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Q01279

- EGFR_MOUSE

UniProt

Q01279 - EGFR_MOUSE

Protein

Epidermal growth factor receptor

Gene

Egfr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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.2 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei747 – 7471ATPPROSITE-ProRule annotation
    Active sitei839 – 8391Proton acceptorPROSITE-ProRule annotation
    Binding sitei857 – 8571ATPPROSITE-ProRule annotation
    Sitei1018 – 10181Important for interaction with PIK3C2BBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi720 – 7289ATPPROSITE-ProRule annotation
    Nucleotide bindingi792 – 7932ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. chromatin binding Source: UniProtKB
    3. epidermal growth factor-activated receptor activity Source: MGI
    4. kinase activity Source: MGI
    5. nitric-oxide synthase regulator activity Source: Ensembl
    6. protein binding Source: UniProtKB
    7. protein tyrosine kinase activity Source: UniProtKB
    8. receptor signaling protein tyrosine kinase activity Source: InterPro
    9. signal transducer activity Source: MGI

    GO - Biological processi

    1. activation of MAPKK activity Source: Ensembl
    2. alkanesulfonate metabolic process Source: Ensembl
    3. astrocyte activation Source: Ensembl
    4. cell morphogenesis Source: MGI
    5. cell proliferation Source: Ensembl
    6. cellular response to amino acid stimulus Source: UniProtKB
    7. cellular response to dexamethasone stimulus Source: Ensembl
    8. cellular response to drug Source: Ensembl
    9. cellular response to estradiol stimulus Source: UniProtKB
    10. cellular response to growth factor stimulus Source: Ensembl
    11. cellular response to mechanical stimulus Source: Ensembl
    12. cerebral cortex cell migration Source: MGI
    13. circadian rhythm Source: Ensembl
    14. digestive tract morphogenesis Source: MGI
    15. diterpenoid metabolic process Source: Ensembl
    16. embryonic placenta development Source: MGI
    17. epidermal growth factor receptor signaling pathway Source: MGI
    18. epidermis development Source: MGI
    19. hair follicle development Source: MGI
    20. hydrogen peroxide metabolic process Source: Ensembl
    21. liver development Source: Ensembl
    22. lung development Source: Ensembl
    23. magnesium ion homeostasis Source: Ensembl
    24. morphogenesis of an epithelial fold Source: MGI
    25. negative regulation of apoptotic process Source: Ensembl
    26. negative regulation of mitotic cell cycle Source: Ensembl
    27. negative regulation of protein catabolic process Source: Ensembl
    28. neuron projection morphogenesis Source: Ensembl
    29. ovulation cycle Source: Ensembl
    30. polysaccharide metabolic process Source: Ensembl
    31. positive regulation of catenin import into nucleus Source: Ensembl
    32. positive regulation of cell migration Source: Ensembl
    33. positive regulation of cell proliferation Source: MGI
    34. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
    35. positive regulation of DNA repair Source: Ensembl
    36. positive regulation of DNA replication Source: Ensembl
    37. positive regulation of epithelial cell proliferation Source: MGI
    38. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    39. positive regulation of fibroblast proliferation Source: BHF-UCL
    40. positive regulation of inflammatory response Source: Ensembl
    41. positive regulation of MAP kinase activity Source: Ensembl
    42. positive regulation of nitric oxide biosynthetic process Source: Ensembl
    43. positive regulation of protein kinase B signaling Source: Ensembl
    44. positive regulation of protein phosphorylation Source: UniProtKB
    45. positive regulation of smooth muscle cell proliferation Source: Ensembl
    46. positive regulation of superoxide anion generation Source: Ensembl
    47. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
    48. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    49. positive regulation of vasoconstriction Source: Ensembl
    50. positive regulation of vasodilation Source: Ensembl
    51. protein autophosphorylation Source: MGI
    52. regulation of cell proliferation Source: MGI
    53. regulation of nitric-oxide synthase activity Source: Ensembl
    54. regulation of peptidyl-tyrosine phosphorylation Source: MGI
    55. response to calcium ion Source: Ensembl
    56. response to cobalamin Source: Ensembl
    57. response to hydroxyisoflavone Source: Ensembl
    58. response to osmotic stress Source: Ensembl
    59. response to oxidative stress Source: Ensembl
    60. response to UV-A Source: Ensembl
    61. salivary gland morphogenesis Source: MGI
    62. signal transduction Source: MGI
    63. single organismal cell-cell adhesion Source: Ensembl
    64. tongue development Source: Ensembl
    65. 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. 3474.
    ReactomeiREACT_188190. PLCG1 events in ERBB2 signaling.
    REACT_188191. Signaling by ERBB2.
    REACT_188528. GRB2 events in ERBB2 signaling.
    REACT_188574. SHC1 events in ERBB2 signaling.
    REACT_188579. Signaling by ERBB4.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198350. EGFR Transactivation by Gastrin.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_203917. EGFR downregulation.
    REACT_206286. GAB1 signalosome.
    REACT_215348. PI3K events in ERBB2 signaling.
    REACT_215461. Signal transduction by L1.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epidermal growth factor receptor (EC:2.7.10.1)
    Gene namesi
    Name:Egfr
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95294. Egfr.

    Subcellular locationi

    Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein By similarity. Golgi apparatus membrane By similarity; Single-pass type I membrane protein By similarity. Nucleus membrane By similarity; Single-pass type I membrane protein By similarity. Endosome. Endosome membrane. Nucleus By similarity
    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) By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    Mice are growth retarded and die at different stages of development depending on their genetic background. Embryonic death is due to placental defects. Mice surviving until birth or later display brain, bone, heart and various epithelial development defects in several organs, including skin, lung and gastrointestinal tract.3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 12101186Epidermal growth factor receptorPRO_0000016666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi128 – 1281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi175 – 1751N-linked (GlcNAc...)1 Publication
    Disulfide bondi190 ↔ 199By similarity
    Disulfide bondi194 ↔ 207By similarity
    Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi215 ↔ 223By similarity
    Disulfide bondi219 ↔ 231By similarity
    Modified residuei229 – 2291PhosphoserineBy similarity
    Disulfide bondi232 ↔ 240By similarity
    Disulfide bondi236 ↔ 248By similarity
    Disulfide bondi251 ↔ 260By similarity
    Disulfide bondi264 ↔ 291By similarity
    Disulfide bondi295 ↔ 307By similarity
    Disulfide bondi311 ↔ 326By similarity
    Disulfide bondi329 ↔ 333By similarity
    Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication
    Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi444 – 4441N-linked (GlcNAc...)1 Publication
    Disulfide bondi506 ↔ 515By similarity
    Disulfide bondi510 ↔ 523By similarity
    Disulfide bondi526 ↔ 535By similarity
    Glycosylationi528 – 5281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi539 ↔ 555By similarity
    Disulfide bondi558 ↔ 571By similarity
    Disulfide bondi562 ↔ 579By similarity
    Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi582 ↔ 591By similarity
    Disulfide bondi595 ↔ 617By similarity
    Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi620 ↔ 628By similarity
    Glycosylationi623 – 6231N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi624 ↔ 636By similarity
    Modified residuei680 – 6801Phosphothreonine; by PKC and PKD/PRKD1By similarity
    Modified residuei695 – 6951Phosphothreonine; by PKD/PRKD1By similarity
    Modified residuei697 – 6971PhosphoserineBy similarity
    Cross-linki718 – 718Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki739 – 739Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki756 – 756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki869 – 869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki931 – 931Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki972 – 972Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei993 – 9931PhosphoserineBy similarity
    Modified residuei997 – 9971PhosphoserineBy similarity
    Modified residuei1000 – 10001Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1018 – 10181Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1028 – 10281PhosphoserineBy similarity
    Modified residuei1041 – 10411PhosphoserineBy similarity
    Modified residuei1043 – 10431PhosphothreonineBy similarity
    Modified residuei1044 – 10441PhosphoserineBy similarity
    Modified residuei1070 – 10701PhosphoserineBy similarity
    Modified residuei1071 – 10711PhosphoserineBy similarity
    Modified residuei1092 – 10921Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1110 – 11101Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1166 – 11661PhosphoserineBy similarity
    Modified residuei1172 – 11721Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei1197 – 11971Phosphotyrosine; alternate1 Publication
    Modified residuei1197 – 11971Phosphotyrosine; by autocatalysis; alternateBy similarity
    Modified residuei1199 – 11991Omega-N-methylated arginineBy similarity

    Post-translational modificationi

    Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occur. Deubiquitinated by OTUD7B, preventing degradation By similarity.By similarity
    Phosphorylated. Phosphorylation of Ser-697 is partial and occurs only if Thr-695 is phosphorylated. Phosphorylation at Thr-680 and Thr-695 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-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 By similarity.By similarity
    Methylated. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197 By similarity.By similarity

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiQ01279.
    PaxDbiQ01279.
    PRIDEiQ01279.

    PTM databases

    PhosphoSiteiQ01279.

    Expressioni

    Gene expression databases

    ArrayExpressiQ01279.
    BgeeiQ01279.
    CleanExiMM_EGFR.
    GenevestigatoriQ01279.

    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. Interacts (via SH2 domains) with GRB2, NCK1 and NCK2. Interacts with EPS8; mediates EPS8 phosphorylation. 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).1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CblP226822EBI-6296235,EBI-640919
    EGFP011333EBI-6296235,EBI-640857From a different organism.
    KrasP328833EBI-6296235,EBI-644267

    Protein-protein interaction databases

    BioGridi199402. 20 interactions.
    DIPiDIP-5763N.
    IntActiQ01279. 9 interactions.
    MINTiMINT-143143.

    Structurei

    3D structure databases

    ProteinModelPortaliQ01279.
    SMRiQ01279. Positions 26-636, 644-1020.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 647623ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini671 – 1210540CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei648 – 67023HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati75 – 300226ApproximateAdd
    BLAST
    Repeati390 – 600211ApproximateAdd
    BLAST
    Domaini714 – 981268Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni690 – 70617Important for dimerization, phosphorylation and activationBy similarityAdd
    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.
    GeneTreeiENSGT00600000084253.
    HOGENOMiHOG000230982.
    HOVERGENiHBG000490.
    InParanoidiQ01279.
    KOiK04361.
    OMAiMRRRHIV.
    PhylomeDBiQ01279.
    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. 4 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q01279-1 [UniParc]FASTAAdd to Basket

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    MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS     50
    LQRMYNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP 100
    LENLQIIRGN ALYENTYALA ILSNYGTNRT GLRELPMRNL QEILIGAVRF 150
    SNNPILCNMD TIQWRDIVQN VFMSNMSMDL QSHPSSCPKC DPSCPNGSCW 200
    GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC TGPRESDCLV 250
    CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV 300
    VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS 350
    INATNIKHFK YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE 400
    ITGFLLIQAW PDNWTDLHAF ENLEIIRGRT KQHGQFSLAV VGLNITSLGL 450
    RSLKEISDGD VIISGNRNLC YANTINWKKL FGTPNQKTKI MNNRAEKDCK 500
    AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN ILEGEPREFV 550
    ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM 600
    GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT 650
    GIVGGLLFIV VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA 700
    PNQAHLRILK ETEFKKIKVL GSGAFGTVYK GLWIPEGEKV KIPVAIKELR 750
    EATSPKANKE ILDEAYVMAS VDNPHVCRLL GICLTSTVQL ITQLMPYGCL 800
    LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL AARNVLVKTP 850
    QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW 900
    SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV 950
    KCWMIDADSR PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY 1000
    RALMDEEDME DVVDADEYLI PQQGFFNSPS TSRTPLLSSL SATSNNSTVA 1050
    CINRNGSCRV KEDAFLQRYS SDPTGAVTED NIDDAFLPVP EYVNQSVPKR 1100
    PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN TAQPTCLSSG 1150
    FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV 1200
    APPSSEFIGA 1210
    Length:1,210
    Mass (Da):134,853
    Last modified:February 1, 1996 - v1
    Checksum:i690E20D46DF2D2F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti539 – 5391C → W in CAA42219. (PubMed:2030916)Curated
    Sequence conflicti991 – 9911L → F in AAA17899. (PubMed:8125255)Curated
    Sequence conflicti1116 – 11172HP → DR in CAA78249. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78987 mRNA. Translation: CAA55587.1.
    U03425 mRNA. Translation: AAA17899.1.
    X59698 mRNA. Translation: CAA42219.1.
    L06864 mRNA. Translation: AAA53029.1.
    Z12608 mRNA. Translation: CAA78249.1.
    CCDSiCCDS24443.1.
    PIRiA53183.
    RefSeqiNP_997538.1. NM_207655.2.
    UniGeneiMm.420648.
    Mm.439882.
    Mm.8534.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X78987 mRNA. Translation: CAA55587.1 .
    U03425 mRNA. Translation: AAA17899.1 .
    X59698 mRNA. Translation: CAA42219.1 .
    L06864 mRNA. Translation: AAA53029.1 .
    Z12608 mRNA. Translation: CAA78249.1 .
    CCDSi CCDS24443.1.
    PIRi A53183.
    RefSeqi NP_997538.1. NM_207655.2.
    UniGenei Mm.420648.
    Mm.439882.
    Mm.8534.

    3D structure databases

    ProteinModelPortali Q01279.
    SMRi Q01279. Positions 26-636, 644-1020.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199402. 20 interactions.
    DIPi DIP-5763N.
    IntActi Q01279. 9 interactions.
    MINTi MINT-143143.

    Chemistry

    BindingDBi Q01279.
    ChEMBLi CHEMBL3608.

    PTM databases

    PhosphoSitei Q01279.

    Proteomic databases

    MaxQBi Q01279.
    PaxDbi Q01279.
    PRIDEi Q01279.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020329 ; ENSMUSP00000020329 ; ENSMUSG00000020122 .
    GeneIDi 13649.
    KEGGi mmu:13649.
    UCSCi uc007ibo.1. mouse.

    Organism-specific databases

    CTDi 1956.
    MGIi MGI:95294. Egfr.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00600000084253.
    HOGENOMi HOG000230982.
    HOVERGENi HBG000490.
    InParanoidi Q01279.
    KOi K04361.
    OMAi MRRRHIV.
    PhylomeDBi Q01279.
    TreeFami TF106002.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.
    Reactomei REACT_188190. PLCG1 events in ERBB2 signaling.
    REACT_188191. Signaling by ERBB2.
    REACT_188528. GRB2 events in ERBB2 signaling.
    REACT_188574. SHC1 events in ERBB2 signaling.
    REACT_188579. Signaling by ERBB4.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198350. EGFR Transactivation by Gastrin.
    REACT_199123. Signaling by constitutively active EGFR.
    REACT_203917. EGFR downregulation.
    REACT_206286. GAB1 signalosome.
    REACT_215348. PI3K events in ERBB2 signaling.
    REACT_215461. Signal transduction by L1.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    ChiTaRSi EGFR. mouse.
    NextBioi 284374.
    PROi Q01279.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01279.
    Bgeei Q01279.
    CleanExi MM_EGFR.
    Genevestigatori Q01279.

    Family and domain databases

    Gene3Di 3.80.20.20. 2 hits.
    InterProi IPR000494. 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 ]
    Pfami PF00757. Furin-like. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF01030. Recep_L_domain. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000619. TyrPK_EGF-R. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00261. FU. 4 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF57184. SSF57184. 2 hits.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Promoter region of the murine fibroblast growth factor receptor 2 (bek/KGFR) gene."
      Avivi A., Skorecki K., Yayon A., Givol D.
      Oncogene 7:1957-1962(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    2. "Expression of the epidermal growth factor receptor gene is regulated in mouse blastocysts during delayed implantation."
      Paria B.C., Das S.K., Andrews G.K., Dey S.K.
      Proc. Natl. Acad. Sci. U.S.A. 90:55-59(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c and CD-1.
      Tissue: Decidua and Liver.
    3. Hibbs M.L.
      Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Liver.
    4. "The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase."
      Luetteke N.C., Phillips H.K., Qiu T.H., Copeland N.G., Earp H.S., Jenkins N.A., Lee D.C.
      Genes Dev. 8:399-413(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: B6/C3.
      Tissue: Liver.
    5. "Comparison of EGF receptor sequences as a guide to study the ligand binding site."
      Avivi A., Lax I., Ullrich A., Schlessinger J., Givol D., Morse B.
      Oncogene 6:673-676(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-714.
      Tissue: Brain.
    6. Eisinger D.P., Serrero G.
      Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 969-1117.
      Strain: C3H.
    7. "Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals."
      Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T., Wong W.T., di Fiore P.P.
      EMBO J. 12:3799-3808(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CELL GROWTH, FUNCTION IN PHOSPHORYLATION OF EPS8, INTERACTION WITH EPS8.
    8. "Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor."
      Miettinen P.J., Berger J.E., Meneses J., Phung Y., Pedersen R.A., Werb Z., Derynck R.
      Nature 376:337-341(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    9. "Targeted disruption of mouse EGF receptor: effect of genetic background on mutant phenotype."
      Threadgill D.W., Dlugosz A.A., Hansen L.A., Tennenbaum T., Lichti U., Yee D., LaMantia C., Mourton T., Herrup K., Harris R.C.
      Science 269:230-234(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    10. "Strain-dependent epithelial defects in mice lacking the EGF receptor."
      Sibilia M., Wagner E.F.
      Science 269:234-238(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    11. "Tyrosine phosphorylation of Eps15 is required for ligand-regulated, but not constitutive, endocytosis."
      Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.
      J. Cell Biol. 150:905-912(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF EPS15, ENZYME REGULATION, ENDOCYTOSIS.
    12. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444.
      Strain: C57BL/6.
      Tissue: Plasma.
    13. "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
      Bernhard O.K., Kapp E.A., Simpson R.J.
      J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175.
      Strain: C57BL/6.
      Tissue: Plasma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiEGFR_MOUSE
    AccessioniPrimary (citable) accession number: Q01279
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 165 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3