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P00533 (EGFR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 208. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
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.31 Ref.38 Ref.40 Ref.42 Ref.43 Ref.44 Ref.50 Ref.69 Ref.73 Ref.74 Ref.75 Ref.82 Ref.84

Isoform 2 may act as an antagonist of EGF action. Ref.31 Ref.38 Ref.40 Ref.42 Ref.43 Ref.44 Ref.50 Ref.69 Ref.73 Ref.74 Ref.75 Ref.82 Ref.84

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.75 Ref.78 Ref.79 Ref.80 Ref.81 Ref.82

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.41 Ref.45 Ref.59 Ref.79

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, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through TCEB1- and TCEB2-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. May interact with EPS8; mediates EPS8 phosphorylation. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Interacts with ATX2. Interacts with GAREM. Interacts (ubiquitinated) with ANKRD13A/B/D; the interaction is direct and may regulate EGFR internalization after EGF stimulation. Interacts with GPER1; the interaction occurs in an estrogen-dependent manner. Interacts (via C-terminal cytoplasmic kinase domain) with ZPR1 (via zinc fingers). Ref.27 Ref.28 Ref.31 Ref.35 Ref.36 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.48 Ref.50 Ref.52 Ref.53 Ref.54 Ref.59 Ref.60 Ref.63 Ref.64 Ref.65 Ref.69 Ref.70 Ref.71 Ref.73 Ref.74 Ref.79 Ref.81 Ref.82 Ref.83 Ref.84 Ref.85 Ref.86

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. Nucleus. Note: In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts (CAF). Ref.50 Ref.52 Ref.59 Ref.64 Ref.65 Ref.71 Ref.73 Ref.82

Isoform 2: Secreted Ref.50 Ref.52 Ref.59 Ref.64 Ref.65 Ref.71 Ref.73 Ref.82.

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. Dephosphorylated by PTPN1 and PTPN2. Ref.17 Ref.25 Ref.29 Ref.34 Ref.40 Ref.47 Ref.59 Ref.68 Ref.70 Ref.78 Ref.79 Ref.81 Ref.82 Ref.86

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. Deubiquitination by OTUD7B prevents degradation.

Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197. Ref.69

Involvement in disease

Lung cancer (LNCR) [MIM:211980]: 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.
Note: The gene represented in this entry is involved in disease pathogenesis.

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_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MAPK cascade

Non-traceable author statement PubMed 15542601. Source: GOC

activation of phospholipase A2 activity by calcium-mediated signaling

Traceable author statement PubMed 12435727. Source: UniProtKB

activation of phospholipase C activity

Traceable author statement PubMed 12435727. Source: UniProtKB

alkanesulfonate metabolic process

Inferred from electronic annotation. Source: Ensembl

astrocyte activation

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

cell proliferation

Inferred from direct assay Ref.50. Source: UniProtKB

cell surface receptor signaling pathway

Inferred from direct assay PubMed 7736574. Source: MGI

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to drug

Inferred from electronic annotation. Source: Ensembl

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to estradiol stimulus

Inferred from direct assay Ref.65. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cerebral cortex cell migration

Inferred from electronic annotation. Source: Ensembl

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

diterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

embryonic placenta development

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Inferred from direct assay PubMed 12435727. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

hair follicle development

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide metabolic process

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

learning or memory

Inferred from sequence or structural similarity. Source: UniProtKB

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

magnesium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelial fold

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 18070883. Source: UniProtKB

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein catabolic process

Inferred from direct assay Ref.50. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

ossification

Non-traceable author statement PubMed 12925580. Source: UniProtKB

ovulation cycle

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.50PubMed 17599051. Source: GOC

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

polysaccharide metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA repair

Inferred from direct assay Ref.50. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay Ref.50. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.65. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay PubMed 10572067. Source: UniProtKB

positive regulation of catenin import into nucleus

Inferred from mutant phenotype PubMed 20302655. Source: BHF-UCL

positive regulation of cell migration

Inferred from mutant phenotype PubMed 12435727. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 7736574. Source: MGI

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 18483258. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 10572067. Source: UniProtKB

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric oxide biosynthetic process

Inferred from direct assay PubMed 12828935. Source: UniProtKB

positive regulation of phosphorylation

Inferred from direct assay PubMed 15082764. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from mutant phenotype PubMed 17655843. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay Ref.65. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of superoxide anion generation

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, glutamatergic

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.65. Source: UniProtKB

positive regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from mutant phenotype PubMed 18070883. Source: UniProtKB

protein insertion into membrane

Traceable author statement PubMed 12435727. Source: UniProtKB

regulation of nitric-oxide synthase activity

Inferred from direct assay PubMed 12828935. Source: UniProtKB

regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 12435727. Source: UniProtKB

response to UV-A

Inferred from direct assay PubMed 18483258. Source: BHF-UCL

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to cobalamin

Inferred from electronic annotation. Source: Ensembl

response to hydroxyisoflavone

Inferred from electronic annotation. Source: Ensembl

response to osmotic stress

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from electronic annotation. Source: Ensembl

response to stress

Non-traceable author statement PubMed 12828935. Source: UniProtKB

salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from direct assay PubMed 10572067. Source: UniProtKB

single organismal cell-cell adhesion

Inferred from mutant phenotype PubMed 12435727. Source: UniProtKB

tongue development

Inferred from electronic annotation. Source: Ensembl

translation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Shc-EGFR complex

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

apical plasma membrane

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Inferred from direct assay PubMed 12646923. Source: BHF-UCL

cell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 12435727PubMed 7588596. Source: UniProtKB

endocytic vesicle

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay PubMed 14702346Ref.52. Source: UniProtKB

endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

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

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from direct assay PubMed 12435727. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 12009895. Source: UniProtKB

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 12828935Ref.50Ref.65. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15465819. Source: HGNC

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

MAP kinase kinase kinase activity

Non-traceable author statement PubMed 15542601. Source: UniProtKB

actin filament binding

Inferred from direct assay PubMed 14702346. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.65. Source: UniProtKB

double-stranded DNA binding

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

enzyme binding

Inferred from physical interaction PubMed 12009895. Source: UniProtKB

epidermal growth factor-activated receptor activity

Inferred from direct assay PubMed 12435727Ref.50. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16777603Ref.81PubMed 20029029PubMed 20359299PubMed 20946980PubMed 21278786PubMed 21480528PubMed 22232519PubMed 22579287PubMed 23374349PubMed 24135280. Source: IntAct

protein binding

Inferred from physical interaction Ref.36PubMed 10572067PubMed 12577067Ref.45Ref.50Ref.52PubMed 17599051PubMed 17909029Ref.79Ref.53PubMed 18824549Ref.54Ref.60PubMed 19602593Ref.65PubMed 2176151Ref.33Ref.28. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 10572067. Source: UniProtKB

protein phosphatase binding

Inferred from physical interaction PubMed 15899872. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay Ref.50PubMed 17599051. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Inferred from electronic annotation. Source: InterPro

transmembrane receptor protein tyrosine kinase activity

Traceable author statement. Source: Reactome

transmembrane signaling receptor activity

Inferred from direct assay PubMed 7736574. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself21EBI-297353,EBI-297353
ABL2P426847EBI-297353,EBI-1102694
AHNAKQ096663EBI-297353,EBI-2555881
AKAP12Q029522EBI-297353,EBI-2562430
ANKS1AQ926252EBI-297353,EBI-1048612
AP2M1Q96CW14EBI-297353,EBI-297683
APBB1O002134EBI-297353,EBI-81694
APBB2Q928704EBI-297353,EBI-79277
APBB3O957042EBI-297353,EBI-286427
APPL1Q9UKG12EBI-297353,EBI-741243
BECN1Q144577EBI-297353,EBI-949378
CALM3P621583EBI-297353,EBI-397435
Calm3P621616EBI-297353,EBI-397530From a different organism.
CBLP2268117EBI-297353,EBI-518228
CblP226822EBI-297353,EBI-640919From a different organism.
CLNKQ7Z7G12EBI-297353,EBI-7878194
CRKP461082EBI-297353,EBI-886
CRKLP461092EBI-297353,EBI-910
CYTH2Q994185EBI-297353,EBI-448974
DOK6Q6PKX42EBI-297353,EBI-2880244
EGFP0113315EBI-297353,EBI-640857
ERBB2P0462615EBI-297353,EBI-641062
ERBB3P2186011EBI-297353,EBI-720706
ERBB4Q153032EBI-297353,EBI-80371
ERRFI1Q9UJM38EBI-297353,EBI-2941912
ESR1P033722EBI-297353,EBI-78473
ESR1P03372-44EBI-297353,EBI-4309277
FKBP8Q143183EBI-297353,EBI-724839
GABARAPL2P605202EBI-297353,EBI-720116
GAPDHP044064EBI-297353,EBI-354056
GRB2P6299329EBI-297353,EBI-401755
HDAC6Q9UBN78EBI-297353,EBI-301697
HSP90AA1P079003EBI-297353,EBI-296047
HSP90AB1P082385EBI-297353,EBI-352572
HSPA1BP081074EBI-297353,EBI-629985
HSPA9P386464EBI-297353,EBI-354932
HSPB1P047923EBI-297353,EBI-352682
IQGAP1P469404EBI-297353,EBI-297509
IRS4O146542EBI-297353,EBI-356594
LYNP079485EBI-297353,EBI-79452
LYNP07948-12EBI-297353,EBI-6895930
MAPK8IP1Q9UQF23EBI-297353,EBI-78404
MAPK8IP2Q133873EBI-297353,EBI-722813
MAST1Q9Y2H92EBI-297353,EBI-3385920
METP085817EBI-297353,EBI-1039152
PIK3C2BO007507EBI-297353,EBI-641107
PIK3R1P279864EBI-297353,EBI-79464
PIK3R2O004592EBI-297353,EBI-346930
PIK3R3Q925694EBI-297353,EBI-79893
PLCG1P191746EBI-297353,EBI-79387
PLCG2P168852EBI-297353,EBI-617403
PTPN1P180314EBI-297353,EBI-968788
Ptpn1P2041711EBI-297353,EBI-916819From a different organism.
RABGEF1Q9UJ414EBI-297353,EBI-913954
RASA1P209367EBI-297353,EBI-1026476
RIN1Q136713EBI-297353,EBI-366017
ROR1Q019738EBI-297353,EBI-6082337
SH2B3Q9UQQ22EBI-297353,EBI-7879749
SHC1P2935326EBI-297353,EBI-78835
SHC2P980773EBI-297353,EBI-7256023
SLC5A1P138663EBI-297353,EBI-1772443
SRCP129316EBI-297353,EBI-621482
STAT3P4076312EBI-297353,EBI-518675
STIP1P319482EBI-297353,EBI-1054052
SYKP434056EBI-297353,EBI-78302
TLN1Q9Y4902EBI-297353,EBI-2462036
TOM1L1O756746EBI-297353,EBI-712991
Trpv3Q8K4242EBI-297353,EBI-2650739From a different organism.
UCHL1P099362EBI-297353,EBI-714860
VAPAQ9P0L02EBI-297353,EBI-1059156
YES1P079473EBI-297353,EBI-515331
YWHAQP273485EBI-297353,EBI-359854
YWHAZP631044EBI-297353,EBI-347088

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

Sites

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

Amino acid modifications

Modified residue2291Phosphoserine Ref.68
Modified residue6781Phosphothreonine; by PKC and PKD/PRKD1 Ref.29
Modified residue6931Phosphothreonine; by PKD/PRKD1 Ref.17 Ref.29 Ref.47 Ref.56 Ref.66
Modified residue6951Phosphoserine Ref.17 Ref.56
Modified residue9911Phosphoserine Ref.47 Ref.57 Ref.66
Modified residue9951Phosphoserine Ref.57
Modified residue9981Phosphotyrosine; by autocatalysis Ref.57 Ref.81
Modified residue10161Phosphotyrosine; by autocatalysis Ref.81
Modified residue10261Phosphoserine Ref.47
Modified residue10391Phosphoserine Ref.57
Modified residue10411Phosphothreonine Ref.57
Modified residue10421Phosphoserine Ref.57
Modified residue10641Phosphoserine Ref.56 Ref.57 Ref.66
Modified residue10691Phosphotyrosine Probable
Modified residue10701Phosphoserine Ref.17
Modified residue10711Phosphoserine Ref.17
Modified residue10811Phosphoserine Ref.56
Modified residue10921Phosphotyrosine; by autocatalysis Ref.40
Modified residue11101Phosphotyrosine; by autocatalysis Ref.25 Ref.40
Modified residue11661Phosphoserine Ref.56 Ref.57
Modified residue11721Phosphotyrosine; by autocatalysis Ref.49
Modified residue11971Phosphotyrosine; by autocatalysis Ref.49 Ref.56 Ref.59 Ref.66 Ref.81
Modified residue11991Omega-N-methylated arginine Ref.69
Glycosylation561N-linked (GlcNAc...) (complex); partial; atypical Ref.37 Ref.39 Ref.47 Ref.73 Ref.84
CAR_000227
Glycosylation731N-linked (GlcNAc...); atypical Ref.84
Glycosylation1281N-linked (GlcNAc...) Ref.32 Ref.39 Ref.47
Glycosylation1751N-linked (GlcNAc...) Ref.32 Ref.39 Ref.47 Ref.73 Ref.84
Glycosylation1961N-linked (GlcNAc...) Ref.39 Ref.47 Ref.73 Ref.84
Glycosylation3521N-linked (GlcNAc...) Ref.37 Ref.39 Ref.47 Ref.61 Ref.73 Ref.74 Ref.84
Glycosylation3611N-linked (GlcNAc...) Ref.37 Ref.39 Ref.47 Ref.73 Ref.74 Ref.84
Glycosylation4131N-linked (GlcNAc...) Ref.32 Ref.39 Ref.47 Ref.61
Glycosylation4441N-linked (GlcNAc...) Ref.32 Ref.39 Ref.47 Ref.73 Ref.74 Ref.84
Glycosylation5281N-linked (GlcNAc...) Ref.32 Ref.39 Ref.47 Ref.74 Ref.84
Glycosylation5681N-linked (GlcNAc...); partial Ref.37 Ref.39 Ref.47 Ref.61 Ref.74
Glycosylation6031N-linked (GlcNAc...); partial Ref.37 Ref.39 Ref.47 Ref.74
Glycosylation6231N-linked (GlcNAc...) (high mannose) Probable
Disulfide bond31 ↔ 58 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond157 ↔ 187 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond190 ↔ 199 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond194 ↔ 207 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond215 ↔ 223 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond219 ↔ 231 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond232 ↔ 240 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond236 ↔ 248 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond251 ↔ 260 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond264 ↔ 291 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond295 ↔ 307 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond311 ↔ 326 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond329 ↔ 333 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond337 ↔ 362 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond470 ↔ 499 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond506 ↔ 515 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond510 ↔ 523 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond526 ↔ 535 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond539 ↔ 555 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond558 ↔ 571 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond562 ↔ 579 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond582 ↔ 591 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond595 ↔ 617 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond620 ↔ 628 Ref.21 Ref.73 Ref.74 Ref.84
Disulfide bond624 ↔ 636 Ref.21 Ref.73 Ref.74 Ref.84
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.92
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; more sensitive to gefitinib than wild-type. Ref.87 Ref.89 Ref.90
VAR_026084
Natural variant7091E → G Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. Ref.87 Ref.90
VAR_069498
Natural variant7091E → K Found in a lung cancer sample. Ref.89
VAR_026085
Natural variant7191G → A Found in a lung cancer sample. Ref.89
VAR_026086
Natural variant7191G → C Found in a lung cancer sample. Ref.87 Ref.89
Corresponds to variant rs28929495 [ dbSNP | Ensembl ].
VAR_026087
Natural variant7191G → D Found in a lung cancer sample. Ref.89
VAR_026088
Natural variant7191G → S Found in a lung cancer sample; somatic mutation; strongly increased kinase activity; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. Ref.78 Ref.87 Ref.88 Ref.89 Ref.90
VAR_019297
Natural variant7241G → S Found in a lung cancer sample. Ref.89
VAR_026089
Natural variant7341E → K Found in a lung cancer sample. Ref.89
VAR_026090
Natural variant746 – 7527ELREATS → D Found in a lung cancer sample.
VAR_069499
Natural variant746 – 7516ELREAT → A Found in a lung cancer sample.
VAR_069500
Natural variant746 – 7505Missing Found in a lung cancer sample. Ref.89
VAR_026092
Natural variant7461Missing Found in a lung cancer sample. Ref.89
VAR_026091
Natural variant747 – 7515Missing Found in a lung cancer sample.
VAR_069501
Natural variant747 – 7493Missing Found in a lung cancer sample.
VAR_026094
Natural variant7471L → F Found in a lung cancer sample. Ref.89
VAR_026093
Natural variant7481R → P Found in a lung cancer sample. Ref.89
VAR_026095
Natural variant752 – 7598Missing Found in a lung cancer sample.
VAR_026096
Natural variant7681S → I Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. Ref.87 Ref.90
Corresponds to variant rs121913465 [ dbSNP | Ensembl ].
VAR_069502
Natural variant7691V → M Found in a lung cancer sample. Ref.87
Corresponds to variant rs147149347 [ dbSNP | Ensembl ].
VAR_069503
Natural variant7871Q → R Found in a lung cancer sample. Ref.89
VAR_026097
Natural variant7901T → M Found in a lung cancer sample; increased kinase activity. Ref.80 Ref.89
VAR_026098
Natural variant8331L → V Found in a lung cancer sample; more sensitive to gefitinib than wild-type. Ref.87 Ref.89 Ref.90
VAR_026099
Natural variant8341V → L Found in a lung cancer sample. Ref.89
VAR_026100
Natural variant8351H → L Found in a lung cancer sample; more sensitive to gefitinib than wild-type. Ref.87 Ref.90
VAR_069504
Natural variant8381L → V Found in a lung cancer sample; more sensitive to gefitinib than wild-type. Ref.87 Ref.90
VAR_069505
Natural variant8581L → M Found in a lung cancer sample. Ref.89
VAR_026101
Natural variant8581L → R Found in a lung cancer sample; somatic mutation; constitutively activated enzyme with strongly increased kinase activity; more sensitive to gefitinib than wild-type. Ref.78 Ref.87 Ref.88 Ref.89 Ref.90
Corresponds to variant rs121434568 [ dbSNP | Ensembl ].
VAR_019298
Natural variant8611L → Q Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. Ref.87 Ref.89 Ref.90
Corresponds to variant rs121913444 [ dbSNP | Ensembl ].
VAR_026102
Natural variant8731G → E Found in a lung cancer sample. Ref.89
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.92
Corresponds to variant rs34352568 [ dbSNP | Ensembl ].
VAR_042095
Natural variant12101A → V. Ref.92
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.73
Mutagenesis2871F → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. Ref.73
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.73
Mutagenesis4291R → E: Abolishes autophosphorylation and activation of downstream kinases. Ref.73
Mutagenesis587 – 5904DGPH → AGPA: Decreases intramolecular interactions and facilitates EGF binding. Ref.74
Mutagenesis6091K → A: Decreases intramolecular interactions and facilitates EGF binding. Ref.74
Mutagenesis6881L → A: Strongly reduced phosphorylation. Ref.81 Ref.82
Mutagenesis6891V → A: Reduced autophosphorylation. Ref.82
Mutagenesis6891V → M: Constitutively activated kinase. Ref.82
Mutagenesis6901E → A: Reduced phosphorylation. Ref.81 Ref.82
Mutagenesis6921L → A or P: Strongly reduced phosphorylation. Ref.81 Ref.82
Mutagenesis6931T → A: Increased phosphorylation. Ref.82
Mutagenesis6931T → D: Strongly reduced phosphorylation. Ref.82
Mutagenesis6941P → A: Strongly reduced phosphorylation. Ref.82
Mutagenesis6991P → A: Reduced phosphorylation. Ref.82
Mutagenesis7001N → A: Abolishes phosphorylation. Ref.82
Mutagenesis7041L → A: Abolishes phosphorylation. Ref.82
Mutagenesis7051R → A: Abolishes phosphorylation. Ref.82
Mutagenesis7061I → A: Abolishes phosphorylation. Ref.82
Mutagenesis7451K → A or M: Abolishes kinase activity. Ref.82
Mutagenesis9741D → A: Strongly reduced phosphorylation.
Mutagenesis9771R → A: Reduced phosphorylation. Ref.81
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.42
Mutagenesis10671Q → G: No effect on interaction with CBLC. Ref.86
Mutagenesis10681R → G: Strongly decreases interaction with CBLC. Ref.86
Mutagenesis10691Y → F: Abolishes interaction with CBLC. Ref.86
Mutagenesis10921Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. Ref.42
Mutagenesis11101Y → F: No change in interaction with PIK3C2B. Ref.42
Mutagenesis11721Y → F: No change in interaction with PIK3C2B. Ref.42
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.42
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

« Hide 'large scale' references
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF AMPHIREGULIN AS LIGAND.
[27]"Binding of zinc finger protein ZPR1 to the epidermal growth factor receptor."
Galcheva-Gargova Z., Konstantinov K.N., Wu I.-H., Klier F.G., Barrett T., Davis R.J.
Science 272:1797-1802(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZPR1.
[28]"Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells."
Gangwani L., Mikrut M., Galcheva-Gargova Z., Davis R.J.
J. Cell Biol. 143:1471-1484(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZPR1.
[29]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-678 AND THR-693.
[30]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF BETACELLULIN/BTC AS LIGAND.
[31]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL.
[32]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-128; ASN-175; ASN-413; ASN-444 AND ASN-528.
[33]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF EPIREGULIN/EREG AS LIGAND.
[34]"Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase."
Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.
Mol. Cell. Biol. 18:1622-1634(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, DEPHOSPHORYLATION BY PTPN1 AND PTPN2.
[35]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AP2M1.
[36]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB2; NCK1 AND NCK2.
[37]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-56; ASN-352; ASN-361; ASN-568 AND ASN-603.
[38]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF RGS16.
[39]"Characterization of glycosylation sites of the epidermal growth factor receptor."
Zhen Y., Caprioli R.M., Staros J.V.
Biochemistry 42:5478-5492(2003) [PubMed] [Europe PMC] [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; ASN-603 AND ASN-623.
[40]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-1092 AND TYR-1110.
[41]"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] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH LRIG1.
[42]"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] [Europe PMC] [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.
[43]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, INTERACTION WITH RIPK1.
[44]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF MUC1, INTERACTION WITH MUC1.
[45]"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] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH SOCS5.
[46]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF EPIGEN/EPGN AS A LIGAND.
[47]"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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
[48]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PELP1.
[49]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1172 AND TYR-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[50]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, FUNCTION IN PCNA PHOSPHORYLATION, INTERACTION WITH PCNA, SUBCELLULAR LOCATION.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNF2, SUBCELLULAR LOCATION.
[53]"Ataxin-2 associates with the endocytosis complex and affects EGF receptor trafficking."
Nonis D., Schmidt M.H., van de Loo S., Eich F., Dikic I., Nowock J., Auburger G.
Cell. Signal. 20:1725-1739(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATX2.
[54]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAB2.
[55]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[56]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-695; SER-1064; SER-1081; SER-1166 AND TYR-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[57]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-991; SER-995; TYR-998; SER-1039; THR-1041; SER-1042; SER-1064 AND SER-1166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[58]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[59]"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] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION BY PTPRJ AND PTPRK, PHOSPHORYLATION AT TYR-1197, DEPHOSPHORYLATION BY PTPRJ, SUBCELLULAR LOCATION, INTERACTION WITH CBL AND GRB2.
[60]"GAREM, a novel adaptor protein for growth factor receptor-bound protein 2, contributes to cellular transformation through the activation of extracellular signal-regulated kinase signaling."
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E., Taniguchi H., Konishi H.
J. Biol. Chem. 284:20206-20214(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GAREM.
[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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352; ASN-413 AND ASN-568.
Tissue: Liver.
[62]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[63]"G protein-coupled receptor 30 expression is up-regulated by EGF and TGF alpha in estrogen receptor alpha-positive cancer cells."
Vivacqua A., Lappano R., De Marco P., Sisci D., Aquila S., De Amicis F., Fuqua S.A., Ando S., Maggiolini M.
Mol. Endocrinol. 23:1815-1826(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPER1.
[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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COPG1, SUBCELLULAR LOCATION, TOPOLOGY.
[65]"Nuclear alternate estrogen receptor GPR30 mediates 17beta-estradiol-induced gene expression and migration in breast cancer-associated fibroblasts."
Madeo A., Maggiolini M.
Cancer Res. 70:6036-6046(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GPER1, SUBCELLULAR LOCATION.
[66]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693; SER-991; SER-1064 AND TYR-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[67]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[68]"Nuclear translocation of epidermal growth factor receptor by Akt-dependent phosphorylation enhances breast cancer-resistant protein expression in gefitinib-resistant cells."
Huang W.C., Chen Y.J., Li L.Y., Wei Y.L., Hsu S.C., Tsai S.L., Chiu P.C., Huang W.P., Wang Y.N., Chen C.H., Chang W.C., Chang W.C., Chen A.J., Tsai C.H., Hung M.C.
J. Biol. Chem. 286:20558-20568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-229.
[69]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND CELL MIGRATION, METHYLATION AT ARG-1199 BY PRMT5, INTERACTION WITH PRMT5 AND PTPN6.
[70]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FER, PHOSPHORYLATION.
[71]"The Ankrd 13 family of UIM-bearing proteins regulates EGF receptor endocytosis from the plasma membrane."
Tanno H., Yamaguchi T., Goto E., Ishido S., Komada M.
Mol. Biol. Cell 23:1343-1353(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD13A; ANKRD13B AND ALKRD13D, UBIQUITINATION, SUBCELLULAR LOCATION.
[72]"Deubiquitination of EGFR by Cezanne-1 contributes to cancer progression."
Pareja F., Ferraro D.A., Rubin C., Cohen-Dvashi H., Zhang F., Aulmann S., Ben-Chetrit N., Pines G., Navon R., Crosetto N., Kostler W., Carvalho S., Lavi S., Schmitt F., Dikic I., Yakhini Z., Sinn P., Mills G.B., Yarden Y.
Oncogene 31:4599-4608(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DEUBIQUITINATION BY OTUD7B.
[73]"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] [Europe PMC] [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.
[74]"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] [Europe PMC] [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.
[75]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 695-1022 IN COMPLEX WITH GW572016, CATALYTIC ACTIVITY, FUNCTION.
[76]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 25-642 IN COMPLEX WITH CETUXIMAB.
[77]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 669-721.
[78]"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] [Europe PMC] [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.
[79]"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] [Europe PMC] [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.
[80]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 695-1022 OF VARIANT MET-790, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANT MET-790.
[81]"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] [Europe PMC] [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.
[82]"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] [Europe PMC] [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.
[83]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 634-677 IN COMPLEX WITH ERBB2, SUBUNIT.
[84]"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] [Europe PMC] [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.
[85]"Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide."
Structural genomics consortium
Submitted (OCT-2010) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 1066-1076 IN COMPLEX WITH CBLB, INTERACTION WITH CBLB.
[86]"Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c."
Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., Yamanashi Y., Yamamoto T., Nakagawa A.
J. Biochem. 152:487-495(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1062-1074 IN COMPLEX WITH CBLC, PHOSPHORYLATION AT TYR-1069, INTERACTION WITH CBLC, MUTAGENESIS OF GLN-1067; ARG-1068 AND TYR-1069.
[87]"High frequency of epidermal growth factor receptor mutations with complex patterns in non-small cell lung cancers related to gefitinib responsiveness in Taiwan."
Huang S.F., Liu H.P., Li L.H., Ku Y.C., Fu Y.N., Tsai H.Y., Chen Y.T., Lin Y.F., Chang W.C., Kuo H.P., Wu Y.C., Chen Y.R., Tsai S.F.
Clin. Cancer Res. 10:8195-8203(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-709; GLY-709; CYS-719; SER-719; 746-GLU--ALA-750 DEL; 746-GLU--THR-751 DELINS ALA; 746-GLU--SER-752 DELINS ASP; 747-LEU--THR-751 DEL; ILE-768; MET-769; VAL-833; LEU-835; VAL-838; ARG-858 AND GLN-861.
[88]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-719 AND ARG-858, POSSIBLE INVOLVEMENT IN LUNG CANCER.
[89]"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] [Europe PMC] [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.
[90]"Distinctive activation patterns in constitutively active and gefitinib-sensitive EGFR mutants."
Chen Y.R., Fu Y.N., Lin C.H., Yang S.T., Hu S.F., Chen Y.T., Tsai S.F., Huang S.F.
Oncogene 25:1205-1215(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS ALA-709; GLY-709; SER-719; ILE-768; VAL-833; LEU-835; VAL-838; ARG-858 AND GLN-861.
[91]"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] [Europe PMC] [Abstract]
Cited for: VARIANT 30-VAL--ARG-297 DEL, POSSIBLE INVOLVEMENT IN LUNG CANCER.
[92]"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] [Europe PMC] [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.
CCDSCCDS47587.1. [P00533-2]
CCDS5514.1. [P00533-1]
CCDS5515.1. [P00533-3]
CCDS5516.1. [P00533-4]
PIRGQHUE. A00641.
RefSeqNP_005219.2. NM_005228.3. [P00533-1]
NP_958439.1. NM_201282.1. [P00533-4]
NP_958440.1. NM_201283.1. [P00533-2]
NP_958441.1. NM_201284.1. [P00533-3]
UniGeneHs.488293.
Hs.605083.

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[»]
2M0BNMR-A/B634-677[»]
2M20NMR-A/B642-697[»]
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/D336-538[»]
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[»]
3QWQX-ray2.75A1-642[»]
3UG1X-ray2.75A695-1022[»]
3UG2X-ray2.50A695-1022[»]
3VJNX-ray2.34A695-1022[»]
3VJOX-ray2.64A695-1022[»]
3VRPX-ray1.52B1062-1074[»]
3VRRX-ray2.00C1062-1074[»]
3W2OX-ray2.35A698-1022[»]
3W2PX-ray2.05A698-1022[»]
3W2QX-ray2.20A698-1022[»]
3W2RX-ray2.05A698-1022[»]
3W2SX-ray1.90A696-1022[»]
3W32X-ray1.80A696-1022[»]
3W33X-ray1.70A696-1022[»]
4G5JX-ray2.80A696-1022[»]
4G5PX-ray3.17A/B696-1022[»]
4HJOX-ray2.75A696-1022[»]
4I1ZX-ray3.00A695-1022[»]
4I20X-ray3.34A695-1022[»]
4I21X-ray3.37A/B695-1022[»]
4I22X-ray1.71A695-1022[»]
4I23X-ray2.80A695-1022[»]
4I24X-ray1.80A/B695-1022[»]
4JQ7X-ray2.73A696-1021[»]
4JQ8X-ray2.83A696-1021[»]
4JR3X-ray2.70A696-1021[»]
4JRVX-ray2.80A696-1021[»]
4KRLX-ray2.85A335-538[»]
4KRMX-ray2.66A/C/E/G/I/K335-538[»]
4KROX-ray3.05A25-642[»]
4KRPX-ray2.82A25-642[»]
4LI5X-ray2.64A696-1020[»]
4LL0X-ray4.00A/B694-1022[»]
4LQMX-ray2.50A694-1022[»]
4LRMX-ray3.53A/B/C/D/E694-1022[»]
DisProtDP00309.
ProteinModelPortalP00533.
SMRP00533. Positions 26-1017.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108276. 469 interactions.
DIPDIP-405N.
IntActP00533. 343 interactions.
MINTMINT-206389.

Chemistry

BindingDBP00533.
ChEMBLCHEMBL2363049.
DrugBankDB00002. Cetuximab.
DB00530. Erlotinib.
DB00317. Gefitinib.
DB01259. Lapatinib.
DB00281. Lidocaine.
DB01269. Panitumumab.
DB00072. Trastuzumab.
GuidetoPHARMACOLOGY1797.

PTM databases

PhosphoSiteP00533.
UniCarbKBP00533.

Polymorphism databases

DMDM2811086.

2D gel databases

SWISS-2DPAGEP00533.

Proteomic databases

MaxQBP00533.
PaxDbP00533.
PeptideAtlasP00533.
PRIDEP00533.

Protocols and materials databases

DNASU1956.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275493; ENSP00000275493; ENSG00000146648. [P00533-1]
ENST00000342916; ENSP00000342376; ENSG00000146648. [P00533-4]
ENST00000344576; ENSP00000345973; ENSG00000146648. [P00533-3]
ENST00000420316; ENSP00000413843; ENSG00000146648. [P00533-2]
GeneID1956.
KEGGhsa:1956.
UCSCuc003tqh.3. human. [P00533-2]
uc003tqi.3. human. [P00533-4]
uc003tqj.3. human. [P00533-3]
uc003tqk.3. human. [P00533-1]

Organism-specific databases

CTD1956.
GeneCardsGC07P055054.
HGNCHGNC:3236. EGFR.
HPACAB000035.
HPA001200.
HPA018530.
MIM131550. gene.
211980. phenotype.
neXtProtNX_P00533.
Orphanet251579. Giant cell glioblastoma.
251576. Gliosarcoma.
357191. Selection of therapeutic option in non-small cell lung carcinoma.
PharmGKBPA7360.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG000490.
InParanoidP00533.
KOK04361.
OMATIANDGC.
PhylomeDBP00533.
TreeFamTF106002.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP00533.

Gene expression databases

ArrayExpressP00533.
BgeeP00533.
GenevestigatorP00533.

Family and domain databases

Gene3D3.80.20.20. 2 hits.
InterProIPR000494. EGF_rcpt_L.
IPR006211. Furin-like_Cys-rich_dom.
IPR006212. Furin_repeat.
IPR009030. Growth_fac_rcpt_N_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016245. Tyr_kinase_EGF/ERB/XmrK_rcpt.
[Graphical view]
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]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF57184. SSF57184. 2 hits.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEGFR. human.
EvolutionaryTraceP00533.
GeneWikiEpidermal_growth_factor_receptor.
GenomeRNAi1956.
NextBio7931.
PMAP-CutDBP00533.
PROP00533.
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: July 9, 2014
This is version 208 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

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

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