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

DASH complex subunit DUO1 (Death upon overproduction protein 1) (Outer kinetochore protein DUO1)

 DUO1_YEAST              Reviewed;         247 AA.
P53168; D6VU80;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
18-JUL-2018, entry version 145.
RecName: Full=DASH complex subunit DUO1;
AltName: Full=Death upon overproduction protein 1;
AltName: Full=Outer kinetochore protein DUO1;
Name=DUO1; OrderedLocusNames=YGL061C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9234674;
DOI=10.1002/(SICI)1097-0061(199707)13:9<861::AID-YEA125>3.0.CO;2-9;
Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
"The characterization of two new clusters of duplicated genes suggests
a 'Lego' organization of the yeast Saccharomyces cerevisiae
chromosomes.";
Yeast 13:861-869(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169869;
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M.,
Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J.,
Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E.,
Clemente M.L., Coblenz A., Coglievina M., Coissac E., Defoor E.,
Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B.,
Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L.,
Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M.,
Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M.,
Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B.,
Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W.,
Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A.,
Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S.,
Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L.,
Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S.,
Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J.,
Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M.,
Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B.,
Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J.,
Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M.,
van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M.,
Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H.,
Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M.,
Zollner A., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
Nature 387:81-84(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-67; ALA-117;
MET-124 AND ALA-157.
PubMed=9817759; DOI=10.1083/jcb.143.4.1029;
Hofmann C., Cheeseman I.M., Goode B.L., McDonald K.L., Barnes G.,
Drubin D.G.;
"Saccharomyces cerevisiae Duo1p and Dam1p, novel proteins involved in
mitotic spindle function.";
J. Cell Biol. 143:1029-1040(1998).
[6]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[7]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[8]
FUNCTION.
PubMed=15664196; DOI=10.1016/j.molcel.2004.12.019;
Westermann S., Avila-Sakar A., Wang H.-W., Niederstrasser H., Wong J.,
Drubin D.G., Nogales E., Barnes G.;
"Formation of a dynamic kinetochore-microtubule interface through
assembly of the Dam1 ring complex.";
Mol. Cell 17:277-290(2005).
[9]
FUNCTION.
PubMed=16415853; DOI=10.1038/nature04409;
Westermann S., Wang H.-W., Avila-Sakar A., Drubin D.G., Nogales E.,
Barnes G.;
"The Dam1 kinetochore ring complex moves processively on
depolymerizing microtubule ends.";
Nature 440:565-569(2006).
[10]
SUBUNIT.
PubMed=16715078; DOI=10.1038/ncb1414;
Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
"Molecular architecture of a kinetochore-microtubule attachment
site.";
Nat. Cell Biol. 8:581-585(2006).
[11]
FUNCTION.
PubMed=16777964; DOI=10.1073/pnas.0602249103;
Asbury C.L., Gestaut D.R., Powers A.F., Franck A.D., Davis T.N.;
"The Dam1 kinetochore complex harnesses microtubule dynamics to
produce force and movement.";
Proc. Natl. Acad. Sci. U.S.A. 103:9873-9878(2006).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[13]
ELECTRON MICROSCOPY OF DASH COMPLEX ALONE AND BOUND TO MICROTUBULES.
PubMed=15640796; DOI=10.1038/nsmb896;
Miranda J.L., Wulf P.D., Sorger P.K., Harrison S.C.;
"The yeast DASH complex forms closed rings on microtubules.";
Nat. Struct. Mol. Biol. 12:138-143(2005).
-!- FUNCTION: Component of the DASH complex, a microtubule-binding
subcomplex of the outer kinetochore that is essential for proper
chromosome segregation. The DASH complex mediates the formation
and maintenance of bipolar kinetochore-microtubule attachments by
forming closed rings around spindle microtubules and establishing
interactions with proteins from the central kinetochore. The DASH
ring complex may both stabilize microtubules during chromosome
attachment in anaphase A, and allow the chromosome to remain
attached to the depolymerizing microtubule in anaphase B.
Microtubule depolymerization proceeds by protofilament splaying
and induces the kinetochore-attached ring to slide longitudinally,
thereby helping to transduce depolymerization energy into pulling
forces to disjoin chromatids. {ECO:0000269|PubMed:15664196,
ECO:0000269|PubMed:16415853, ECO:0000269|PubMed:16777964,
ECO:0000269|PubMed:9817759}.
-!- SUBUNIT: The DASH complex is an approximately 210 kDa
heterodecamer, which consists of ASK1, DAD1, DAD2, DAD3, DAD4,
DAM1, DUO1, HSK3, SPC19 and SPC34, with an apparent stoichiometry
of one copy of each subunit. DASH oligomerizes into a 50 nm ring
composed of about 16 molecules that encircles the microtubule.
Integrity of the complex and interactions with central kinetochore
proteins are regulated by the spindle assembly checkpoint kinase
IPL1. {ECO:0000269|PubMed:16715078}.
-!- INTERACTION:
P35734:ASK1; NbExp=9; IntAct=EBI-23800, EBI-26682;
Q12248:DAD1; NbExp=7; IntAct=EBI-23800, EBI-35662;
P36162:DAD2; NbExp=2; IntAct=EBI-23800, EBI-26515;
P53267:DAM1; NbExp=6; IntAct=EBI-23800, EBI-23268;
P25293:NAP1; NbExp=2; IntAct=EBI-23800, EBI-11850;
P32337:PSE1; NbExp=5; IntAct=EBI-23800, EBI-9159;
Q03954:SPC19; NbExp=5; IntAct=EBI-23800, EBI-38809;
P36131:SPC34; NbExp=5; IntAct=EBI-23800, EBI-26401;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:9817759}. Cytoplasm, cytoskeleton, spindle pole
{ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9817759}.
Chromosome, centromere, kinetochore {ECO:0000269|PubMed:9817759}.
Note=Associates with the mitotic spindle and the kinetochore.
{ECO:0000269|PubMed:9817759}.
-!- MISCELLANEOUS: Present with 996 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the DASH complex DUO1 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; Z72583; CAA96764.1; -; Genomic_DNA.
EMBL; AY558484; AAS56810.1; -; Genomic_DNA.
EMBL; BK006941; DAA08041.1; -; Genomic_DNA.
PIR; S64065; S64065.
RefSeq; NP_011454.1; NM_001180926.1.
ProteinModelPortal; P53168; -.
SMR; P53168; -.
BioGrid; 33186; 431.
ComplexPortal; CPX-1041; DASH complex.
DIP; DIP-1287N; -.
IntAct; P53168; 23.
MINT; P53168; -.
STRING; 4932.YGL061C; -.
CarbonylDB; P53168; -.
iPTMnet; P53168; -.
MaxQB; P53168; -.
PaxDb; P53168; -.
PRIDE; P53168; -.
EnsemblFungi; YGL061C; YGL061C; YGL061C.
GeneID; 852819; -.
KEGG; sce:YGL061C; -.
EuPathDB; FungiDB:YGL061C; -.
SGD; S000003029; DUO1.
HOGENOM; HOG000112294; -.
InParanoid; P53168; -.
KO; K11570; -.
OMA; IPQIFDQ; -.
OrthoDB; EOG092C5CMI; -.
BioCyc; YEAST:G3O-30569-MONOMER; -.
PRO; PR:P53168; -.
Proteomes; UP000002311; Chromosome VII.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0042729; C:DASH complex; IDA:SGD.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0072686; C:mitotic spindle; IEA:InterPro.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:1990758; P:mitotic sister chromatid biorientation; IBA:GO_Central.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IDA:SGD.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:SGD.
InterPro; IPR013960; DASH_Duo1.
Pfam; PF08651; DASH_Duo1; 1.
1: Evidence at protein level;
Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
Chromosome partition; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Kinetochore; Microtubule; Mitosis; Nucleus;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 247 DASH complex subunit DUO1.
/FTId=PRO_0000215595.
COILED 152 180 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MUTAGEN 67 67 E->K: In DUO1-1; produces abnormal
spindles resulting in growth arrest at 37
degrees Celsius; when associated with V-
157. {ECO:0000269|PubMed:9817759}.
MUTAGEN 117 117 A->T: In DUO1-2; produces abnormal
spindles resulting in growth arrest at 37
degrees Celsius; when associated with I-
124. {ECO:0000269|PubMed:9817759}.
MUTAGEN 124 124 M->I: In DUO1-2; produces abnormal
spindles resulting in growth arrest at 37
degrees Celsius; when associated with T-
117. {ECO:0000269|PubMed:9817759}.
MUTAGEN 157 157 A->V: In DUO1-1; produces abnormal
spindles resulting in growth arrest at 37
degrees Celsius; when associated with K-
67. {ECO:0000269|PubMed:9817759}.
SEQUENCE 247 AA; 27473 MW; 787F8AF869E3C978 CRC64;
MSEQSQLDDS TIDKLIPQIF NEMRSNLNNT TNKFPKSTGG GASDNISANS NSIRSFNSIT
TQSLLKESES LDKITAMIKN VTAALKNNLP VYVNQVHEVC KSTNSILDSW INIHSQAGYI
HKLMSDQTYL KLINDRLHNE NVNTNDEDGS TLHNVIALKK KEILDLRQKL ENRKGEKDAA
PAKPPNQGLN PRYGVQSGRR PVPSAGISNN GRVRKTHVPA SKRPSGIPRV TNRWTKPTAS
SSRKMFR


Related products :

Catalog number Product name Quantity
20-372-60258 NDC80 homolog. kinetochore complex component (S.cerevisiae) (NDC80) - Mouse monoclonal anti-human KNTC2 antibody; HsHec1; Kinetochore-associated protein 2; Highly expressed in cancer protein; Retinobl 0.1 mg
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.1 mg
15-288-21448A AP-3 complex subunit beta-2 - Adapter-related protein complex 3 beta-2 subunit; Beta3B-adaptin; Adaptor protein complex AP-3 beta-2 subunit; AP-3 complex beta-2 subunit; Clathrin assembly protein comp 0.05 mg
EIAAB26607 HEC,HEC1,Highly expressed in cancer protein,Homo sapiens,HsHec1,Human,Kinetochore protein Hec1,Kinetochore protein NDC80 homolog,Kinetochore-associated protein 2,KNTC2,NDC80,Retinoblastoma-associated
30-917 FEM1B is a component of an E3 ubiquitin-protein ligase complex, in which it may act as a substrate recognition subunit. It involved in apoptosis by acting as a death receptor-associated protein that m 0.05 mg
EIAAB33317 Complex III subunit 9,Complex III subunit X,Cytochrome b-c1 complex subunit 9,Cytochrome c1 non-heme 7 kDa protein,Homo sapiens,HSPC119,Human,Ubiquinol-cytochrome c reductase complex 7.2 kDa protein,U
EIAAB33316 Complex III subunit 9,Complex III subunit X,Cytochrome b-c1 complex subunit 9,Cytochrome c1 non-heme 7 kDa protein,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 7.2 kDa protein,Uqcr10
EIAAB33318 Bos taurus,Bovine,Complex III subunit 9,Complex III subunit X,Cytochrome b-c1 complex subunit 9,Cytochrome c1 non-heme 7 kDa protein,Ubiquinol-cytochrome c reductase complex 7.2 kDa protein,UQCR10
EIAAB33312 Complex III subunit 8,Complex III subunit VIII,Cytochrome b-c1 complex subunit 8,Low molecular mass ubiquinone-binding protein,Qpc,Rat,Rattus norvegicus,Ubiquinol-cytochrome c reductase complex 9.5 kD
EIAAB33305 Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Homo sapiens,Human,Mitochondrial hinge protein,Ubiquinol-cytochrom
EIAAB33310 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Homo sapiens,Human,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQBP,UQCRB
EIAAB33299 Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Homo sapiens,Human,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,UQCR,UQCR11
EIAAB33306 Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Mitochondrial hinge protein,Rat,Rattus norvegicus,Ubiquinol-cytoch
EIAAB33308 Complex III subunit 6,Complex III subunit VIII,Cytochrome b-c1 complex subunit 6, mitochondrial,Cytochrome c1 non-heme 11 kDa protein,Mitochondrial hinge protein,Mouse,Mus musculus,Ubiquinol-cytochrom
EIAAB33300 Bos taurus,Bovine,Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,UQCR,UQCR11
EIAAB33298 Complex III subunit 10,Complex III subunit XI,Cytochrome b-c1 complex subunit 10,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 6.4 kDa protein,Uqcr,Uqcr11
EIAAB26608 Hec1,Kinetochore protein Hec1,Kinetochore protein NDC80 homolog,Kinetochore-associated protein 2,Kntc2,Mouse,Mus musculus,Ndc80
EIAAB08150 CAP-G2,Chromosome-associated protein G2,Condensin-2 complex subunit G2,Leucine zipper protein 5,Luzp5,More than blood protein,Mouse,Mtb,Mus musculus,Ncapg2,Non-SMC condensin II complex subunit G2
EIAAB33309 Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,Mouse,Mus musculus,Ubiquinol-cytochrome c reductase complex 14 kDa protein,Uqcrb
EIAAB33311 Bos taurus,Bovine,Complex III subunit 7,Complex III subunit VII,Cytochrome b-c1 complex subunit 7,QP-C,Ubiquinol-cytochrome c reductase complex 14 kDa protein,UQCRB
5401 Spindle and kinetochore associated complex subunit 1 0.1 mg
5403 Spindle and kinetochore associated complex subunit 2 0.5 mg
5401 Spindle and kinetochore associated complex subunit 1 0.5 mg
5405 Spindle and kinetochore associated complex subunit 3 0.1 mg
5403 Spindle and kinetochore associated complex subunit 2 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