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

Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)

 SGK1_RAT                Reviewed;         430 AA.
Q06226;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
25-OCT-2017, entry version 134.
RecName: Full=Serine/threonine-protein kinase Sgk1;
EC=2.7.11.1;
AltName: Full=Serum/glucocorticoid-regulated kinase 1;
Name=Sgk1; Synonyms=Sgk;
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].
STRAIN=Fischer 344;
PubMed=8455596; DOI=10.1128/MCB.13.4.2031;
Webster M.K., Goya L., Ge Y., Maiyar A.C., Firestone G.L.;
"Characterization of sgk, a novel member of the serine/threonine
protein kinase gene family which is transcriptionally induced by
glucocorticoids and serum.";
Mol. Cell. Biol. 13:2031-2040(1993).
[2]
INDUCTION BY CNS INJURY.
PubMed=7854047; DOI=10.1016/0169-328X(94)90090-6;
Imaizumi K., Tsuda M., Wanaka A., Tohyama M., Takagi T.;
"Differential expression of sgk mRNA, a member of the Ser/Thr protein
kinase gene family, in rat brain after CNS injury.";
Brain Res. Mol. Brain Res. 26:189-196(1994).
[3]
INDUCTION BY FSH.
PubMed=7740159;
Richards J.S., Fitzpatrick S.L., Clemens J.W., Morris J.K.,
Alliston T., Sirois J.;
"Ovarian cell differentiation: a cascade of multiple hormones,
cellular signals, and regulated genes.";
Recent Prog. Horm. Res. 50:223-254(1995).
[4]
INDUCTION BY P53.
TISSUE=Mammary epithelium;
PubMed=8647846; DOI=10.1074/jbc.271.21.12414;
Maiyar A.C., Huang A.J., Phu P.T., Cha H.H., Firestone G.L.;
"p53 stimulates promoter activity of the sgk. serum/glucocorticoid-
inducible serine/threonine protein kinase gene in rodent mammary
epithelial cells.";
J. Biol. Chem. 271:12414-12422(1996).
[5]
PHOSPHORYLATION AT THR-256.
PubMed=10357815; DOI=10.1093/emboj/18.11.3024;
Park J., Leong M.L., Buse P., Maiyar A.C., Firestone G.L.,
Hemmings B.A.;
"Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI
3-kinase-stimulated signaling pathway.";
EMBO J. 18:3024-3033(1999).
[6]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=10051674; DOI=10.1073/pnas.96.5.2514;
Chen S.-Y., Bhargava A., Mastroberardino L., Meijer O.C., Wang J.,
Buse P., Firestone G.L., Verrey F., Pearce D.;
"Epithelial sodium channel regulated by aldosterone-induced protein
sgk.";
Proc. Natl. Acad. Sci. U.S.A. 96:2514-2519(1999).
[7]
FUNCTION IN REGULATION OF SLC1A6/EAAT4.
PubMed=15504348; DOI=10.1016/j.bbrc.2004.09.193;
Boehmer C., Philippin M., Rajamanickam J., Mack A., Broer S.,
Palmada M., Lang F.;
"Stimulation of the EAAT4 glutamate transporter by SGK protein kinase
isoforms and PKB.";
Biochem. Biophys. Res. Commun. 324:1242-1248(2004).
[8]
FUNCTION IN PHOSPHORYLATION OF MAPT/TAU, AND INTERACTION WITH
MAPT/TAU.
PubMed=16982696; DOI=10.1128/MCB.01017-06;
Yang Y.C., Lin C.H., Lee E.H.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite
formation through microtubule depolymerization by SGK1 and by SGK1
phosphorylation of tau.";
Mol. Cell. Biol. 26:8357-8370(2006).
[9]
FUNCTION IN PHOSPHORYLATION OF MAPK1/ERK2, AND INTERACTION WITH
MAPK3/ERK1; MAPK1/ERK2; MAP2K1/MEK1 AND MAP2K2/MEK2.
PubMed=19447520; DOI=10.1016/j.jhep.2009.02.027;
Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J.,
Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M.,
Hur G.M.;
"Protein kinase SGK1 enhances MEK/ERK complex formation through the
phosphorylation of ERK2: implication for the positive regulatory role
of SGK1 on the ERK function during liver regeneration.";
J. Hepatol. 51:67-76(2009).
-!- FUNCTION: Serine/threonine-protein kinase which is involved in the
regulation of a wide variety of ion channels, membrane
transporters, cellular enzymes, transcription factors, neuronal
excitability, cell growth, proliferation, survival, migration and
apoptosis. Plays an important role in cellular stress response.
Contributes to regulation of renal Na(+) retention, renal K(+)
elimination, salt appetite, gastric acid secretion, intestinal
Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt
sensitivity of blood pressure, salt sensitivity of peripheral
glucose uptake, cardiac repolarization and memory consolidation.
Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2,
K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial
Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2
and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2,
SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid
transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine
transporter: SLC6A8, Na(+)/dicarboxylate cotransporter:
SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter:
SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates
carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT,
SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes:
GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors:
CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport
into epithelial cells by enhancing the stability and expression of
SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L
ubiquitin E3 ligase, promoting its interaction with 14-3-3
proteins, thereby preventing it from binding to SCNN1A/ENAC and
targeting it for degradation. Regulates store-operated Ca(+2)
entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1
directly via its phosphorylation or indirectly via increased
interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and
activates MDM2-dependent ubiquitination of p53/TP53.
Phosphorylates SLC2A4/GLUT4 and up-regulates its activity.
Phosphorylates APBB1/FE65 and promotes its localization to the
nucleus. Phosphorylates FBXW7 and plays an inhibitory role in the
NOTCH1 signaling. Phosphorylates FOXO1 resulting in its
relocalization from the nucleus to the cytoplasm. Phosphorylates
FOXO3, promoting its exit from the nucleus and interference with
FOXO3-dependent transcription. Phosphorylates BRAF and
MAP3K3/MEKK3 and inhibits their activity. Phosphorylates
SLC9A3/NHE3 in response to dexamethasone, resulting in its
activation and increased localization at the cell membrane.
Phosphorylates CREB1. Necessary for vascular remodeling during
angiogenesis (By similarity). Phosphorylates MAPT/TAU and mediates
microtubule depolymerization and neurite formation in hippocampal
neurons. Phosphorylates MAPK1/ERK2 and activates it by enhancing
its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. May also play an
important role in the development of particular groups of neurons
in the postnatal brain. {ECO:0000250, ECO:0000269|PubMed:15504348,
ECO:0000269|PubMed:16982696, ECO:0000269|PubMed:19447520}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Two specific sites, one in the kinase domain
(Thr-256) and the other in the C-terminal regulatory region (Ser-
421), need to be phosphorylated for its full activation.
Phosphorylation at Ser-396 and Ser-400 are also essential for its
activity. Activated by WNK1, WNK2, WNK3 and WNK4 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms a trimeric complex
with FBXW7 and NOTCH1. Interacts with MAPK3/ERK1, MAPK1/ERK2,
MAP2K1/MEK1, MAP2K2/MEK2, NEDD4, NEDD4L, MAPK7, CREB1,
SLC9A3R2/NHERF2 and KCNJ1/ROMK1. Associates with the mammalian
target of rapamycin complex 2 (mTORC2) via an interaction with
MAPKAP1/SIN1 (By similarity). Interacts with MAPT/TAU.
{ECO:0000250, ECO:0000269|PubMed:16982696,
ECO:0000269|PubMed:19447520}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Cell
membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=The
subcellular localization is controlled by the cell cycle, as well
as by exposure to specific hormones and environmental stress
stimuli. In proliferating cells, it shuttles between the nucleus
and cytoplasm in synchrony with the cell cycle, and in
serum/growth factor-stimulated cells it resides in the nucleus. In
contrast, after exposure to environmental stress or treatment with
glucocorticoids, it is detected in the cytoplasm and with certain
stress conditions is associated with the mitochondria. In
osmoregulation through the epithelial sodium channel, it can be
localized to the cytoplasmic surface of the cell membrane.
Nuclear, upon phosphorylation (By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in most tissues with highest levels
in the ovary, thymus and lung. In the kidney, expressed within
glomeruli of the cortex, at low levels in outer medulla and
moderate levels in inner medulla and papilla.
{ECO:0000269|PubMed:10051674}.
-!- INDUCTION: Up-regulated by aldosterone in distal nephron (tubules)
of the kidney. By dexamethasone and serum. By tumor suppressor p53
in mammary epithelial tumor cells. By FSH in granulosa cells. By
injury to the central nervous system.
{ECO:0000269|PubMed:10051674, ECO:0000269|PubMed:7740159,
ECO:0000269|PubMed:7854047, ECO:0000269|PubMed:8647846}.
-!- PTM: Regulated by phosphorylation. Activated by phosphorylation on
Ser-421 by mTORC2, transforming it into a substrate for PDPK1
which phosphorylates it on Thr-256. Phosphorylation on Ser-396 and
Ser-400 are also essential for its activity. Phosphorylation on
Ser-78 by MAPK7 is required for growth factor-induced cell cycle
progression (By similarity). {ECO:0000250}.
-!- PTM: Ubiquitinated by NEDD4L; which promotes proteasomal
degradation. Ubiquitinated by SYVN1 at the endoplasmic reticulum;
which promotes rapid proteasomal degradation and maintains a high
turnover rate in resting cells (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L01624; AAA42137.1; -; mRNA.
PIR; A48094; A48094.
UniGene; Rn.4636; -.
ProteinModelPortal; Q06226; -.
SMR; Q06226; -.
IntAct; Q06226; 1.
MINT; MINT-5114766; -.
STRING; 10116.ENSRNOP00000057871; -.
iPTMnet; Q06226; -.
PhosphoSitePlus; Q06226; -.
PaxDb; Q06226; -.
PRIDE; Q06226; -.
RGD; 3668; Sgk1.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOVERGEN; HBG108317; -.
InParanoid; Q06226; -.
PhylomeDB; Q06226; -.
BRENDA; 2.7.11.1; 5301.
PRO; PR:Q06226; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; IPI:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0048037; F:cofactor binding; IPI:RGD.
GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0048156; F:tau protein binding; IPI:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:RGD.
GO; GO:0043402; P:glucocorticoid mediated signaling pathway; IMP:RGD.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0007616; P:long-term memory; IMP:RGD.
GO; GO:0007019; P:microtubule depolymerization; IDA:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:RGD.
GO; GO:0048812; P:neuron projection morphogenesis; IDA:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
GO; GO:0030307; P:positive regulation of cell growth; IDA:RGD.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
GO; GO:0006468; P:protein phosphorylation; TAS:RGD.
GO; GO:0051726; P:regulation of cell cycle; IMP:RGD.
GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
GO; GO:0008542; P:visual learning; IMP:RGD.
Gene3D; 3.30.1520.10; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR036871; PX_dom_sf.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Apoptosis; ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
Disulfide bond; Endoplasmic reticulum; Kinase; Membrane;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Stress response;
Transferase; Ubl conjugation.
CHAIN 1 430 Serine/threonine-protein kinase Sgk1.
/FTId=PRO_0000086645.
DOMAIN 98 354 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 355 430 AGC-kinase C-terminal.
NP_BIND 104 112 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 60 Necessary for localization to the
mitochondria. {ECO:0000250}.
MOTIF 131 141 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 131 141 Glu/Lys-rich.
ACT_SITE 222 222 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 127 127 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 78 78 Phosphoserine; by MAPK7.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 256 256 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:10357815}.
MOD_RES 368 368 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 400 400 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
DISULFID 193 193 Interchain (with C-258). {ECO:0000250}.
DISULFID 258 258 Interchain (with C-193). {ECO:0000250}.
SEQUENCE 430 AA; 48927 MW; 0D5845B04156F26D CRC64;
MTVKTEAARS TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KLANNSYACK HPEVQSYLKI
SQPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE
EAFYAVKVLQ KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN
GGELFYHLQR ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD
FGLCKENIEH NGTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR
NTAEMYDNIL NKPLQLKNIT NSARHLLEGL LQKDRTKRLG AKDDFMEIKS HIFFSLINWD
DLINKKITPP FNPNVSGPSD LRHFDPEFTE EPVPSSIGRS PDSILVTASV KEAAEAFLGF
SYAPPMDSFL


Related products :

Catalog number Product name Quantity
CSB-EL021189HU Human Serine per threonine-protein kinase Sgk1(SGK1) ELISA kit 96T
H0336 Serine threonine-protein kinase Sgk1 (SGK1), Mouse, ELISA Kit 96T
H0335 Serine threonine-protein kinase Sgk1 (SGK1), Human, ELISA Kit 96T
H0337 Serine threonine-protein kinase Sgk1 (SGK1), Rabbit, ELISA Kit 96T
H0334 Serine threonine-protein kinase Sgk1 (SGK1), Chicken, ELISA Kit 96T
H0333 Serine threonine-protein kinase Sgk1 (SGK1), Bovine, ELISA Kit 96T
H0338 Serine threonine-protein kinase Sgk1 (SGK1), Rat, ELISA Kit 96T
SGK1_RAT ELISA Kit FOR Serine per threonine-protein kinase Sgk1; organism: Rat; gene name: Sgk1 96T
SGK1_MOUSE ELISA Kit FOR Serine per threonine-protein kinase Sgk1; organism: Mouse; gene name: Sgk1 96T
SGK1_HUMAN Human ELISA Kit FOR Serine per threonine-protein kinase Sgk1 96T
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB38131 Oryctolagus cuniculus,Rabbit,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
EIAAB38132 Homo sapiens,Human,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
EIAAB38130 Rat,Rattus norvegicus,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,Sgk,Sgk1
EIAAB38135 Bos taurus,Bovine,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
EIAAB38134 Mouse,Mus musculus,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,Sgk,Sgk1
EIAAB38133 Chicken,Gallus gallus,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
15-288-21987A Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.1 mg
15-288-21987B Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.1 mg
15-288-21987B Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.05 mg
15-288-21987A Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.05 mg
10-288-21987F Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 0.05 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