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

COP9 signalosome complex subunit 5b (Signalosome subunit 5b) (EC 3.4.-.-) (Jun activation domain-binding homolog 2)

 CSN5B_ARATH             Reviewed;         358 AA.
Q9FVU9; O82523;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
28-FEB-2018, entry version 119.
RecName: Full=COP9 signalosome complex subunit 5b;
Short=Signalosome subunit 5b;
EC=3.4.-.-;
AltName: Full=Jun activation domain-binding homolog 2;
Name=CSN5B {ECO:0000303|PubMed:23424245};
Synonyms=AJH2 {ECO:0000303|PubMed:9811788},
CSN5A {ECO:0000303|PubMed:11742986};
OrderedLocusNames=At1g71230 {ECO:0000312|Araport:AT1G71230};
ORFNames=F3I17.12 {ECO:0000312|EMBL:AAG51882.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND SUBUNIT.
TISSUE=Seedling;
PubMed=9811788; DOI=10.1105/tpc.10.11.1779;
Kwok S.F., Solano R., Tsuge T., Chamovitz D.A., Ecker J.R., Matsui M.,
Deng X.-W.;
"Arabidopsis homologs of a c-Jun coactivator are present both in
monomeric form and in the COP9 complex, and their abundance is
differentially affected by the pleiotropic cop/det/fus mutations.";
Plant Cell 10:1779-1790(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
PubMed=11742986; DOI=10.1093/emboj/20.24.7096;
Fu H., Reis N., Lee Y., Glickman M.H., Vierstra R.;
"Subunit interaction maps for the regulatory particle of the 26S
proteasome and the COP9 signalosome.";
EMBO J. 20:7096-7107(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION.
PubMed=11337587; DOI=10.1126/science.1059776;
Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
"Interactions of the COP9 signalosome with the E3 ubiquitin ligase
SCF(TIR1) in mediating auxin response.";
Science 292:1379-1382(2001).
[7]
INTERACTION WITH CSN4 AND CSN6.
PubMed=12615944; DOI=10.1105/tpc.009092;
Serino G., Su H., Peng Z., Tsuge T., Wei N., Gu H., Deng X.-W.;
"Characterization of the last subunit of the Arabidopsis COP9
signalosome: implications for the overall structure and origin of the
complex.";
Plant Cell 15:719-731(2003).
[8]
FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND MUTAGENESIS OF HIS-142;
HIS-144; CYS-149; ASP-155 AND ASP-175.
PubMed=15486099; DOI=10.1105/tpc.104.025999;
Gusmaroli G., Feng S., Deng X.W.;
"The Arabidopsis CSN5A and CSN5B subunits are present in distinct COP9
signalosome complexes, and mutations in their JAMM domains exhibit
differential dominant negative effects on development.";
Plant Cell 16:2984-3001(2004).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17307927; DOI=10.1105/tpc.106.047571;
Gusmaroli G., Figueroa P., Serino G., Deng X.W.;
"Role of the MPN subunits in COP9 signalosome assembly and activity,
and their regulatory interaction with Arabidopsis Cullin3-based E3
ligases.";
Plant Cell 19:564-581(2007).
[10]
INTERACTION WITH CYT1.
PubMed=23424245; DOI=10.1105/tpc.112.106880;
Wang J., Yu Y., Zhang Z., Quan R., Zhang H., Ma L., Deng X.W.,
Huang R.;
"Arabidopsis CSN5B interacts with VTC1 and modulates ascorbic acid
synthesis.";
Plant Cell 25:625-636(2013).
-!- FUNCTION: Probable protease subunit of the COP9 signalosome
complex (CSN), a complex involved in various cellular and
developmental processes such as photomorphogenesis and auxin and
jasmonate responses. The CSN complex is an essential regulator of
the ubiquitin (Ubl) conjugation pathway by mediating the
deneddylation of the cullin subunits of the SCF-type E3 ligase
complexes, leading to decrease the Ubl ligase activity of SCF. In
the complex, it probably acts as the catalytic center that
mediates the cleavage of Nedd8 from cullins. It however has no
metalloprotease activity by itself and requires the other subunits
of the CSN complex (By similarity). The CSN complex is involved in
repression of photomorphogenesis in darkness by regulating the
activity of COP1-containing Ubl ligase complexes. The complex is
also required for degradation of PSIAA6 by regulating the activity
of the Ubl ligase SCF-TIR complex. Not involved in CSN's
deneddylation/derubylation activity (PubMed:15486099,
PubMed:17307927). Essential for the structural integrity of the
CSN holocomplex (PubMed:17307927). {ECO:0000250,
ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:15486099,
ECO:0000269|PubMed:17307927, ECO:0000269|PubMed:9811788}.
-!- COFACTOR:
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
Evidence={ECO:0000250};
-!- SUBUNIT: Component of the CSN complex, probably composed of CSN1,
CSN2, CSN3, CSN4, CSN5 (CSN5A or CSN5B), CSN6 (CSN6A or CSN6B),
CSN7 and CSN8 (PubMed:9811788, PubMed:12615944, PubMed:15486099).
CSN5A or CSN5B are present within distinct CSN complexes each
containing only one copy of CSN5 (PubMed:15486099). Interacts with
itself (PubMed:9811788). In the complex, it is located in the
center and probably interacts directly with CSN4 and CSN6A or
CSN6B (PubMed:9811788, PubMed:12615944). Also exists as monomeric
form (PubMed:9811788). Interacts with CYT1 in vitro and in planta
(PubMed:23424245). {ECO:0000269|PubMed:12615944,
ECO:0000269|PubMed:15486099, ECO:0000269|PubMed:23424245,
ECO:0000269|PubMed:9811788}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9811788}.
Nucleus {ECO:0000269|PubMed:9811788}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
flowers and roots. Expressed at lower level in seedlings and
siliques. {ECO:0000269|PubMed:9811788}.
-!- DOMAIN: The JAMM motif is essential for the protease activity of
the CSN complex resulting in deneddylation of cullins. It
constitutes the catalytic center of the complex (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype and no effect on the
derubylation of CUL1 (PubMed:15486099, PubMed:17307927). Csn5a and
csn5b double mutants are lethal at the seedling stage
(PubMed:17307927). {ECO:0000269|PubMed:15486099,
ECO:0000269|PubMed:17307927}.
-!- SIMILARITY: Belongs to the peptidase M67A family. CSN5 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF087412; AAC36343.1; -; mRNA.
EMBL; AF395061; AAL58104.1; -; mRNA.
EMBL; AC016162; AAG51882.1; -; Genomic_DNA.
EMBL; CP002684; AEE35176.1; -; Genomic_DNA.
EMBL; AF411778; AAL06468.1; -; mRNA.
EMBL; AY124816; AAM70525.1; -; mRNA.
PIR; H96736; H96736.
PIR; T52042; T52042.
RefSeq; NP_177279.1; NM_105792.2.
UniGene; At.17922; -.
UniGene; At.68950; -.
ProteinModelPortal; Q9FVU9; -.
SMR; Q9FVU9; -.
BioGrid; 28683; 42.
IntAct; Q9FVU9; 59.
STRING; 3702.AT1G71230.1; -.
MEROPS; M67.A02; -.
PaxDb; Q9FVU9; -.
PRIDE; Q9FVU9; -.
EnsemblPlants; AT1G71230.1; AT1G71230.1; AT1G71230.
GeneID; 843463; -.
Gramene; AT1G71230.1; AT1G71230.1; AT1G71230.
KEGG; ath:AT1G71230; -.
Araport; AT1G71230; -.
TAIR; locus:2032288; AT1G71230.
eggNOG; KOG1554; Eukaryota.
eggNOG; COG1310; LUCA.
HOGENOM; HOG000116528; -.
InParanoid; Q9FVU9; -.
KO; K09613; -.
OMA; PHYFKQI; -.
OrthoDB; EOG09360E02; -.
PhylomeDB; Q9FVU9; -.
Reactome; R-ATH-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-ATH-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-ATH-8951664; Neddylation.
PRO; PR:Q9FVU9; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q9FVU9; baseline and differential.
Genevisible; Q9FVU9; AT.
GO; GO:0008180; C:COP9 signalosome; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0010387; P:COP9 signalosome assembly; IMP:TAIR.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0010100; P:negative regulation of photomorphogenesis; IGI:TAIR.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:TAIR.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:TAIR.
GO; GO:0000338; P:protein deneddylation; IGI:TAIR.
GO; GO:0009585; P:red, far-red light phototransduction; IEA:UniProtKB-KW.
GO; GO:2000082; P:regulation of L-ascorbic acid biosynthetic process; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IGI:TAIR.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR037518; MPN.
Pfam; PF01398; JAB; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Developmental protein;
Hydrolase; Metal-binding; Metalloprotease; Nucleus;
Phytochrome signaling pathway; Protease; Reference proteome;
Signalosome; Zinc.
CHAIN 1 358 COP9 signalosome complex subunit 5b.
/FTId=PRO_0000194842.
DOMAIN 59 196 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOTIF 142 155 JAMM motif. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 142 142 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 144 144 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 155 155 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q8LAZ7}.
MUTAGEN 142 142 H->A: No effect on CSN complex integrity
and no effect on CUL1 derubylation.
{ECO:0000269|PubMed:15486099}.
MUTAGEN 144 144 H->A: No effect on CSN complex integrity
and no effect on CUL1 derubylation.
{ECO:0000269|PubMed:15486099}.
MUTAGEN 149 149 C->A: No effect on CSN complex integrity
and no effect on CUL1 derubylation.
{ECO:0000269|PubMed:15486099}.
MUTAGEN 155 155 D->N: No effect on CSN complex integrity
and no effect on CUL1 derubylation.
{ECO:0000269|PubMed:15486099}.
MUTAGEN 175 175 D->E,N: No effect on CSN complex
integrity and no effect on CUL1
derubylation.
{ECO:0000269|PubMed:15486099}.
CONFLICT 160 160 R -> T (in Ref. 1; AAC36343).
{ECO:0000305}.
SEQUENCE 358 AA; 40318 MW; 4890F2D35F6FB410 CRC64;
MEGSSSTIAR KTWELENSIL TVDSPDSTSD NIFYYDDTSQ TRFQQEKPWE NDPHYFKRVK
ISALALLKMV VHARSGGTIE IMGLMQGKTD GDTIIVMDAF ALPVEGTETR VNAQDDAYEY
MVEYSQTNKL AGRLENVVGW YHSHPGYGCW LSGIDVSTQR LNQQHQEPFL AVVIDPTRTV
SAGKVEIGAF RTYSKGYKPP DEPVSEYQTI PLNKIEDFGV HCKQYYSLDV TYFKSSLDSH
LLDLLWNKYW VNTLSSSPLL GNGDYVAGQI SDLAEKLEQA ESHLVQSRFG GVVPSSLHKK
KEDESQLTKI TRDSAKITVE QVHGLMSQVI KDELFNSMRQ SNNKSPTDSS DPDPMITY


Related products :

Catalog number Product name Quantity
EIAAB09626 COP9 homolog,COP9 signalosome complex subunit 8,COPS8,CSN8,hCOP9,Homo sapiens,Human,JAB1-containing signalosome subunit 8,SGN8,Signalosome subunit 8
EIAAB09614 COP9 signalosome complex subunit 5,COPS5,CSN5,Homo sapiens,Human,JAB1,Jun activation domain-binding protein 1,SGN5,Signalosome subunit 5
EIAAB09624 COP9 homolog,COP9 signalosome complex subunit 8,Cops8,Csn8,JAB1-containing signalosome subunit 8,Rat,Rattus norvegicus,SGN8,Signalosome subunit 8
EIAAB09625 COP9 homolog,COP9 signalosome complex subunit 8,Cops8,Csn8,JAB1-containing signalosome subunit 8,Mouse,Mus musculus,SGN8,Signalosome subunit 8
18-001-30018 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.1 mg
18-003-43113 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.05 mg Aff Pur
18-003-43113 COP9 signalosome complex subunit 2 - Signalosome subunit 2; SGN2; JAB1-containing signalosome subunit 2; Thyroid receptor-interacting protein 15; Alien homolog Polyclonal 0.1 mg Protein A
EIAAB09600 Alien homolog,COP9 signalosome complex subunit 2,Cops2,Csn2,JAB1-containing signalosome subunit 2,Rat,Rattus norvegicus,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interactin
EIAAB09613 COP9 signalosome complex subunit 5,Cops5,Csn5,Jab1,Jun activation domain-binding protein 1,Kic2,Kip1 C-terminus-interacting protein 2,Mouse,Mus musculus,SGN5,Signalosome subunit 5
EIAAB09602 Alien homolog,COP9 signalosome complex subunit 2,Cops2,Csn2,JAB1-containing signalosome subunit 2,Mouse,Mus musculus,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
EIAAB09618 COP9 signalosome complex subunit 6,COPS6,CSN6,Homo sapiens,Human,hVIP,HVIP,JAB1-containing signalosome subunit 6,MOV34 homolog,SGN6,Signalosome subunit 6,Vpr-interacting protein
EIAAB09601 Alien homolog,COP9 signalosome complex subunit 2,COPS2,CSN2,Homo sapiens,Human,JAB1-containing signalosome subunit 2,SGN2,Signalosome subunit 2,Thyroid receptor-interacting protein 15,TR-interacting p
EIAAB09598 COP9 signalosome complex subunit 1,Cops1,Csn1,G protein pathway suppressor 1,Gps1,GPS-1,JAB1-containing signalosome subunit 1,Mouse,Mus musculus,SGN1,Signalosome subunit 1
EIAAB09609 COP9 signalosome complex subunit 4,COPS4,CSN4,Homo sapiens,Human,JAB1-containing signalosome subunit 4,SGN4,Signalosome subunit 4
EIAAB09603 COP9 signalosome complex subunit 3,COPS3,CSN3,Homo sapiens,Human,JAB1-containing signalosome subunit 3,SGN3,Signalosome subunit 3
EIAAB09621 COP9 signalosome complex subunit 7b,COPS7B,CSN7B,Homo sapiens,Human,JAB1-containing signalosome subunit 7b,SGN7b,Signalosome subunit 7b
EIAAB09619 COP9 signalosome complex subunit 7a,COPS7A,CSN7A,Dermal papilla-derived protein 10,DERP10,Homo sapiens,Human,JAB1-containing signalosome subunit 7a,SGN7a,Signalosome subunit 7a
EIAAB09620 COP9 signalosome complex subunit 7a,Cops7a,Csn7a,JAB1-containing signalosome subunit 7a,Mouse,Mus musculus,SGN7a,Signalosome subunit 7a
EIAAB09606 COP9 signalosome complex subunit 3,Cops3,Csn3,JAB1-containing signalosome subunit 3,Mouse,Mus musculus,SGN3,Signalosome subunit 3
EIAAB09622 COP9 signalosome complex subunit 7b,Cops7b,Csn7b,JAB1-containing signalosome subunit 7b,Mouse,Mus musculus,SGN7b,Signalosome subunit 7b
EIAAB09612 COP9 signalosome complex subunit 4,Cops4,Csn4,JAB1-containing signalosome subunit 4,Mouse,Mus musculus,SGN4,Signalosome subunit 4
EIAAB09608 COP9 signalosome complex subunit 4,Cops4,Csn4,JAB1-containing signalosome subunit 4,Rat,Rattus norvegicus,SGN4,Signalosome subunit 4
EIAAB09617 COP9 signalosome complex subunit 6,Cops6,Csn6,JAB1-containing signalosome subunit 6,Mouse,Mus musculus,SGN6,Signalosome subunit 6
EIAAB09597 COP9 signalosome complex subunit 1,COPS1,CSN1,G protein pathway suppressor 1,GPS1,GPS-1,Homo sapiens,Human,JAB1-containing signalosome subunit 1,Protein MFH,SGN1,Signalosome subunit 1
EIAAB09599 COP9 signalosome complex subunit 1,Cops1,Csn1,G protein pathway suppressor 1,Gps1,GPS-1,JAB1-containing signalosome subunit 1,MFH protein,Rat,Rattus norvegicus,SGN1,Signalosome subunit 1


 

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