) [PubMed: 7679104] [Abstract]
Cited for: IDENTIFICATION OF AMPHIREGULIN AS LIGAND.
[27]"Cell-type specific phosphorylation of threonines T654 and T669 by PKD defines the signal capacity of the EGF receptor."
Bagowski C.P., Stein-Gerlach M., Choidas A., Ullrich A.
EMBO J. 18:5567-5576(1999) [PubMed: 10523301] [Abstract]
Cited for: PHOSPHORYLATION AT THR-678 AND THR-693.
[28]"Recombinant human betacellulin. Molecular structure, biological activities, and receptor interaction."
Watanabe T., Shintani A., Nakata M., Shing Y., Folkman J., Igarashi K., Sasada R.
J. Biol. Chem. 269:9966-9973(1994) [PubMed: 8144591] [Abstract]
Cited for: IDENTIFICATION OF BETACELLULIN/BTC AS LIGAND.
[29]"Tyrosine phosphorylation of the c-cbl proto-oncogene protein product and association with epidermal growth factor (EGF) receptor upon EGF stimulation."
Galisteo M.L., Dikic I., Batzer A.G., Langdon W.Y., Schlessinger J.
J. Biol. Chem. 270:20242-20245(1995) [PubMed: 7657591] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
[30]"Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts."
Smith K.D., Davies M.J., Bailey D., Renouf D.V., Hounsell E.F.
Growth Factors 13:121-132(1996) [PubMed: 8962717] [Abstract]
Cited for: GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
[31]"Epiregulin binds to epidermal growth factor receptor and ErbB-4 and induces tyrosine phosphorylation of epidermal growth factor receptor, ErbB-2, ErbB-3 and ErbB-4."
Komurasaki T., Toyoda H., Uchida D., Morimoto S.
Oncogene 15:2841-2848(1997) [PubMed: 9419975] [Abstract]
Cited for: IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND.
[32]"Inhibition of the receptor-binding function of clathrin adaptor protein AP-2 by dominant-negative mutant mu2 subunit and its effects on endocytosis."
Nesterov A., Carter R.E., Sorkina T., Gill G.N., Sorkin A.
EMBO J. 18:2489-2499(1999) [PubMed: 10228163] [Abstract]
Cited for: INTERACTION WITH AP2M1.
[33]"Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck."
Braverman L.E., Quilliam L.A.
J. Biol. Chem. 274:5542-5549(1999) [PubMed: 10026169] [Abstract]
Cited for: INTERACTION WITH GRB2; NCK1 AND NCK2.
[34]"Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor."
Sato C., Kim J.-H., Abe Y., Saito K., Yokoyama S., Kohda D.
J. Biochem. 127:65-72(2000) [PubMed: 10731668] [Abstract]
Cited for: GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
[35]"RGS16 function is regulated by epidermal growth factor receptor-mediated tyrosine phosphorylation."
Derrien A., Druey K.M.
J. Biol. Chem. 276:48532-48538(2001) [PubMed: 11602604] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RGS16.
[36]"Identification and characterization of signal transducer and activator of transcription 3 recruitment sites within the epidermal growth factor receptor."
Shao H., Cheng H.Y., Cook R.G., Tweardy D.J.
Cancer Res. 63:3923-3930(2003) [PubMed: 12873986] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-1092 AND TYR-1110.
[37]"LRIG1 restricts growth factor signaling by enhancing receptor ubiquitylation and degradation."
Gur G., Rubin C., Katz M., Amit I., Citri A., Nilsson J., Amariglio N., Henriksson R., Rechavi G., Hedman H., Wides R., Yarden Y.
EMBO J. 23:3270-3281(2004) [PubMed: 15282549] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH LRIG1.
[38]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[39]"Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors."
Arcaro A., Zvelebil M.J., Wallasch C., Ullrich A., Waterfield M.D., Domin J.
Mol. Cell. Biol. 20:3817-3830(2000) [PubMed: 10805725] [Abstract]
Cited for: FUNCTION IN EGFR SIGNALING, IDENTIFICATION IN A COMPLEX WITH PIK3C2A AND ERBB2, IDENTIFICATION IN A COMPLEX WITH PIK3C2B AND ERBB2, INTERACTION WITH PIK3C2B, MUTAGENESIS OF TYR-1016; TYR-1092; TYR-1110; TYR-1172 AND TYR-1197.
[40]"The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome."
Habib A.A., Chatterjee S., Park S.-K., Ratan R.R., Lefebvre S., Vartanian T.
J. Biol. Chem. 276:8865-8874(2001) [PubMed: 11116146] [Abstract]
Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, INTERACTION WITH RIPK1.
[41]"The epidermal growth factor receptor regulates interaction of the human DF3/MUC1 carcinoma antigen with c-Src and beta-catenin."
Li Y., Ren J., Yu W., Li Q., Kuwahara H., Yin L., Carraway K.L. III, Kufe D.
J. Biol. Chem. 276:35239-35242(2001) [PubMed: 11483589] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MUC1, INTERACTION WITH MUC1.
[42]"Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling."
Kario E., Marmor M.D., Adamsky K., Citri A., Amit I., Amariglio N., Rechavi G., Yarden Y.
J. Biol. Chem. 280:7038-7048(2005) [PubMed: 15590694] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH SOCS5.
[43]"Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity."
Kochupurakkal B.S., Harari D., Di-Segni A., Maik-Rachline G., Lyass L., Gur G., Kerber G., Citri A., Lavi S., Eilam R., Chalifa-Caspi V., Eshhar Z., Pikarsky E., Pinkas-Kramarski R., Bacus S.S., Yarden Y.
J. Biol. Chem. 280:8503-8512(2005) [PubMed: 15611079] [Abstract]
Cited for: IDENTIFICATION OF EPIGEN/EPGN AS A LIGAND.
[44]"Extended Range Proteomic Analysis (ERPA): a new and sensitive LC-MS platform for high sequence coverage of complex proteins with extensive post-translational modifications-comprehensive analysis of beta-casein and epidermal growth factor receptor (EGFR)."
Wu S.L., Kim J., Hancock W.S., Karger B.
J. Proteome Res. 4:1155-1170(2005) [PubMed: 16083266] [Abstract]
Cited for: GLYCOSYLATION AT ASN-56; ASN-128; ASN-175; ASN-196; ASN-352; ASN-361; ASN-413; ASN-444; ASN-528; ASN-568 AND ASN-603, PHOSPHORYLATION AT THR-693; SER-991 AND SER-1026, MASS SPECTROMETRY.
[45]"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1069; TYR-1092; SER-1166 AND TYR-1172, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[46]"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.
Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-978, MASS SPECTROMETRY.
Tissue: Hepatoma.
[47]"Functional implications of altered subcellular localization of PELP1 in breast cancer cells."
Vadlamudi R.K., Manavathi B., Balasenthil S., Nair S.S., Yang Z., Sahin A.A., Kumar R.
Cancer Res. 65:7724-7732(2005) [PubMed: 16140940] [Abstract]
Cited for: INTERACTION WITH PELP1.
[48]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-995; TYR-998; SER-1064; TYR-1069; TYR-1092; TYR-1110; TYR-1138; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[49]"Tyrosine phosphorylation controls PCNA function through protein stability."
Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C., McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.
Nat. Cell Biol. 8:1359-1368(2006) [PubMed: 17115032] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
[50]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-869; TYR-1092; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Lung carcinoma.
[51]"Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia."
Groenestege W.M.T., Thebault S., van der Wijst J., van den Berg D., Janssen R., Tejpar S., van den Heuvel L.P., van Cutsem E., Hoenderop J.G., Knoers N.V., Bindels R.J.
J. Clin. Invest. 117:2260-2267(2007) [PubMed: 17671655] [Abstract]
Cited for: TISSUE SPECIFICITY.
[52]"Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation."
Shen F., Lin Q., Gu Y., Childress C., Yang W.
Mol. Biol. Cell 18:732-742(2007) [PubMed: 17182860] [Abstract]
Cited for: INTERACTION WITH TNF2, SUBCELLULAR LOCATION.
[53]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[54]"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks."
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; TYR-998; SER-1166; TYR-1069; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[55]"Phosphorylation-dependent binding of 14-3-3 terminates signalling by the Gab2 docking protein."
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P., Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D., Guilhaus M., James D.E., Daly R.J.
EMBO J. 27:2305-2316(2008) [PubMed: 19172738] [Abstract]
Cited for: INTERACTION WITH GAB2.
[56]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693 AND SER-991, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[57]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; THR-725; SER-991; SER-1025; SER-1026; SER-1037; SER-1039; SER-1042; SER-1064; SER-1081; SER-1166 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[58]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-991; THR-993; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1045; SER-1064 AND SER-1166, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[59]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[60]"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis."
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F., Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.
Curr. Biol. 19:1788-1798(2009) [PubMed: 19836242] [Abstract]
Cited for: ENZYME REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, INTERACTION WITH CBL AND GRB2.
[61]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568, MASS SPECTROMETRY.
Tissue: Liver.
[62]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-998; TYR-1016; TYR-1092; TYR-1110; TYR-1138; TYR-1172 AND TYR-1197, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[63]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, MASS SPECTROMETRY.
[64]"COPI-mediated retrograde trafficking from the Golgi to the ER regulates EGFR nuclear transport."
Wang Y.N., Wang H., Yamaguchi H., Lee H.J., Lee H.H., Hung M.C.
Biochem. Biophys. Res. Commun. 399:498-504(2010) [PubMed: 20674546] [Abstract]
Cited for: INTERACTION WITH COPG, SUBCELLULAR LOCATION, TOPOLOGY.
[65]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[66]"Crosstalk between Arg 1175 methylation and Tyr 1173 phosphorylation negatively modulates EGFR-mediated ERK activation."
Hsu J.M., Chen C.T., Chou C.K., Kuo H.P., Li L.Y., Lin C.Y., Lee H.J., Wang Y.N., Liu M., Liao H.W., Shi B., Lai C.C., Bedford M.T., Tsai C.H., Hung M.C.
Nat. Cell Biol. 13:174-181(2011) [PubMed: 21258366] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199 BY PRMT5, INTERACTION WITH PRMT5 AND PTPN6.
[67]"FER tyrosine kinase (FER) overexpression mediates resistance to quinacrine through EGF-dependent activation of NF-kappaB."
Guo C., Stark G.R.
Proc. Natl. Acad. Sci. U.S.A. 108:7968-7973(2011) [PubMed: 21518868] [Abstract]
Cited for: INTERACTION WITH FER, PHOSPHORYLATION.
[68]"Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains."
Ogiso H., Ishitani R., Nureki O., Fukai S., Yamanaka M., Kim J.H., Saito K., Sakamoto A., Inoue M., Shirouzu M., Yokoyama S.
Cell 110:775-787(2002) [PubMed: 12297050] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-646 IN COMPLEX WITH EGF, FUNCTION IN MAPK1 AND/OR MAPK3 ACTIVATION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-275; PHE-287; ARG-309 AND ARG-429, DISULFIDE BONDS, GLYCOSYLATION AT ASN-56; ASN-175; ASN-196; ASN-352; ASN-361 AND ASN-444.
[69]"EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization."
Ferguson K.M., Berger M.B., Mendrola J.M., Cho H.S., Leahy D.J., Lemmon M.A.
Mol. Cell 11:507-517(2003) [PubMed: 12620237] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-642 IN COMPLEX WITH EGF, FUNCTION, SUBUNIT, MUTAGENESIS OF 587-ASP--HIS-590 AND LYS-609, DISULFIDE BONDS, GLYCOSYLATION AT ASN-352; ASN-361; ASN-444; ASN-528; ASN-568 AND ASN-603.
[70]"A unique structure for epidermal growth factor receptor bound to GW572016 (Lapatinib): relationships among protein conformation, inhibitor off-rate, and receptor activity in tumor cells."
Wood E.R., Truesdale A.T., McDonald O.B., Yuan D., Hassell A., Dickerson S.H., Ellis B., Pennisi C., Horne E., Lackey K., Alligood K.J., Rusnak D.W., Gilmer T.M., Shewchuk L.
Cancer Res. 64:6652-6659(2004) [PubMed: 15374980] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH GW572016, CATALYTIC ACTIVITY, FUNCTION.
[71]"Structural basis for inhibition of the epidermal growth factor receptor by cetuximab."
Li S., Schmitz K.R., Jeffrey P.D., Wiltzius J.J., Kussie P., Ferguson K.M.
Cancer Cell 7:301-311(2005) [PubMed: 15837620] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-642 IN COMPLEX WITH CETUXIMAB.
[72]"A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor."
Choowongkomon K., Carlin C.R., Sonnichsen F.D.
J. Biol. Chem. 280:24043-24052(2005) [PubMed: 15840573] [Abstract]
Cited for: STRUCTURE BY NMR OF 669-721.
[73]"Structures of lung cancer-derived EGFR mutants and inhibitor complexes: mechanism of activation and insights into differential inhibitor sensitivity."
Yun C.H., Boggon T.J., Li Y., Woo M.S., Greulich H., Meyerson M., Eck M.J.
Cancer Cell 11:217-227(2007) [PubMed: 17349580] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS) OF 696-1022 OF WILD-TYPE AND VARIANTS SER-719 AND ARG-858 IN COMPLEXES WITH ATP ANALOGS AND SYNTHETIC INHIBITORS, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, CHARACTERIZATION OF VARIANTS SER-719 AND ARG-858.
[74]"Inhibition of the EGF receptor by binding of MIG6 to an activating kinase domain interface."
Zhang X., Pickin K.A., Bose R., Jura N., Cole P.A., Kuriyan J.
Nature 450:741-744(2007) [PubMed: 18046415] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 702-1022 IN COMPLEX WITH ERRFI1, ENZYME REGULATION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, SUBUNIT, INTERACTION WITH ERRFI1.
[75]"The T790M mutation in EGFR kinase causes drug resistance by increasing the affinity for ATP."
Yun C.H., Mengwasser K.E., Toms A.V., Woo M.S., Greulich H., Wong K.K., Meyerson M., Eck M.J.
Proc. Natl. Acad. Sci. U.S.A. 105:2070-2075(2008) [PubMed: 18227510] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 695-1022 OF VARIANT MET-790, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT MET-790.
[76]"Mechanism for activation of the EGF receptor catalytic domain by the juxtamembrane segment."
Jura N., Endres N.F., Engel K., Deindl S., Das R., Lamers M.H., Wemmer D.E., Zhang X., Kuriyan J.
Cell 137:1293-1307(2009) [PubMed: 19563760] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF 696-1022, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-998; TYR-1016 AND TYR-1197, MUTAGENESIS OF LEU-688; GLU-690; LEU-692; ARG-977 AND 1005-GLU-ASP-1006, SUBUNIT.
[77]"The juxtamembrane region of the EGF receptor functions as an activation domain."
Red Brewer M., Choi S.H., Alvarado D., Moravcevic K., Pozzi A., Lemmon M.A., Carpenter G.
Mol. Cell 34:641-651(2009) [PubMed: 19560417] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 669-1022 OF MUTANT MET-745, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LEU-688; VAL-689; GLU-690; LEU-692; THR-693; PRO-694; PRO-699; ASN-700; LEU-704; ARG-705; ILE-706 AND LYS-745.
[78]"Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases."
Mineev K.S., Bocharov E.V., Pustovalova Y.E., Bocharova O.V., Chupin V.V., Arseniev A.S.
J. Mol. Biol. 400:231-243(2010) [PubMed: 20471394] [Abstract]
Cited for: STRUCTURE BY NMR OF 634-677 IN COMPLEX WITH ERBB2, SUBUNIT.
[79]"Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor."
Lu C., Mi L.Z., Grey M.J., Zhu J., Graef E., Yokoyama S., Springer T.A.
Mol. Cell. Biol. 30:5432-5443(2010) [PubMed: 20837704] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-638 IN COMPLEX WITH EGF, FUNCTION, SUBUNIT, DISULFIDE BONDS, GLYCOSYLATION AT ASN-56; ASN-73; ASN-175; ASN-196; ASN-352; ASN-361; ASN-444 AND ASN-528.
[80]"EGFR mutations in lung cancer: correlation with clinical response to gefitinib therapy."
Paez J.G., Janne P.A., Lee J.C., Tracy S., Greulich H., Gabriel S., Herman P., Kaye F.J., Lindeman N., Boggon T.J., Naoki K., Sasaki H., Fujii Y., Eck M.J., Sellers W.R., Johnson B.E., Meyerson M.
Science 304:1497-1500(2004) [PubMed: 15118125] [Abstract]
Cited for: VARIANTS SER-719 AND ARG-858, POSSIBLE INVOLVEMENT IN LUNG CANCER.
[81]"Distinct epidermal growth factor receptor and KRAS mutation patterns in non-small cell lung cancer patients with different tobacco exposure and clinicopathologic features."
Tam I.Y.S., Chung L.P., Suen W.S., Wang E., Wong M.C.M., Ho K.K., Lam W.K., Chiu S.W., Girard L., Minna J.D., Gazdar A.F., Wong M.P.
Clin. Cancer Res. 12:1647-1653(2006) [PubMed: 16533793] [Abstract]
Cited for: VARIANTS ALA-709; LYS-709; ALA-719; ASP-719; CYS-719; SER-719; SER-724; LYS-734; GLU-746 DEL; PHE-747; 747-LEU--GLU-749 DEL; PRO-748; 752-SER--ILE-759 DEL; ARG-787; MET-790; VAL-833; LEU-834; MET-858; ARG-858; GLN-861 AND GLU-873, POSSIBLE INVOLVEMENT IN LUNG CANCER.
[82]"Epidermal growth factor receptor variant III mutations in lung tumorigenesis and sensitivity to tyrosine kinase inhibitors."
Ji H., Zhao X., Yuza Y., Shimamura T., Li D., Protopopov A., Jung B.L., McNamara K., Xia H., Glatt K.A., Thomas R.K., Sasaki H., Horner J.W., Eck M., Mitchell A., Sun Y., Al-Hashem R., Bronson R.T. expand/collapse author list , Rabindran S.K., Discafani C.M., Maher E., Shapiro G.I., Meyerson M., Wong K.K.
Proc. Natl. Acad. Sci. U.S.A. 103:7817-7822(2006) [PubMed: 16672372] [Abstract]
Cited for: VARIANT 30-VAL--ARG-297 DEL, POSSIBLE INVOLVEMENT IN LUNG CANCER.
[83]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-521; ARG-1034 AND VAL-1210.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00588 mRNA. Translation: CAA25240.1.
U95089 mRNA. Translation: AAB53063.1.
U48722 mRNA. Translation: AAC50802.1.
U48723 Genomic DNA. Translation: AAC50804.1.
U48724 Genomic DNA. Translation: AAC50796.1.
U48725 Genomic DNA. Translation: AAC50797.1.
U48726 Genomic DNA. Translation: AAC50798.1.
U48727 Genomic DNA. Translation: AAC50799.1.
U48728 Genomic DNA. Translation: AAC50800.1.
U48729 Genomic DNA. Translation: AAC50801.1.
AF288738 Genomic DNA. Translation: AAG35786.1.
AF288738 Genomic DNA. Translation: AAG35787.1.
AF288738 Genomic DNA. Translation: AAG35788.1.
AF288738 Genomic DNA. Translation: AAG35789.1.
AF288738 Genomic DNA. Translation: AAG35790.1.
AY698024 mRNA. Translation: AAT97979.1.
AY588246 Genomic DNA. Translation: AAS83109.1.
AF277897 mRNA. Translation: AAK01080.1.
AF125253 mRNA. Translation: AAG43240.1.
AF125539, AF125538 Genomic DNA. Translation: AAG43243.1.
X06370 Genomic DNA. Translation: CAA29668.1.
X00663 mRNA. Translation: CAA25282.1.
M38425 Genomic DNA. Translation: AAA63171.1.
M11234 Genomic DNA. Translation: AAA52370.1.
IPIIPI00018274.
IPI00221346.
IPI00221347.
IPI00221348.
PIRGQHUE. A00641.
RefSeqNP_005219.2. NM_005228.3.
NP_958439.1. NM_201282.1.
NP_958440.1. NM_201283.1.
NP_958441.1. NM_201284.1.
UniGeneHs.488293.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DNQmodel-A25-336[»]
1DNRmodel-A337-645[»]
1IVOX-ray3.30A/B25-646[»]
1M14X-ray2.60A695-1022[»]
1M17X-ray2.60A695-1022[»]
1MOXX-ray2.50A/B25-525[»]
1NQLX-ray2.80A25-642[»]
1XKKX-ray2.40A695-1022[»]
1YY9X-ray2.60A25-642[»]
1Z9INMR-A669-721[»]
2EB2X-ray2.50A695-1022[»]
2EB3X-ray2.84A695-1022[»]
2EXPmodel-A311-326[»]
2EXQmodel-A27-536[»]
2GS2X-ray2.80A696-1022[»]
2GS6X-ray2.60A696-1022[»]
2GS7X-ray2.60A/B696-1022[»]
2ITNX-ray2.47A696-1019[»]
2ITOX-ray3.25A696-1022[»]
2ITPX-ray2.74A696-1022[»]
2ITQX-ray2.68A696-1022[»]
2ITTX-ray2.73A696-1022[»]
2ITUX-ray2.80A696-1022[»]
2ITVX-ray2.47A696-1022[»]
2ITWX-ray2.88A696-1022[»]
2ITXX-ray2.98A696-1022[»]
2ITYX-ray3.42A696-1022[»]
2ITZX-ray2.72A696-1022[»]
2J5EX-ray3.10A696-1022[»]
2J5FX-ray3.00A696-1022[»]
2J6MX-ray3.10A696-1022[»]
2JITX-ray3.10A/B696-1022[»]
2JIUX-ray3.05A/B695-1022[»]
2JIVX-ray3.50A/B695-1022[»]
2KS1NMR-B634-677[»]
2RF9X-ray3.50A/B696-1022[»]
2RFDX-ray3.60A/B702-1022[»]
2RFEX-ray2.90A/B/C/D702-1022[»]
2RGPX-ray2.00A702-1016[»]
3B2UX-ray2.58A/B/E/I/M/P/S/V335-538[»]
3B2VX-ray3.30A25-642[»]
3BELX-ray2.30A702-1016[»]
3BUOX-ray2.60A/C1063-1075[»]
3C09X-ray3.20A/D335-538[»]
3G5VX-ray2.00C311-326[»]
3G5YX-ray1.59E311-326[»]
3GOPX-ray2.80A669-1022[»]
3GT8X-ray2.96A/B/C/D696-1022[»]
3IKAX-ray2.90A/B694-1022[»]
3LZBX-ray2.70A/B/C/D/E/F/G/H696-983[»]
3NJPX-ray3.30A/B25-638[»]
3OB2X-ray2.10A1063-1074[»]
3OP0X-ray2.52C/D1066-1076[»]
3P0YX-ray1.80A334-538[»]
3PFVX-ray2.27C/D1066-1076[»]
3POZX-ray1.50A696-1022[»]
ProteinModelPortalP00533.
SMRP00533. Positions 26-1003.
DisProtDP00309.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-405N.
DIP-5764N.
IntActP00533. 205 interactions.
MINTMINT-206389.
STRINGP00533.

PTM databases

GlycoSuiteDBP00533.
PhosphoSiteP00533.

Polymorphism databases

DMDM2811086.

2D gel databases

SWISS-2DPAGEP00533.

Proteomic databases

PeptideAtlasP00533.
PRIDEP00533.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275493; ENSP00000275493; ENSG00000146648.
GeneID1956.
KEGGhsa:1956.
UCSCuc003tqi.1. human.
uc003tqj.1. human.
uc003tqk.1. human.

Organism-specific databases

CTD1956.
GeneCardsGC07P055054.
H-InvDBHIX0025338.
HGNCHGNC:3236. EGFR.
HPACAB000035.
HPA001200.
HPA018530.
MIM131550. gene.
211980. phenotype.
neXtProtNX_P00533.
Orphanet360. Glioblastoma.
PharmGKBPA7360.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG000490.
InParanoidP00533.
OMAMRRRHIV.
PhylomeDBP00533.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
Pathway_Interaction_DBa6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
arf6cyclingpathway. Arf6 signaling events.
endothelinpathway. Endothelins.
lysophospholipid_pathway. LPA receptor mediated events.
telomerasepathway. Regulation of Telomerase.
ptp1bpathway. Signaling events mediated by PTP1B.
syndecan_3_pathway. Syndecan-3-mediated signaling events.
txa2pathway. Thromboxane A2 receptor signaling.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP00533.
BgeeP00533.
GenevestigatorP00533.
GermOnlineENSG00000146648. Homo sapiens.

Family and domain databases

InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
KOK04361.
PfamPF00757. Furin-like. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF01030. Recep_L_domain. 2 hits.
[Graphical view]
PIRSFPIRSF000619. TyrPK_EGF-R. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00261. FU. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF57184. Grow_fac_recept. 2 hits.
SSF56112. Kinase_like. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB00002. Cetuximab.
DB00530. Erlotinib.
DB00317. Gefitinib.
DB01259. Lapatinib.
DB00281. Lidocaine.
DB01269. Panitumumab.
DB00072. Trastuzumab.
NextBio7931.
PMAP-CutDBP00533.
SOURCESearch...

Entry information

Entry nameEGFR_HUMAN
AccessionPrimary (citable) accession number: P00533
Secondary accession number(s): O00688 expand/collapse secondary AC list , O00732, P06268, Q14225, Q68GS5, Q92795, Q9BZS2, Q9GZX1, Q9H2C9, Q9H3C9, Q9UMD7, Q9UMD8, Q9UMG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 179 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families