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E3 ubiquitin-protein ligase Topors (EC 2.3.2.27) (RING-type E3 ubiquitin transferase Topors) (SUMO1-protein E3 ligase Topors) (Topoisomerase I-binding RING finger protein) (Topoisomerase I-binding arginine/serine-rich protein) (Tumor suppressor p53-binding protein 3) (p53-binding protein 3) (p53BP3)

 TOPRS_MOUSE             Reviewed;        1033 AA.
Q80Z37; Q3U5B5; Q3UPZ1; Q3USN3; Q3UZ55; Q8BXP2; Q8CFF5; Q8CGC8;
Q920L3;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
28-FEB-2018, entry version 122.
RecName: Full=E3 ubiquitin-protein ligase Topors;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase Topors {ECO:0000305};
AltName: Full=SUMO1-protein E3 ligase Topors;
AltName: Full=Topoisomerase I-binding RING finger protein;
AltName: Full=Topoisomerase I-binding arginine/serine-rich protein;
AltName: Full=Tumor suppressor p53-binding protein 3;
Short=p53-binding protein 3;
Short=p53BP3;
Name=Topors;
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 [MRNA], FUNCTION, INTERACTION WITH PARK7 AND TP53,
AND SUBCELLULAR LOCATION.
STRAIN=C57BL/6J;
PubMed=15703819;
Shinbo Y., Taira T., Niki T., Iguchi-Ariga S.M.M., Ariga H.;
"DJ-1 restores p53 transcription activity inhibited by
Topors/p53BP3.";
Int. J. Oncol. 26:641-648(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TP53,
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=15735665; DOI=10.1038/sj.onc.1208554;
Lin L., Ozaki T., Takada Y., Kageyama H., Nakamura Y., Hata A.,
Zhang J.H., Simonds W.F., Nakagawara A., Koseki H.;
"Topors, a p53 and topoisomerase I-binding RING finger protein, is a
coactivator of p53 in growth suppression induced by DNA damage.";
Oncogene 24:3385-3396(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland, and 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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-824.
STRAIN=C57BL/6J;
TISSUE=Corpora quadrigemina, Lung, Retina, and Thymus;
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).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-861; SER-863;
SER-909; SER-911; SER-999; SER-1016 AND SER-1025, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Functions as an E3 ubiquitin-protein ligase and as a E3
SUMO1-protein ligase. Probable tumor suppressor involved in cell
growth, cell proliferation and apoptosis that regulates p53/TP53
stability through ubiquitin-dependent degradation. May regulate
chromatin modification through sumoylation of several chromatin
modification-associated proteins. May be involved in DNA-damage-
induced cell death through IKBKE sumoylation.
{ECO:0000269|PubMed:15703819, ECO:0000269|PubMed:15735665}.
-!- 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.
-!- SUBUNIT: Interacts with TOP1. Interacts with the SUMO1 conjugating
enzyme UBE2I. Interacts with SUMO1. Interacts with NKX3-1;
polyubiquitinates NKX3-1 and induces its proteasomal degradation.
Interacts with SIN3A; sumoylates SIN3A. Interacts with IKBKE;
induced by DNA damage (By similarity). Interacts with p53/TP53.
Interacts with PARK7/DJ-1. {ECO:0000250|UniProtKB:Q9NS56,
ECO:0000269|PubMed:15703819, ECO:0000269|PubMed:15735665}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15703819,
ECO:0000269|PubMed:15735665}. Nucleus, PML body
{ECO:0000250|UniProtKB:Q9NS56}. Note=Localizes to discrete nuclear
foci which partly overlap with PML nuclear bodies. Targeted to PML
nuclear bodies upon DNA damage. {ECO:0000250|UniProtKB:Q9NS56}.
-!- INDUCTION: By genotoxic agents such as cisplatin and camptothecin.
{ECO:0000269|PubMed:15735665}.
-!- PTM: Phosphorylation at Ser-99 regulates the E3 ubiquitin-protein
ligase activity but not the SUMO1-protein ligase activity.
Phosphorylation at Ser-718 increases the E3 ubiquitin-protein
ligase activity versus the E3 SUMO1-protein ligase activity
resulting in increased p53/TP53 ubiquitination and degradation.
{ECO:0000250|UniProtKB:Q9NS56}.
-!- PTM: Sumoylated. {ECO:0000250|UniProtKB:Q9NS56}.
-!- SEQUENCE CAUTION:
Sequence=AAH37141.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB072395; BAB69457.1; -; mRNA.
EMBL; AB104865; BAC65157.1; -; mRNA.
EMBL; BC037141; AAH37141.1; ALT_SEQ; mRNA.
EMBL; BC040797; AAH40797.1; -; mRNA.
EMBL; AK044564; BAC31981.2; -; mRNA.
EMBL; AK134075; BAE22003.1; -; mRNA.
EMBL; AK140250; BAE24298.1; -; mRNA.
EMBL; AK143025; BAE25253.1; -; mRNA.
EMBL; AK153743; BAE32164.1; -; mRNA.
CCDS; CCDS38710.1; -.
RefSeq; NP_598858.2; NM_134097.3.
UniGene; Mm.251548; -.
ProteinModelPortal; Q80Z37; -.
SMR; Q80Z37; -.
BioGrid; 222976; 5.
IntAct; Q80Z37; 1.
MINT; Q80Z37; -.
STRING; 10090.ENSMUSP00000046843; -.
iPTMnet; Q80Z37; -.
PhosphoSitePlus; Q80Z37; -.
EPD; Q80Z37; -.
MaxQB; Q80Z37; -.
PaxDb; Q80Z37; -.
PeptideAtlas; Q80Z37; -.
PRIDE; Q80Z37; -.
Ensembl; ENSMUST00000042575; ENSMUSP00000046843; ENSMUSG00000036822.
GeneID; 106021; -.
KEGG; mmu:106021; -.
UCSC; uc008shi.1; mouse.
CTD; 10210; -.
MGI; MGI:2146189; Topors.
eggNOG; KOG4430; Eukaryota.
eggNOG; ENOG410XQZR; LUCA.
GeneTree; ENSGT00530000064170; -.
HOVERGEN; HBG080410; -.
InParanoid; Q80Z37; -.
KO; K10631; -.
OMA; FIHEFIS; -.
OrthoDB; EOG091G089U; -.
PhylomeDB; Q80Z37; -.
TreeFam; TF339497; -.
PRO; PR:Q80Z37; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000036822; -.
CleanEx; MM_TOPORS; -.
Genevisible; Q80Z37; MM.
GO; GO:0005814; C:centriole; ISO:MGI.
GO; GO:0036064; C:ciliary basal body; IDA:BHF-UCL.
GO; GO:0000930; C:gamma-tubulin complex; ISO:MGI.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0032391; C:photoreceptor connecting cilium; IDA:BHF-UCL.
GO; GO:0016605; C:PML body; ISS:UniProtKB.
GO; GO:0000922; C:spindle pole; ISO:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
GO; GO:0003823; F:antigen binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0044547; F:DNA topoisomerase binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019789; F:SUMO transferase activity; ISS:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:MGI.
GO; GO:0051457; P:maintenance of protein location in nucleus; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0051443; P:positive regulation of ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; DNA damage; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 1033 E3 ubiquitin-protein ligase Topors.
/FTId=PRO_0000232627.
ZN_FING 104 143 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 52 376 Required for DNA-binding. {ECO:0000250}.
REGION 438 654 Interaction with SUMO1. {ECO:0000250}.
REGION 438 574 Sumoylation and localization to discrete
nuclear foci. {ECO:0000250}.
REGION 457 879 Interaction with TOP1. {ECO:0000250}.
REGION 457 731 Interaction with p53/TP53. {ECO:0000250}.
REGION 851 914 Interaction with UBE2I. {ECO:0000250}.
COMPBIAS 579 787 Arg-rich.
COMPBIAS 877 892 Lys-rich.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS56}.
MOD_RES 500 500 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS56}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS56}.
MOD_RES 718 718 Phosphoserine; by PLK1.
{ECO:0000250|UniProtKB:Q9NS56}.
MOD_RES 734 734 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NS56}.
MOD_RES 861 861 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 863 863 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 909 909 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 999 999 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1016 1016 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 74 74 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 77 77 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 84 84 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 89 89 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 160 160 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 251 251 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 561 561 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 701 701 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 818 818 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CROSSLNK 834 834 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NS56}.
CONFLICT 40 40 S -> F (in Ref. 1; BAB69457).
{ECO:0000305}.
CONFLICT 623 623 L -> P (in Ref. 3; AAH40797).
{ECO:0000305}.
CONFLICT 657 657 S -> A (in Ref. 1; BAB69457).
{ECO:0000305}.
CONFLICT 682 682 S -> A (in Ref. 3; AAH40797).
{ECO:0000305}.
SEQUENCE 1033 AA; 117082 MW; 3A99C00491D7EFD2 CRC64;
MGSQPPPPGS PLSREEGEAP PLVPAEEGRR RSRRVRLRGS CRHRPSLLSR RELASNGPAV
PATASSEIMA SAAKEFKMDN FSPKAGTSKL QQTVPADASP DSKCPICLDR FDNVSYLDRC
LHKFCFRCVQ EWSKNKAECP LCKQPFDSIF HSVRAEDDFK EYVLRPSYNG SFTNPEVRRF
RYRTTMTRER SASLYSPSST VSRRTTTPPD SGVLFEGLGI STRPRDVDIP QFMRQMALRG
PTTTDERSLR KIQEQDIINF RRTLYRAGVR VRSIEDGGRY RDISAEFFRR NPACLHRLVP
WLKRELTVLF GAHGSLVNIV QHIIMSNVTR YDLESQAFVS DLRPFLLNRT EHFIHEFISF
ARSPFNMAAF DQHANYDCPP SSEEGSRSDS SVITISPDEA ETQELDMNAS TVRQAPWDDE
TPGPSYSSSE QVHVGVSSLL NSSDSSDEEL VSGGTTSQIQ GVQTNDDVNN DSDSSSDNCV
IVGFVKPLAE RTPELVELSS DSEELGPYEK VETVKTQEQE QSYSSGDSDV SRASSPRSVL
GKDEQMSKSH CDSDTRISSK KEEKRSTSLP APRDSSSTRG DRVCSPYNHR HRKGGRSRSS
DSRSQSRSGH DPRNHRKHGK KRLRNKRSRS RESSSRPRAR KDKKRSRTRD SSWSRRSQTL
SLSSGSTSRS RSRSSDHGKR RSRSRNRDRY YLRNNYGSKY KWEYTYYSRN KDRDGYESSY
RRRTLSRAHY SRQSSSPEFR IQSFSERTNA RKKNHSERKY YYYERRRSRS VSSNRSRTTS
AGPDRVRNEK PGGKRKYKTR HLEGTSEEAQ PAREFTSKGK DSHYQKSKLD GSYKNESDSF
SDSRSSDRET KHKRRRRRTR SLSVEIVYEG KATDTSKHHK KKKKKHKKKH KKHHGDNTSR
SPVVITIDSD SDGESEVKAG IECSNGSLPQ PIQDGAFETK DVVTIEDELG VLDKDCDVTA
LADDLSTSQT VENCDSPAVP VEQTLDVREE STFASDLESQ SSNVSIQAEP SRPVPSPRTS
LSSVSPGRDC DVS


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