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

Casein kinase I isoform alpha (CKI-alpha) (DmCK1) (EC 2.7.11.1)

 KC1A_DROME              Reviewed;         337 AA.
P54367; A4V4D3; Q0KHT2; Q9VYK2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
12-SEP-2018, entry version 171.
RecName: Full=Casein kinase I isoform alpha;
Short=CKI-alpha;
Short=DmCK1;
EC=2.7.11.1;
Name=CkIalpha; Synonyms=CKI; ORFNames=CG2028;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Canton-S; TISSUE=Embryo;
Glover C.V.C., Kandala G.;
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, COFACTOR,
SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
STRAIN=Canton-S; TISSUE=Embryo;
PubMed=8832407;
Santos J.A., Logarinho E., Tapia C., Allende C.C., Allende J.E.,
Sunkel C.E.;
"The casein kinase 1 alpha gene of Drosophila melanogaster is
developmentally regulated and the kinase activity of the protein
induced by DNA damage.";
J. Cell Sci. 109:1847-1856(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
FUNCTION.
PubMed=11955436; DOI=10.1016/S0092-8674(02)00685-2;
Liu C., Li Y., Semenov M., Han C., Baeg G.-H., Tan Y., Zhang Z.,
Lin X., He X.;
"Control of beta-catenin phosphorylation/degradation by a dual-kinase
mechanism.";
Cell 108:837-847(2002).
[7]
FUNCTION.
PubMed=11927557; DOI=10.1093/emboj/21.7.1733;
Yanagawa S., Matsuda Y., Lee J.S., Matsubayashi H., Sese S.,
Kadowaki T., Ishimoto A.;
"Casein kinase I phosphorylates the Armadillo protein and induces its
degradation in Drosophila.";
EMBO J. 21:1733-1742(2002).
[8]
FUNCTION.
PubMed=15616566; DOI=10.1038/nature03179;
Jia J., Tong C., Wang B., Luo L., Jiang J.;
"Hedgehog signalling activity of Smoothened requires phosphorylation
by protein kinase A and casein kinase I.";
Nature 432:1045-1050(2004).
[9]
SUBCELLULAR LOCATION, AND INTERACTION WITH COS.
PubMed=15691767; DOI=10.1016/j.devcel.2005.01.001;
Zhang W., Zhao Y., Tong C., Wang G., Wang B., Jia J., Jiang J.;
"Hedgehog-regulated Costal2-kinase complexes control phosphorylation
and proteolytic processing of Cubitus interruptus.";
Dev. Cell 8:267-278(2005).
[10]
FUNCTION.
PubMed=16326393; DOI=10.1016/j.devcel.2005.10.006;
Jia J., Zhang L., Zhang Q., Tong C., Wang B., Hou F., Amanai K.,
Jiang J.;
"Phosphorylation by double-time/CKIepsilon and CKIalpha targets
cubitus interruptus for Slimb/beta-TRCP-mediated proteolytic
processing.";
Dev. Cell 9:819-830(2005).
[11]
FUNCTION, AND MUTAGENESIS OF GLY-43.
PubMed=22095083; DOI=10.1534/genetics.111.133827;
Legent K., Steinhauer J., Richard M., Treisman J.E.;
"A screen for X-linked mutations affecting Drosophila photoreceptor
differentiation identifies Casein kinase 1alpha as an essential
negative regulator of wingless signaling.";
Genetics 190:601-616(2012).
[12]
FUNCTION.
PubMed=25723539; DOI=10.1371/journal.pgen.1005014;
Nguyen H.Q., Nye J., Buster D.W., Klebba J.E., Rogers G.C., Bosco G.;
"Drosophila casein kinase I alpha regulates homolog pairing and genome
organization by modulating condensin II subunit Cap-H2 levels.";
PLoS Genet. 11:E1005014-E1005014(2015).
-!- FUNCTION: Casein kinases are operationally defined by their
preferential utilization of acidic proteins such as caseins as
substrates. Can phosphorylate a large number of proteins. Negative
regulator of wg signaling (PubMed:22095083). Phosphorylates arm
directly or indirectly and stimulates its degradation which
prevents inappropriate wg signaling (PubMed:11955436,
PubMed:11927557, PubMed:22095083). Phosphorylates smo which
promotes its accumulation at the cell surface and its signaling
activity in response to hh (PubMed:15616566). Together with dco,
regulates proteolytic processing of ci by phosphorylating it which
promotes its binding to slmb, the F-box recognition component of
the SCF(slmb) E3 ubiquitin-protein ligase required for ci
processing (PubMed:16326393). Inhibits condensin II interphase
activity by promoting degradation of the Cap-H2 regulatory subunit
and limiting the levels of chromatin-bound Cap-H2 which regulates
interphase chromosome organization (PubMed:25723539).
{ECO:0000269|PubMed:11927557, ECO:0000269|PubMed:11955436,
ECO:0000269|PubMed:15616566, ECO:0000269|PubMed:16326393,
ECO:0000269|PubMed:22095083, ECO:0000269|PubMed:25723539,
ECO:0000269|PubMed:8832407}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8832407};
-!- ACTIVITY REGULATION: Activity increases following DNA damage.
{ECO:0000269|PubMed:8832407}.
-!- SUBUNIT: Interacts with cos. {ECO:0000269|PubMed:15691767}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15691767,
ECO:0000269|PubMed:8832407}. Nucleus {ECO:0000269|PubMed:15691767,
ECO:0000269|PubMed:8832407}. Note=Levels in the nucleus are
significantly increased after DNA damage.
{ECO:0000269|PubMed:8832407}.
-!- DEVELOPMENTAL STAGE: Expressed during early embryogenesis and in
adult females (at protein level). {ECO:0000269|PubMed:8832407}.
-!- PTM: Phosphorylated. The dephosphorylated kinase is active in the
cytoplasm while the active kinase in the nucleus is
phosphorylated. {ECO:0000269|PubMed:8832407}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA64358.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={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; U55848; AAB16904.1; -; mRNA.
EMBL; X94695; CAA64358.1; ALT_INIT; mRNA.
EMBL; AE014298; AAF48192.1; -; Genomic_DNA.
EMBL; AE014298; AAN09313.1; -; Genomic_DNA.
EMBL; AY069346; AAL39491.1; -; mRNA.
RefSeq; NP_001162737.1; NM_001169266.3.
RefSeq; NP_001285163.1; NM_001298234.1.
RefSeq; NP_001285164.1; NM_001298235.1.
RefSeq; NP_511140.1; NM_078585.6.
RefSeq; NP_727631.1; NM_167331.4.
RefSeq; NP_727632.1; NM_167332.3.
UniGene; Dm.2166; -.
ProteinModelPortal; P54367; -.
SMR; P54367; -.
BioGrid; 58615; 10.
DIP; DIP-22041N; -.
IntAct; P54367; 2.
STRING; 7227.FBpp0073513; -.
PaxDb; P54367; -.
PRIDE; P54367; -.
EnsemblMetazoa; FBtr0073680; FBpp0073513; FBgn0015024.
EnsemblMetazoa; FBtr0073682; FBpp0073515; FBgn0015024.
EnsemblMetazoa; FBtr0300380; FBpp0289609; FBgn0015024.
EnsemblMetazoa; FBtr0340408; FBpp0309354; FBgn0015024.
EnsemblMetazoa; FBtr0345162; FBpp0311372; FBgn0015024.
EnsemblMetazoa; FBtr0345163; FBpp0311373; FBgn0015024.
GeneID; 32221; -.
KEGG; dme:Dmel_CG2028; -.
UCSC; CG2028-RC; d. melanogaster.
CTD; 32221; -.
FlyBase; FBgn0015024; CkIalpha.
eggNOG; KOG1164; Eukaryota.
eggNOG; ENOG410XPGP; LUCA.
GeneTree; ENSGT00920000148982; -.
HOGENOM; HOG000148802; -.
InParanoid; P54367; -.
KO; K08957; -.
OMA; GPDYMYL; -.
OrthoDB; EOG091G0AFG; -.
PhylomeDB; P54367; -.
BRENDA; 2.7.11.1; 1994.
Reactome; R-DME-209155; Phosphorylation of AXN and APC.
Reactome; R-DME-209159; Assembly of the CI containing complexes.
Reactome; R-DME-209190; Phosphorylation of CI.
Reactome; R-DME-209214; Phosphorylation of SMO.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-209396; Phosphorylation of ARM.
Reactome; R-DME-209413; Assembly of the 'destruction complex'.
Reactome; R-DME-209440; Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM.
Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
Reactome; R-DME-432553; Phosphorylation of PER and TIM.
SignaLink; P54367; -.
GenomeRNAi; 32221; -.
PRO; PR:P54367; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0015024; Expressed in 32 organ(s), highest expression level in embryo.
ExpressionAtlas; P54367; baseline and differential.
Genevisible; P54367; DM.
GO; GO:0030877; C:beta-catenin destruction complex; ISS:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:FlyBase.
GO; GO:0000902; P:cell morphogenesis; IMP:FlyBase.
GO; GO:0007623; P:circadian rhythm; TAS:Reactome.
GO; GO:0006281; P:DNA repair; IDA:FlyBase.
GO; GO:0042593; P:glucose homeostasis; IMP:FlyBase.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:FlyBase.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:FlyBase.
GO; GO:0006468; P:protein phosphorylation; IDA:FlyBase.
GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium;
Nucleotide-binding; Nucleus; Reference proteome;
Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
CHAIN 1 337 Casein kinase I isoform alpha.
/FTId=PRO_0000192848.
DOMAIN 20 288 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 26 34 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 139 139 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 49 49 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MUTAGEN 43 43 G->D: In 8B12; death primarily during
embryogenesis and early larval stages
with no obvious cuticle patterning
defects. {ECO:0000269|PubMed:22095083}.
CONFLICT 331 337 GKPLIAD -> ASP (in Ref. 2; CAA64358).
{ECO:0000305}.
SEQUENCE 337 AA; 39535 MW; 495144945093E69D CRC64;
MDKMRILKES RPEIIVGGKY RVIRKIGSGS FGDIYLGMSI QSGEEVAIKM ESAHARHPQL
LYEAKLYRIL SGGVGFPRIR HHGKEKNFNT LVMDLLGPSL EDLFNFCTRH FTIKTVLMLV
DQMIGRLEYI HLKCFIHRDI KPDNFLMGIG RHCNKLFLID FGLAKKFRDP HTRHHIVYRE
DKNLTGTARY ASINAHLGIE QSRRDDMESL GYVMMYFNRG VLPWQGMKAN TKQQKYEKIS
EKKMSTPIEV LCKGSPAEFS MYLNYCRSLR FEEQPDYMYL RQLFRILFRT LNHQYDYIYD
WTMLKQKTHQ GQPNPAILLE QLDKDKEKQN GKPLIAD


Related products :

Catalog number Product name Quantity
orb80789 Human Casein Kinase alpha protein Casein Kinase alpha Human Recombinant is non-glycosylated polypeptide having a molecular mass of 45.1 kDa. Casein Kinase is purified by proprietary chromatographic te 3
orb80887 Zea Mays Casein Kinase alpha protein Casein Kinase alpha Zea Mays Recombinant is non-glycosylated polypeptide having a molecular mass of 39.2 kDa. Casein Kinase is purified by proprietary chromatograp 3
26-627 Casein kinase II is a serine_threonine protein kinase that phosphorylates acidic proteins such as casein. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subu 0.05 mg
U1250h CLIA Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
E1250h ELISA Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
E1250h ELISA kit Homo sapiens,Human,Lamina-associated polypeptide 2, isoform alpha,LAP2,Thymopoietin isoform alpha,Thymopoietin-related peptide isoform alpha,TMPO,TP alpha,TPRP isoform alpha 96T
KC1A_RAT Rat ELISA Kit FOR Casein kinase I isoform alpha 96T
ant-442 Mouse Anti Human Casein kinase I isoform alpha 20
ant-442 Mouse Anti Human Casein kinase I isoform alpha 5
CSB-EL006065RA Rat Casein kinase I isoform alpha(CSNK1A1) ELISA kit 96T
ant-442 Mouse Anti Human Casein kinase I isoform alpha 100
CSB-EL006065PI Pig Casein kinase I isoform alpha(CSNK1A1) ELISA kit SpeciesPig 96T
ant-442 Mouse Anti Human Casein kinase I isoform alpha CSNK1A1 20
abx108048 Polyclonal Rabbit Casein kinase I isoform alpha Antibody (HRP) 100 μg
OETAbs442 Casein kinase I isoform alpha, Mouse Anti Human 5
'C11354-1 Casein kinase I isoform alpha-like antibody Ab host: Rabbit 50 Вµg
'C11354-2 Casein kinase I isoform alpha-like antibody Ab host: Rabbit 0.1 mg
CSB-EL006065RA Rat Casein kinase I isoform alpha(CSNK1A1) ELISA kit SpeciesRat 96T
ant-442 Mouse Anti Human Casein kinase I isoform alpha CSNK1A1 100
GTX112052 Casein kinase I isoform alpha-like Rabbit antibody Ab Aff - Purified 0.1 ml
'AP14740CP-N Casein kinase I isoform alpha-like Control Peptide antibody CP 0.1 mg
abx109601 Polyclonal Rabbit Casein kinase I isoform alpha Antibody 100 μg
CSB-EL006065BO Bovine Casein kinase I isoform alpha(CSNK1A1) ELISA kit 96T
'ARP52809_P050 Casein kinase I isoform alpha-like antibody Host rabbit 50
'AP14739CP-N Casein kinase I isoform alpha-like Control Peptide antibody CP 0.1 mg


 

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