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

Phosphatidylinositol 4-kinase type 2-alpha (EC 2.7.1.67) (55 kDa type II phosphatidylinositol 4-kinase) (Phosphatidylinositol 4-kinase type II-alpha)

 P4K2A_RAT               Reviewed;         478 AA.
Q99M64;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
23-MAY-2018, entry version 107.
RecName: Full=Phosphatidylinositol 4-kinase type 2-alpha;
EC=2.7.1.67 {ECO:0000269|PubMed:11244087};
AltName: Full=55 kDa type II phosphatidylinositol 4-kinase;
AltName: Full=Phosphatidylinositol 4-kinase type II-alpha;
Name=Pi4k2a; Synonyms=Pi4kii;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
LOCATION, AND PALMITOYLATION.
TISSUE=Brain;
PubMed=11244087; DOI=10.1074/jbc.C000861200;
Barylko B., Gerber S.H., Binns D.D., Grichine N., Khvotchev M.,
Suedhof T.C., Albanesi J.P.;
"A novel family of phosphatidylinositol 4-kinases conserved from yeast
to humans.";
J. Biol. Chem. 276:7705-7708(2001).
[2]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-50, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[3]
TISSUE SPECIFICITY.
PubMed=19581584; DOI=10.1073/pnas.0903011106;
Simons J.P., Al-Shawi R., Minogue S., Waugh M.G., Wiedemann C.,
Evangelou S., Loesch A., Sihra T.S., King R., Warner T.T., Hsuan J.J.;
"Loss of phosphatidylinositol 4-kinase 2alpha activity causes late
onset degeneration of spinal cord axons.";
Proc. Natl. Acad. Sci. U.S.A. 106:11535-11539(2009).
[4]
SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-60 AND LEU-61, SUBUNIT, AND
INTERACTION WITH BLOC1S5 AND DTNBP1.
PubMed=21998198; DOI=10.1091/mbc.E11-07-0592;
Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A.,
Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
"The schizophrenia susceptibility factor dysbindin and its associated
complex sort cargoes from cell bodies to the synapse.";
Mol. Biol. Cell 22:4854-4867(2011).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-9; SER-46 AND
SER-461, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Membrane-bound phosphatidylinositol-4 kinase (PI4-
kinase) that catalyzes the phosphorylation of phosphatidylinositol
(PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that
plays important roles in endocytosis, Golgi function, protein
sorting and membrane trafficking and is required for prolonged
survival of neurons. Besides, phosphorylation of
phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate
(PI4P) is the first committed step in the generation of
phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the
second messenger inositol 1,4,5-trisphosphate (InsP3).
{ECO:0000269|PubMed:11244087, ECO:0000305}.
-!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
1-phosphatidyl-1D-myo-inositol 4-phosphate.
{ECO:0000269|PubMed:11244087}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=88 uM for ATP;
KM=45 uM for PtdIns;
-!- SUBUNIT: Associates with the BLOC-1 and the AP-3 complexes; the
BLOC-1 complex is required for optimal binding of PI4K2A to the
AP-3 complex. Interacts with BLOC1S5 and DTNBP1 (PubMed:21998198).
Interacts with FOS; this interaction may enhance
phosphatidylinositol phosphorylation activity (By similarity).
Interacts with ITCH (By similarity).
{ECO:0000250|UniProtKB:Q2TBE6, ECO:0000269|PubMed:21998198}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Membrane raft
{ECO:0000250|UniProtKB:Q9BTU6}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q2TBE6}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000250|UniProtKB:Q2TBE6}. Cell
junction, synapse, synaptosome {ECO:0000250|UniProtKB:Q2TBE6}.
Mitochondrion {ECO:0000250|UniProtKB:Q2TBE6}. Endosome
{ECO:0000269|PubMed:21998198}. Cytoplasmic vesicle
{ECO:0000269|PubMed:21998198}. Cell membrane
{ECO:0000250|UniProtKB:Q9BTU6}. Membrane
{ECO:0000269|PubMed:11244087}; Lipid-anchor
{ECO:0000269|PubMed:11244087}. Note=Found in subdomains of the
plasma membrane termed non-caveolar membrane rafts. Localized in
neuronal cell body. Transported from neuronal cell body to neuron
projections in a BLOC-1- and AP-3-complexes-dependent manner (By
similarity). Enriched in neurite tips and neuron projections in a
BLOC-1- and AP-3-complexes-dependent manner.
{ECO:0000250|UniProtKB:Q2TBE6, ECO:0000269|PubMed:21998198}.
-!- TISSUE SPECIFICITY: Detected in adult brain, especially in neurons
in the cerebellum, brain cortex, dorsal root ganglion and spinal
cord (at protein level). {ECO:0000269|PubMed:19581584}.
-!- PTM: Ubiquitinated by ITCH; this does not lead to proteasomal
degradation. {ECO:0000250|UniProtKB:Q9BTU6}.
-!- PTM: Palmitoylated (PubMed:11244087). Palmitoylated by ZDHHC3 and
ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-
dependent, and required for TGN localization (By similarity).
{ECO:0000250|UniProtKB:Q9BTU6, ECO:0000269|PubMed:11244087}.
-!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
subfamily. {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; AY029199; AAK33002.1; -; mRNA.
RefSeq; NP_446187.1; NM_053735.1.
UniGene; Rn.162533; -.
SMR; Q99M64; -.
BioGrid; 250373; 1.
IntAct; Q99M64; 2.
MINT; Q99M64; -.
STRING; 10116.ENSRNOP00000019874; -.
iPTMnet; Q99M64; -.
PhosphoSitePlus; Q99M64; -.
SwissPalm; Q99M64; -.
PaxDb; Q99M64; -.
PRIDE; Q99M64; -.
Ensembl; ENSRNOT00000019874; ENSRNOP00000019874; ENSRNOG00000014675.
GeneID; 114554; -.
KEGG; rno:114554; -.
UCSC; RGD:620485; rat.
CTD; 55361; -.
RGD; 620485; Pi4k2a.
eggNOG; KOG2381; Eukaryota.
eggNOG; ENOG410XP06; LUCA.
GeneTree; ENSGT00390000010434; -.
HOGENOM; HOG000294076; -.
HOVERGEN; HBG059542; -.
InParanoid; Q99M64; -.
KO; K13711; -.
OMA; GVRDSDW; -.
OrthoDB; EOG091G09F3; -.
PhylomeDB; Q99M64; -.
TreeFam; TF314740; -.
Reactome; R-RNO-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-RNO-1660514; Synthesis of PIPs at the Golgi membrane.
Reactome; R-RNO-1660516; Synthesis of PIPs at the early endosome membrane.
PRO; PR:Q99M64; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000014675; -.
Genevisible; Q99M64; RN.
GO; GO:0031083; C:BLOC-1 complex; IEA:Ensembl.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0031901; C:early endosome membrane; IDA:RGD.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070382; C:exocytic vesicle; IDA:RGD.
GO; GO:0035838; C:growing cell tip; IDA:UniProtKB.
GO; GO:0044231; C:host cell presynaptic membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0031224; C:intrinsic component of membrane; ISS:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IDA:RGD.
GO; GO:0035651; F:AP-3 adaptor complex binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:0002561; P:basophil degranulation; IMP:RGD.
GO; GO:0007032; P:endosome organization; IBA:GO_Central.
GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISS:UniProtKB.
InterPro; IPR000403; PI3/4_kinase_cat_dom.
Pfam; PF00454; PI3_PI4_kinase; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasmic vesicle; Endosome;
Golgi apparatus; Kinase; Lipoprotein; Membrane; Mitochondrion;
Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
Synapse; Synaptosome; Transferase; Ubl conjugation.
CHAIN 1 478 Phosphatidylinositol 4-kinase type 2-
alpha.
/FTId=PRO_0000285160.
DOMAIN 132 437 PI3K/PI4K.
NP_BIND 130 136 ATP. {ECO:0000250|UniProtKB:Q9BTU6}.
NP_BIND 260 263 ATP. {ECO:0000250|UniProtKB:Q9BTU6}.
REGION 156 158 Important for substrate binding.
{ECO:0000250|UniProtKB:Q9BTU6}.
REGION 164 177 Important for interaction with membranes.
{ECO:0000250|UniProtKB:Q9BTU6}.
REGION 267 275 Important for interaction with membranes.
{ECO:0000250|UniProtKB:Q9BTU6}.
REGION 358 367 Important for interaction with membranes.
{ECO:0000250|UniProtKB:Q9BTU6}.
BINDING 151 151 ATP. {ECO:0000250|UniProtKB:Q9BTU6}.
BINDING 345 345 ATP. {ECO:0000250|UniProtKB:Q9BTU6}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9BTU6}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BTU6}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 50 50 Phosphoserine.
{ECO:0000244|PubMed:16641100}.
MOD_RES 461 461 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
LIPID 173 173 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9BTU6}.
LIPID 174 174 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9BTU6}.
LIPID 176 176 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9BTU6}.
LIPID 177 177 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q9BTU6}.
MUTAGEN 60 60 L->A: Reduces targeting to synaptic
vesicles and neurite tips; when
associated with A-61.
{ECO:0000269|PubMed:21998198}.
MUTAGEN 61 61 L->A: Reduces targeting to synaptic
vesicles and neurite tips; when
associated with A-60.
{ECO:0000269|PubMed:21998198}.
SEQUENCE 478 AA; 54305 MW; EBE4BFFB4574FD1F CRC64;
MDETSPLVSP ERAQPPEYTF PSVSGAHFPQ VPGGAVRVAA AGSGPSPPCS PGHDRERQPL
LDRARGAAAQ GQTHTVAAQA QALAAQAAVA VHAVQTHRER NDFPEDPEFE VVVRQAEIAI
ECSIYPERIY QGSSGSYFVK DSQGRIIAVF KPKNEEPYGN LNPKWTKWLQ KLCCPCCFGR
DCLVLNQGYL SEAGASLVDQ KLELNIVPRT KVVYLASETF NYSAIDRVKS RGKRLALEKV
PKVGQRFNRI GLPPKVGSFQ LFVEGYKDAD YWLRRFEAEP LPENTNRQLL LQFERLVVLD
YIIRNTDRGN DNWLIKYDYP MDNPNCRDTD WVMVREPVIK VAAIDNGLAF PLKHPDSWRA
YPFYWAWLPQ AKVPFSQEIK DLILPKISDP NFVKDLEEDL YELFKKDPGF DRGQFHKQIA
VMRGQILNLT QALKDNKSPL HLVQMPPVIV ETARSHQRSS SESYTQSFQS RKPFFSWW


Related products :

Catalog number Product name Quantity
EIAAB29552 55 kDa type II phosphatidylinositol 4-kinase,Phosphatidylinositol 4-kinase type 2-alpha,Phosphatidylinositol 4-kinase type II-alpha,Pi4k2a,Pi4kii,Rat,Rattus norvegicus
EIAAB31015 68 kDa type I phosphatidylinositol-4-phosphate 5-kinase alpha,Homo sapiens,Human,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha,PIP5K1A,P
EIAAB31014 68 kDa type I phosphatidylinositol-4-phosphate 5-kinase,Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinos
EIAAB30994 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Diphosphoinositide kinase 2-alpha,Homo sapiens,Human,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-kina
EIAAB30996 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Diphosphoinositide kinase 2-alpha,Mouse,Mus musculus,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-kina
EIAAB31018 Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,Pip5k1a,Pip5k1b,PI
EIAAB29554 Homo sapiens,Human,Phosphatidylinositol 4-kinase type 2-alpha,Phosphatidylinositol 4-kinase type II-alpha,PI4K2A
EIAAB31234 Homo sapiens,Human,hVps34,Phosphatidylinositol 3-kinase catalytic subunit type 3,Phosphatidylinositol 3-kinase p100 subunit,Phosphoinositide-3-kinase class 3,PI3K type 3,PI3-kinase type 3,PIK3C3,PtdIn
EIAAB29553 Mouse,Mus musculus,Phosphatidylinositol 4-kinase type 2-alpha,Phosphatidylinositol 4-kinase type II-alpha,Pi4k2a
EIAAB31017 Phosphatidylinositol-4-phosphate 5-kinase type I alpha,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,Pip5k1a,Pip5k1b,PIP5K1-beta,PIP5KIalp
EIAAB30997 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Chicken,Diphosphoinositide kinase 2-alpha,Gallus gallus,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-k
EIAAB30998 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Diphosphoinositide kinase 2-alpha,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha,PI(
EIAAB30995 1-phosphatidylinositol-5-phosphate 4-kinase 2-alpha,Diphosphoinositide kinase 2-alpha,Phosphatidylinositol-5-phosphate 4-kinase type II alpha,Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha,PI(
EIAAB31231 Phosphatidylinositol 3-kinase catalytic subunit type 3,Phosphoinositide-3-kinase class 3,PI3K type 3,PI3-kinase type 3,Pik3c3,PtdIns-3-kinase type 3,Rat,Rattus norvegicus,Vps34
EIAAB31232 Mouse,Mus musculus,Phosphatidylinositol 3-kinase catalytic subunit type 3,Phosphoinositide-3-kinase class 3,PI3K type 3,PI3-kinase type 3,Pik3c3,PtdIns-3-kinase type 3
EIAAB31233 Phosphatidylinositol 3-kinase catalytic subunit type 3,Phosphoinositide-3-kinase class 3,PI3K type 3,PI3-kinase type 3,Pig,PIK3C3,PtdIns-3-kinase type 3,Sus scrofa
EIAAB30999 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta,Diphosphoinositide kinase 2-beta,Homo sapiens,Human,Phosphatidylinositol-5-phosphate 4-kinase type II beta,Phosphatidylinositol-5-phosphate 4-kinase
EIAAB31002 Homo sapiens,Human,Phosphatidylinositol-5-phosphate 4-kinase type II gamma,Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma,PI(5)P 4-kinase type II gamma,PIP4K2C,PIP4KII-gamma,PIP5K2C
EIAAB31019 Homo sapiens,Human,Phosphatidylinositol-4-phosphate 5-kinase type I beta,Phosphatidylinositol-4-phosphate 5-kinase type-1 beta,PIP5K1B,PIP5K1-beta,PIP5KIbeta,Protein STM-7,PtdIns(4)P-5-kinase 1 beta,S
EIAAB31022 Homo sapiens,Human,KIAA0589,Phosphatidylinositol-4-phosphate 5-kinase type I gamma,Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma,PIP5K1C,PIP5K1-gamma,PIP5KIgamma,PtdIns(4)P-5-kinase 1 gamma
EIAAB31021 Kiaa0589,Mouse,Mus musculus,Phosphatidylinositol-4-phosphate 5-kinase type I gamma,Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma,Pip5k1c,PIP5K1-gamma,PIP5KIgamma,PtdIns(4)P-5-kinase 1 gamma
EIAAB31001 1-phosphatidylinositol-5-phosphate 4-kinase 2-beta,Diphosphoinositide kinase 2-beta,Mouse,Mus musculus,Phosphatidylinositol-5-phosphate 4-kinase type II beta,Phosphatidylinositol-5-phosphate 4-kinase
EIAAB31003 Mouse,Mus musculus,Phosphatidylinositol-5-phosphate 4-kinase type II gamma,Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma,PI(5)P 4-kinase type II gamma,Pip4k2c,PIP4KII-gamma,Pip5k2c
EIAAB31004 Phosphatidylinositol-5-phosphate 4-kinase type II gamma,Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma,PI(5)P 4-kinase type II gamma,Pip4k2c,PIP4KII-gamma,Pip5k2c,Rat,Rattus norvegicus
EIAAB31005 Bos taurus,Bovine,Phosphatidylinositol-5-phosphate 4-kinase type II gamma,Phosphatidylinositol-5-phosphate 4-kinase type-2 gamma,PI(5)P 4-kinase type II gamma,PIP4K2C,PIP4KII-gamma,PIP5K2C


 

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