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

Sorting nexin-33 (SH3 and PX domain-containing protein 3)

 SNX33_HUMAN             Reviewed;         574 AA.
Q8WV41; B1NM17;
04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
22-NOV-2017, entry version 142.
RecName: Full=Sorting nexin-33;
AltName: Full=SH3 and PX domain-containing protein 3;
Name=SNX33; Synonyms=SH3PX3, SH3PXD3C, SNX30;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ADAM15.
PubMed=16374509; DOI=10.1038/sj.embor.7400596;
Kaerkkaeinen S., Hiipakka M., Wang J.-H., Kleino I.,
Vaehae-Jaakkola M., Renkema G.H., Liss M., Wagner R., Saksela K.;
"Identification of preferred protein interactions by phage-display of
the human Src homology-3 proteome.";
EMBO Rep. 7:186-191(2006).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH DNM1 AND DNM2,
SUBCELLULAR LOCATION, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=18353773; DOI=10.1074/jbc.M801531200;
Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H.,
Kremmer E., Seed B., Baumeister R., Haass C., Lichtenthaler S.F.;
"A novel sorting nexin modulates endocytic trafficking and alpha-
secretase cleavage of the amyloid precursor protein.";
J. Biol. Chem. 283:14257-14268(2008).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Stomach;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
FUNCTION.
PubMed=18419754; DOI=10.1111/j.1600-0854.2008.00750.x;
Heiseke A., Schobel S., Lichtenthaler S.F., Vorberg I., Groschup M.H.,
Kretzschmar H., Schatzl H.M., Nunziante M.;
"The novel sorting nexin SNX33 interferes with cellular PrP formation
by modulation of PrP shedding.";
Traffic 9:1116-1129(2008).
[8]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH WASL.
PubMed=19487689; DOI=10.1074/jbc.M109.007278;
Zhang J., Zhang X., Guo Y., Xu L., Pei D.;
"Sorting nexin 33 induces mammalian cell micronucleated phenotype and
actin polymerization by interacting with Wiskott-Aldrich syndrome
protein.";
J. Biol. Chem. 284:21659-21669(2009).
[10]
INTERACTION WITH ADAM15.
PubMed=19718658; DOI=10.1002/jcb.22317;
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
"Alternative splicing of ADAM15 regulates its interactions with
cellular SH3 proteins.";
J. Cell. Biochem. 108:877-885(2009).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=21048941; DOI=10.1371/journal.pone.0013763;
Wang J.T., Kerr M.C., Karunaratne S., Jeanes A., Yap A.S.,
Teasdale R.D.;
"The SNX-PX-BAR family in macropinocytosis: the regulation of
macropinosome formation by SNX-PX-BAR proteins.";
PLoS ONE 5:E13763-E13763(2010).
[12]
FUNCTION, DOMAIN, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=20964629; DOI=10.1042/BJ20100709;
Dislich B., Than M.E., Lichtenthaler S.F.;
"Specific amino acids in the BAR domain allow homodimerization and
prevent heterodimerization of sorting nexin 33.";
Biochem. J. 433:75-83(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22718350; DOI=10.1242/jcs.105981;
Ma M.P., Chircop M.;
"SNX9, SNX18 and SNX33 are required for progression through and
completion of mitosis.";
J. Cell Sci. 125:4372-4382(2012).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-92, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 212-574.
Structural genomics consortium (SGC);
"Structure of human sorting nexin 33.";
Submitted (DEC-2012) to the PDB data bank.
-!- FUNCTION: Plays a role in the reorganization of the cytoskeleton,
endocytosis and cellular vesicle trafficking via its interactions
with membranes, WASL, DNM1 and DNM2. Acts both during interphase
and at the end of mitotic cell divisions. Required for efficient
progress through mitosis and cytokinesis. Required for normal
formation of the cleavage furrow at the end of mitosis. Modulates
endocytosis of cell-surface proteins, such as APP and PRNP; this
then modulates the secretion of APP and PRNP peptides. Promotes
membrane tubulation (in vitro). May promote the formation of
macropinosomes. {ECO:0000269|PubMed:18353773,
ECO:0000269|PubMed:18419754, ECO:0000269|PubMed:19487689,
ECO:0000269|PubMed:20964629, ECO:0000269|PubMed:21048941,
ECO:0000269|PubMed:22718350}.
-!- SUBUNIT: Homodimer (via BAR domain). Interacts with ADAM15.
Interacts with FASLG. Interacts (via SH3 domain) with DNM1 and
DNM2. Interacts with WASL. {ECO:0000269|PubMed:16374509,
ECO:0000269|PubMed:18353773, ECO:0000269|PubMed:19487689,
ECO:0000269|PubMed:19718658, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:20964629}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2481535, EBI-2481535;
Q13444:ADAM15; NbExp=2; IntAct=EBI-2481535, EBI-77818;
Q05193:DNM1; NbExp=2; IntAct=EBI-2481535, EBI-713135;
Q7L190:DPPA4; NbExp=4; IntAct=EBI-2481535, EBI-710457;
P48023:FASLG; NbExp=2; IntAct=EBI-2481535, EBI-495538;
Q96HR8:NAF1; NbExp=3; IntAct=EBI-2481535, EBI-2515597;
Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-2481535, EBI-77848;
P42768:WAS; NbExp=3; IntAct=EBI-2481535, EBI-346375;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Peripheral
membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane;
Peripheral membrane protein; Cytoplasmic side. Note=Primarily
cytosolic, but a minor proportion is membrane-bound
(PubMed:18353773). Not associated with membranes
(PubMed:21048941). {ECO:0000269|PubMed:18353773,
ECO:0000269|PubMed:21048941}.
-!- TISSUE SPECIFICITY: Detected in heart and pancreas.
{ECO:0000269|PubMed:18353773}.
-!- DOMAIN: The PX and BAR domains mediate association with membranes
and are required for membrane tubulation.
{ECO:0000269|PubMed:20964629}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:18353773}.
-!- SIMILARITY: Belongs to the sorting nexin family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; EF219141; ABN09670.1; -; mRNA.
EMBL; EF653821; ABV26009.1; -; mRNA.
EMBL; AL833039; CAH56299.1; -; mRNA.
EMBL; CH471136; EAW99243.1; -; Genomic_DNA.
EMBL; BC018775; AAH18775.1; -; mRNA.
CCDS; CCDS10283.1; -.
RefSeq; NP_001305075.1; NM_001318146.1.
RefSeq; NP_695003.1; NM_153271.1.
UniGene; Hs.8705; -.
PDB; 4AKV; X-ray; 2.65 A; A/B=212-574.
PDBsum; 4AKV; -.
ProteinModelPortal; Q8WV41; -.
SMR; Q8WV41; -.
BioGrid; 129214; 17.
IntAct; Q8WV41; 17.
MINT; MINT-2792452; -.
STRING; 9606.ENSP00000311427; -.
iPTMnet; Q8WV41; -.
PhosphoSitePlus; Q8WV41; -.
BioMuta; SNX33; -.
DMDM; 74751538; -.
EPD; Q8WV41; -.
MaxQB; Q8WV41; -.
PaxDb; Q8WV41; -.
PeptideAtlas; Q8WV41; -.
PRIDE; Q8WV41; -.
DNASU; 257364; -.
Ensembl; ENST00000308527; ENSP00000311427; ENSG00000173548.
GeneID; 257364; -.
KEGG; hsa:257364; -.
UCSC; uc002bau.4; human.
CTD; 257364; -.
EuPathDB; HostDB:ENSG00000173548.8; -.
GeneCards; SNX33; -.
H-InvDB; HIX0012446; -.
HGNC; HGNC:28468; SNX33.
HPA; HPA040988; -.
neXtProt; NX_Q8WV41; -.
OpenTargets; ENSG00000173548; -.
PharmGKB; PA162404345; -.
eggNOG; KOG2528; Eukaryota.
eggNOG; ENOG410XPHZ; LUCA.
GeneTree; ENSGT00510000046469; -.
HOGENOM; HOG000261633; -.
HOVERGEN; HBG009996; -.
InParanoid; Q8WV41; -.
KO; K17923; -.
OMA; GSMVGRN; -.
OrthoDB; EOG091G07IM; -.
PhylomeDB; Q8WV41; -.
TreeFam; TF314082; -.
ChiTaRS; SNX33; human.
GenomeRNAi; 257364; -.
PRO; PR:Q8WV41; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000173548; -.
CleanEx; HS_SNX30; -.
CleanEx; HS_SNX33; -.
ExpressionAtlas; Q8WV41; baseline and differential.
Genevisible; Q8WV41; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0036089; P:cleavage furrow formation; IMP:UniProtKB.
GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0044351; P:macropinocytosis; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0045806; P:negative regulation of endocytosis; IDA:UniProtKB.
GO; GO:2000009; P:negative regulation of protein localization to cell surface; IDA:UniProtKB.
GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:2000010; P:positive regulation of protein localization to cell surface; IDA:UniProtKB.
GO; GO:0017038; P:protein import; IDA:UniProtKB.
Gene3D; 1.20.1270.60; -; 1.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR027267; AH/BAR_dom_sf.
InterPro; IPR001683; Phox.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR028642; SNX33.
InterPro; IPR014536; Snx9_fam.
InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
PANTHER; PTHR10555:SF121; PTHR10555:SF121; 1.
Pfam; PF10456; BAR_3_WASP_bdg; 1.
Pfam; PF00787; PX; 1.
Pfam; PF14604; SH3_9; 1.
PIRSF; PIRSF027744; Snx9; 1.
SMART; SM00312; PX; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF64268; SSF64268; 1.
PROSITE; PS50195; PX; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Endocytosis; Membrane; Mitosis; Phosphoprotein;
Protein transport; Reference proteome; SH3 domain; Transport.
CHAIN 1 574 Sorting nexin-33.
/FTId=PRO_0000311948.
DOMAIN 1 61 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 230 340 PX. {ECO:0000255|PROSITE-
ProRule:PRU00147}.
DOMAIN 371 574 BAR.
COMPBIAS 112 122 Poly-Asp.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
STRAND 213 215 {ECO:0000244|PDB:4AKV}.
STRAND 220 223 {ECO:0000244|PDB:4AKV}.
STRAND 232 235 {ECO:0000244|PDB:4AKV}.
STRAND 252 256 {ECO:0000244|PDB:4AKV}.
STRAND 259 261 {ECO:0000244|PDB:4AKV}.
STRAND 263 265 {ECO:0000244|PDB:4AKV}.
HELIX 267 280 {ECO:0000244|PDB:4AKV}.
STRAND 282 284 {ECO:0000244|PDB:4AKV}.
TURN 302 304 {ECO:0000244|PDB:4AKV}.
HELIX 305 318 {ECO:0000244|PDB:4AKV}.
HELIX 323 325 {ECO:0000244|PDB:4AKV}.
HELIX 327 333 {ECO:0000244|PDB:4AKV}.
HELIX 339 349 {ECO:0000244|PDB:4AKV}.
HELIX 355 360 {ECO:0000244|PDB:4AKV}.
HELIX 371 407 {ECO:0000244|PDB:4AKV}.
HELIX 409 427 {ECO:0000244|PDB:4AKV}.
HELIX 432 434 {ECO:0000244|PDB:4AKV}.
HELIX 437 459 {ECO:0000244|PDB:4AKV}.
HELIX 460 462 {ECO:0000244|PDB:4AKV}.
HELIX 465 504 {ECO:0000244|PDB:4AKV}.
HELIX 510 568 {ECO:0000244|PDB:4AKV}.
HELIX 569 571 {ECO:0000244|PDB:4AKV}.
SEQUENCE 574 AA; 65265 MW; 7CE51C0F35DDBC3C CRC64;
MALKGRALYD FHSENKEEIS IQQDEDLVIF SETSLDGWLQ GQNSRGETGL FPASYVEIVR
SGISTNHADY SSSPAGSPGA QVSLYNSPSV ASPARSGGGS GFLSNQGSFE EDDDDDWDDW
DDGCTVVEEP RAGGLGTNGH PPLNLSYPGA YPSQHMAFRP KPPLERQDSL ASAKRGSVVG
RNLNRFSCFV RSGVEAFILG DVPMMAKIAE TYSIEMGPRG PQWKANPHPF ACSVEDPTKQ
TKFKGIKSYI SYKLTPTHAA SPVYRRYKHF DWLYNRLLHK FTVISVPHLP EKQATGRFEE
DFIEKRKRRL ILWMDHMTSH PVLSQYEGFQ HFLSCLDDKQ WKMGKRRAEK DEMVGASFLL
TFQIPTEHQD LQDVEDRVDT FKAFSKKMDD SVLQLSTVAS ELVRKHVGGF RKEFQKLGSA
FQAISHSFQM DPPFCSEALN SAISHTGRTY EAIGEMFAEQ PKNDLFQMLD TLSLYQGLLS
NFPDIIHLQK GAFAKVKESQ RMSDEGRMVQ DEADGIRRRC RVVGFALQAE MNHFHQRREL
DFKHMMQNYL RQQILFYQRV GQQLEKTLRM YDNL


Related products :

Catalog number Product name Quantity
EIAAB39085 Homo sapiens,Human,SH3 and PX domain-containing protein 3B,SH3PXD3B,SNAG1,SNX18,Sorting nexin-18,Sorting nexin-associated Golgi protein 1
EIAAB39086 Mouse,Mus musculus,Snag1,Snx18,Sorting nexin-18,Sorting nexin-associated Golgi protein 1
EIAAB39137 Homo sapiens,Human,Protein SDP1,SH3 and PX domain-containing protein 1,SH3 and PX domain-containing protein 3A,SH3PX1,SH3PXD3A,SNX9,Sorting nexin-9
EIAAB39071 Homo sapiens,Human,KIAA0713,RGS domain- and PHOX domain-containing protein,RGS-PX1,SNX13,Sorting nexin-13
EIAAB39095 C20orf161,Homo sapiens,Human,SNX21,SNXL,SNX-L,Sorting nexin L,Sorting nexin-21
EIAAB39118 Homo sapiens,Human,SNX32,SNX6B,Sorting nexin-32,Sorting nexin-6B
EIAAB39121 Mouse,Mus musculus,SH3 and PX domain-containing protein 3,Sh3px3,Snx33,Sorting nexin-33
EIAAB39119 Mouse,Mus musculus,Snx32,Snx6b,Sorting nexin-32,Sorting nexin-6B
26-960 SNX5 is a member of the sorting nexin family. Members of this family contain a phox (PX) domain, which is a phosphoinositide binding domain, and are involved in intracellular trafficking. This protein 0.05 mg
EIAAB36431 Homo sapiens,Human,Putative RUN domain-containing protein 2B,RUNDC2B,RUNDC2L,RUNDC2-like protein,SNX29P1,Sorting nexin 29 protein pseudogene 1
EIAAB39120 Homo sapiens,Human,SH3 and PX domain-containing protein 3,SH3PX3,SH3PXD3C,SNX30,SNX33,Sorting nexin-33
PE013254h Recombinant human Sorting nexin-3 protein 50ug
PE013244h Recombinant human Sorting nexin-3 protein 200ug
PE013254h Recombinant human Sorting nexin-3 protein 5mg
orb81375 Human Sorting Nexin 1 protein Proteins 1
PE013254h Recombinant human Sorting nexin-3 protein 200ug
E9875h Human Sorting Nexin Associated Golgi Protein 1 ELI 96T
PE013244h Recombinant human Sorting nexin-3 protein 50ug
PE013254h Recombinant human Sorting nexin-3 protein 1mg
PE013244h Recombinant human Sorting nexin-3 protein 1mg
PE013244h Recombinant human Sorting nexin-3 protein 5mg
15-288-22561 Sorting nexin-2 - Transformation-related gene 9 protein Polyclonal 0.05 mg
15-288-22561 Sorting nexin-2 - Transformation-related gene 9 protein Polyclonal 0.1 mg
15-5034 Antigens Sorting nexin-3 protein, Human, Recombinant, E.coli 10
EIAAB39111 Mouse,Mus musculus,SDP3 protein,Snx3,Sorting nexin-3


 

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