Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed]

 RASK_RAT                Reviewed;         189 AA.
P08644; P46203; P97914;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 3.
23-MAY-2018, entry version 174.
RecName: Full=GTPase KRas;
AltName: Full=K-Ras 2;
AltName: Full=Ki-Ras;
AltName: Full=c-K-ras;
AltName: Full=c-Ki-ras;
Contains:
RecName: Full=GTPase KRas, N-terminally processed;
Flags: Precursor;
Name=Kras; Synonyms=Kras2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B), MUTAGENESIS, AND FUNCTION.
STRAIN=Noble; TISSUE=Kidney;
PubMed=8058308;
Higinbotham K.G., Rice J.M., Buzard G.S., Perantoni A.O.;
"Activation of the K-ras gene by insertion mutations in chemically
induced rat renal mesenchymal tumors.";
Oncogene 9:2455-2459(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
PubMed=3023884; DOI=10.1128/MCB.6.4.1349;
Tahira T., Hayashi K., Ochiai M., Tsuchida N., Nagao M., Sugimura T.;
"Structure of the c-Ki-ras gene in a rat fibrosarcoma induced by 1,8-
dinitropyrene.";
Mol. Cell. Biol. 6:1349-1351(1986).
[4]
NUCLEOTIDE SEQUENCE OF 1-37.
PubMed=3009041;
Iritani A., Katayama N., Tahira T., Hayashi K., Tsuchida N.;
"Nucleotide sequence of exon I of the rat c-K-ras gene.";
Bull. Tokyo Med. Dent. Univ. 33:35-40(1986).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28, AND FUNCTION.
PubMed=3110778; DOI=10.1073/pnas.84.14.4974;
McMahon G., Davis E., Wogan G.N.;
"Characterization of c-Ki-ras oncogene alleles by direct sequencing of
enzymatically amplified DNA from carcinogen-induced tumors.";
Proc. Natl. Acad. Sci. U.S.A. 84:4974-4978(1987).
[6]
INTERACTION WITH PHLPP.
PubMed=12594205; DOI=10.1074/jbc.M213214200;
Shimizu K., Okada M., Nagai K., Fukada Y.;
"Suprachiasmatic nucleus circadian oscillatory protein, a novel
binding partner of K-Ras in the membrane rafts, negatively regulates
MAPK pathway.";
J. Biol. Chem. 278:14920-14925(2003).
[7]
INTERACTION WITH RGS14.
PubMed=19319189; DOI=10.1371/journal.pone.0004884;
Willard F.S., Willard M.D., Kimple A.J., Soundararajan M.,
Oestreich E.A., Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J.,
Zylka M.J., Snider W.D., Siderovski D.P.;
"Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras
effector.";
PLoS ONE 4:E4884-E4884(2009).
-!- FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase
activity (By similarity). Plays an important role in the
regulation of cell proliferation (PubMed:3110778). Plays a role in
promoting oncogenic events by inducing transcriptional silencing
of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells
in a ZNF304-dependent manner (By similarity).
{ECO:0000250|UniProtKB:P01116, ECO:0000269|PubMed:3110778}.
-!- ENZYME REGULATION: Alternates between an inactive form bound to
GDP and an active form bound to GTP. Activated by a guanine
nucleotide-exchange factor (GEF) and inactivated by a GTPase-
activating protein (GAP). Interaction with SOS1 promotes exchange
of bound GDP by GTP. {ECO:0000250|UniProtKB:P01116}.
-!- SUBUNIT: Interacts with SOS1 (By similarity). Interacts (when
farnesylated) with PDE6D; this promotes dissociation from the cell
membrane (By similarity). Interacts with PHLPP. Interacts (active
GTP-bound form preferentially) with RGS14.
{ECO:0000250|UniProtKB:P01116, ECO:0000269|PubMed:12594205,
ECO:0000269|PubMed:19319189}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P01116}; Lipid-anchor
{ECO:0000250|UniProtKB:P01116}; Cytoplasmic side
{ECO:0000250|UniProtKB:P01116}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P01116}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Isoforms differ in the C-terminal region which is
encoded by two alternative exons (IVA and IVB).;
Name=2A;
IsoId=P08644-1; Sequence=Displayed;
Name=2B;
IsoId=P08644-2, P46203-1;
Sequence=VSP_011144, VSP_011145;
-!- PTM: Acetylation at Lys-104 prevents interaction with guanine
nucleotide exchange factors (GEFs).
{ECO:0000250|UniProtKB:P01116}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U09793; AAB60458.1; -; mRNA.
EMBL; AABR03032592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M12260; AAA42011.1; -; Genomic_DNA.
EMBL; M12259; AAA42011.1; JOINED; Genomic_DNA.
EMBL; M54870; AAA40937.1; -; Genomic_DNA.
EMBL; M16970; AAA41494.1; -; Genomic_DNA.
PIR; I58402; I58402.
RefSeq; NP_113703.1; NM_031515.3. [P08644-2]
RefSeq; XP_008761576.1; XM_008763354.2. [P08644-2]
RefSeq; XP_017447931.1; XM_017592442.1. [P08644-1]
RefSeq; XP_017447932.1; XM_017592443.1. [P08644-1]
UniGene; Rn.24554; -.
PDB; 1N4S; X-ray; 2.60 A; M/N/O/P/Q/R=185-188.
PDBsum; 1N4S; -.
ProteinModelPortal; P08644; -.
SMR; P08644; -.
BioGrid; 246680; 9.
STRING; 10116.ENSRNOP00000012588; -.
iPTMnet; P08644; -.
PhosphoSitePlus; P08644; -.
SwissPalm; P08644; -.
PaxDb; P08644; -.
PRIDE; P08644; -.
Ensembl; ENSRNOT00000012588; ENSRNOP00000012588; ENSRNOG00000009338. [P08644-1]
Ensembl; ENSRNOT00000012887; ENSRNOP00000012887; ENSRNOG00000009338. [P08644-2]
GeneID; 24525; -.
KEGG; rno:24525; -.
UCSC; RGD:2981; rat. [P08644-1]
CTD; 3845; -.
RGD; 2981; Kras.
eggNOG; KOG0395; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00860000133672; -.
HOGENOM; HOG000233973; -.
HOVERGEN; HBG009351; -.
InParanoid; P08644; -.
KO; K07827; -.
OMA; QSWAVNM; -.
OrthoDB; EOG091G0UAU; -.
PhylomeDB; P08644; -.
TreeFam; TF312796; -.
Reactome; R-RNO-1169092; Activation of RAS in B cells.
Reactome; R-RNO-1250347; SHC1 events in ERBB4 signaling.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-171007; p38MAPK events.
Reactome; R-RNO-179812; GRB2 events in EGFR signaling.
Reactome; R-RNO-180336; SHC1 events in EGFR signaling.
Reactome; R-RNO-186763; Downstream signal transduction.
Reactome; R-RNO-1963640; GRB2 events in ERBB2 signaling.
Reactome; R-RNO-210993; Tie2 Signaling.
Reactome; R-RNO-2179392; EGFR Transactivation by Gastrin.
Reactome; R-RNO-2424491; DAP12 signaling.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-375165; NCAM signaling for neurite out-growth.
Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-RNO-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-RNO-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-RNO-5654699; SHC-mediated cascade:FGFR2.
Reactome; R-RNO-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-RNO-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-RNO-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-RNO-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-RNO-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
Reactome; R-RNO-5673000; RAF activation.
Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
Reactome; R-RNO-5674135; MAP2K and MAPK activation.
Reactome; R-RNO-5675221; Negative regulation of MAPK pathway.
Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
Reactome; R-RNO-8851805; MET activates RAS signaling.
Reactome; R-RNO-8951936; RUNX3 regulates p14-ARF.
PRO; PR:P08644; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000009338; -.
ExpressionAtlas; P08644; baseline and differential.
Genevisible; P08644; RN.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0019003; F:GDP binding; IDA:RGD.
GO; GO:0019002; F:GMP binding; IDA:RGD.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
GO; GO:0030275; F:LRR domain binding; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:RGD.
GO; GO:0038002; P:endocrine signaling; IEA:Ensembl.
GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEP:RGD.
GO; GO:0021897; P:forebrain astrocyte development; IEA:Ensembl.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0001889; P:liver development; IEP:RGD.
GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:RGD.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD.
GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:RGD.
GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl.
GO; GO:0007265; P:Ras protein signal transduction; IEA:Ensembl.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0035900; P:response to isolation stress; IEP:RGD.
GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0008542; P:visual learning; IEA:Ensembl.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR020849; Small_GTPase_Ras-type.
PANTHER; PTHR24070; PTHR24070; 1.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51421; RAS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
Methylation; Nucleotide-binding; Palmitate; Prenylation;
Proto-oncogene; Reference proteome.
CHAIN 1 186 GTPase KRas.
/FTId=PRO_0000082644.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:P01116}.
CHAIN 2 186 GTPase KRas, N-terminally processed.
/FTId=PRO_0000326483.
PROPEP 187 189 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281294.
NP_BIND 10 18 GTP. {ECO:0000250|UniProtKB:P01116}.
NP_BIND 29 35 GTP. {ECO:0000250|UniProtKB:P01116}.
NP_BIND 59 60 GTP. {ECO:0000250|UniProtKB:P01116}.
NP_BIND 116 119 GTP. {ECO:0000250|UniProtKB:P01116}.
REGION 166 185 Hypervariable region.
MOTIF 32 40 Effector region.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P01116}.
MOD_RES 2 2 N-acetylthreonine; in GTPase KRas, N-
terminally processed.
{ECO:0000250|UniProtKB:P01116}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000250|UniProtKB:P01116}.
MOD_RES 186 186 Cysteine methyl ester. {ECO:0000250}.
LIPID 180 180 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 186 186 S-farnesyl cysteine.
{ECO:0000250|UniProtKB:P01116}.
VAR_SEQ 151 153 RVE -> GVD (in isoform 2B).
{ECO:0000303|PubMed:8058308}.
/FTId=VSP_011144.
VAR_SEQ 165 189 QYRLKKISKEEKTPGCVKIKKCVIM -> KHKEKMSKDGKK
KKKKSRTRCIVM (in isoform 2B).
{ECO:0000303|PubMed:8058308}.
/FTId=VSP_011145.
CONFLICT 12 12 G -> C (in Ref. 3; AAA42011).
{ECO:0000305}.
CONFLICT 47 47 D -> H (in Ref. 3; AAA42011).
{ECO:0000305}.
SEQUENCE 189 AA; 21656 MW; 97345422E01D2C81 CRC64;
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL
PSRTVDTKQA QELARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC
VKIKKCVIM


Related products :

Catalog number Product name Quantity
SPC-173C RAS Antibody, GTPase Hras, GTPase Kras, GTPase Nras, Ha Ras, K Ras, K ras p21, KRAS, NRAS, p21ras, RASH1, Polyclonal, Host Rabbit , Species reactivity Human, Mouse, Rat, Bovine 25ug
SPC-173D RAS Antibody, GTPase Hras, GTPase Kras, GTPase Nras, Ha Ras, K Ras, K ras p21, KRAS, NRAS, p21ras, RASH2, Polyclonal, Host Rabbit , Species reactivity Human, Mouse, Rat, Bovine 100ug
EIAAB33823 c-Ki-ras,c-K-ras,GTPase KRas,Homo sapiens,Human,Ki-Ras,KRAS,K-Ras 2,KRAS2,RASK2
RASK_MOUSE ELISA Kit FOR GTPase KRas; organism: Mouse; gene name: Kras 96T
EIAAB33822 c-Ki-ras,c-K-ras,GTPase KRas,Ki-Ras,Kras,K-Ras 2,Kras2,Rat,Rattus norvegicus
EIAAB33824 c-Ki-ras,c-K-ras,GTPase KRas,Ki-Ras,Kras,K-Ras 2,Kras2,Mouse,Mus musculus
CSB-EL012493HU Human GTPase KRas(KRAS) ELISA kit SpeciesHuman 96T
UT-E04898 Human GTPase Kras (KRas) ELISA Kit 96T
UB-E04898 Human GTPase Kras(kRas)ELISA Kit 96T
CSB-EL012493HU Human GTPase KRas(KRAS) ELISA kit 96T
QY-E04898 Human GTPase Kras(kRas)ELISA Kit 96T
CSB-EL012493DO Dog GTPase KRas(KRAS) ELISA kit 96T
CSB-E13921r Rat GTPase KRas ELISA Kit 96T
CSB-E13921r Rat GTPase KRas ELISA Kit SpeciesRat 96T
CSB-RP139674h Recombinant human GTPase KRas 500ug
CSB-RP139694h Recombinant human GTPase KRas 500ug
PE139674h Recombinant human GTPase KRas protein 5mg
PE139674h Recombinant human GTPase KRas protein 1mg
CSB-E17149m Mouse GTPase KRas ELISA Kit SpeciesMouse 96T
abx108323 Polyclonal Rabbit GTPase KRas Antibody (HRP) 100 μg
PE139674h Recombinant human GTPase KRas protein 50ug
abx109846 Polyclonal Rabbit GTPase KRas Antibody 100 μg
PE139674h Recombinant human GTPase KRas protein 200ug
CSB-RP139694h Recombinant human GTPase KRas Source: E.coli 1mg
abx105485 Polyclonal Rabbit GTPase KRas Antibody (Biotin) 100 μg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur