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Epidermal growth factor receptor (EC 2.7.10.1)

 EGFR_MOUSE              Reviewed;        1210 AA.
Q01279;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 201.
RecName: Full=Epidermal growth factor receptor;
EC=2.7.10.1;
Flags: Precursor;
Name=Egfr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=1408137;
Avivi A., Skorecki K., Yayon A., Givol D.;
"Promoter region of the murine fibroblast growth factor receptor 2
(bek/KGFR) gene.";
Oncogene 7:1957-1962(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ, and CD-1; TISSUE=Decidua, and Liver;
PubMed=7678348; DOI=10.1073/pnas.90.1.55;
Paria B.C., Das S.K., Andrews G.K., Dey S.K.;
"Expression of the epidermal growth factor receptor gene is regulated
in mouse blastocysts during delayed implantation.";
Proc. Natl. Acad. Sci. U.S.A. 90:55-59(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
Hibbs M.L.;
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=B6/C3; TISSUE=Liver;
PubMed=8125255; DOI=10.1101/gad.8.4.399;
Luetteke N.C., Phillips H.K., Qiu T.H., Copeland N.G., Earp H.S.,
Jenkins N.A., Lee D.C.;
"The mouse waved-2 phenotype results from a point mutation in the EGF
receptor tyrosine kinase.";
Genes Dev. 8:399-413(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-714.
TISSUE=Brain;
PubMed=2030916;
Avivi A., Lax I., Ullrich A., Schlessinger J., Givol D., Morse B.;
"Comparison of EGF receptor sequences as a guide to study the ligand
binding site.";
Oncogene 6:673-676(1991).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 969-1117.
STRAIN=C3H/HeJ;
Eisinger D.P., Serrero G.;
Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION IN CELL GROWTH, FUNCTION IN PHOSPHORYLATION OF EPS8, AND
INTERACTION WITH EPS8.
PubMed=8404850;
Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T.,
Wong W.T., di Fiore P.P.;
"Eps8, a substrate for the epidermal growth factor receptor kinase,
enhances EGF-dependent mitogenic signals.";
EMBO J. 12:3799-3808(1993).
[8]
DISRUPTION PHENOTYPE.
PubMed=7630400; DOI=10.1038/376337a0;
Miettinen P.J., Berger J.E., Meneses J., Phung Y., Pedersen R.A.,
Werb Z., Derynck R.;
"Epithelial immaturity and multiorgan failure in mice lacking
epidermal growth factor receptor.";
Nature 376:337-341(1995).
[9]
DISRUPTION PHENOTYPE.
PubMed=7618084; DOI=10.1126/science.7618084;
Threadgill D.W., Dlugosz A.A., Hansen L.A., Tennenbaum T., Lichti U.,
Yee D., LaMantia C., Mourton T., Herrup K., Harris R.C.;
"Targeted disruption of mouse EGF receptor: effect of genetic
background on mutant phenotype.";
Science 269:230-234(1995).
[10]
DISRUPTION PHENOTYPE.
PubMed=7618085; DOI=10.1126/science.7618085;
Sibilia M., Wagner E.F.;
"Strain-dependent epithelial defects in mice lacking the EGF
receptor.";
Science 269:234-238(1995).
[11]
FUNCTION IN PHOSPHORYLATION OF EPS15, ENZYME REGULATION, AND
ENDOCYTOSIS.
PubMed=10953014; DOI=10.1083/jcb.150.4.905;
Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.;
"Tyrosine phosphorylation of Eps15 is required for ligand-regulated,
but not constitutive, endocytosis.";
J. Cell Biol. 150:905-912(2000).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352 AND ASN-444.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=16944957; DOI=10.1021/pr060186m;
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
Gevaert K.;
"Proteome-wide characterization of N-glycosylation events by diagonal
chromatography.";
J. Proteome Res. 5:2438-2447(2006).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-175.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION.
PubMed=20639532; DOI=10.1093/nar/gkq634;
Peng S.C., Lai Y.T., Huang H.Y., Huang H.D., Huang Y.S.;
"A novel role of CPEB3 in regulating EGFR gene transcription via
association with Stat5b in neurons.";
Nucleic Acids Res. 38:7446-7457(2010).
[17]
UBIQUITINATION BY RNF115 AND RNF126, AND INTERACTION WITH RNF115 AND
RNF126.
PubMed=23418353; DOI=10.1242/jcs.116129;
Smith C.J., Berry D.M., McGlade C.J.;
"The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal
sorting of the epidermal growth factor receptor.";
J. Cell Sci. 126:1366-1380(2013).
[18]
INTERACTION WITH GPRC5A.
PubMed=25744720; DOI=10.1158/0008-5472.CAN-14-2005;
Zhong S., Yin H., Liao Y., Yao F., Li Q., Zhang J., Jiao H., Zhao Y.,
Xu D., Liu S., Song H., Gao Y., Liu J., Ma L., Pang Z., Yang R.,
Ding C., Sun B., Lin X., Ye X., Guo W., Han B., Zhou B.P., Chin Y.E.,
Deng J.;
"Lung tumor suppressor GPRC5A binds EGFR and restrains its effector
signaling.";
Cancer Res. 75:1801-1814(2015).
-!- FUNCTION: 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. Plays
a role in enhancing learning and memory performance
(PubMed:20639532). {ECO:0000269|PubMed:10953014,
ECO:0000269|PubMed:20639532, ECO:0000269|PubMed:8404850}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: 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. {ECO:0000269|PubMed:10953014}.
-!- SUBUNIT: 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 ELOC- and ELOB-
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 GAREM1. 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.
Interacts with GPRC5A (via its transmembrane domain)
(PubMed:25744720). Interacts with FAM83B; positively regulates
EGFR inducing its autophospharylation in absence of stimulation by
EGF (By similarity). Interacts with LAPTM4B; positively correlates
with EGFR activation (By similarity).
{ECO:0000250|UniProtKB:P00533, ECO:0000269|PubMed:23418353,
ECO:0000269|PubMed:25744720, ECO:0000269|PubMed:8404850}.
-!- INTERACTION:
Q15109:AGER (xeno); NbExp=2; IntAct=EBI-6296235, EBI-1646426;
P22682:Cbl; NbExp=2; IntAct=EBI-6296235, EBI-640919;
P01133:EGF (xeno); NbExp=3; IntAct=EBI-6296235, EBI-640857;
P32883:Kras; NbExp=3; IntAct=EBI-6296235, EBI-644267;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Golgi apparatus membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Nucleus membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}. Endosome. Endosome membrane. Nucleus
{ECO:0000250}. 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). {ECO:0000250}.
-!- PTM: 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. {ECO:0000250|UniProtKB:P00533,
ECO:0000269|PubMed:23418353}.
-!- PTM: 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). {ECO:0000250}.
-!- PTM: Methylated. Methylation at Arg-1199 by PRMT5 positively
stimulates phosphorylation at Tyr-1197 (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:7618084, ECO:0000269|PubMed:7618085,
ECO:0000269|PubMed:7630400}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. EGF receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X78987; CAA55587.1; -; mRNA.
EMBL; U03425; AAA17899.1; -; mRNA.
EMBL; X59698; CAA42219.1; -; mRNA.
EMBL; L06864; AAA53029.1; -; mRNA.
EMBL; Z12608; CAA78249.1; -; mRNA.
CCDS; CCDS24443.1; -.
PIR; A53183; A53183.
RefSeq; NP_997538.1; NM_207655.2.
UniGene; Mm.420648; -.
UniGene; Mm.439882; -.
UniGene; Mm.8534; -.
ProteinModelPortal; Q01279; -.
SMR; Q01279; -.
BioGrid; 199402; 22.
CORUM; Q01279; -.
DIP; DIP-5763N; -.
IntAct; Q01279; 13.
MINT; MINT-143143; -.
STRING; 10090.ENSMUSP00000020329; -.
BindingDB; Q01279; -.
ChEMBL; CHEMBL3608; -.
iPTMnet; Q01279; -.
PhosphoSitePlus; Q01279; -.
SwissPalm; Q01279; -.
PaxDb; Q01279; -.
PeptideAtlas; Q01279; -.
PRIDE; Q01279; -.
Ensembl; ENSMUST00000020329; ENSMUSP00000020329; ENSMUSG00000020122.
GeneID; 13649; -.
KEGG; mmu:13649; -.
UCSC; uc007ibo.1; mouse.
CTD; 1956; -.
MGI; MGI:95294; Egfr.
eggNOG; KOG1025; Eukaryota.
eggNOG; ENOG410XNSR; LUCA.
GeneTree; ENSGT00760000118799; -.
HOGENOM; HOG000230982; -.
HOVERGEN; HBG000490; -.
InParanoid; Q01279; -.
KO; K04361; -.
OMA; VCRKCHP; -.
OrthoDB; EOG091G00NO; -.
PhylomeDB; Q01279; -.
TreeFam; TF106002; -.
BRENDA; 2.7.10.1; 3474.
Reactome; R-MMU-1227986; Signaling by ERBB2.
Reactome; R-MMU-1236394; Signaling by ERBB4.
Reactome; R-MMU-1250196; SHC1 events in ERBB2 signaling.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-177929; Signaling by EGFR.
Reactome; R-MMU-179812; GRB2 events in EGFR signaling.
Reactome; R-MMU-180292; GAB1 signalosome.
Reactome; R-MMU-180336; SHC1 events in EGFR signaling.
Reactome; R-MMU-182971; EGFR downregulation.
Reactome; R-MMU-1963642; PI3K events in ERBB2 signaling.
Reactome; R-MMU-212718; EGFR interacts with phospholipase C-gamma.
Reactome; R-MMU-2179392; EGFR Transactivation by Gastrin.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-8847993; ERBB2 Activates PTK6 Signaling.
Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
Reactome; R-MMU-8857538; PTK6 promotes HIF1A stabilization.
Reactome; R-MMU-8863795; Downregulation of ERBB2 signaling.
ChiTaRS; Egfr; mouse.
PRO; PR:Q01279; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020122; -.
CleanEx; MM_EGFR; -.
ExpressionAtlas; Q01279; baseline and differential.
Genevisible; Q01279; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0031901; C:early endosome membrane; ISO:MGI.
GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0010008; C:endosome membrane; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0097489; C:multivesicular body, internal vesicle lumen; ISO:MGI.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0045202; C:synapse; IEA:Ensembl.
GO; GO:0051015; F:actin filament binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0048408; F:epidermal growth factor binding; IDA:MGI.
GO; GO:0005006; F:epidermal growth factor-activated receptor activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0016301; F:kinase activity; IDA:MGI.
GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0004871; F:signal transducer activity; IDA:MGI.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; IEA:InterPro.
GO; GO:0004888; F:transmembrane signaling receptor activity; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0000186; P:activation of MAPKK activity; IEA:Ensembl.
GO; GO:0048143; P:astrocyte activation; IEA:Ensembl.
GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:UniProtKB.
GO; GO:0071276; P:cellular response to cadmium ion; ISO:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:MGI.
GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
GO; GO:0048546; P:digestive tract morphogenesis; IMP:MGI.
GO; GO:0016101; P:diterpenoid metabolic process; IEA:Ensembl.
GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
GO; GO:0008544; P:epidermis development; IMP:MGI.
GO; GO:0061029; P:eyelid development in camera-type eye; IGI:MGI.
GO; GO:0001942; P:hair follicle development; IMP:MGI.
GO; GO:0042743; P:hydrogen peroxide metabolic process; IEA:Ensembl.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0010960; P:magnesium ion homeostasis; IEA:Ensembl.
GO; GO:0007494; P:midgut development; IEA:Ensembl.
GO; GO:0060571; P:morphogenesis of an epithelial fold; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1905208; P:negative regulation of cardiocyte differentiation; ISO:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISO:MGI.
GO; GO:0048812; P:neuron projection morphogenesis; IEA:Ensembl.
GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; ISO:MGI.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IEA:Ensembl.
GO; GO:0045780; P:positive regulation of bone resorption; IEA:Ensembl.
GO; GO:0035413; P:positive regulation of catenin import into nucleus; ISO:MGI.
GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0031659; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; ISO:MGI.
GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISO:MGI.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0042327; P:positive regulation of phosphorylation; ISO:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:1902722; P:positive regulation of prolactin secretion; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:MGI.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IEA:Ensembl.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; ISO:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0046328; P:regulation of JNK cascade; ISO:MGI.
GO; GO:0050999; P:regulation of nitric-oxide synthase activity; ISO:MGI.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0033590; P:response to cobalamin; IEA:Ensembl.
GO; GO:0033594; P:response to hydroxyisoflavone; IEA:Ensembl.
GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
GO; GO:0070141; P:response to UV-A; ISO:MGI.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
GO; GO:0007165; P:signal transduction; IDA:MGI.
GO; GO:0043586; P:tongue development; IEA:Ensembl.
GO; GO:0006412; P:translation; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 3.80.20.20; -; 4.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR006211; Furin-like_Cys-rich_dom.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR032778; GF_recep_IV.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000494; Rcpt_L-dom.
InterPro; IPR036941; Rcpt_L-dom_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
Pfam; PF00757; Furin-like; 1.
Pfam; PF14843; GF_recep_IV; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF01030; Recep_L_domain; 2.
PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00261; FU; 4.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF57184; SSF57184; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Developmental protein;
Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
Golgi apparatus; Isopeptide bond; Kinase; Membrane; Methylation;
Nucleotide-binding; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1210 Epidermal growth factor receptor.
/FTId=PRO_0000016666.
TOPO_DOM 25 647 Extracellular. {ECO:0000255}.
TRANSMEM 648 670 Helical. {ECO:0000255}.
TOPO_DOM 671 1210 Cytoplasmic. {ECO:0000255}.
REPEAT 75 300 Approximate.
REPEAT 390 600 Approximate.
DOMAIN 714 981 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 720 728 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 792 793 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 690 706 Important for dimerization,
phosphorylation and activation.
{ECO:0000250}.
ACT_SITE 839 839 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 747 747 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 857 857 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 1018 1018 Important for interaction with PIK3C2B.
{ECO:0000250}.
MOD_RES 229 229 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 680 680 Phosphothreonine; by PKC and PKD/PRKD1.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 695 695 Phosphothreonine; by PKD/PRKD1.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 993 993 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 997 997 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1000 1000 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1018 1018 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1028 1028 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1041 1041 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1043 1043 Phosphothreonine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1044 1044 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1070 1070 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1071 1071 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1092 1092 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1110 1110 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1166 1166 Phosphoserine.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1172 1172 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1197 1197 Phosphotyrosine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 1199 1199 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:P00533}.
MOD_RES 1199 1199 Omega-N-methylated arginine; alternate.
{ECO:0000250}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 175 175 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 444 444 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16944957}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 568 568 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 623 623 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 190 199 {ECO:0000250}.
DISULFID 194 207 {ECO:0000250}.
DISULFID 215 223 {ECO:0000250}.
DISULFID 219 231 {ECO:0000250}.
DISULFID 232 240 {ECO:0000250}.
DISULFID 236 248 {ECO:0000250}.
DISULFID 251 260 {ECO:0000250}.
DISULFID 264 291 {ECO:0000250}.
DISULFID 295 307 {ECO:0000250}.
DISULFID 311 326 {ECO:0000250}.
DISULFID 329 333 {ECO:0000250}.
DISULFID 506 515 {ECO:0000250}.
DISULFID 510 523 {ECO:0000250}.
DISULFID 526 535 {ECO:0000250}.
DISULFID 539 555 {ECO:0000250}.
DISULFID 558 571 {ECO:0000250}.
DISULFID 562 579 {ECO:0000250}.
DISULFID 582 591 {ECO:0000250}.
DISULFID 595 617 {ECO:0000250}.
DISULFID 620 628 {ECO:0000250}.
DISULFID 624 636 {ECO:0000250}.
CROSSLNK 718 718 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 739 739 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 756 756 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 869 869 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 931 931 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CROSSLNK 972 972 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P00533}.
CONFLICT 539 539 C -> W (in Ref. 5; CAA42219).
{ECO:0000305}.
CONFLICT 991 991 L -> F (in Ref. 4; AAA17899).
{ECO:0000305}.
CONFLICT 1116 1117 HP -> DR (in Ref. 6; CAA78249).
{ECO:0000305}.
SEQUENCE 1210 AA; 134853 MW; 690E20D46DF2D2F5 CRC64;
MRPSGTARTT LLVLLTALCA AGGALEEKKV CQGTSNRLTQ LGTFEDHFLS LQRMYNNCEV
VLGNLEITYV QRNYDLSFLK TIQEVAGYVL IALNTVERIP LENLQIIRGN ALYENTYALA
ILSNYGTNRT GLRELPMRNL QEILIGAVRF SNNPILCNMD TIQWRDIVQN VFMSNMSMDL
QSHPSSCPKC DPSCPNGSCW GGGEENCQKL TKIICAQQCS HRCRGRSPSD CCHNQCAAGC
TGPRESDCLV CQKFQDEATC KDTCPPLMLY NPTTYQMDVN PEGKYSFGAT CVKKCPRNYV
VTDHGSCVRA CGPDYYEVEE DGIRKCKKCD GPCRKVCNGI GIGEFKDTLS INATNIKHFK
YCTAISGDLH ILPVAFKGDS FTRTPPLDPR ELEILKTVKE ITGFLLIQAW PDNWTDLHAF
ENLEIIRGRT KQHGQFSLAV VGLNITSLGL RSLKEISDGD VIISGNRNLC YANTINWKKL
FGTPNQKTKI MNNRAEKDCK AVNHVCNPLC SSEGCWGPEP RDCVSCQNVS RGRECVEKCN
ILEGEPREFV ENSECIQCHP ECLPQAMNIT CTGRGPDNCI QCAHYIDGPH CVKTCPAGIM
GENNTLVWKY ADANNVCHLC HANCTYGCAG PGLQGCEVWP SGPKIPSIAT GIVGGLLFIV
VVALGIGLFM RRRHIVRKRT LRRLLQEREL VEPLTPSGEA PNQAHLRILK ETEFKKIKVL
GSGAFGTVYK GLWIPEGEKV KIPVAIKELR EATSPKANKE ILDEAYVMAS VDNPHVCRLL
GICLTSTVQL ITQLMPYGCL LDYVREHKDN IGSQYLLNWC VQIAKGMNYL EDRRLVHRDL
AARNVLVKTP QHVKITDFGL AKLLGAEEKE YHAEGGKVPI KWMALESILH RIYTHQSDVW
SYGVTVWELM TFGSKPYDGI PASDISSILE KGERLPQPPI CTIDVYMIMV KCWMIDADSR
PKFRELILEF SKMARDPQRY LVIQGDERMH LPSPTDSNFY RALMDEEDME DVVDADEYLI
PQQGFFNSPS TSRTPLLSSL SATSNNSTVA CINRNGSCRV KEDAFLQRYS SDPTGAVTED
NIDDAFLPVP EYVNQSVPKR PAGSVQNPVY HNQPLHPAPG RDLHYQNPHS NAVGNPEYLN
TAQPTCLSSG FNSPALWIQK GSHQMSLDNP DYQQDFFPKE TKPNGIFKGP TAENAEYLRV
APPSSEFIGA


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