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

Histone-lysine N-methyltransferase set-2 (EC 2.1.1.43) (SET domain-containing protein 2)

 SET2_CAEEL              Reviewed;        1507 AA.
Q18221; Q95QU6; Q95QU7;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-APR-2003, sequence version 2.
25-OCT-2017, entry version 131.
RecName: Full=Histone-lysine N-methyltransferase set-2;
EC=2.1.1.43 {ECO:0000269|PubMed:20555324, ECO:0000269|PubMed:21527717};
AltName: Full=SET domain-containing protein 2;
Name=set-2; ORFNames=C26E6.9;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[2]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND ALTERNATIVE
SPLICING.
PubMed=11729150;
Xu L., Strome S.;
"Depletion of a novel SET-domain protein enhances the sterility of
mes-3 and mes-4 mutants of Caenorhabditis elegans.";
Genetics 159:1019-1029(2001).
[3]
FUNCTION.
PubMed=12242227;
Colaiacovo M.P., Stanfield G.M., Reddy K.C., Reinke V., Kim S.K.,
Villeneuve A.M.;
"A targeted RNAi screen for genes involved in chromosome morphogenesis
and nuclear organization in the Caenorhabditis elegans germline.";
Genetics 162:113-128(2002).
[4]
FUNCTION.
PubMed=12724425; DOI=10.1128/MCB.23.10.3681-3691.2003;
Jedrusik M.A., Schulze E.;
"Telomeric position effect variegation in Saccharomyces cerevisiae by
Caenorhabditis elegans linker histones suggests a mechanistic
connection between germ line and telomeric silencing.";
Mol. Cell. Biol. 23:3681-3691(2003).
[5]
FUNCTION.
PubMed=17967446; DOI=10.1016/j.ydbio.2007.09.035;
Simonet T., Dulermo R., Schott S., Palladino F.;
"Antagonistic functions of SET-2/SET1 and HPL/HP1 proteins in C.
elegans development.";
Dev. Biol. 312:367-383(2007).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=20555324; DOI=10.1038/nature09195;
Greer E.L., Maures T.J., Hauswirth A.G., Green E.M., Leeman D.S.,
Maro G.S., Han S., Banko M.R., Gozani O., Brunet A.;
"Members of the H3K4 trimethylation complex regulate lifespan in a
germline-dependent manner in C. elegans.";
Nature 466:383-387(2010).
[7]
FUNCTION.
PubMed=22012258; DOI=10.1038/nature10572;
Greer E.L., Maures T.J., Ucar D., Hauswirth A.G., Mancini E.,
Lim J.P., Benayoun B.A., Shi Y., Brunet A.;
"Transgenerational epigenetic inheritance of longevity in
Caenorhabditis elegans.";
Nature 479:365-371(2011).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH WDR-5.1.
PubMed=21527717; DOI=10.1073/pnas.1019290108;
Xiao Y., Bedet C., Robert V.J., Simonet T., Dunkelbarger S.,
Rakotomalala C., Soete G., Korswagen H.C., Strome S., Palladino F.;
"Caenorhabditis elegans chromatin-associated proteins SET-2 and ASH-2
are differentially required for histone H3 Lys 4 methylation in
embryos and adult germ cells.";
Proc. Natl. Acad. Sci. U.S.A. 108:8305-8310(2011).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25124442; DOI=10.1126/science.1255885;
Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
Jarriault S.;
"Sequential histone-modifying activities determine the robustness of
transdifferentiation.";
Science 345:826-829(2014).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=28379943; DOI=10.1038/nature21686;
Han S., Schroeder E.A., Silva-Garcia C.G., Hebestreit K., Mair W.B.,
Brunet A.;
"Mono-unsaturated fatty acids link H3K4me3 modifiers to C. elegans
lifespan.";
Nature 544:185-190(2017).
-!- FUNCTION: Histone methyltransferase that specifically di- and
trimethylates 'Lys-4' of histone H3 at all developmental stages
and in adult germ cells (PubMed:21527717, PubMed:20555324). H3
'Lys-4' methylation represents a specific tag for epigenetic
transcriptional activation (PubMed:21527717). Implicated in the
epigenetic inheritance of lifespan over several generations
(PubMed:22012258). Acts in the germline to limit the longevity of
the soma, probably by regulating a lipid metabolism pathway that
signals from the germline to the intestine, thereby preventing
accumulation of mono-unsaturated fatty acids (PubMed:20555324,
PubMed:28379943). Methylation in the germline is required for
germline development and fertility, possibly by ensuring genome
stability (PubMed:21527717, PubMed:12242227). May act redundantly
with mes-3 and mes-4 proteins in the development of a fertile
germline (PubMed:11729150). Required for RNAi (PubMed:17967446).
Functions as an antagonist of hpl-1 and hpl-2 activity in growth
and somatic gonad development (PubMed:17967446). Cooperates with
jmjd-3.1 and egl-27 to ensure robust transdifferentiation of the Y
rectal cell to the PDA motor neuron during larval development
(PubMed:25124442). {ECO:0000269|PubMed:11729150,
ECO:0000269|PubMed:12242227, ECO:0000269|PubMed:12724425,
ECO:0000269|PubMed:17967446, ECO:0000269|PubMed:20555324,
ECO:0000269|PubMed:21527717, ECO:0000269|PubMed:22012258,
ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:28379943}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:20555324, ECO:0000269|PubMed:21527717}.
-!- SUBUNIT: Interacts with wdr-5.1. {ECO:0000269|PubMed:21527717}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11729150}.
Note=Localized in mitotic and mid-late-stage meiotic nuclei but is
undetectable in early pachytene nuclei.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=a; Synonyms=L;
IsoId=Q18221-1; Sequence=Displayed;
Name=b; Synonyms=S;
IsoId=Q18221-2; Sequence=VSP_007217, VSP_007218;
Name=c;
IsoId=Q18221-3; Sequence=VSP_038347;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all cells of embryo. In L1 larva,
it is predominantly expressed in Z2 and Z3 primordial germ cells.
In adults, it is predominantly expressed in the germline.
{ECO:0000269|PubMed:11729150}.
-!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in
disruption of invariant Y-to-PDA transdifferentiation
(PubMed:25124442). Results in decreased trimethylation at 'Lys-4'
of histone H3 (PubMed:20555324). Leads to an extension of lifespan
(PubMed:20555324). Leads to a deregulation of fat metabolism and
to an enrichment of mono-unsaturated fatty acids
(PubMed:28379943). {ECO:0000269|PubMed:20555324,
ECO:0000269|PubMed:25124442, ECO:0000269|PubMed:28379943}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; FO080680; CCD65735.1; -; Genomic_DNA.
EMBL; FO080680; CCD65734.1; -; Genomic_DNA.
EMBL; FO080680; CCD65736.1; -; Genomic_DNA.
PIR; A88445; A88445.
RefSeq; NP_498039.1; NM_065638.3. [Q18221-3]
RefSeq; NP_498040.1; NM_065639.4. [Q18221-1]
RefSeq; NP_498041.1; NM_065640.3. [Q18221-2]
UniGene; Cel.8145; -.
ProteinModelPortal; Q18221; -.
SMR; Q18221; -.
BioGrid; 40896; 2.
ELM; Q18221; -.
STRING; 6239.C26E6.9c.1; -.
EPD; Q18221; -.
PaxDb; Q18221; -.
PeptideAtlas; Q18221; -.
EnsemblMetazoa; C26E6.9a; C26E6.9a; WBGene00004782. [Q18221-1]
GeneID; 175662; -.
KEGG; cel:CELE_C26E6.9; -.
UCSC; C26E6.9a; c. elegans. [Q18221-1]
CTD; 175662; -.
WormBase; C26E6.9a; CE27735; WBGene00004782; set-2. [Q18221-1]
WormBase; C26E6.9b; CE01158; WBGene00004782; set-2. [Q18221-2]
WormBase; C26E6.9c; CE27736; WBGene00004782; set-2. [Q18221-3]
eggNOG; KOG1080; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
HOGENOM; HOG000021414; -.
InParanoid; Q18221; -.
KO; K11422; -.
OMA; TIAQDEM; -.
OrthoDB; EOG091G00IV; -.
Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
PRO; PR:Q18221; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00004782; -.
GO; GO:0005634; C:nucleus; IDA:WormBase.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:WormBase.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
GO; GO:0051568; P:histone H3-K4 methylation; IDA:WormBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
InterPro; IPR024657; COMPASS_Set1_N-SET.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF00076; RRM_1; 1.
Pfam; PF00856; SET; 1.
SMART; SM01291; N-SET; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00360; RRM; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Complete proteome;
Developmental protein; Methyltransferase; Nucleus; Reference proteome;
RNA-binding; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase.
CHAIN 1 1507 Histone-lysine N-methyltransferase set-2.
/FTId=PRO_0000097695.
DOMAIN 128 199 RRM.
DOMAIN 1368 1485 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1491 1507 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
COMPBIAS 296 354 Pro-rich.
COMPBIAS 554 664 Pro-rich.
COMPBIAS 870 1011 Ser-rich.
VAR_SEQ 1 768 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_007217.
VAR_SEQ 769 831 MDELSRKVAEDIRQQIMRQCFAALDEKLHLKAIADEEKRKK
EREEKARQEAEKPSNHLIADMM -> MYNNSAPYLNHSSLN
TVRKKVVTVRRVLPSLPPPPPPPPSLYPPCSVFKVPYIPQR
VYRSINS (in isoform b). {ECO:0000305}.
/FTId=VSP_007218.
VAR_SEQ 831 831 M -> MPSQ (in isoform c). {ECO:0000305}.
/FTId=VSP_038347.
SEQUENCE 1507 AA; 171683 MW; E7D9689DA720C34A CRC64;
MSTHDMNHHP PRKSHSKRDK PSSSNSGPKI ENHKCKWAWQ KVFETGKSFL RRDGFPQDCK
SKEDFERIKR TGVRKTSENM LEDPRKNFES LQQSSVYQTN SFRNPRYLCR AHLRVDSYYC
TIPPKREVSL FNMDDNCTEV LLRDFAKDCG KVEKAYVCIH PETKRHMKMA YVKFATVKEA
HNFYSMYHAQ NLLATKCTPR IDPFLSILNE EYEVATNGQV LPILPDDLAS IDPSVLRDLR
ANFLRDQNEK YELAMRNTYE DEGGMLSGVI MDTSDHYERD YTMDHDVGPS SMKMSPIPPP
PIKEESPPPP PPPPVASVSN LAPVPSVQLP YYNNIQPSSS TMHMPEFRPT EPPPSYSRED
PYRSTSRSSL SRHRNRSRSP SDGMDRSGRS SSRRTHRRPE SRNGSKNANG DVVKYETYKM
EKRKIKYEGG NKKYEQVHIK ERTAVIRGKN QLENVSSESA SGSSSVDTYP DFSDEERKKK
KRPKSPNRSK KDSRAFGWDS TDESDEDTRR RRSGRSQNRS SERKFQTTSS SSTRRELSST
HTNSVPNLKS HETPPPPPPK GHPSVHLQTP YQHVQPQMIP ATYYNLPPQH MAPPPITTSL
PPFCDFSQPP PGFTPTFKPI TNAPLPTPYQ ASNIPQPGLV QIAALSAAPE PFSSIPGPPP
GPAPIQEDVG RAESPEKPSL SERFSGIFGP TQREEPAQVE VEYDYPLKHS ESHDDRHSLE
DMDVEVSSDG ETVSNVEKIE CMEEKKRQDL ERIAIARTPI VKKCKKRMMD ELSRKVAEDI
RQQIMRQCFA ALDEKLHLKA IADEEKRKKE REEKARQEAE KPSNHLIADM MTLYNNQSFA
SSSRGFYRKQ KPIPKSHPKH QEHHHHAKAS VSTPVHSSST SRNSSVAPTP QRTVSTSSSS
SSAATSARVS EDESDSDSTP GEVQRRKTSV LSNDKRRRRA SFSSTSIQSS PERQRDVSSS
SRTSSSSSTS SMKQEETADE KSRKRKLIMS SDESSTTGST ATSVVSSRQS SLEPQQEKTD
GEPPKKKSQT DFISERVSKI EGEERPLPEP VETSGPIIGD SSYLPYKIVH WEKAGIIEMN
LPANSIRAHE YHPFTTEHCY FGIDDPRQPK IQIFDHSPCK SEPGSEPLKI TPAPWGPIDN
VAETGPLIYM DVVTAPKTVQ KKQKPRKQVF EKDPYEYYEP PPTKRPAPPP RFKKTFKPRS
EEEKKKIIGD CEDLPDLEDQ WYLRAALNEM QSEVKSADEL PWKKMLTFKE MLRSEDPLLR
LNPIRSKKGL PDAFYEDEEL DGVIPVAAGC SRARPYEKMT MKQKRSLVRR PDNESHPTAI
FSERDETAIR HQHLASKDMR LLQRRLLTSL GDANNDFFKI NQLKFRKKMI KFARSRIHGW
GLYAMESIAP DEMIVEYIGQ TIRSLVAEER EKAYERRGIG SSYLFRIDLH HVIDATKRGN
FARFINHSCQ PNCYAKVLTI EGEKRIVIYS RTIIKKGEEI TYDYKFPIED DKIDCLCGAK
TCRGYLN


Related products :

Catalog number Product name Quantity
EIAAB37955 ERG-associated protein with SET domain,ESET,H3-K9-HMTase 4,Histone H3-K9 methyltransferase 4,Histone-lysine N-methyltransferase SETDB1,Homo sapiens,Human,KIAA0067,KMT1E,Lysine N-methyltransferase 1E,S
EIAAB37951 Histone-lysine N-methyltransferase SETD1A,Homo sapiens,hSET1A,Human,KIAA0339,KMT2F,Lysine N-methyltransferase 2F,SET domain-containing protein 1A,SET1,Set1_Ash2 histone methyltransferase complex subun
EIAAB11717 DOT1L,DOT1-like protein,H3-K79-HMTase,Histone H3-K79 methyltransferase,Histone-lysine N-methyltransferase, H3 lysine-79 specific,Homo sapiens,Human,KIAA1814,KMT4,Lysine N-methyltransferase 4
EIAAB37975 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Homo sapiens,Human,KIAA1717,KMT7,Lysine N-methyltransferase 7,SET domain-containing protein 7,SET7,SET
EIAAB37977 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Homo sapiens,Human,KMT5A,Lysine N-methyltransferase 5A,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PRSET7
EIAAB12652 Ehmt1,Euchromatic histone-lysine N-methyltransferase 1,Euhmtase1,Eu-HMTase1,G9a-like protein 1,GLP,Glp,GLP1,Histone-lysine N-methyltransferase EHMT1,Kmt1d,Lysine N-methyltransferase 1D,Mouse,Mus muscu
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB37979 Bos taurus,Bovine,H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,SET
EIAAB37978 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Mouse,Mus musculus,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,Se
EIAAB37958 C13orf4,Chronic lymphocytic leukemia deletion region gene 8 protein,CLLD8,Histone-lysine N-methyltransferase SETDB2,Homo sapiens,Human,KMT1F,Lysine N-methyltransferase 1F,SET domain bifurcated 2,SETDB
EIAAB12653 EHMT1,Euchromatic histone-lysine N-methyltransferase 1,EUHMTASE1,Eu-HMTase1,G9a-like protein 1,GLP,GLP,GLP1,H3-K9-HMTase 5,Histone H3-K9 methyltransferase 5,Histone-lysine N-methyltransferase EHMT1,Ho
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
EIAAB12654 Bat8,Ehmt2,Euchromatic histone-lysine N-methyltransferase 2,G9a,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Mouse,Mus muscul
EIAAB12655 BAT8,C6orf30,EHMT2,Euchromatic histone-lysine N-methyltransferase 2,G9A,H3-K9-HMTase 3,Histone H3-K9 methyltransferase 3,Histone-lysine N-methyltransferase EHMT2,HLA-B-associated transcript 8,Homo sap
EIAAB37976 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Kiaa1717,Mouse,Mus musculus,SET domain-containing protein 7,Set7,SET7_9,Set9,Setd7
EIAAB27931 H3-K36-HMTase,H4-K20-HMTase,Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific,Mouse,Mus musculus,NR-binding SET domain-containing protein,Nsd1,Nuclear receptor-binding SET dom
EIAAB32313 Gm92,Mouse,Mus musculus,PR domain zinc finger protein 6,PR domain-containing protein 6,PR domain-containing protein in smooth muscle,Prdm6,Prism,Putative histone-lysine N-methyltransferase PRDM6
EIAAB38903 Bos taurus,Bovine,Histone methyltransferase SMYD2,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
EIAAB38904 Histone methyltransferase SMYD2,N-lysine methyltransferase SMYD2,Rat,Rattus norvegicus,SET and MYND domain-containing protein 2,Smyd2
EIAAB38901 Histone methyltransferase SMYD2,Mouse,Mus musculus,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,Smyd2
EIAAB38902 Histone methyltransferase SMYD2,N-lysine methyltransferase SMYD2,Pig,SET and MYND domain-containing protein 2,SMYD2,Sus scrofa
EIAAB27933 Homo sapiens,Human,KIAA1090,MMSET,Multiple myeloma SET domain-containing protein,NSD2,Nuclear SET domain-containing protein 2,Probable histone-lysine N-methyltransferase NSD2,Protein trithorax-5,TRX5,


 

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