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

E3 ubiquitin-protein ligase SMURF1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF1) (SMAD ubiquitination regulatory factor 1) (SMAD-specific E3 ubiquitin-protein ligase 1)

 SMUF1_MOUSE             Reviewed;         731 AA.
Q9CUN6; Q3U412; Q8K300;
13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
23-MAY-2018, entry version 157.
RecName: Full=E3 ubiquitin-protein ligase SMURF1;
EC=2.3.2.26 {ECO:0000250|UniProtKB:Q9HCE7};
AltName: Full=HECT-type E3 ubiquitin transferase SMURF1;
AltName: Full=SMAD ubiquitination regulatory factor 1;
AltName: Full=SMAD-specific E3 ubiquitin-protein ligase 1;
Name=Smurf1;
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND INTERACTION WITH MAVS.
PubMed=23087404; DOI=10.4049/jimmunol.1201445;
Wang Y., Tong X., Ye X.;
"Ndfip1 negatively regulates RIG-I-dependent immune signaling by
enhancing E3 ligase Smurf1-mediated MAVS degradation.";
J. Immunol. 189:5304-5313(2012).
-!- FUNCTION: E3 ubiquitin-protein ligase that acts as a negative
regulator of BMP signaling pathway (By similarity). Mediates
ubiquitination and degradation of SMAD1 and SMAD5, 2 receptor-
regulated SMADs specific for the BMP pathway (By similarity).
Promotes ubiquitination and subsequent proteasomal degradation of
TRAF family members and RHOA (By similarity). Promotes
ubiquitination and subsequent proteasomal degradation of MAVS
(PubMed:23087404). Plays a role in dendrite formation by
melanocytes (By similarity). {ECO:0000250|UniProtKB:Q9HCE7,
ECO:0000269|PubMed:23087404}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:Q9HCE7}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with TRAF4 (By similarity). Interacts (via HECT
domain) with FBXL15 (via LRR repeats) (By similarity). Interacts
with SMAD7 and TGFBR1; SMAD7 recruits SMURF1 to TGFBR1 and
regulates TGF-beta receptor degradation (By similarity). Interacts
with MAVS; the interaction is mediated by NDFIP1
(PubMed:23087404). {ECO:0000250|UniProtKB:Q9HCE7,
ECO:0000269|PubMed:23087404}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}.
-!- DOMAIN: The C2 domain mediates membrane localization and substrate
selection. {ECO:0000250}.
-!- PTM: Auto-ubiquitinated in presence of NDFIP1. Ubiquitinated by
the SCF(FBXL15) complex at Lys-355 and Lys-357, leading to its
degradation by the proteasome. Lys-357 is the primary
ubiquitination site. {ECO:0000250|UniProtKB:Q9HCE7}.
-!- SEQUENCE CAUTION:
Sequence=BAB29770.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AK015264; BAB29770.2; ALT_INIT; mRNA.
EMBL; AK154491; BAE32623.1; -; mRNA.
EMBL; BC029097; AAH29097.1; -; mRNA.
CCDS; CCDS39380.1; -.
RefSeq; NP_001033716.1; NM_001038627.1.
RefSeq; NP_083714.3; NM_029438.3.
UniGene; Mm.27735; -.
ProteinModelPortal; Q9CUN6; -.
SMR; Q9CUN6; -.
BioGrid; 217743; 14.
CORUM; Q9CUN6; -.
IntAct; Q9CUN6; 3.
MINT; Q9CUN6; -.
STRING; 10090.ENSMUSP00000082827; -.
iPTMnet; Q9CUN6; -.
PhosphoSitePlus; Q9CUN6; -.
MaxQB; Q9CUN6; -.
PaxDb; Q9CUN6; -.
PRIDE; Q9CUN6; -.
Ensembl; ENSMUST00000085684; ENSMUSP00000082827; ENSMUSG00000038780.
GeneID; 75788; -.
KEGG; mmu:75788; -.
UCSC; uc009alv.1; mouse.
CTD; 57154; -.
MGI; MGI:1923038; Smurf1.
eggNOG; KOG0940; Eukaryota.
eggNOG; COG5021; LUCA.
GeneTree; ENSGT00760000118966; -.
HOGENOM; HOG000208451; -.
HOVERGEN; HBG004134; -.
InParanoid; Q9CUN6; -.
KO; K04678; -.
PhylomeDB; Q9CUN6; -.
TreeFam; TF323658; -.
BRENDA; 6.3.2.19; 3474.
Reactome; R-MMU-201451; Signaling by BMP.
Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
Reactome; R-MMU-5632684; Hedgehog 'on' state.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q9CUN6; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000038780; -.
CleanEx; MM_SMURF1; -.
ExpressionAtlas; Q9CUN6; baseline and differential.
Genevisible; Q9CUN6; MM.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0070411; F:I-SMAD binding; ISO:MGI.
GO; GO:0070412; F:R-SMAD binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
GO; GO:0061736; P:engulfment of target by autophagosome; ISO:MGI.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0030279; P:negative regulation of ossification; IMP:MGI.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; IMP:ParkinsonsUK-UCL.
GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
GO; GO:0034394; P:protein localization to cell surface; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; ISO:MGI.
GO; GO:0016567; P:protein ubiquitination; IMP:MGI.
GO; GO:0032801; P:receptor catabolic process; ISO:MGI.
GO; GO:0061753; P:substrate localization to autophagosome; ISO:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; ISO:MGI.
CDD; cd00078; HECTc; 1.
CDD; cd00201; WW; 2.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR024928; E3_ub_ligase_SMURF1.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
Pfam; PF00168; C2; 1.
Pfam; PF00632; HECT; 1.
Pfam; PF00397; WW; 2.
PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
SMART; SM00239; C2; 1.
SMART; SM00119; HECTc; 1.
SMART; SM00456; WW; 2.
SUPFAM; SSF51045; SSF51045; 2.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS50237; HECT; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 2.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Differentiation;
Isopeptide bond; Membrane; Phosphoprotein; Reference proteome; Repeat;
Transferase; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1 731 E3 ubiquitin-protein ligase SMURF1.
/FTId=PRO_0000120327.
DOMAIN 1 99 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 234 267 WW 1. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 280 313 WW 2. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
DOMAIN 394 731 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
COMPBIAS 144 147 Poly-Gly.
ACT_SITE 699 699 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000250|UniProtKB:Q9HCE7}.
CROSSLNK 355 355 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9HCE7}.
CROSSLNK 357 357 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q9HCE7}.
CONFLICT 63 63 N -> S (in Ref. 2; AAH29097).
{ECO:0000305}.
CONFLICT 204 204 D -> N (in Ref. 1; BAB29770).
{ECO:0000305}.
CONFLICT 213 213 R -> Q (in Ref. 1; BAB29770).
{ECO:0000305}.
CONFLICT 218 218 R -> Q (in Ref. 1; BAB29770).
{ECO:0000305}.
CONFLICT 278 278 E -> G (in Ref. 1; BAE32623).
{ECO:0000305}.
CONFLICT 334 334 S -> N (in Ref. 1; BAB29770).
{ECO:0000305}.
CONFLICT 446 446 T -> K (in Ref. 1; BAB29770).
{ECO:0000305}.
CONFLICT 671 673 Missing (in Ref. 1; BAB29770 and 2;
AAH29097). {ECO:0000305}.
SEQUENCE 731 AA; 83356 MW; F0A7A1B019CC9D3E CRC64;
MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS TDTVKNTLDP
KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL LSNAISRLKD TGYQRLDLCK
LNPSDTDAVR GQIVVSLQTR DRIGGGGSVV DCRGLLENEG TVYEDSGPGR PLSCLMEEPA
PYTDGTGAAA GGGNCRFVES PSQDQRLLVQ RLRNPEVRGP LQTPQNRPHG HQSPELPEGY
EQRTTVQGQV YFLHTQTGVS TWHDPRIPRD LNSVNCDELG PLPPGWEVRS TVSGRIYFVD
HNNRTTQFTD PRLHHIMNHQ CQLKEPSQPL QLPSEGSVED EELPAQRYER DLVQKLKVLR
HELSLQQPQA GHCRIEVSRE EIFEESYRQI MKMRPKDLKK RLMVKFRGEE GLDYGGVARE
WLYLLCHEML NPYYGLFQYS TDNIYTLQIN PDSSINPDHL SYFHFVGRIM GLAVFHGHYI
NGGFTVPFYK QLLGKPIQLS DLESVDPELH KSLVWILEND ITPVLDHTFC VEHNAFGRIL
QHELKPNGRN VPVTEENKKE YVRLYVNWRF MRGIEAQFLA LQKGFNELIP QHLLKPFDQK
ELELIIGGLD KIDLNDWKSN TRLKHCVADS NIVRWFWQAV ETFDEERRAR LLQFVTGSTR
VPLQGFKALQ GSTGAAGPRL FTIHLIDANT DNLPKAHTCF NRIDIPPYES YEKLYEKLLT
AVEETCGFAV E


Related products :

Catalog number Product name Quantity
EIAAB38890 E3 ubiquitin-protein ligase SMURF1,Homo sapiens,hSMURF1,Human,KIAA1625,SMAD ubiquitination regulatory factor 1,SMAD-specific E3 ubiquitin-protein ligase 1,SMURF1
EIAAB38889 E3 ubiquitin-protein ligase SMURF1,Mouse,Mus musculus,SMAD ubiquitination regulatory factor 1,SMAD-specific E3 ubiquitin-protein ligase 1,Smurf1
EIAAB38891 E3 ubiquitin-protein ligase SMURF2,Homo sapiens,hSMURF2,Human,SMAD ubiquitination regulatory factor 2,SMAD-specific E3 ubiquitin-protein ligase 2,SMURF2
EIAAB38892 E3 ubiquitin-protein ligase SMURF2,Mouse,Mus musculus,SMAD ubiquitination regulatory factor 2,SMAD-specific E3 ubiquitin-protein ligase 2,Smurf2
SMURF1 SMURF1 Gene SMAD specific E3 ubiquitin protein ligase 1
CSB-EL021860MO Mouse SMAD specific E3 ubiquitin protein ligase 1 (SMURF1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL021860HU Human SMAD specific E3 ubiquitin protein ligase 1 (SMURF1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL021860MO Mouse E3 ubiquitin-protein ligase SMURF1(SMURF1) ELISA kit SpeciesMouse 96T
CSB-EL021860HU Human E3 ubiquitin-protein ligase SMURF1(SMURF1) ELISA kit SpeciesHuman 96T
CSB-EL021860MO Mouse E3 ubiquitin-protein ligase SMURF1(SMURF1) ELISA kit 96T
CSB-EL021860HU Human E3 ubiquitin-protein ligase SMURF1(SMURF1) ELISA kit 96T
SMUF1_MOUSE ELISA Kit FOR E3 ubiquitin-protein ligase SMURF1; organism: Mouse; gene name: Smurf1 96T
E2373h Human SMAD Specific E3 Ubiquitin Protein Ligase 2 96T
E2374h Human SMAD Specific E3 Ubiquitin Protein Ligase 1 96T
25-845 HACE1 contains 6 ANK repeats and 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain. HACE1 is an E3 ubiquitin-protein ligase that may function in cellular proteins degradation. 0.05 mg
EIAAB45118 E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,EDD,EDD1,hHYD,Homo sapiens,Human,HYD,Hyperplastic discs protein homolog,KIAA0896,Progestin-induced protein,UBR5
EIAAB45119 E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,Edd,Edd1,Hyperplastic discs protein homolog,Kiaa0896,Mouse,Mus musculus,Ubr5
EIAAB45120 100 kDa protein,Dd5,E3 ubiquitin-protein ligase UBR5,E3 ubiquitin-protein ligase, HECT domain-containing 1,Edd,Edd1,Hyd,Hyperplastic discs protein homolog,Rat,Rattus norvegicus,Ubr5
CSB-EL021861HU Human SMAD specific E3 ubiquitin protein ligase 2 (SMURF2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL021861MO Mouse SMAD specific E3 ubiquitin protein ligase 2 (SMURF2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
SMURF2 SMURF2 Gene SMAD specific E3 ubiquitin protein ligase 2
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB25831 C1orf166,E3 ubiquitin-protein ligase MUL1,GIDE,Growth inhibition and death E3 ligase,Homo sapiens,Human,MAPL,Mitochondrial ubiquitin ligase activator of NFKB 1,Mitochondrial-anchored protein ligase,MU
29-830 ARIH1 might act as an E3 ubiquitin-protein ligase, or as part of the E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3_UBCM4, and then transfers it to 0.1 mg


 

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