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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.

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 – 7471ATP By similarity
Active sitei839 – 8391Proton acceptor By similarity
Binding sitei857 – 8571ATP By similarity
Sitei1018 – 10181Important for interaction with PIK3C2B By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi720 – 7289ATP By similarity
Nucleotide bindingi792 – 7932ATP By similarity

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 DNA repair Source: Ensembl
  32. positive regulation of DNA replication Source: Ensembl
  33. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  34. positive regulation of MAP kinase activity Source: Ensembl
  35. positive regulation of catenin import into nucleus Source: Ensembl
  36. positive regulation of cell migration Source: Ensembl
  37. positive regulation of cell proliferation Source: MGI
  38. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
  39. positive regulation of epithelial cell proliferation Source: MGI
  40. positive regulation of fibroblast proliferation Source: BHF-UCL
  41. positive regulation of inflammatory response 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 UV-A Source: Ensembl
  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. 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
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.

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; Single-pass type I membrane protein By similarity. Golgi apparatus membrane; Single-pass type I membrane protein By similarity. Nucleus membrane; 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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 647623Extracellular Reviewed prediction
Add
BLAST
Transmembranei648 – 67023Helical; Reviewed prediction
Add
BLAST
Topological domaini671 – 1210540Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. apical plasma membrane Source: Ensembl
  3. basolateral plasma membrane Source: MGI
  4. cell surface Source: Ensembl
  5. endocytic vesicle Source: MGI
  6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  7. endosome Source: UniProtKB
  8. endosome 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
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 – 2424 Reviewed prediction
Add
BLAST
Chaini25 – 12101186Epidermal growth factor receptor
PRO_0000016666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi128 – 1281N-linked (GlcNAc...) Reviewed prediction
Glycosylationi175 – 1751N-linked (GlcNAc...)1 Publication
Disulfide bondi190 ↔ 199 By similarity
Disulfide bondi194 ↔ 207 By similarity
Glycosylationi196 – 1961N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi215 ↔ 223 By similarity
Disulfide bondi219 ↔ 231 By similarity
Modified residuei229 – 2291Phosphoserine By similarity
Disulfide bondi232 ↔ 240 By similarity
Disulfide bondi236 ↔ 248 By similarity
Disulfide bondi251 ↔ 260 By similarity
Disulfide bondi264 ↔ 291 By similarity
Disulfide bondi295 ↔ 307 By similarity
Disulfide bondi311 ↔ 326 By similarity
Disulfide bondi329 ↔ 333 By similarity
Glycosylationi352 – 3521N-linked (GlcNAc...)1 Publication
Glycosylationi413 – 4131N-linked (GlcNAc...) Reviewed prediction
Glycosylationi444 – 4441N-linked (GlcNAc...)1 Publication
Disulfide bondi506 ↔ 515 By similarity
Disulfide bondi510 ↔ 523 By similarity
Disulfide bondi526 ↔ 535 By similarity
Glycosylationi528 – 5281N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi539 ↔ 555 By similarity
Disulfide bondi558 ↔ 571 By similarity
Disulfide bondi562 ↔ 579 By similarity
Glycosylationi568 – 5681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi582 ↔ 591 By similarity
Disulfide bondi595 ↔ 617 By similarity
Glycosylationi603 – 6031N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi620 ↔ 628 By similarity
Glycosylationi623 – 6231N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi624 ↔ 636 By similarity
Modified residuei680 – 6801Phosphothreonine; by PKC and PKD/PRKD1 By similarity
Modified residuei695 – 6951Phosphothreonine; by PKD/PRKD1 By similarity
Modified residuei697 – 6971Phosphoserine By 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 – 9931Phosphoserine By similarity
Modified residuei997 – 9971Phosphoserine By similarity
Modified residuei1000 – 10001Phosphotyrosine; by autocatalysis By similarity
Modified residuei1018 – 10181Phosphotyrosine; by autocatalysis By similarity
Modified residuei1028 – 10281Phosphoserine By similarity
Modified residuei1041 – 10411Phosphoserine By similarity
Modified residuei1043 – 10431Phosphothreonine By similarity
Modified residuei1044 – 10441Phosphoserine By similarity
Modified residuei1070 – 10701Phosphoserine By similarity
Modified residuei1071 – 10711Phosphoserine By similarity
Modified residuei1092 – 10921Phosphotyrosine; by autocatalysis By similarity
Modified residuei1110 – 11101Phosphotyrosine; by autocatalysis By similarity
Modified residuei1166 – 11661Phosphoserine By similarity
Modified residuei1172 – 11721Phosphotyrosine; by autocatalysis By similarity
Modified residuei1197 – 11971Phosphotyrosine; alternate1 Publication
Modified residuei1197 – 11971Phosphotyrosine; by autocatalysis; alternate By similarity
Modified residuei1199 – 11991Omega-N-methylated arginine By 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.
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.
Methylated. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati75 – 300226Approximate
Add
BLAST
Repeati390 – 600211Approximate
Add
BLAST
Domaini714 – 981268Protein kinase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni690 – 70617Important for dimerization, phosphorylation and activation By similarity
Add
BLAST

Sequence similaritiesi

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

Sequence conflict

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

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 ]
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Publicationsi

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  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: September 3, 2014
This is version 164 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

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