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

DNA methyltransferase 1-associated protein 1 (DNMAP1) (DNMT1-associated protein 1) (MAT1-mediated transcriptional repressor)

 DMAP1_MOUSE             Reviewed;         468 AA.
Q9JI44; Q99LM0; Q9CSS9; Q9DB33;
21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 154.
RecName: Full=DNA methyltransferase 1-associated protein 1;
Short=DNMAP1;
Short=DNMT1-associated protein 1;
AltName: Full=MAT1-mediated transcriptional repressor;
Name=Dmap1; Synonyms=Mmtr;
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] (ISOFORM 1).
STRAIN=C57BL/6J;
PubMed=10888872; DOI=10.1038/77023;
Rountree M.R., Bachman K.E., Baylin S.B.;
"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
replication foci.";
Nat. Genet. 25:269-277(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=129/Sv;
Shin J.H., Kim C.G.;
"MMTR is a novel transcriptional regulator involved in MAT1-mediated
transcriptional repression.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-257 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N;
TISSUE=Mammary gland, and Olfactory epithelium;
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]
FUNCTION, AND INTERACTION WITH DAXX.
PubMed=14978102; DOI=10.4049/jimmunol.172.5.2985;
Muromoto R., Sugiyama K., Takachi A., Imoto S., Sato N., Yamamoto T.,
Oritani K., Shimoda K., Matsuda T.;
"Physical and functional interactions between Daxx and DNA
methyltransferase 1-associated protein, DMAP1.";
J. Immunol. 172:2985-2993(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-446, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
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: Involved in transcription repression and activation. Its
interaction with HDAC2 may provide a mechanism for histone
deacetylation in heterochromatin following replication of DNA at
late firing origins. Can also repress transcription independently
of histone deacetylase activity. May specifically potentiate DAXX-
mediated repression of glucocorticoid receptor-dependent
transcription. Component of the NuA4 histone acetyltransferase
(HAT) complex which is involved in transcriptional activation of
select genes principally by acetylation of nucleosomal histones H4
and H2A. This modification may both alter nucleosome - DNA
interactions and promote interaction of the modified histones with
other proteins which positively regulate transcription. This
complex may be required for the activation of transcriptional
programs associated with oncogene and proto-oncogene mediated
growth induction, tumor suppressor mediated growth arrest and
replicative senescence, apoptosis, and DNA repair. NuA4 may also
play a direct role in DNA repair when recruited to sites of DNA
damage. Participates in the nuclear localization of URI1 and
increases its transcriptional corepressor activity (By
similarity). {ECO:0000250, ECO:0000269|PubMed:14978102}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5/TIP60 and the subunits
EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of a NuA4-
related complex which contains EP400, TRRAP/PAF400, SRCAP,
BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. DMAP1 also forms a complex
with DNMT1 and HDAC2. Throughout S phase it interacts directly
with the N-terminus of DNMT1, which serves to recruit DMAP1 to
replication foci. DMAP1 interacts with ING1, a component of the
mSIN3A transcription repressor complex, although this interaction
is not required for recruitment of ING1 to heterochromatin.
Interacts directly with the transcriptional corepressor TSG101.
Interacts with URI1 (By similarity). Interacts with the pro-
apoptotic protein DAXX. {ECO:0000250,
ECO:0000269|PubMed:14978102}.
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
Note=Targeted to replication foci throughout S phase by DNMT1.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9JI44-1; Sequence=Displayed;
Name=2;
IsoId=Q9JI44-2; Sequence=VSP_003850, VSP_003851;
Note=May be due to intron retention. No experimental
confirmation available.;
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF265229; AAF87080.1; -; mRNA.
EMBL; AF438610; AAL31640.1; -; mRNA.
EMBL; AK005270; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK012055; BAB27996.3; -; mRNA.
EMBL; BC002321; AAH02321.1; -; mRNA.
EMBL; BC045160; AAH45160.1; -; mRNA.
CCDS; CCDS18536.1; -. [Q9JI44-1]
RefSeq; NP_075667.1; NM_023178.2. [Q9JI44-1]
RefSeq; XP_006503329.1; XM_006503266.2. [Q9JI44-1]
RefSeq; XP_006503330.1; XM_006503267.3. [Q9JI44-1]
RefSeq; XP_006503331.1; XM_006503268.3. [Q9JI44-1]
UniGene; Mm.29142; -.
ProteinModelPortal; Q9JI44; -.
SMR; Q9JI44; -.
BioGrid; 211314; 10.
CORUM; Q9JI44; -.
IntAct; Q9JI44; 20.
MINT; MINT-1172683; -.
STRING; 10090.ENSMUSP00000099748; -.
iPTMnet; Q9JI44; -.
PhosphoSitePlus; Q9JI44; -.
EPD; Q9JI44; -.
PaxDb; Q9JI44; -.
PeptideAtlas; Q9JI44; -.
PRIDE; Q9JI44; -.
Ensembl; ENSMUST00000102687; ENSMUSP00000099748; ENSMUSG00000009640. [Q9JI44-1]
GeneID; 66233; -.
KEGG; mmu:66233; -.
UCSC; uc008uiw.1; mouse. [Q9JI44-1]
CTD; 55929; -.
MGI; MGI:1913483; Dmap1.
eggNOG; KOG2656; Eukaryota.
eggNOG; ENOG410XSA4; LUCA.
GeneTree; ENSGT00390000016466; -.
HOGENOM; HOG000007018; -.
HOVERGEN; HBG051364; -.
InParanoid; Q9JI44; -.
KO; K11324; -.
OMA; CKRFDLR; -.
OrthoDB; EOG091G0B27; -.
PhylomeDB; Q9JI44; -.
TreeFam; TF354261; -.
PRO; PR:Q9JI44; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000009640; -.
CleanEx; MM_DMAP1; -.
Genevisible; Q9JI44; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005657; C:replication fork; IDA:MGI.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; ISS:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
GO; GO:0006281; P:DNA repair; IEA:InterPro.
GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; ISS:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR032563; DAMP1_SANT-like.
InterPro; IPR008468; DMAP1.
InterPro; IPR027109; Swc4/Dmap1.
PANTHER; PTHR12855; PTHR12855; 2.
Pfam; PF05499; DMAP1; 1.
Pfam; PF16282; SANT_DAMP1_like; 1.
ProDom; PD492828; DMAP1; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Cytoplasm; Growth regulation; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 468 DNA methyltransferase 1-associated
protein 1.
/FTId=PRO_0000079936.
DOMAIN 149 199 SANT.
COILED 225 275 {ECO:0000255}.
COMPBIAS 406 411 Poly-Ala.
COMPBIAS 455 461 Poly-Ser.
MOD_RES 446 446 Phosphothreonine.
{ECO:0000244|PubMed:15345747}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000250|UniProtKB:Q9NPF5}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NPF5}.
CROSSLNK 214 214 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9NPF5}.
VAR_SEQ 242 323 AEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQR
RTERKAPKKKLPQKKEAEKPAVPETAGIKFPDFKSAGVTLR
-> ITSSTPPSTAQLSLPPGPFTSSPFLWSLFLPSLQESPY
LWSLIDNLVSRQLPSHLLPHSPHTHGSISCFAGGRGGVPPT
GAA (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_003850.
VAR_SEQ 324 468 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_003851.
SEQUENCE 468 AA; 53130 MW; CDDADF2165801C9B CRC64;
MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL
LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF TNPARKDGAM FFHWRRAAEE
GKDYPFARFN KTVQVPVYSE QEYQLYLHDD AWTKAETDHL FDLSRRFDLR FVVIHDRYDH
QQFKKRSVED LKERYYHICA KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ
VAEEEYLLQE LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE
KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV ELSPTPTEEL
VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR AGVLGAPAAA AVGPTPASAE
PTVSESGLGL DPTKDTIIDV VGAPLTPNSR KRRESASSSS SVKKAKKP


Related products :

Catalog number Product name Quantity
EIAAB11451 Dmap1,DNA methyltransferase 1-associated protein 1,DNMAP1,DNMT1-associated protein 1,MAT1-mediated transcriptional repressor,Mmtr,Mouse,Mus musculus
EIAAB11450 DMAP1,DNA methyltransferase 1-associated protein 1,DNMAP1,DNMT1-associated protein 1,Homo sapiens,Human,KIAA1425
18-003-43273 DNA methyltransferase 1-associated protein 1 - DNMT1-associated protein 1; DNMAP1 Polyclonal 0.1 mg Protein A
18-003-43272 DNA methyltransferase 1-associated protein 1 - DNMT1-associated protein 1; DNMAP1 Polyclonal 0.1 mg Protein A
26-995 IRF2BP1 acts as a transcriptional repressor. IRF2BP1 also acts as a transcriptional corepressor in a IRF2-dependent manner. This repression is not mediated at least in part by histone deacetylase acti 0.05 mg
EIAAB47329 58 kDa repressor protein,Rat,Rattus norvegicus,Rp58,rRP58,Transcriptional repressor RP58,Zfp238,Zinc finger protein 238,Znf238
EIAAB47327 58 kDa repressor protein,Mouse,Mus musculus,Rp58,Transcriptional repressor RP58,Zfp238,Zfp-238,Zinc finger protein 238,Znf238
EIAAB11615 AIM,CXXC9,CXXC-type zinc finger protein 9,DNA (cytosine-5)-methyltransferase 1,DNA methyltransferase HsaI,DNA MTase HsaI,DNMT,Dnmt1,DNMT1,Homo sapiens,Human,M.HsaI,MCMT
EIAAB47328 58 kDa repressor protein,Homo sapiens,Human,RP58,TAZ1,TAZ-1,Transcriptional repressor RP58,Translin-associated zinc finger protein 1,ZBTB18,Zinc finger and BTB domain-containing protein 18,Zinc finger
18-003-43092 Max-interacting transcriptional repressor MAD4 - Max-associated protein 4; MAX dimerization protein 4 Polyclonal 0.1 mg Protein A
18-003-42283 Max-interacting transcriptional repressor MAD4 - Max-associated protein 4; MAX dimerization protein 4 Polyclonal 0.05 mg Aff Pur
18-003-42283 Max-interacting transcriptional repressor MAD4 - Max-associated protein 4; MAX dimerization protein 4 Polyclonal 0.1 mg Protein A
18-003-43092 Max-interacting transcriptional repressor MAD4 - Max-associated protein 4; MAX dimerization protein 4 Polyclonal 0.05 mg Aff Pur
18-003-43330 CDNA FLJ32157 fis. clone PLACE6000205. moderately similar to TRANSCRIPTIONAL REPRESSOR PROTEIN YY1 - Zinc finger protein 42 Polyclonal 0.05 mg Aff Pur
EIAAB44713 Delta transcription factor,Mouse,Mus musculus,NF-E1,Transcriptional repressor protein YY1,Ucrbp,UCR-motif DNA-binding protein,Yin and yang 1,Yy1,YY-1
28-168 ZMYND11 was first identified by its ability to bind the adenovirus E1A protein. The protein localizes to the nucleus. It functions as a transcriptional repressor, and expression of E1A inhibits this r 0.1 mg
28-167 ZMYND11 was first identified by its ability to bind the adenovirus E1A protein. The protein localizes to the nucleus. It functions as a transcriptional repressor, and expression of E1A inhibits this r 0.1 mg
28-409 The FLJ12644 gene encodes a protein may act as a transcriptional repressor in mitogen-activated protein kinase signaling pathway to mediate cellular functions. 0.1 mg
31-196 EVX1 is a member of the vertebrate eve-related homeo box family. This protein acts as a transcriptional repressor. A similar protein in mice is critical for early embryogenesis. 0.1 mg
27-683 The tumor suppressor WT1 represses and activates transcription. Anti-Prostate Apoptosis Response Protein Par-4 (PAWR) is a WT1-interacting protein that itself functions as a transcriptional repressor. 0.1 mg
27-492 The tumor suppressor WT1 represses and activates transcription. Anti-Prostate Apoptosis Response Protein Par-4 (PAWR) is a WT1-interacting protein that itself functions as a transcriptional repressor. 0.05 mg
CH59 Recombinant Human Transcriptional repressor protein YY1 1 mg
CSB-EL026297HU Human Transcriptional repressor protein YY1(YY1) ELISA kit 96T
CSB-EL026297MO Mouse Transcriptional repressor protein YY1(YY1) ELISA kit 96T
CH59 Recombinant Human Transcriptional repressor protein YY1 50 ug


 

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