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P00533

- EGFR_HUMAN

UniProt

P00533 - EGFR_HUMAN

Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 210 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin.
    Isoform 2 may act as an antagonist of EGF action.

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.6 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Endocytosis and inhibition of the activated EGFR by phosphatases like PTPRJ and PTPRK constitute immediate regulatory mechanisms. Upon EGF-binding phosphorylates EPS15 that regulates EGFR endocytosis and activity. Moreover, inducible feedback inhibitors including LRIG1, SOCS4, SOCS5 and ERRFI1 constitute alternative regulatory mechanisms for the EGFR signaling.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei745 – 7451ATP
    Active sitei837 – 8371Proton acceptorPROSITE-ProRule annotation
    Binding sitei855 – 8551ATP
    Sitei1016 – 10161Important for interaction with PIK3C2B

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi718 – 7269ATP
    Nucleotide bindingi790 – 7912ATP

    GO - Molecular functioni

    1. actin filament binding Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. chromatin binding Source: UniProtKB
    4. double-stranded DNA binding Source: UniProtKB
    5. enzyme binding Source: UniProtKB
    6. epidermal growth factor-activated receptor activity Source: UniProtKB
    7. identical protein binding Source: IntAct
    8. MAP kinase kinase kinase activity Source: UniProtKB
    9. protein binding Source: UniProtKB
    10. protein heterodimerization activity Source: UniProtKB
    11. protein phosphatase binding Source: UniProtKB
    12. protein tyrosine kinase activity Source: UniProtKB
    13. receptor signaling protein tyrosine kinase activity Source: InterPro
    14. transmembrane receptor protein tyrosine kinase activity Source: Reactome
    15. transmembrane signaling receptor activity Source: MGI

    GO - Biological processi

    1. activation of phospholipase A2 activity by calcium-mediated signaling Source: UniProtKB
    2. activation of phospholipase C activity Source: UniProtKB
    3. alkanesulfonate metabolic process Source: Ensembl
    4. astrocyte activation Source: Ensembl
    5. axon guidance Source: Reactome
    6. cell proliferation Source: UniProtKB
    7. cell surface receptor signaling pathway Source: MGI
    8. cellular response to dexamethasone stimulus Source: Ensembl
    9. cellular response to drug Source: Ensembl
    10. cellular response to epidermal growth factor stimulus Source: UniProtKB
    11. cellular response to estradiol stimulus Source: UniProtKB
    12. cellular response to mechanical stimulus Source: Ensembl
    13. cerebral cortex cell migration Source: Ensembl
    14. circadian rhythm Source: Ensembl
    15. digestive tract morphogenesis Source: Ensembl
    16. diterpenoid metabolic process Source: Ensembl
    17. embryonic placenta development Source: Ensembl
    18. epidermal growth factor receptor signaling pathway Source: UniProtKB
    19. Fc-epsilon receptor signaling pathway Source: Reactome
    20. fibroblast growth factor receptor signaling pathway Source: Reactome
    21. hair follicle development Source: Ensembl
    22. hydrogen peroxide metabolic process Source: Ensembl
    23. innate immune response Source: Reactome
    24. learning or memory Source: UniProtKB
    25. liver development Source: Ensembl
    26. lung development Source: Ensembl
    27. magnesium ion homeostasis Source: Ensembl
    28. MAPK cascade Source: GOC
    29. morphogenesis of an epithelial fold Source: Ensembl
    30. negative regulation of apoptotic process Source: UniProtKB
    31. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    32. negative regulation of mitotic cell cycle Source: Ensembl
    33. negative regulation of protein catabolic process Source: UniProtKB
    34. neurotrophin TRK receptor signaling pathway Source: Reactome
    35. ossification Source: UniProtKB
    36. ovulation cycle Source: Ensembl
    37. peptidyl-tyrosine phosphorylation Source: GOC
    38. phosphatidylinositol-mediated signaling Source: Reactome
    39. polysaccharide metabolic process Source: Ensembl
    40. positive regulation of catenin import into nucleus Source: BHF-UCL
    41. positive regulation of cell migration Source: UniProtKB
    42. positive regulation of cell proliferation Source: MGI
    43. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: BHF-UCL
    44. positive regulation of DNA repair Source: UniProtKB
    45. positive regulation of DNA replication Source: UniProtKB
    46. positive regulation of epithelial cell proliferation Source: UniProtKB
    47. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    48. positive regulation of fibroblast proliferation Source: Ensembl
    49. positive regulation of inflammatory response Source: Ensembl
    50. positive regulation of MAP kinase activity Source: UniProtKB
    51. positive regulation of nitric oxide biosynthetic process Source: UniProtKB
    52. positive regulation of phosphorylation Source: UniProtKB
    53. positive regulation of protein kinase B signaling Source: BHF-UCL
    54. positive regulation of protein phosphorylation Source: UniProtKB
    55. positive regulation of smooth muscle cell proliferation Source: Ensembl
    56. positive regulation of superoxide anion generation Source: Ensembl
    57. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    58. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    59. positive regulation of vasoconstriction Source: Ensembl
    60. positive regulation of vasodilation Source: Ensembl
    61. protein autophosphorylation Source: UniProtKB
    62. protein insertion into membrane Source: UniProtKB
    63. regulation of nitric-oxide synthase activity Source: UniProtKB
    64. regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
    65. response to calcium ion Source: Ensembl
    66. response to cobalamin Source: Ensembl
    67. response to hydroxyisoflavone Source: Ensembl
    68. response to osmotic stress Source: Ensembl
    69. response to oxidative stress Source: Ensembl
    70. response to stress Source: UniProtKB
    71. response to UV-A Source: BHF-UCL
    72. salivary gland morphogenesis Source: Ensembl
    73. signal transduction Source: UniProtKB
    74. single organismal cell-cell adhesion Source: UniProtKB
    75. tongue development Source: Ensembl
    76. translation Source: Ensembl

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 2681.
    ReactomeiREACT_115596. Signaling by ERBB4.
    REACT_115720. PLCG1 events in ERBB2 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115854. GRB2 events in ERBB2 signaling.
    REACT_115993. SHC1 events in ERBB2 signaling.
    REACT_116008. PI3K events in ERBB2 signaling.
    REACT_121096. EGFR Transactivation by Gastrin.
    REACT_12478. EGFR interacts with phospholipase C-gamma.
    REACT_12484. EGFR downregulation.
    REACT_12578. GAB1 signalosome.
    REACT_12579. SHC1 events in EGFR signaling.
    REACT_12606. GRB2 events in EGFR signaling.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_22272. Signal transduction by L1.
    REACT_75829. PIP3 activates AKT signaling.
    REACT_9417. Signaling by EGFR.
    SignaLinkiP00533.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:EGFR
    Synonyms:ERBB, ERBB1, HER1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3236. EGFR.

    Subcellular locationi

    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).

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. basolateral plasma membrane Source: BHF-UCL
    3. cell surface Source: Ensembl
    4. cytoplasm Source: UniProtKB
    5. endocytic vesicle Source: Ensembl
    6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    7. endosome Source: UniProtKB
    8. endosome membrane Source: UniProtKB-SubCell
    9. extracellular space Source: UniProtKB
    10. Golgi membrane Source: UniProtKB-SubCell
    11. integral component of membrane Source: UniProtKB-KW
    12. membrane Source: UniProtKB
    13. membrane raft Source: UniProtKB
    14. nuclear membrane Source: UniProtKB-SubCell
    15. nucleus Source: UniProtKB
    16. perinuclear region of cytoplasm Source: Ensembl
    17. plasma membrane Source: HGNC
    18. receptor complex Source: MGI
    19. Shc-EGFR complex Source: BHF-UCL

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The gene represented in this entry is involved in disease pathogenesis.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi275 – 2751Y → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication
    Mutagenesisi287 – 2871F → A: Strongly reduced autophosphorylation and activation of downstream kinases; when associated with A-309. 1 Publication
    Mutagenesisi309 – 3091R → 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. 1 Publication
    Mutagenesisi429 – 4291R → E: Abolishes autophosphorylation and activation of downstream kinases. 1 Publication
    Mutagenesisi587 – 5904DGPH → AGPA: Decreases intramolecular interactions and facilitates EGF binding.
    Mutagenesisi609 – 6091K → A: Decreases intramolecular interactions and facilitates EGF binding. 1 Publication
    Mutagenesisi688 – 6881L → A: Strongly reduced phosphorylation. 2 Publications
    Mutagenesisi689 – 6891V → A: Reduced autophosphorylation. 1 Publication
    Mutagenesisi689 – 6891V → M: Constitutively activated kinase. 1 Publication
    Mutagenesisi690 – 6901E → A: Reduced phosphorylation. 2 Publications
    Mutagenesisi692 – 6921L → A or P: Strongly reduced phosphorylation. 2 Publications
    Mutagenesisi693 – 6931T → A: Increased phosphorylation. 1 Publication
    Mutagenesisi693 – 6931T → D: Strongly reduced phosphorylation. 1 Publication
    Mutagenesisi694 – 6941P → A: Strongly reduced phosphorylation. 1 Publication
    Mutagenesisi699 – 6991P → A: Reduced phosphorylation. 1 Publication
    Mutagenesisi700 – 7001N → A: Abolishes phosphorylation. 1 Publication
    Mutagenesisi704 – 7041L → A: Abolishes phosphorylation. 1 Publication
    Mutagenesisi705 – 7051R → A: Abolishes phosphorylation. 1 Publication
    Mutagenesisi706 – 7061I → A: Abolishes phosphorylation. 1 Publication
    Mutagenesisi745 – 7451K → A or M: Abolishes kinase activity. 1 Publication
    Mutagenesisi974 – 9741D → A: Strongly reduced phosphorylation.
    Mutagenesisi977 – 9771R → A: Reduced phosphorylation. 1 Publication
    Mutagenesisi1005 – 10062ED → RK: Constitutively activated kinase.
    Mutagenesisi1016 – 10161Y → 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. 1 Publication
    Mutagenesisi1067 – 10671Q → G: No effect on interaction with CBLC. 1 Publication
    Mutagenesisi1068 – 10681R → G: Strongly decreases interaction with CBLC. 1 Publication
    Mutagenesisi1069 – 10691Y → F: Abolishes interaction with CBLC. 1 Publication
    Mutagenesisi1092 – 10921Y → F: No change in interaction with PIK3C2B. Abolishes interaction with PIK3C2B; when associated with F-1197 and F-1016. 1 Publication
    Mutagenesisi1110 – 11101Y → F: No change in interaction with PIK3C2B. 1 Publication
    Mutagenesisi1172 – 11721Y → F: No change in interaction with PIK3C2B. 1 Publication
    Mutagenesisi1197 – 11971Y → 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. 1 Publication

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi211980. phenotype.
    Orphaneti251579. Giant cell glioblastoma.
    251576. Gliosarcoma.
    357191. Selection of therapeutic option in non-small cell lung carcinoma.
    PharmGKBiPA7360.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24242 PublicationsAdd
    BLAST
    Chaini25 – 12101186Epidermal growth factor receptorPRO_0000016665Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 58
    Glycosylationi56 – 561N-linked (GlcNAc...) (complex); partial; atypical5 PublicationsCAR_000227
    Glycosylationi73 – 731N-linked (GlcNAc...); atypical1 Publication
    Glycosylationi128 – 1281N-linked (GlcNAc...)3 Publications
    Disulfide bondi157 ↔ 187
    Glycosylationi175 – 1751N-linked (GlcNAc...)5 Publications
    Disulfide bondi190 ↔ 199
    Disulfide bondi194 ↔ 207
    Glycosylationi196 – 1961N-linked (GlcNAc...)4 Publications
    Disulfide bondi215 ↔ 223
    Disulfide bondi219 ↔ 231
    Modified residuei229 – 2291Phosphoserine1 Publication
    Disulfide bondi232 ↔ 240
    Disulfide bondi236 ↔ 248
    Disulfide bondi251 ↔ 260
    Disulfide bondi264 ↔ 291
    Disulfide bondi295 ↔ 307
    Disulfide bondi311 ↔ 326
    Disulfide bondi329 ↔ 333
    Disulfide bondi337 ↔ 362
    Glycosylationi352 – 3521N-linked (GlcNAc...)7 Publications
    Glycosylationi361 – 3611N-linked (GlcNAc...)6 Publications
    Glycosylationi413 – 4131N-linked (GlcNAc...)4 Publications
    Glycosylationi444 – 4441N-linked (GlcNAc...)6 Publications
    Disulfide bondi470 ↔ 499
    Disulfide bondi506 ↔ 515
    Disulfide bondi510 ↔ 523
    Disulfide bondi526 ↔ 535
    Glycosylationi528 – 5281N-linked (GlcNAc...)5 Publications
    Disulfide bondi539 ↔ 555
    Disulfide bondi558 ↔ 571
    Disulfide bondi562 ↔ 579
    Glycosylationi568 – 5681N-linked (GlcNAc...); partial5 Publications
    Disulfide bondi582 ↔ 591
    Disulfide bondi595 ↔ 617
    Glycosylationi603 – 6031N-linked (GlcNAc...); partial4 Publications
    Disulfide bondi620 ↔ 628
    Glycosylationi623 – 6231N-linked (GlcNAc...) (high mannose)1 Publication
    Disulfide bondi624 ↔ 636
    Modified residuei678 – 6781Phosphothreonine; by PKC and PKD/PRKD11 Publication
    Modified residuei693 – 6931Phosphothreonine; by PKD/PRKD15 Publications
    Modified residuei695 – 6951Phosphoserine2 Publications
    Cross-linki716 – 716Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki737 – 737Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki754 – 754Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki867 – 867Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki929 – 929Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki970 – 970Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei991 – 9911Phosphoserine3 Publications
    Modified residuei995 – 9951Phosphoserine1 Publication
    Modified residuei998 – 9981Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1016 – 10161Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei1026 – 10261Phosphoserine1 Publication
    Modified residuei1039 – 10391Phosphoserine1 Publication
    Modified residuei1041 – 10411Phosphothreonine1 Publication
    Modified residuei1042 – 10421Phosphoserine1 Publication
    Modified residuei1064 – 10641Phosphoserine3 Publications
    Modified residuei1069 – 10691Phosphotyrosine1 Publication
    Modified residuei1070 – 10701Phosphoserine1 Publication
    Modified residuei1071 – 10711Phosphoserine1 Publication
    Modified residuei1081 – 10811Phosphoserine1 Publication
    Modified residuei1092 – 10921Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei1110 – 11101Phosphotyrosine; by autocatalysis2 Publications
    Modified residuei1166 – 11661Phosphoserine2 Publications
    Modified residuei1172 – 11721Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei1197 – 11971Phosphotyrosine; by autocatalysis5 Publications
    Modified residuei1199 – 11991Omega-N-methylated arginine1 Publication

    Post-translational modificationi

    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 PTPN2.11 Publications
    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.3 Publications
    Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.6 Publications

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP00533.
    PaxDbiP00533.
    PeptideAtlasiP00533.
    PRIDEiP00533.

    2D gel databases

    SWISS-2DPAGEP00533.

    PTM databases

    PhosphoSiteiP00533.
    UniCarbKBiP00533.

    Miscellaneous databases

    PMAP-CutDBP00533.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.1 Publication

    Gene expression databases

    ArrayExpressiP00533.
    BgeeiP00533.
    GenevestigatoriP00533.

    Organism-specific databases

    HPAiCAB000035.
    HPA001200.
    HPA018530.

    Interactioni

    Subunit structurei

    Binding of the ligand triggers homo- and/or heterodimerization of the receptor triggering its autophosphorylation. Heterodimer with ERBB2. Interacts with ERRFI1; inhibits dimerization of the kinase domain and autophosphorylation. Part of a complex with ERBB2 and either PIK3C2A or PIK3C2B. Interacts with GRB2; an adapter protein coupling the receptor to downstream signaling pathways. Interacts with GAB2; involved in signaling downstream of EGFR. Interacts with STAT3; mediates EGFR downstream signaling in cell proliferation. Interacts with RIPK1; involved in NF-kappa-B activation. Interacts (autophosphorylated) with CBL, CBLB and CBLC; involved in EGFR ubiquitination and regulation. Interacts with SOCS5; regulates EGFR degradation through TCEB1- and TCEB2-mediated ubiquitination and proteasomal degradation. Interacts with PRMT5; methylates EGFR and enhances interaction with PTPN6. Interacts (phosphorylated) with PTPN6; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with COPG1; essential for regulation of EGF-dependent nuclear transport of EGFR by retrograde trafficking from the Golgi to the ER. Interacts with TNK2; this interaction is dependent on EGF stimulation and kinase activity of EGFR. Interacts with PCNA; positively regulates PCNA. Interacts with PELP1. Interacts with MUC1. Interacts with AP2M1. Interacts with FER. 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).35 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself22EBI-297353,EBI-297353
    Q53FC73EBI-297353,EBI-9356749
    Q96BE02EBI-297353,EBI-9356686
    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.
    CDC37Q165439EBI-297353,EBI-295634
    CDH1P128302EBI-297353,EBI-727477
    CLNKQ7Z7G12EBI-297353,EBI-7878194
    CRKP461082EBI-297353,EBI-886
    CRKLP461092EBI-297353,EBI-910
    CTNNA1P352214EBI-297353,EBI-701918
    CYTH2Q994185EBI-297353,EBI-448974
    DOK6Q6PKX42EBI-297353,EBI-2880244
    EGFP0113316EBI-297353,EBI-640857
    ERBB2P0462618EBI-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
    HSP90AB1Q6PK502EBI-297353,EBI-9356629
    HSPA1BP081075EBI-297353,EBI-629985
    HSPA9P386464EBI-297353,EBI-354932
    HSPB1P047923EBI-297353,EBI-352682
    IGFBP3P179363EBI-297353,EBI-715709
    IQGAP1P469404EBI-297353,EBI-297509
    IRS4O146542EBI-297353,EBI-356594
    LRRK1Q38SD22EBI-297353,EBI-1050422
    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
    PIK3R1P279865EBI-297353,EBI-79464
    PIK3R2O004592EBI-297353,EBI-346930
    PIK3R3Q925695EBI-297353,EBI-79893
    PLCG1P191746EBI-297353,EBI-79387
    PLCG2P168853EBI-297353,EBI-617403
    PrkdcP973134EBI-297353,EBI-2272005From a different organism.
    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
    STAT3P4076313EBI-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

    Protein-protein interaction databases

    BioGridi108276. 516 interactions.
    DIPiDIP-405N.
    IntActiP00533. 357 interactions.
    MINTiMINT-206389.

    Structurei

    Secondary structure

    1
    1210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 434
    Helixi44 – 5512
    Beta strandi59 – 6810
    Helixi77 – 815
    Beta strandi84 – 874
    Beta strandi89 – 935
    Helixi101 – 1033
    Turni114 – 1163
    Beta strandi117 – 1226
    Beta strandi125 – 1295
    Beta strandi145 – 1528
    Helixi159 – 1613
    Helixi164 – 1663
    Helixi170 – 1734
    Helixi195 – 1973
    Beta strandi199 – 2035
    Helixi204 – 2063
    Beta strandi211 – 2144
    Beta strandi223 – 2275
    Helixi228 – 2303
    Beta strandi236 – 24510
    Beta strandi248 – 2569
    Beta strandi259 – 2635
    Beta strandi267 – 2704
    Turni272 – 2743
    Beta strandi275 – 2795
    Beta strandi285 – 2873
    Beta strandi290 – 2945
    Turni296 – 2983
    Beta strandi299 – 3013
    Beta strandi305 – 3106
    Beta strandi313 – 3153
    Beta strandi318 – 3203
    Beta strandi323 – 3253
    Beta strandi330 – 3323
    Beta strandi336 – 3383
    Turni340 – 3423
    Helixi343 – 3453
    Beta strandi349 – 3513
    Turni353 – 3553
    Helixi356 – 3594
    Beta strandi363 – 3675
    Beta strandi369 – 3713
    Helixi373 – 3775
    Turni380 – 3834
    Helixi389 – 3979
    Beta strandi400 – 4034
    Beta strandi405 – 4073
    Helixi418 – 4203
    Turni433 – 4353
    Beta strandi436 – 4427
    Beta strandi458 – 4647
    Helixi472 – 4743
    Helixi477 – 4804
    Beta strandi481 – 4833
    Beta strandi488 – 4947
    Helixi496 – 5016
    Turni507 – 5093
    Beta strandi515 – 5195
    Helixi520 – 5223
    Beta strandi523 – 5264
    Beta strandi531 – 5333
    Beta strandi535 – 5373
    Beta strandi541 – 5466
    Beta strandi548 – 5514
    Beta strandi554 – 5574
    Beta strandi560 – 5623
    Beta strandi566 – 5683
    Beta strandi570 – 5756
    Beta strandi578 – 58710
    Beta strandi590 – 5945
    Beta strandi597 – 5993
    Helixi602 – 6043
    Beta strandi607 – 6115
    Beta strandi615 – 6195
    Beta strandi629 – 6324
    Helixi633 – 6353
    Beta strandi643 – 6464
    Helixi648 – 66922
    Beta strandi671 – 6733
    Helixi679 – 6846
    Helixi685 – 6873
    Beta strandi688 – 6925
    Beta strandi694 – 6974
    Beta strandi703 – 7064
    Helixi709 – 7113
    Beta strandi712 – 72110
    Beta strandi724 – 7318
    Turni734 – 7363
    Beta strandi740 – 7467
    Beta strandi748 – 7503
    Turni753 – 7553
    Helixi756 – 76813
    Beta strandi772 – 7743
    Beta strandi777 – 79115
    Beta strandi794 – 7974
    Helixi798 – 8047
    Helixi806 – 8083
    Helixi811 – 83020
    Helixi840 – 8423
    Beta strandi843 – 8475
    Beta strandi850 – 8534
    Helixi858 – 8625
    Turni863 – 8653
    Helixi867 – 8715
    Beta strandi873 – 8775
    Helixi878 – 8803
    Helixi883 – 8886
    Helixi893 – 90816
    Turni909 – 9113
    Turni914 – 9174
    Helixi920 – 9223
    Helixi923 – 9286
    Beta strandi937 – 9393
    Helixi941 – 95010
    Helixi955 – 9573
    Helixi961 – 97212
    Helixi975 – 9784
    Helixi984 – 9863
    Turni992 – 9943
    Helixi996 – 10027
    Beta strandi1004 – 10107
    Helixi1013 – 10164
    Beta strandi1068 – 10703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    DisProtiDP00309.
    ProteinModelPortaliP00533.
    SMRiP00533. Positions 26-1017.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00533.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 645621ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini669 – 1210542CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei646 – 66823HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati75 – 300226ApproximateAdd
    BLAST
    Repeati390 – 600211ApproximateAdd
    BLAST
    Domaini712 – 979268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni688 – 70417Important for dimerization, phosphorylation and activationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG000490.
    InParanoidiP00533.
    KOiK04361.
    OMAiTIANDGC.
    PhylomeDBiP00533.
    TreeFamiTF106002.

    Family and domain databases

    Gene3Di3.80.20.20. 2 hits.
    InterProiIPR000494. 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]
    PfamiPF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00261. FU. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P00533-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS     50
    LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP 100
    LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF 150
    SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW 200
    GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV 250
    CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 300
    VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS 350
    INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE 400
    ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL 450
    RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK 500
    ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN LLEGEPREFV 550
    ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM 600
    GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM 650
    VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN 700
    QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA 750
    TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD 800
    YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH 850
    VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY 900
    GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC 950
    WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA 1000
    LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI 1050
    DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR 1100
    PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST 1150
    FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV 1200
    APQSSEFIGA 1210
    Length:1,210
    Mass (Da):134,277
    Last modified:November 1, 1997 - v2
    Checksum:iD8A2A50B4EFB6ED2
    GO
    Isoform 2 (identifier: P00533-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:405
    Mass (Da):44,664
    Checksum:iF5DEB31787EF1822
    GO
    Isoform 3 (identifier: P00533-3) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:705
    Mass (Da):77,312
    Checksum:i4CF149492FF1650C
    GO
    Isoform 4 (identifier: P00533-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:628
    Mass (Da):69,228
    Checksum:i3A00A5511A3B6AE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti540 – 5401N → K in CAA25240. (PubMed:6328312)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 297268Missing Variant EGFR vIII; found in a lung cancer sample; somatic mutation; induces lung cancer when exogenously expressed. 1 Publication
    VAR_066493Add
    BLAST
    Natural varianti98 – 981R → Q.1 Publication
    Corresponds to variant rs17289589 [ dbSNP | Ensembl ].
    VAR_019293
    Natural varianti266 – 2661P → R.1 Publication
    Corresponds to variant rs17336639 [ dbSNP | Ensembl ].
    VAR_019294
    Natural varianti521 – 5211R → K.2 Publications
    Corresponds to variant rs2227983 [ dbSNP | Ensembl ].
    VAR_019295
    Natural varianti674 – 6741V → I Slightly increased autophosphorylation. 1 Publication
    Corresponds to variant rs17337079 [ dbSNP | Ensembl ].
    VAR_019296
    Natural varianti709 – 7091E → A Found in a lung cancer sample; more sensitive to gefitinib than wild-type. 2 Publications
    VAR_026084
    Natural varianti709 – 7091E → G Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. 1 Publication
    VAR_069498
    Natural varianti709 – 7091E → K Found in a lung cancer sample. 1 Publication
    VAR_026085
    Natural varianti719 – 7191G → A Found in a lung cancer sample. 1 Publication
    VAR_026086
    Natural varianti719 – 7191G → C Found in a lung cancer sample. 2 Publications
    Corresponds to variant rs28929495 [ dbSNP | Ensembl ].
    VAR_026087
    Natural varianti719 – 7191G → D Found in a lung cancer sample. 1 Publication
    VAR_026088
    Natural varianti719 – 7191G → 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. 3 Publications
    VAR_019297
    Natural varianti724 – 7241G → S Found in a lung cancer sample. 1 Publication
    VAR_026089
    Natural varianti734 – 7341E → K Found in a lung cancer sample. 1 Publication
    VAR_026090
    Natural varianti746 – 7527ELREATS → D Found in a lung cancer sample.
    VAR_069499
    Natural varianti746 – 7516ELREAT → A Found in a lung cancer sample.
    VAR_069500
    Natural varianti746 – 7505Missing Found in a lung cancer sample.
    VAR_026092
    Natural varianti746 – 7461Missing Found in a lung cancer sample. 1 Publication
    VAR_026091
    Natural varianti747 – 7515Missing Found in a lung cancer sample.
    VAR_069501
    Natural varianti747 – 7493Missing Found in a lung cancer sample. 1 Publication
    VAR_026094
    Natural varianti747 – 7471L → F Found in a lung cancer sample. 1 Publication
    VAR_026093
    Natural varianti748 – 7481R → P Found in a lung cancer sample. 1 Publication
    VAR_026095
    Natural varianti752 – 7598Missing Found in a lung cancer sample.
    VAR_026096
    Natural varianti768 – 7681S → I Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. 1 Publication
    Corresponds to variant rs121913465 [ dbSNP | Ensembl ].
    VAR_069502
    Natural varianti769 – 7691V → M Found in a lung cancer sample. 1 Publication
    Corresponds to variant rs147149347 [ dbSNP | Ensembl ].
    VAR_069503
    Natural varianti787 – 7871Q → R Found in a lung cancer sample. 1 Publication
    VAR_026097
    Natural varianti790 – 7901T → M Found in a lung cancer sample; increased kinase activity. 1 Publication
    VAR_026098
    Natural varianti833 – 8331L → V Found in a lung cancer sample; more sensitive to gefitinib than wild-type. 2 Publications
    VAR_026099
    Natural varianti834 – 8341V → L Found in a lung cancer sample. 1 Publication
    VAR_026100
    Natural varianti835 – 8351H → L Found in a lung cancer sample; more sensitive to gefitinib than wild-type. 1 Publication
    VAR_069504
    Natural varianti838 – 8381L → V Found in a lung cancer sample; more sensitive to gefitinib than wild-type. 1 Publication
    VAR_069505
    Natural varianti858 – 8581L → M Found in a lung cancer sample. 1 Publication
    VAR_026101
    Natural varianti858 – 8581L → R Found in a lung cancer sample; somatic mutation; constitutively activated enzyme with strongly increased kinase activity; more sensitive to gefitinib than wild-type. 3 Publications
    Corresponds to variant rs121434568 [ dbSNP | Ensembl ].
    VAR_019298
    Natural varianti861 – 8611L → Q Found in a lung cancer sample; constitutively activated kinase with higher levels of basal autophosphorylation; more sensitive to gefitinib than wild-type. 2 Publications
    Corresponds to variant rs121913444 [ dbSNP | Ensembl ].
    VAR_026102
    Natural varianti873 – 8731G → E Found in a lung cancer sample. 1 Publication
    VAR_026103
    Natural varianti962 – 9621R → G.1 Publication
    Corresponds to variant rs17337451 [ dbSNP | Ensembl ].
    VAR_019299
    Natural varianti988 – 9881H → P.1 Publication
    Corresponds to variant rs17290699 [ dbSNP | Ensembl ].
    VAR_019300
    Natural varianti1034 – 10341L → R.1 Publication
    Corresponds to variant rs34352568 [ dbSNP | Ensembl ].
    VAR_042095
    Natural varianti1210 – 12101A → V.1 Publication
    Corresponds to variant rs35918369 [ dbSNP | Ensembl ].
    VAR_042096

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei404 – 4052FL → LS in isoform 2. 4 PublicationsVSP_002887
    Alternative sequencei406 – 1210805Missing in isoform 2. 4 PublicationsVSP_002888Add
    BLAST
    Alternative sequencei628 – 70578CTGPG…QALLR → PGNESLKAMLFCLFKLSSCN QSNDGSVSHQSGSPAAQESC LGWIPSLLPSEFQLGWGGCS HLHAWPSASVIITASSCH in isoform 3. 1 PublicationVSP_002889Add
    BLAST