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

Genome polyprotein [Cleaved into: Protein VP0 (P1AB) (Virion protein 0); Protein VP3 (P1C) (Virion protein 3); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Protein 3B (P3B) (VPg); Protease 3C (P3C) (EC 3.4.22.28) (EC 3.4.22.29) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]

 POLG_HPE2W              Reviewed;        2179 AA.
O73556;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
28-MAR-2018, entry version 130.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=P1AB;
AltName: Full=Virion protein 0;
Contains:
RecName: Full=Protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Protein 2A;
Short=P2A;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Protein 3B;
Short=P3B;
AltName: Full=VPg;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28;
EC=3.4.22.29;
AltName: Full=Picornain 3C;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48;
Human parechovirus 2 (strain Williamson) (HPeV-2) (Echovirus 23).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Parechovirus.
NCBI_TaxID=122962;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=9820139; DOI=10.1099/0022-1317-79-11-2641;
Ghazi F., Hughes P.J., Hyypiae T., Stanway G.;
"Molecular analysis of human parechovirus type 2 (formerly echovirus
23).";
J. Gen. Virol. 79:2641-2650(1998).
-!- FUNCTION: Protein 2A: Is not a protease. {ECO:0000250}.
-!- FUNCTION: Protein 2B: Affects membrane integrity and cause an
increase in membrane permeability. {ECO:0000250}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes. It displays RNA-
binding, nucleotide binding and NTPase activities (By similarity).
{ECO:0000250}.
-!- FUNCTION: Protein 3A, via its hydrophobic domain, serves as
membrane anchor. {ECO:0000250}.
-!- FUNCTION: Protease 3C: cysteine protease that generates mature
viral proteins from the precursor polyprotein. In addition to its
proteolytic activity, it binds to viral RNA, and thus influences
viral genome replication. RNA and substrate bind cooperatively to
the protease (By similarity). {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Tyr-|-Gly bond in the
picornavirus polyprotein.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- SUBCELLULAR LOCATION: Protein VP3: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein VP1: Virion {ECO:0000250}. Host
cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host cytoplasmic vesicle
membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the
surface of intracellular membrane vesicles that are induced after
virus infection as the site for viral RNA replication. These
vesicles are derived from the endoplasmic reticulum (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Protein 3B: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum (By similarity). {ECO:0000250}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
linked to the 5'-end of genomic RNA. This uridylylated form acts
as a nucleotide-peptide primer for the polymerase (By similarity).
{ECO:0000250}.
-!- PTM: Specific enzymatic cleavages yield mature proteins. All
cleavages are catalyzed by P3C.
-!- SIMILARITY: Belongs to the picornaviruses polyprotein family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ005695; CAA06679.1; -; Genomic_RNA.
ProteinModelPortal; O73556; -.
OrthoDB; VOG090000BA; -.
Proteomes; UP000000670; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0019015; C:viral genome; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039520; P:induction by virus of host autophagy; ISS:UniProtKB.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039611; P:suppression by virus of host translation initiation factor activity; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 2.
Gene3D; 2.60.120.20; -; 3.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
InterPro; IPR009419; VPP_parechovir_P3A.
InterPro; IPR009407; VPP_parechovir_P3B.
Pfam; PF06344; Parecho_VpG; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF06363; Picorna_P3A; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
3: Inferred from homology;
ATP-binding; Capsid protein; Complete proteome;
Covalent protein-RNA linkage; Helicase; Host cytoplasm;
Host cytoplasmic vesicle; Host membrane; Host-virus interaction;
Hydrolase; Ion channel; Ion transport; Lipoprotein; Membrane;
Myristate; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; Reference proteome; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase; Transport;
Viral attachment to host cell; Viral ion channel;
Viral RNA replication; Virion; Virus entry into host cell.
CHAIN 1 289 Protein VP0. {ECO:0000255}.
/FTId=PRO_0000039750.
CHAIN 290 542 Protein VP3. {ECO:0000255}.
/FTId=PRO_0000039751.
CHAIN 543 775 Protein VP1. {ECO:0000255}.
/FTId=PRO_0000039752.
CHAIN 776 922 Protein 2A. {ECO:0000255}.
/FTId=PRO_0000039753.
CHAIN 923 1044 Protein 2B. {ECO:0000255}.
/FTId=PRO_0000039754.
CHAIN 1045 1373 Protein 2C. {ECO:0000255}.
/FTId=PRO_0000039755.
CHAIN 1374 1490 Protein 3A. {ECO:0000255}.
/FTId=PRO_0000039756.
CHAIN 1491 1510 Protein 3B. {ECO:0000255}.
/FTId=PRO_0000039757.
CHAIN 1511 1710 Protease 3C. {ECO:0000255}.
/FTId=PRO_0000039758.
CHAIN 1711 2179 RNA-directed RNA polymerase 3D-POL.
{ECO:0000255}.
/FTId=PRO_0000039759.
DOMAIN 1156 1317 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1944 2058 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1184 1191 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
MOTIF 763 765 Cell attachment site. {ECO:0000255}.
ACT_SITE 1549 1549 For protease 3C activity. {ECO:0000255}.
ACT_SITE 1580 1580 For protease 3C activity. {ECO:0000255}.
ACT_SITE 1669 1669 For protease 3C activity. {ECO:0000255}.
SITE 775 776 Cleavage; by protease 2A. {ECO:0000255}.
MOD_RES 1493 1493 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
SEQUENCE 2179 AA; 245874 MW; 96803C0BB8856664 CRC64;
METIKSIADM ATGVTKTIDA TINSVNEIIT NTDNASGGDI LTKVADDASN ILGPNCYATT
SEPENKDVVQ ATTTVNTTNL TQHPSAPTLP FTPDFSNVDT FHSMAYDTTT GSKNPNKLVR
LTTHAWASTL QRGHQIDHVN LPVDFWDEQR KPAYGHAKYF AAVRCGFHFQ VQVNVNQGTA
GSALVVYEPK PVVDYDKDLE FGAFTNLPHV LMNLAETTQA DLCIPYVADT NYVKTDSSDL
GQLKVYVWTP LSIPSGSSNQ VDVTILGSLL QLDFQNPRVY GQNVDIYDTA PSKPIPLRKT
KYLTMSTKYK WTRNKVDIAE GPGSMNMANV LSTTAAQSVA LVGERAFYDP RTAGSKSRFD
DLVKISQLFS VMADSTTPSA NHGIDQKGYF KWSANSDPQA IVHRNLVHLN LFPNLKVFEN
SYSYFRGSLI IRLSVYASTF NRGRLNGFFP NSSTDETSEI DNAIYTICDI GSDNSFEITI
PYSFSTWMRK THGKPIGLFQ IEVLNRLTYN YSSPNEVYCI VQGKMGQDAK FFCPTGSLVT
FQNSWGSQMD LTDPLCIEDS VEDCKQTITP TELGLTSAQD DGPLGNDKPN YFLNFKSMNV
DIFTVSHTKV DNIFGRAWFA HVHDFTNDGL WRQGLEFPKE GHGALSLLFA YFTGELNIHV
LFLSDRGFLR VGHTYDTETN RTNFLSSSGI ITVPAGEQMT LSVPSYSNKP LRTVRSSNAL
GYLLCKPLLT GTSSGRIEIF LSLRCPNFFF PLPAPKPATR KYRGDLATWS DQSPYGRQGK
KQLMKLAYLD RGFYKHYGIV VGDDVYQLDS DDIFKTALTG KAKFTKTRLT PDWVVEEECE
LDYFRIKYLE SSVNSEHIFS VDNNCETIAK DIFGSHSLSQ HQQIGLIGTI LLTAGLMSTI
KTPVNPTTIK EFFNHAIEGD EQGLSLLVQK CTTFFSSAAT ELLDNDLVKF IIKILVRILC
YMVLYCHKPN ILTTACLSTL LVMDVTSSSV LSPSCKALMQ CLMDGDVKKL AEVVAESMSN
TDDDEIKEQI CDTVKYTKQI LSNQGPFKGF NEISTAFRHI DWWIQTLLKI KDMVLSVFKP
SVEKRAVEWL ERNKEHVCSI LDYASDIIVK SKDQTKMKTQ EFYQRYNDCL SKFKPIMAMC
FRSCHNSISN TVYRLFQELA RIPNRMATQN DLIRVEPIGI WIQGEPGQGK SFLTHTLSKQ
LQKTCGLQGI YTNPTASEFM DGYDNQDIHL IDDLGQTRKE RDIEMLCNCI SSDPDIVPMA
HLEEKGKFYT SKLVIATTNK PDFSSTVLLD SGALRRRFPY IMHIRAAKHY SKSGKLNVSQ
AMPHMSTGEC WEVSKNGRDW ETLKLKELID KITVDYKERI ANYNTWKKQL EDQTLDDLDD
AVSYIKHNYP DAIPYIDEYL NIEMSTLIEQ MEAFIEPKPS VFKCFASRVG DKIKEASREV
VKWFSDKLKS MLNFVERNKA WLTVVSAVTS AIGILLLVTK IFKKEESKDE RAYNPTLPVA
KPKGTFPVSQ REFKNEAPYD GQLEHIISQM AYITGSTTGH ITHCAGYQHD EIILHGHSIK
YLEQEEELTL HYKNKVFPIE QPSVTQVTLG GKPMDLAIVK CKLPFRFKKN SKYYTNKIGT
ESMLIWMTEQ GIITKEVQRV HHSGGIKTRE GTESTKTISY TVKSCKGMCG GLLISKVEGN
FKILGMHIAG NGEMGVAIPF NFLKNDMSDQ GIVTEVTPIQ PMYINTKSQI HKSPVYGAVE
VKMGPAVLSK SDTRLEEPVD CLVKKSASKY RVNKFQVNNE LWQGVKACVK SKFREIFGVN
GIVDMKTAIL GTSHVNSMDL STSAGYSFVK SGYKKKDLIC LEPFSVSPML EKLVQEKFHN
LLKGNQITTI FNTCLKDELR KLDKIATGKT RCIEACEIDY CIVYRMIMME IYDKIYQTPC
YYSGLAVGIN PYRDWHFMIN ALNDYNYEMD YSQYDGSLSS MLLWEAVQVL AYCHDSPDLV
MQLHKPVIDS DHVVFNERWL IHGGMPSGSP CTTVLNSLCN LMMCIYTTNL ISPGIDCLPI
VYGDDVILSL DKEIEPERLQ SIMAESFGAE VTGSRKDEPP SLKPRMEVEF LKRKPGYFPE
STFIVGKLDT ENMIQHLMWM KNFSTFKQQL QSYLMELCLH GKDTYQHYVK ILNPYLKEWN
IPVDDYEVVI GKLVPMVFD


Related products :

Catalog number Product name Quantity
EIAAB43299 HIV-1 Nef-interacting protein,Homo sapiens,Human,hVAN,KIAA0113,Naf1,NAF1,Nef-associated factor 1,Nip40-1,TNFAIP3-interacting protein 1,TNIP1,VAN,Virion-associated nuclear shuttling protein
EIAAB43298 A20-binding inhibitor of NF-kappa-B activation,ABIN,Abin,Mouse,Mus musculus,mVAN,Naf1,Naf1,Nef-associated factor 1,TNFAIP3-interacting protein 1,Tnip1,VAN,Virion-associated nuclear shuttling protein
EIAAB35745 A34.5,Anti-sense to ERCC-1 protein,Ase1,ASE-1,Cd3eap,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Mouse,Mus musculus,Paf49,RNA polymerase I-associ
PR-797 VP16GST VP16(411-490), herpes simplex virus virion transactivating protein human, recombinant, E. coli 10
EIAAB35746 A34.5,Antisense to ERCC-1 protein,ASE1,ASE-1,CAST,CAST,CD3EAP,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Homo sapiens,Human,PAF49,RNA polymerase
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
PR-797 VP16GST VP16(411_490), herpes simplex virus virion transactivating protein human, recombinant, E. coli 10 µg
PR-797 VP16GST VP16(411_490), herpes simplex virus virion transactivating protein human, recombinant, E. coli 10µg
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2
25-986 LECT1 is a glycosylated transmembrane protein that is cleaved to form a mature, secreted protein. The mature protein promotes chondrocyte growth and inhibits angiogenesis. The mature protein likely pl 0.05 mg
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
E0739b ELISA kit Bos taurus,Bovine,CDK5,CDKN5,Cell division protein kinase 5,Cyclin-dependent kinase 5,PDPK,Proline-directed protein kinase 33 kDa subunit,Serine_threonine-protein kinase PSSALRE,Tau protein 96T
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA kit G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB29586 Mouse,Mus musculus,p53-induced gene 11 protein,Pig11,Tp53i11,Transformation related protein 53 inducible protein 11,Trp53i11,Tumor protein p53-inducible protein 11


 

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