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

Ubiquitin-conjugating enzyme E2 N (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme N) (Protein bendless) (Ubiquitin carrier protein N) (Ubiquitin-conjugating enzyme E2-17 kDa) (Ubiquitin-protein ligase D3) (Ubiquitin-protein ligase N)

 UBE2N_DROME             Reviewed;         151 AA.
P35128; A9YHJ7; Q9VY67;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=Ubiquitin-conjugating enzyme E2 N;
EC=2.3.2.23;
AltName: Full=E2 ubiquitin-conjugating enzyme N;
AltName: Full=Protein bendless;
AltName: Full=Ubiquitin carrier protein N;
AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa;
AltName: Full=Ubiquitin-protein ligase D3;
AltName: Full=Ubiquitin-protein ligase N;
Name=ben; Synonyms=UbcD3; ORFNames=CG18319;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DISRUPTION PHENOTYPE.
PubMed=8394720; DOI=10.1016/0896-6273(93)90182-Q;
Muralidhar M., Thomas J.B.;
"The Drosophila bendless gene encodes a neural protein related to
ubiquitin-conjugating enzymes.";
Neuron 11:253-266(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8182464;
Oh C.E., McMahon R., Benzer S., Tanouye M.A.;
"Bendless, a Drosophila gene affecting neuronal connectivity, encodes
a ubiquitin-conjugating enzyme homolog.";
J. Neurosci. 14:3166-3179(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ZW104, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140, ZW141,
ZW142, ZW143, and ZW144;
PubMed=17989248; DOI=10.1101/gr.6691007;
Andolfatto P.;
"Hitchhiking effects of recurrent beneficial amino acid substitutions
in the Drosophila melanogaster genome.";
Genome Res. 17:1755-1762(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[5]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
-!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
proteins.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- INTERACTION:
Q9VRL1:Uev1A; NbExp=4; IntAct=EBI-101550, EBI-192329;
-!- DISRUPTION PHENOTYPE: Mutants in this gene exhibit several,
largely neuronal defects including lesions affecting the neuronal
connectivity of the giant fiber with the "jumping muscle", and the
axons of photoreceptor cells R7 and R8 fail to make the proper
right-angle turn into the medulla (hence the term "bendless").
{ECO:0000269|PubMed:8394720}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L20126; AAA28392.1; -; mRNA.
EMBL; S70118; AAB30753.1; -; mRNA.
EMBL; EU217226; ABW92183.1; -; Genomic_DNA.
EMBL; EU217227; ABW92184.1; -; Genomic_DNA.
EMBL; EU217228; ABW92185.1; -; Genomic_DNA.
EMBL; EU217229; ABW92186.1; -; Genomic_DNA.
EMBL; EU217230; ABW92187.1; -; Genomic_DNA.
EMBL; EU217231; ABW92188.1; -; Genomic_DNA.
EMBL; EU217232; ABW92189.1; -; Genomic_DNA.
EMBL; EU217233; ABW92190.1; -; Genomic_DNA.
EMBL; EU217234; ABW92191.1; -; Genomic_DNA.
EMBL; EU217235; ABW92192.1; -; Genomic_DNA.
EMBL; EU217236; ABW92193.1; -; Genomic_DNA.
EMBL; EU217237; ABW92194.1; -; Genomic_DNA.
EMBL; AE014298; AAF48338.1; -; Genomic_DNA.
EMBL; AY069527; AAL39672.1; -; mRNA.
PIR; S35793; S35793.
RefSeq; NP_001162752.1; NM_001169281.2.
RefSeq; NP_001245663.1; NM_001258734.2.
RefSeq; NP_001259540.1; NM_001272611.2.
RefSeq; NP_001259541.1; NM_001272612.2.
RefSeq; NP_511150.1; NM_078595.3.
UniGene; Dm.2088; -.
ProteinModelPortal; P35128; -.
SMR; P35128; -.
BioGrid; 58728; 12.
DIP; DIP-22866N; -.
IntAct; P35128; 3.
MINT; MINT-1003000; -.
STRING; 7227.FBpp0073686; -.
PaxDb; P35128; -.
PRIDE; P35128; -.
EnsemblMetazoa; FBtr0073855; FBpp0073686; FBgn0000173.
EnsemblMetazoa; FBtr0300566; FBpp0289793; FBgn0000173.
EnsemblMetazoa; FBtr0307296; FBpp0298297; FBgn0000173.
EnsemblMetazoa; FBtr0332843; FBpp0305066; FBgn0000173.
EnsemblMetazoa; FBtr0332844; FBpp0305067; FBgn0000173.
GeneID; 32358; -.
KEGG; dme:Dmel_CG18319; -.
UCSC; CG18319-RA; d. melanogaster.
CTD; 32358; -.
FlyBase; FBgn0000173; ben.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00540000070023; -.
InParanoid; P35128; -.
KO; K10580; -.
OMA; YFDVTIQ; -.
OrthoDB; EOG091G0VPD; -.
PhylomeDB; P35128; -.
Reactome; R-DME-446652; Interleukin-1 family signaling.
Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-DME-937039; IRAK1 recruits IKK complex.
Reactome; R-DME-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-DME-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
SignaLink; P35128; -.
UniPathway; UPA00143; -.
GenomeRNAi; 32358; -.
PRO; PR:P35128; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0000173; -.
ExpressionAtlas; P35128; differential.
Genevisible; P35128; DM.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
GO; GO:0035370; C:UBC13-UEV1A complex; IDA:FlyBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IPI:FlyBase.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:FlyBase.
GO; GO:0007412; P:axon target recognition; IMP:FlyBase.
GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
GO; GO:0007629; P:flight behavior; IMP:FlyBase.
GO; GO:0007625; P:grooming behavior; IMP:FlyBase.
GO; GO:0007630; P:jump response; IMP:FlyBase.
GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
GO; GO:0008594; P:photoreceptor cell morphogenesis; IMP:FlyBase.
GO; GO:0010942; P:positive regulation of cell death; IGI:FlyBase.
GO; GO:0046330; P:positive regulation of JNK cascade; IGI:FlyBase.
GO; GO:0045977; P:positive regulation of mitotic cell cycle, embryonic; IMP:FlyBase.
GO; GO:1902916; P:positive regulation of protein polyubiquitination; IMP:FlyBase.
GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
GO; GO:0000209; P:protein polyubiquitination; IDA:FlyBase.
GO; GO:0072347; P:response to anesthetic; IMP:FlyBase.
GO; GO:0006979; P:response to oxidative stress; IMP:FlyBase.
GO; GO:0060074; P:synapse maturation; IMP:FlyBase.
GO; GO:0051124; P:synaptic growth at neuromuscular junction; IMP:FlyBase.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Nucleotide-binding;
Reference proteome; Transferase; Ubl conjugation pathway.
CHAIN 1 151 Ubiquitin-conjugating enzyme E2 N.
/FTId=PRO_0000082521.
ACT_SITE 87 87 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
SEQUENCE 151 AA; 17236 MW; 1D096E72A7AEA420 CRC64;
MSSLPRRIIK ETQRLMQEPV PGINAIPDEN NARYFHVIVT GPNDSPFEGG VFKLELFLPE
DYPMSAPKVR FITKIYHPNI DRLGRICLDV LKDKWSPALQ IRTILLSIQA LLSAPNPDDP
LANDVAELWK VNEAEAIRNA REWTQKYAVE D


Related products :

Catalog number Product name Quantity
EIAAB44898 Bendless-like ubiquitin-conjugating enzyme,BLU,Homo sapiens,Human,Ubc13,UBE2N,Ubiquitin carrier protein N,Ubiquitin-conjugating enzyme E2 N,Ubiquitin-protein ligase N
EIAAB44901 Homo sapiens,Human,KIAA1734,UBE2O,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase
EIAAB44899 Bendless-like ubiquitin-conjugating enzyme,Blu,Mouse,Mus musculus,Ubc13,Ube2n,Ubiquitin carrier protein N,Ubiquitin-conjugating enzyme E2 N,Ubiquitin-protein ligase N
EIAAB44900 Bendless-like ubiquitin-conjugating enzyme,Rat,Rattus norvegicus,Ube2n,Ubiquitin carrier protein N,Ubiquitin-conjugating enzyme E2 N,Ubiquitin-protein ligase N
EIAAB44902 Kiaa1734,Mouse,Mus musculus,Ube2o,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase
EIAAB44905 E2epf,Mouse,Mus musculus,Ube2s,Ubiquitin carrier protein S,Ubiquitin-conjugating enzyme E2 S,Ubiquitin-conjugating enzyme E2-24 kDa,Ubiquitin-conjugating enzyme E2-EPF5,Ubiquitin-protein ligase S
18-003-42472 Ubiquitin-conjugating enzyme E2 N - EC 6.3.2.19; Ubiquitin-protein ligase N; Ubiquitin carrier protein N; Ubc13; Bendless-like ubiquitin-conjugating enzyme Polyclonal 0.1 mg Protein A
EIAAB44778 Mouse,Mus musculus,Ube2d1,Ubiquitin carrier protein D1,Ubiquitin-conjugating enzyme E2 D1,Ubiquitin-conjugating enzyme E2(17)KB 1,Ubiquitin-conjugating enzyme E2-17 kDa 1,Ubiquitin-protein ligase D1
EIAAB44788 Mouse,Mus musculus,Ube2d3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protein ligase D3
EIAAB44779 Rat,Rattus norvegicus,Ube2d1,Ubiquitin carrier protein D1,Ubiquitin-conjugating enzyme E2 D1,Ubiquitin-conjugating enzyme E2(17)KB 1,Ubiquitin-conjugating enzyme E2-17 kDa 1,Ubiquitin-protein ligase D
E1063h ELISA hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
U1063h CLIA hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
E1063h ELISA kit hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
U1063Rb CLIA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063Rb ELISA kit HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063Rb ELISA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063r ELISA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
U1063r CLIA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063r ELISA kit HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
EIAAB44754 Homo sapiens,Human,Putative ubiquitin-conjugating enzyme E2 D2-like protein,UBE2D2L,UBE2DNL,Ubiquitin carrier protein D2-like,Ubiquitin-conjugating enzyme E2D N-terminal-like,Ubiquitin-protein ligase
EIAAB44789 Homo sapiens,Human,UBC5C,UBCH5C,UBE2D3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protei
EIAAB44903 E2EPF,E2-EPF,Homo sapiens,Human,OK_SW-cl.73,UBE2S,Ubiquitin carrier protein S,Ubiquitin-conjugating enzyme E2 S,Ubiquitin-conjugating enzyme E2-24 kDa,Ubiquitin-conjugating enzyme E2-EPF5,Ubiquitin-pr
EIAAB44783 Mouse,Mus musculus,Ubc4,Ubch4,Ubch5b,Ube2d2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiquitin-p
EIAAB44891 Homo sapiens,Human,UbcH2,UBE2H,Ubiquitin carrier protein H,Ubiquitin-conjugating enzyme E2 H,Ubiquitin-conjugating enzyme E2-20K,Ubiquitin-protein ligase H
EIAAB44820 Oryctolagus cuniculus,Rabbit,UBE2Q2,Ubiquitin carrier protein Q2,Ubiquitin-conjugating enzyme E2 Q2,Ubiquitin-conjugating enzyme UBCi,Ubiquitin-protein ligase Q2


 

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