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P00533

- EGFR_HUMAN

UniProt

P00533 - EGFR_HUMAN

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Protein

Epidermal growth factor receptor

Gene

EGFR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 heterodimerization activity Source: UniProtKB
  10. protein phosphatase binding Source: UniProtKB
  11. protein tyrosine kinase activity Source: UniProtKB
  12. receptor signaling protein tyrosine kinase activity Source: InterPro
  13. transmembrane receptor protein tyrosine kinase activity Source: Reactome
  14. transmembrane signaling receptor activity Source: MGI
  15. ubiquitin protein ligase binding Source: UniProtKB

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

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 Source: UniProtKB-KW
  7. endosome Source: UniProtKB
  8. endosome membrane Source: UniProtKB
  9. extracellular space Source: UniProtKB
  10. focal adhesion Source: UniProtKB
  11. Golgi apparatus Source: UniProtKB-KW
  12. integral component of membrane Source: UniProtKB-KW
  13. membrane Source: UniProtKB
  14. membrane raft Source: UniProtKB
  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
Complete GO annotation...

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. 1 Publication
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. 1 Publication
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-methylarginine1 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. Ubiquitinated by RNF115 and RNF126 (By similarity).By similarity3 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

BgeeiP00533.
ExpressionAtlasiP00533. baseline and differential.
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). Interacts with RNF115 and RNF126.36 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself23EBI-297353,EBI-297353
Q53FC73EBI-297353,EBI-9356749
Q96BE02EBI-297353,EBI-9356686
ABL1P005192EBI-297353,EBI-375543
ABL2P426848EBI-297353,EBI-1102694
AHNAKQ096663EBI-297353,EBI-2555881
AKAP12Q029522EBI-297353,EBI-2562430
ANKS1AQ926255EBI-297353,EBI-1048612
AP2M1Q96CW14EBI-297353,EBI-297683
APBB1O002134EBI-297353,EBI-81694
APBB2Q928706EBI-297353,EBI-79277
APBB3O957042EBI-297353,EBI-286427
APPL1Q9UKG12EBI-297353,EBI-741243
AURKAO149654EBI-297353,EBI-448680
BECN1Q144577EBI-297353,EBI-949378
BLKP514512EBI-297353,EBI-2105445
CALM3P621584EBI-297353,EBI-397435
Calm3P621616EBI-297353,EBI-397530From a different organism.
CAMLGP490692EBI-297353,EBI-1748958
CAV1Q031355EBI-297353,EBI-603614
CBLP2268117EBI-297353,EBI-518228
CblP226822EBI-297353,EBI-640919From a different organism.
CDC37Q165439EBI-297353,EBI-295634
CDH1P128303EBI-297353,EBI-727477
CISHQ9NSE23EBI-297353,EBI-617866
CLNKQ7Z7G12EBI-297353,EBI-7878194
CRKP461083EBI-297353,EBI-886
CRKP46108-13EBI-297353,EBI-287556
CRKLP461093EBI-297353,EBI-910
CTNNA1P352214EBI-297353,EBI-701918
CTNND1O607164EBI-297353,EBI-701927
CTTNQ142473EBI-297353,EBI-351886
CYTH2Q994185EBI-297353,EBI-448974
DOK6Q6PKX42EBI-297353,EBI-2880244
EGFP0113316EBI-297353,EBI-640857
EPS8Q129292EBI-297353,EBI-375576
ERBB2P0462620EBI-297353,EBI-641062
ERBB3P2186012EBI-297353,EBI-720706
ERBB4Q153032EBI-297353,EBI-80371
ERRFI1Q9UJM38EBI-297353,EBI-2941912
ESR1P033722EBI-297353,EBI-78473
ESR1P03372-44EBI-297353,EBI-4309277
FGRP097692EBI-297353,EBI-1383732
FKBP8Q143183EBI-297353,EBI-724839
GAB1Q134803EBI-297353,EBI-517684
GABARAPL2P605202EBI-297353,EBI-720116
GAPDHP044066EBI-297353,EBI-354056
GRAP2O757912EBI-297353,EBI-740418
GRB2P6299332EBI-297353,EBI-401755
HCKP086312EBI-297353,EBI-346340
HDAC6Q9UBN711EBI-297353,EBI-301697
HDAC7Q8WUI42EBI-297353,EBI-1048378
HSP90AA1P079005EBI-297353,EBI-296047
HSP90AB1P082388EBI-297353,EBI-352572
HSP90AB1Q6PK502EBI-297353,EBI-9356629
HSPA1BP081076EBI-297353,EBI-629985
HSPA8P111425EBI-297353,EBI-351896
HSPA9P386464EBI-297353,EBI-354932
HSPB1P047923EBI-297353,EBI-352682
IGFBP3P179363EBI-297353,EBI-715709
IQGAP1P469404EBI-297353,EBI-297509
IRS4O146542EBI-297353,EBI-356594
LATO435612EBI-297353,EBI-1222766
LCP2Q130942EBI-297353,EBI-346946
LRRK1Q38SD22EBI-297353,EBI-1050422
LYNP079486EBI-297353,EBI-79452
LYNP07948-12EBI-297353,EBI-6895930
MAPK8IP1Q9UQF23EBI-297353,EBI-78404
MAPK8IP2Q133874EBI-297353,EBI-722813
MAST1Q9Y2H92EBI-297353,EBI-3385920
METP085817EBI-297353,EBI-1039152
MUC1P159413EBI-297353,EBI-2804728
NCK1P163333EBI-297353,EBI-389883
NR3C1P041502EBI-297353,EBI-493507
PDGFRAP162343EBI-297353,EBI-2861522
PIK3C2BO007509EBI-297353,EBI-641107
PIK3R1P279865EBI-297353,EBI-79464
PIK3R2O004593EBI-297353,EBI-346930
PIK3R3Q925696EBI-297353,EBI-79893
PLCG1P191746EBI-297353,EBI-79387
PLCG2P168855EBI-297353,EBI-617403
PRKCAP172522EBI-297353,EBI-1383528
PrkdcP973134EBI-297353,EBI-2272005From a different organism.
PTK2Q053973EBI-297353,EBI-702142
PTPN1P180316EBI-297353,EBI-968788
Ptpn1P2041711EBI-297353,EBI-916819From a different organism.
PTPN12Q052093EBI-297353,EBI-2266035
PTPN22Q9Y2R22EBI-297353,EBI-1211241
RABGEF1Q9UJ414EBI-297353,EBI-913954
RAPH1Q70E732EBI-297353,EBI-3940924
RASA1P209367EBI-297353,EBI-1026476
RIN1Q136713EBI-297353,EBI-366017
ROR1Q019738EBI-297353,EBI-6082337
SFNP319478EBI-297353,EBI-476295
SH2B1Q9NRF22EBI-297353,EBI-310491
SH2B3Q9UQQ22EBI-297353,EBI-7879749
SH2D3AQ9BRG22EBI-297353,EBI-2339271
SHC1P2935326EBI-297353,EBI-78835
SHC1P29353-74EBI-297353,EBI-9691288
SHC2P980773EBI-297353,EBI-7256023
SHC4Q6S5L82EBI-297353,EBI-9453524
SLAQ132392EBI-297353,EBI-726214
SLC5A1P138663EBI-297353,EBI-1772443
SRCP129317EBI-297353,EBI-621482
STAT1P422246EBI-297353,EBI-1057697
STAT3P4076314EBI-297353,EBI-518675
STAT5AP422293EBI-297353,EBI-749537
STIP1P319482EBI-297353,EBI-1054052
STUB1Q9UNE73EBI-297353,EBI-357085
SYKP434056EBI-297353,EBI-78302
TGFAP011352EBI-297353,EBI-1034374
TLN1Q9Y4902EBI-297353,EBI-2462036
TLR2O606032EBI-297353,EBI-973722
TNS3Q68CZ24EBI-297353,EBI-1220488
TOM1L1O756746EBI-297353,EBI-712991
TRAF2Q129333EBI-297353,EBI-355744
Trpv3Q8K4242EBI-297353,EBI-2650739From a different organism.
TUBA1AQ71U363EBI-297353,EBI-302552
TXNP105994EBI-297353,EBI-594644
UCHL1P099362EBI-297353,EBI-714860
VAPAQ9P0L02EBI-297353,EBI-1059156
YES1P079473EBI-297353,EBI-515331
YWHAQP273486EBI-297353,EBI-359854
YWHAZP631045EBI-297353,EBI-347088
ZAP70P434032EBI-297353,EBI-1211276

Protein-protein interaction databases

BioGridi108276. 524 interactions.
DIPiDIP-405N.
IntActiP00533. 430 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.
GeneTreeiENSGT00760000118799.
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

        10         20         30         40         50
MRPSGTAGAA LLALLAALCP ASRALEEKKV CQGTSNKLTQ LGTFEDHFLS
60 70 80 90 100
LQRMFNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP
110 120 130 140 150
LENLQIIRGN MYYENSYALA VLSNYDANKT GLKELPMRNL QEILHGAVRF
160 170 180 190 200
SNNPALCNVE SIQWRDIVSS DFLSNMSMDF QNHLGSCQKC DPSCPNGSCW
210 220 230 240 250
GAGEENCQKL TKIICAQQCS GRCRGKSPSD CCHNQCAAGC TGPRESDCLV
260 270 280 290 300
CRKFRDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
310 320 330 340 350
VTDHGSCVRA CGADSYEMEE DGVRKCKKCE GPCRKVCNGI GIGEFKDSLS
360 370 380 390 400
INATNIKHFK NCTSISGDLH ILPVAFRGDS FTHTPPLDPQ ELDILKTVKE
410 420 430 440 450
ITGFLLIQAW PENRTDLHAF ENLEIIRGRT KQHGQFSLAV VSLNITSLGL
460 470 480 490 500
RSLKEISDGD VIISGNKNLC YANTINWKKL FGTSGQKTKI ISNRGENSCK
510 520 530 540 550
ATGQVCHALC SPEGCWGPEP RDCVSCRNVS RGRECVDKCN LLEGEPREFV
560 570 580 590 600
ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGVM
610 620 630 640 650
GENNTLVWKY ADAGHVCHLC HPNCTYGCTG PGLEGCPTNG PKIPSIATGM
660 670 680 690 700
VGALLLLLVV ALGIGLFMRR RHIVRKRTLR RLLQERELVE PLTPSGEAPN
710 720 730 740 750
QALLRILKET EFKKIKVLGS GAFGTVYKGL WIPEGEKVKI PVAIKELREA
760 770 780 790 800
TSPKANKEIL DEAYVMASVD NPHVCRLLGI CLTSTVQLIT QLMPFGCLLD
810 820 830 840 850
YVREHKDNIG SQYLLNWCVQ IAKGMNYLED RRLVHRDLAA RNVLVKTPQH
860 870 880 890 900
VKITDFGLAK LLGAEEKEYH AEGGKVPIKW MALESILHRI YTHQSDVWSY
910 920 930 940 950
GVTVWELMTF GSKPYDGIPA SEISSILEKG ERLPQPPICT IDVYMIMVKC
960 970 980 990 1000
WMIDADSRPK FRELIIEFSK MARDPQRYLV IQGDERMHLP SPTDSNFYRA
1010 1020 1030 1040 1050
LMDEEDMDDV VDADEYLIPQ QGFFSSPSTS RTPLLSSLSA TSNNSTVACI
1060 1070 1080 1090 1100
DRNGLQSCPI KEDSFLQRYS SDPTGALTED SIDDTFLPVP EYINQSVPKR
1110 1120 1130 1140 1150
PAGSVQNPVY HNQPLNPAPS RDPHYQDPHS TAVGNPEYLN TVQPTCVNST
1160 1170 1180 1190 1200
FDSPAHWAQK GSHQISLDNP DYQQDFFPKE AKPNGIFKGS TAENAEYLRV
1210
APQSSEFIGA
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. 1 Publication
VAR_069499
Natural varianti746 – 7516ELREAT → A Found in a lung cancer sample. 1 Publication
VAR_069500
Natural varianti746 – 7505Missing Found in a lung cancer sample. 1 Publication
VAR_026092
Natural varianti746 – 7461Missing Found in a lung cancer sample. 1 Publication
VAR_026091
Natural varianti747 – 7515Missing Found in a lung cancer sample. 1 Publication
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. 1 Publication
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