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

40S ribosomal protein S15 (RIG protein) (Small ribosomal subunit protein uS19)

 RS15_HUMAN              Reviewed;         145 AA.
P62841; A5D8V9; P11174; Q3KRA1; Q9UDC2;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
20-DEC-2017, entry version 145.
RecName: Full=40S ribosomal protein S15;
AltName: Full=RIG protein;
AltName: Full=Small ribosomal subunit protein uS19 {ECO:0000303|PubMed:24524803};
Name=RPS15; Synonyms=RIG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2821540; DOI=10.1073/pnas.84.19.6659;
Inoue C., Shiga K., Takasawa S., Kitagawa M., Yamamoto H., Okamoto H.;
"Evolutionary conservation of the insulinoma gene rig and its possible
function.";
Proc. Natl. Acad. Sci. U.S.A. 84:6659-6662(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2159154; DOI=10.1073/pnas.87.9.3594;
Shiga K., Yamamoto H., Okamoto H.;
"Isolation and characterization of the human homologue of rig and its
pseudogenes: the functional gene has features characteristic of
housekeeping genes.";
Proc. Natl. Acad. Sci. U.S.A. 87:3594-3598(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Yu L., Zhao S.Y.;
"Cloning and characterization of human insulinoma protein.";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 11-145.
TISSUE=Brain;
PubMed=1466847;
Rosenblatt J.D., Tomkins P., Rosenthal M., Kacena A., Chan G.,
Valderama R., Harrington W. Jr., Saxton E., Diagne A., Zhao J.-Q.,
Mitsuyasu R.T., Weisbart R.H.;
"Progressive spastic myelopathy in a patient co-infected with HIV-1
and HTLV-II: autoantibodies to the human homologue of rig in blood and
cerebrospinal fluid.";
AIDS 6:1151-1158(1992).
[6]
PROTEIN SEQUENCE OF 101-116.
TISSUE=Placenta;
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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).
[10]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-108, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[14]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- INTERACTION:
Q7L622:G2E3; NbExp=3; IntAct=EBI-372635, EBI-751757;
Q5S007:LRRK2; NbExp=9; IntAct=EBI-372635, EBI-5323863;
-!- SIMILARITY: Belongs to the universal ribosomal protein uS19
family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J02984; AAA36036.1; -; mRNA.
EMBL; M32405; AAA36568.1; -; Genomic_DNA.
EMBL; AF145025; AAP97277.1; -; mRNA.
EMBL; BC064908; AAH64908.1; -; mRNA.
EMBL; BC105810; AAI05811.1; -; mRNA.
EMBL; BC141832; AAI41833.1; -; mRNA.
CCDS; CCDS12067.1; -.
PIR; A35908; R3HU15.
RefSeq; NP_001009.1; NM_001018.4.
UniGene; Hs.406683; -.
PDB; 4UG0; EM; -; SP=1-145.
PDB; 4V6X; EM; 5.00 A; AP=1-145.
PDB; 5A2Q; EM; 3.90 A; P=1-145.
PDB; 5AJ0; EM; 3.50 A; BP=1-145.
PDB; 5FLX; EM; 3.90 A; P=1-145.
PDB; 5LKS; EM; 3.60 A; SP=1-145.
PDB; 5OA3; EM; 4.30 A; P=1-145.
PDB; 5T2C; EM; 3.60 A; Ax=1-145.
PDB; 5VYC; X-ray; 6.00 A; P1/P2/P3/P4/P5/P6=1-145.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5OA3; -.
PDBsum; 5T2C; -.
PDBsum; 5VYC; -.
ProteinModelPortal; P62841; -.
SMR; P62841; -.
BioGrid; 112123; 150.
CORUM; P62841; -.
IntAct; P62841; 23.
MINT; MINT-5004408; -.
STRING; 9606.ENSP00000467676; -.
iPTMnet; P62841; -.
PhosphoSitePlus; P62841; -.
SwissPalm; P62841; -.
BioMuta; RPS15; -.
DMDM; 51338641; -.
EPD; P62841; -.
MaxQB; P62841; -.
PaxDb; P62841; -.
PeptideAtlas; P62841; -.
PRIDE; P62841; -.
TopDownProteomics; P62841; -.
DNASU; 6209; -.
Ensembl; ENST00000592588; ENSP00000467466; ENSG00000115268.
GeneID; 6209; -.
KEGG; hsa:6209; -.
UCSC; uc002lsp.2; human.
CTD; 6209; -.
DisGeNET; 6209; -.
EuPathDB; HostDB:ENSG00000115268.9; -.
GeneCards; RPS15; -.
HGNC; HGNC:10388; RPS15.
HPA; HPA054510; -.
HPA; HPA057793; -.
MalaCards; RPS15; -.
MIM; 180535; gene.
neXtProt; NX_P62841; -.
OpenTargets; ENSG00000115268; -.
PharmGKB; PA34787; -.
eggNOG; KOG0898; Eukaryota.
eggNOG; COG0185; LUCA.
GeneTree; ENSGT00390000000475; -.
HOGENOM; HOG000111561; -.
HOVERGEN; HBG000709; -.
InParanoid; P62841; -.
KO; K02958; -.
PhylomeDB; P62841; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RPS15; human.
EvolutionaryTrace; P62841; -.
GeneWiki; RPS15; -.
GenomeRNAi; 6209; -.
PMAP-CutDB; P62841; -.
PRO; PR:P62841; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000115268; -.
CleanEx; HS_RPS15; -.
ExpressionAtlas; P62841; baseline and differential.
Genevisible; P62841; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
GO; GO:0042274; P:ribosomal small subunit biogenesis; IMP:UniProtKB.
GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:UniProtKB.
GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; IC:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
Gene3D; 3.30.860.10; -; 1.
HAMAP; MF_00531; Ribosomal_S19; 1.
InterPro; IPR002222; Ribosomal_S19.
InterPro; IPR020934; Ribosomal_S19_CS.
InterPro; IPR023575; Ribosomal_S19_SF.
InterPro; IPR005713; Ribosomal_S19A/S15e.
PANTHER; PTHR11880; PTHR11880; 1.
Pfam; PF00203; Ribosomal_S19; 1.
PIRSF; PIRSF002144; Ribosomal_S19; 1.
PRINTS; PR00975; RIBOSOMALS19.
SUPFAM; SSF54570; SSF54570; 1.
TIGRFAMs; TIGR01025; uS19_arch; 1.
PROSITE; PS00323; RIBOSOMAL_S19; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Isopeptide bond; Reference proteome;
Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 145 40S ribosomal protein S15.
/FTId=PRO_0000130027.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CROSSLNK 108 108 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
SEQUENCE 145 AA; 17040 MW; CA2C682302C7B387 CRC64;
MAEVEQKKKR TFRKFTYRGV DLDQLLDMSY EQLMQLYSAR QRRRLNRGLR RKQHSLLKRL
RKAKKEAPPM EKPEVVKTHL RDMIILPEMV GSMVGVYNGK TFNQVEIKPE MIGHYLGEFS
ITYKPVKHGR PGIGATHSSR FIPLK


Related products :

Catalog number Product name Quantity
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
29-214 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
29-215 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
29-216 RPL6 is a ribosomal protein that is a component of the 60S subunit. RPL6 belongs to the L6E family of ribosomal proteins. It is located in the cytoplasm. The protein can bind specifically to domain C 0.1 mg
EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
EIAAB34981 60S ribosomal protein L22,EAP,EBER-associated protein,Epstein-Barr virus small RNA-associated protein,Heparin-binding protein HBp15,Homo sapiens,Human,RPL22
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
EIAAB35181 C15orf15,Homo sapiens,Human,My024,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,RPL24L,RSL24D1
EIAAB36079 40S ribosomal protein S2,40S ribosomal protein S4,Homo sapiens,Human,Protein LLRep3,RPS2,RPS4
26-118 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPL39 is a 39S subunit protein. Mammalian mitochondrial ribosomal proteins are encoded by nuclear genes 0.05 mg
EIAAB35073 60S ribosomal protein L36a,60S ribosomal protein L44,Cell growth-inhibiting gene 15 protein,Cell migration-inducing gene 6 protein,GIG15,Homo sapiens,Human,MIG6,RPL36A,RPL44
29-101 Mammalian mitochondrial ribosomal proteins help in protein synthesis within the mitochondrion. Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS15 is 0.1 mg
EIAAB35249 39S ribosomal protein L23, mitochondrial,Homo sapiens,Human,L23 mitochondrial-related protein,L23MRP,L23mt,MRPL23,MRP-L23,Ribosomal protein L23-like,RPL23L
EIAAB35154 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Rat,Rattus norvegicus,Rplp0
EIAAB33379 60S ribosomal protein L39 pseudogene 5,Homo sapiens,Human,Putative 60S ribosomal protein L39-like 5,RPL39P5
EIAAB35156 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Arbp,Mouse,Mus musculus,Rplp0
EIAAB35158 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Homo sapiens,Human,RPLP0
18-783-75538 RABBIT ANTI RIBOSOMAL S6 KINASE 2 (C-TERMINAL) - RIBOSOMAL PROTEIN S6 KINASE ALPHA-2; EC 2.7.11.1; S6K-alpha 2; 90 kDa ribosomal protein S6 kinase 2; p90-RSK 2; Ribosomal S6 kinase 3; RSK-3; pp90RSK3; 0.1 ml
29-221 RPL32 is a ribosomal protein that is a component of the 60S subunit. RPL32 belongs to the L32E family of ribosomal proteins. It is located in the cytoplasm. Although some studies have mapped this gene 0.1 mg
EIAAB35072 60S ribosomal protein L36a,60S ribosomal protein L44,Rat,Rattus norvegicus,Rpl36a,Rpl44
EIAAB35071 60S ribosomal protein L36a,60S ribosomal protein L44,Mouse,Mus musculus,Rpl36a,Rpl44
EIAAB35096 60S ribosomal protein L39-2,60S ribosomal protein L39-like,Homo sapiens,Human,RPL39L,RPL39L1
EIAAB35157 60S acidic ribosomal protein P0,60S ribosomal protein L10E,Bos taurus,Bovine,RPLP0


 

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