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

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.21) (EC 2.7.4.24) (InsP6 and PP-IP5 kinase)

 VIP1_YEAST              Reviewed;        1146 AA.
Q06685; D6VZ44;
09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-NOV-2018, entry version 140.
RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase;
EC=2.7.4.21;
EC=2.7.4.24;
AltName: Full=InsP6 and PP-IP5 kinase;
Name=VIP1; OrderedLocusNames=YLR410W;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION.
PubMed=10388810;
Feoktistova A., McCollum D., Ohi R., Gould K.L.;
"Identification and characterization of Schizosaccharomyces pombe
asp1(+), a gene that interacts with mutations in the Arp2/3 complex
and actin.";
Genetics 152:895-908(1999).
[4]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=YAL6B;
PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200;
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,
Mann M., Jensen O.N.;
"Quantitative phosphoproteomics applied to the yeast pheromone
signaling pathway.";
Mol. Cell. Proteomics 4:310-327(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[8]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-487 AND HIS-548.
PubMed=17412958; DOI=10.1126/science.1139099;
Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E.,
Haystead T.A., Ribeiro A.A., York J.D.;
"A conserved family of enzymes that phosphorylate inositol
hexakisphosphate.";
Science 316:106-109(2007).
[9]
FUNCTION.
PubMed=17412959; DOI=10.1126/science.1139080;
Lee Y.-S., Mulugu S., York J.D., O'Shea E.K.;
"Regulation of a cyclin-CDK-CDK inhibitor complex by inositol
pyrophosphates.";
Science 316:109-112(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-77, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-895 AND
SER-1107, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Bifunctional inositol kinase that acts in concert with
the IP6K kinases to synthesize the diphosphate group-containing
inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-
InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4
(PubMed:17412958). Phosphorylates inositol hexakisphosphate
(InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn
phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively,
phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from
InsP6, to produce (PP)2-InsP4 (By similarity). Required for
maintaining cellular integrity, normal growth and interactions
with the ARP complex (PubMed:10388810). Acts as a regulator of the
PHO80-PHO85 cyclin/cyclin-dependent kinase (CDK) complex, thereby
regulating signaling of phosphate availability (PubMed:17412959).
Required for the function of the cortical actin cytoskeleton,
possibly by participating in correct F-actin localization and
ensuring polarized growth (PubMed:10388810). Regulates polarized
growth and modulates interphase microtubule cytoskeleton.
Regulates microtubule dynamics without the requirement of
microtubule plus-end tracking protein Mal3. Required for growth
zone selection (By similarity). {ECO:0000250|UniProtKB:O74429,
ECO:0000250|UniProtKB:Q6PFW1, ECO:0000269|PubMed:10388810,
ECO:0000269|PubMed:17412958, ECO:0000269|PubMed:17412959}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.
{ECO:0000269|PubMed:17412958}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate. {ECO:0000269|PubMed:17412958}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-
pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate)
2,3,4,6-tetrakisphosphate. {ECO:0000269|PubMed:17412958}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.
{ECO:0000269|PubMed:17412958}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Cytoplasm, cytoskeleton {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The N-terminal kinase domain produces inositol
polyphosphates. The C-terminal acid phosphatase-like domain binds
inositol polyphosphates and negatively regulates their
accumulation. The C-terminal domain reduces the amount of inositol
pyrophosphates in a dose-dependent manner in vitro.
{ECO:0000250|UniProtKB:O74429}.
-!- MISCELLANEOUS: Present with 8810 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
subfamily. {ECO:0000305}.
-!- CAUTION: Although related to histidine acid phosphatase proteins,
it lacks the conserved active sites, suggesting that it has no
phosphatase activity. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U20162; AAB67497.1; -; Genomic_DNA.
EMBL; BK006945; DAA09710.1; -; Genomic_DNA.
PIR; S59376; S59376.
RefSeq; NP_013514.1; NM_001182298.1.
ProteinModelPortal; Q06685; -.
SMR; Q06685; -.
BioGrid; 31667; 520.
IntAct; Q06685; 31.
MINT; Q06685; -.
STRING; 4932.YLR410W; -.
iPTMnet; Q06685; -.
MaxQB; Q06685; -.
PaxDb; Q06685; -.
PRIDE; Q06685; -.
EnsemblFungi; YLR410W; YLR410W; YLR410W.
GeneID; 851126; -.
KEGG; sce:YLR410W; -.
SGD; S000004402; VIP1.
GeneTree; ENSGT00390000009048; -.
HOGENOM; HOG000177917; -.
InParanoid; Q06685; -.
OMA; PWLFRER; -.
OrthoDB; EOG092C0FUM; -.
BioCyc; YEAST:MONOMER3O-224; -.
Reactome; R-SCE-1855167; Synthesis of pyrophosphates in the cytosol.
PRO; PR:Q06685; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0102092; F:5-diphosphoinositol pentakisphosphate 3-kinase activity; IEA:UniProtKB-EC.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; IBA:GO_Central.
GO; GO:0000829; F:inositol heptakisphosphate kinase activity; IDA:SGD.
GO; GO:0052723; F:inositol hexakisphosphate 1-kinase activity; IDA:SGD.
GO; GO:0052724; F:inositol hexakisphosphate 3-kinase activity; IDA:SGD.
GO; GO:0000830; F:inositol hexakisphosphate 4-kinase activity; IDA:SGD.
GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; IEA:UniProtKB-EC.
GO; GO:0000831; F:inositol hexakisphosphate 6-kinase activity; IDA:SGD.
GO; GO:0000828; F:inositol hexakisphosphate kinase activity; IBA:GO_Central.
GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:SGD.
GO; GO:0051516; P:regulation of bipolar cell growth; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
CDD; cd07061; HP_HAP_like; 1.
InterPro; IPR013651; ATP-grasp_RimK-type.
InterPro; IPR000560; His_Pase_clade-2.
InterPro; IPR037446; His_Pase_VIP1.
InterPro; IPR029033; His_PPase_superfam.
PANTHER; PTHR12750; PTHR12750; 1.
Pfam; PF00328; His_Phos_2; 1.
Pfam; PF08443; RimK; 1.
SUPFAM; SSF53254; SSF53254; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 1146 Inositol hexakisphosphate and
diphosphoinositol-pentakisphosphate
kinase.
/FTId=PRO_0000270924.
NP_BIND 402 405 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 412 414 ATP. {ECO:0000250|UniProtKB:O43314}.
NP_BIND 487 489 ATP. {ECO:0000250|UniProtKB:O43314}.
REGION 197 198 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 377 378 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 492 495 Substrate binding.
{ECO:0000250|UniProtKB:O43314}.
REGION 530 597 Polyphosphoinositide-binding domain.
{ECO:0000250|UniProtKB:Q6PFW1}.
BINDING 278 278 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 351 351 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 358 358 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 377 377 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 414 414 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 428 428 Substrate.
{ECO:0000250|UniProtKB:O43314}.
BINDING 430 430 ATP. {ECO:0000250|UniProtKB:O43314}.
BINDING 475 475 ATP. {ECO:0000250|UniProtKB:O43314}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 54 54 Phosphoserine.
{ECO:0000244|PubMed:17330950}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 895 895 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 1107 1107 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 487 487 D->A: Abolishes enzyme activity.
{ECO:0000269|PubMed:17412958}.
MUTAGEN 548 548 H->A: Does not affect enzyme activity.
{ECO:0000269|PubMed:17412958}.
SEQUENCE 1146 AA; 129755 MW; D69E44EAD16490F9 CRC64;
MSGIKKEPIE SDEVPQQETK NNLPSAPSEM SPLFLNKNTQ KAMQSIAPIL EGFSPKTSAS
ENMSLKLPPP GIQDDHSEEN LTVHDTLQRT ISTALGNGNN TNTVTTSGLK KADSESKSEA
DPEGLSNSNI VNDADNINSI SKTGSPHLPQ GTMDAEQTNM GTNSVPTSSA SSRKSSTSHP
KPRLPKVGKI GVCAMDAKVL SKPMRHILNR LIEHGEFETV IFGDKVILDE RIENWPTCDF
LISFFSSGFP LDKAIKYVKL RKPFIINDLI MQKILWDRRL CLQVLEAYNV PTPPRLEISR
DGGPRANEEL RAKLREHGVE VKPVEEPEWK MVDDDTLEVD GKTMTKPFVE KPVDGEDHNI
YIYYHSKNGG GGRRLFRKVG NKSSEFDPTL VHPRTEGSYI YEQFMDTDNF EDVKAYTIGE
NFCHAETRKS PVVDGIVRRN THGKEVRYIT ELSDEEKTIA GKVSKAFSQM ICGFDLLRVS
GKSYVIDVNG FSFVKDNKAY YDSCANILRS TFIEAKKKMD MEKKNLPIIR EEKEQKWVFK
GLAIIIRHAD RTPKQKFKHS FTSPIFISLL KGHKEEVVIR NVNDLKIVLQ ALRIALDEKA
GNPAKIKVLA NALEKKLNFP GTKIQLKPVL NKENEVEKVQ FILKWGGEPT HSAKYQATEL
GEQMRQDFDL LNKSILQNIK IFSSSERRVL HTAQYWTRAL FGADELGSDE ISIRKDLLDD
SNAAKDLMDK VKKKLKPLLR EGKEAPPQFA WPSKMPEPYL VIKRVVELMN YHKKIMDNNF
AKKDVNSMQT RWCTSEDPSL FKERWDKLFK EFNNAEKVDP SKISELYDTM KYDALHNRQF
LENIFDPGLP NEAIADELGS HSLVDRYPIN VLAKNNFKII DSHSMNNSGK NSSNSVGSLG
WVLESGKTST ARNPKSSSQF DEPRFMQLRE LYKLAKVLFD FICPKEYGIS DAEKLDIGLL
TSLPLAKQIL NDIGDMKNRE TPACVAYFTK ESHIYTLLNI IYESGIPMRI ARNALPELDY
LSQITFELYE STDASGQKSH SIRLKMSPGC HTQDPLDVQL DDRHYISCIP KISLTKHLDM
DYVQQKLRNK FTRVIMPPKF TPVNITSPNL SFQKRKTRRK SVSVEKLKRP ASSGSSSSTS
VNKTLD


Related products :

Catalog number Product name Quantity
EIAAB45789 Diphosphoinositol pentakisphosphate kinase 1,Hisppd2a,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1,InsP6 and PP-IP
EIAAB45790 Diphosphoinositol pentakisphosphate kinase 1,Hisppd2a,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1,InsP6 and PP-IP
EIAAB45792 Diphosphoinositol pentakisphosphate kinase 2,Hisppd1,Histidine acid phosphatase domain-containing protein 1,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2,InsP6 and PP-IP5
EIAAB45788 Bos taurus,Bovine,Diphosphoinositol pentakisphosphate kinase 1,HISPPD2A,Histidine acid phosphatase domain-containing protein 2A,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
EIAAB45793 Diphosphoinositol pentakisphosphate kinase 2,HISPPD1,Histidine acid phosphatase domain-containing protein 1,Homo sapiens,hsVIP2,Human,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate
EIAAB45791 Diphosphoinositol pentakisphosphate kinase 1,HISPPD2A,Histidine acid phosphatase domain-containing protein 2A,Homo sapiens,hsVIP1,Human,Inositol hexakisphosphate and diphosphoinositol-pentakisphosphat
CSB-EL010373HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2(HISPPD1) ELISA kit 96T
CSB-EL010374HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1(HISPPD2A) ELISA kit 96T
CSB-EL010374HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1(HISPPD2A) ELISA kit SpeciesHuman 96T
CSB-EL010373HU Human Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2(HISPPD1) ELISA kit SpeciesHuman 96T
VIP1_MOUSE ELISA Kit FOR Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1; organism: Mouse; gene name: Ppip5k1 96T
VIP2_MOUSE ELISA Kit FOR Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2; organism: Mouse; gene name: Ppip5k2 96T
PPL PPIP5K2 Gene diphosphoinositol pentakisphosphate kinase 2
E12625h Human Diphosphoinositol Pentakisphosphate Kinase 1 96T
E12626h Human Diphosphoinositol Pentakisphosphate Kinase 2 96T
PPKB PPIP5K1 Gene diphosphoinositol pentakisphosphate kinase 1
E15053h Rat ELISA Kit FOR Inositol-pentakisphosphate 2-kinase 96T
201-20-2827 IPPK{inositol 1,3,4,5,6-pentakisphosphate 2-kinase}rabbit.pAb 0.2ml
CSB-EL011783RA Rat Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
IQCA1 IPPK Gene inositol 1,3,4,5,6-pentakisphosphate 2-kinase
26-980 Inositol phosphates (IPs) and diphosphoinositol phosphates (PP-IPs), also known as inositol pyrophosphates, act as cell signaling molecules. HISPPD1 has both IP6 kinase (EC 2.7.4.21) and PP-IP5 (also 0.05 mg
CSB-EL011783HU Human Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
CSB-EL011783RA Rat Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit SpeciesRat 96T
CSB-EL011783MO Mouse Inositol-pentakisphosphate 2-kinase(IPPK) ELISA kit 96T
SMYD1_HUMAN Rat ELISA Kit FOR Inositol hexakisphosphate kinase 1 96T


 

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





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | 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
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | 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

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 | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | 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 | 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 | 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 | Gentaur