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Q01279

- EGFR_MOUSE

UniProt

Q01279 - EGFR_MOUSE

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Protein

Epidermal growth factor receptor

Gene

Egfr

Organism
Mus musculus (Mouse)
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.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 tyrosine kinase activity Source: UniProtKB
  7. receptor signaling protein tyrosine kinase activity Source: InterPro
  8. 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. peptidyl-tyrosine phosphorylation Source: GOC
  31. polysaccharide metabolic process Source: Ensembl
  32. positive regulation of catenin import into nucleus Source: Ensembl
  33. positive regulation of cell migration Source: Ensembl
  34. positive regulation of cell proliferation Source: MGI
  35. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
  36. positive regulation of DNA repair Source: Ensembl
  37. positive regulation of DNA replication Source: Ensembl
  38. positive regulation of epithelial cell proliferation Source: MGI
  39. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  40. positive regulation of fibroblast proliferation Source: BHF-UCL
  41. positive regulation of inflammatory response Source: Ensembl
  42. positive regulation of MAP kinase activity Source: Ensembl
  43. positive regulation of nitric oxide biosynthetic process Source: Ensembl
  44. positive regulation of protein kinase B signaling Source: Ensembl
  45. positive regulation of protein phosphorylation Source: UniProtKB
  46. positive regulation of smooth muscle cell proliferation Source: Ensembl
  47. positive regulation of superoxide anion generation Source: Ensembl
  48. positive regulation of synaptic transmission, glutamatergic Source: Ensembl
  49. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  50. positive regulation of vasoconstriction Source: Ensembl
  51. positive regulation of vasodilation Source: Ensembl
  52. protein autophosphorylation Source: MGI
  53. regulation of cell proliferation Source: MGI
  54. regulation of nitric-oxide synthase activity Source: Ensembl
  55. regulation of peptidyl-tyrosine phosphorylation Source: MGI
  56. response to calcium ion Source: Ensembl
  57. response to cobalamin Source: Ensembl
  58. response to hydroxyisoflavone Source: Ensembl
  59. response to osmotic stress Source: Ensembl
  60. response to oxidative stress Source: Ensembl
  61. response to UV-A Source: Ensembl
  62. salivary gland morphogenesis Source: MGI
  63. signal transduction Source: MGI
  64. single organismal cell-cell adhesion Source: Ensembl
  65. tongue development Source: Ensembl
  66. 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. 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.
REACT_236516. EGFR interacts with phospholipase C-gamma.
REACT_242976. Signaling by EGFR.
REACT_245103. GRB2 events in EGFR signaling.
REACT_260286. SHC1 events in EGFR 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 647623ExtracellularSequence AnalysisAdd
BLAST
Transmembranei648 – 67023HelicalSequence AnalysisAdd
BLAST
Topological domaini671 – 1210540CytoplasmicSequence AnalysisAdd
BLAST

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 Source: UniProtKB-KW
  6. endosome Source: UniProtKB
  7. Golgi apparatus Source: UniProtKB-KW
  8. integral component of membrane Source: UniProtKB-KW
  9. intracellular Source: MGI
  10. membrane raft Source: Ensembl
  11. nucleus Source: BHF-UCL
  12. perinuclear region of cytoplasm Source: BHF-UCL
  13. plasma membrane Source: MGI
  14. receptor complex Source: MGI
Complete GO annotation...

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 occurs. Deubiquitinated by OTUD7B, preventing degradation (By similarity). Ubiquitinated by RNF115 and RNF126.By similarity1 Publication
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

BgeeiQ01279.
CleanExiMM_EGFR.
ExpressionAtlasiQ01279. baseline and differential.
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). Interacts with RNF115 and RNF126.By similarity2 Publications

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 26-1005.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118799.
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

« Hide

        10         20         30         40         50
MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS
60 70 80 90 100
LQRMYNNCEV VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP
110 120 130 140 150
LENLQIIRGN ALYENTYALA ILSNYGTNRT GLRELPMRNL QEILIGAVRF
160 170 180 190 200
SNNPILCNMD TIQWRDIVQN VFMSNMSMDL QSHPSSCPKC DPSCPNGSCW
210 220 230 240 250
GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC TGPRESDCLV
260 270 280 290 300
CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
310 320 330 340 350
VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS
360 370 380 390 400
INATNIKHFK YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE
410 420 430 440 450
ITGFLLIQAW PDNWTDLHAF ENLEIIRGRT KQHGQFSLAV VGLNITSLGL
460 470 480 490 500
RSLKEISDGD VIISGNRNLC YANTINWKKL FGTPNQKTKI MNNRAEKDCK
510 520 530 540 550
AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN ILEGEPREFV
560 570 580 590 600
ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM
610 620 630 640 650
GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT
660 670 680 690 700
GIVGGLLFIV VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA
710 720 730 740 750
PNQAHLRILK ETEFKKIKVL GSGAFGTVYK GLWIPEGEKV KIPVAIKELR
760 770 780 790 800
EATSPKANKE ILDEAYVMAS VDNPHVCRLL GICLTSTVQL ITQLMPYGCL
810 820 830 840 850
LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL AARNVLVKTP
860 870 880 890 900
QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW
910 920 930 940 950
SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV
960 970 980 990 1000
KCWMIDADSR PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY
1010 1020 1030 1040 1050
RALMDEEDME DVVDADEYLI PQQGFFNSPS TSRTPLLSSL SATSNNSTVA
1060 1070 1080 1090 1100
CINRNGSCRV KEDAFLQRYS SDPTGAVTED NIDDAFLPVP EYVNQSVPKR
1110 1120 1130 1140 1150
PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN TAQPTCLSSG
1160 1170 1180 1190 1200
FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV
1210
APPSSEFIGA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 26-1005.
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 ENSGT00760000118799.
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.
REACT_236516. EGFR interacts with phospholipase C-gamma.
REACT_242976. Signaling by EGFR.
REACT_245103. GRB2 events in EGFR signaling.
REACT_260286. SHC1 events in EGFR signaling.

Miscellaneous databases

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

Gene expression databases

Bgeei Q01279.
CleanExi MM_EGFR.
ExpressionAtlasi Q01279. baseline and differential.
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

« Hide 'large scale' publications
  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.
  15. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBQUITINATION BY RNF115 AND RNF126, INTERACTION WITH RNF115 AND RNF126.

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: November 26, 2014
This is version 167 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

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