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

Histone H4

 H4_CHICK                Reviewed;         103 AA.
P62801; P02304; P02305;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 134.
RecName: Full=Histone H4;
Name=H4-I;
and
Name=H4-II;
and
Name=H4-III;
and
Name=H4-IV;
and
Name=H4-V;
and
Name=H4-VI;
and
Name=H4-VII;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=4000938; DOI=10.1093/nar/13.4.1369;
Wang S.W., Robins A.J., D'Andrea R., Wells J.R.E.;
"Inverted duplication of histone genes in chicken and disposition of
regulatory sequences.";
Nucleic Acids Res. 13:1369-1387(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6190814;
Sugarman B.J., Dodgson J.B., Engel J.D.;
"Genomic organization, DNA sequence, and expression of chicken
embryonic histone genes.";
J. Biol. Chem. 258:9005-9016(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4-III AND H4-IV).
PubMed=1748315; DOI=10.1016/0378-1119(91)90452-H;
Nakayama T., Takechi S., Ohshige T., Kondo K., Yamamoto K.;
"Nucleotide sequences of two members of the chicken H4 histone-
encoding gene family.";
Gene 108:311-312(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (H4-VI AND H4-VII).
STRAIN=White leghorn; TISSUE=Liver;
PubMed=8804862; DOI=10.1093/dnares/3.2.95;
Takami Y., Higashio M., Fukuoka T., Takechi S., Nakayama T.;
"Organization of the chicken histone genes in a major gene cluster and
generation of an almost complete set of the core histone protein
sequences.";
DNA Res. 3:95-99(1996).
[5]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
PubMed=1946434; DOI=10.1073/pnas.88.22.10148;
Arents G., Burlingame R.W., Wang B.-C., Love W.E., Moudrianakis E.N.;
"The nucleosomal core histone octamer at 3.1 A resolution: a
tripartite protein assembly and a left-handed superhelix.";
Proc. Natl. Acad. Sci. U.S.A. 88:10148-10152(1991).
[6]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=11092917; DOI=10.1107/S0907444900011847;
Harp J.M., Hanson B.L., Timm D.E., Bunick G.J.;
"Asymmetries in the nucleosome core particle at 2.5 A resolution.";
Acta Crystallogr. D 56:1513-1534(2000).
-!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers. The octamer wraps
approximately 147 bp of DNA.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13
(H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the
genome but not in heterochromatin. {ECO:0000250|UniProtKB:P62805}.
-!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs
methylation. {ECO:0000250|UniProtKB:P62805}.
-!- PTM: Monomethylation and asymmetric dimethylation at Arg-4
(H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation
at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed
by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the
PRDM1/PRMT5 complex may play a crucial role in the germ-cell
lineage (By similarity). {ECO:0000250|UniProtKB:P62805}.
-!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21
(H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by
SET8. Trimethylation is performed by KMT5B and KMT5C and induces
gene silencing (By similarity). {ECO:0000250|UniProtKB:P62805}.
-!- PTM: Phosphorylated by PAK2 at Ser-48 (H4S47ph). This
phosphorylation increases the association of H3.3-H4 with the
histone chaperone HIRA, thus promoting nucleosome assembly of
H3.3-H4 and inhibiting nucleosome assembly of H3.1-H4 (By
similarity). {ECO:0000250|UniProtKB:P62805}.
-!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
ultraviolet irradiation. This may weaken the interaction between
histones and DNA and facilitate DNA accessibility to repair
proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in
response to DNA damage. The exact role of H4K91ub1 in DNA damage
response is still unclear but it may function as a licensing
signal for additional histone H4 post-translational modifications
such as H4 Lys-21 methylation (H4K20me) (By similarity).
{ECO:0000250|UniProtKB:P62805}.
-!- PTM: Sumoylated, which is associated with transcriptional
repression. {ECO:0000250|UniProtKB:P62805}.
-!- PTM: Butyrylation of histones marks active promoters and competes
with histone acetylation. {ECO:0000250|UniProtKB:P62806}.
-!- SIMILARITY: Belongs to the histone H4 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X02218; CAA26137.1; -; Genomic_DNA.
EMBL; X02218; CAA26140.1; -; Genomic_DNA.
EMBL; J00866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M74533; AAA73091.1; -; Genomic_DNA.
EMBL; M74534; AAA73092.1; -; Genomic_DNA.
EMBL; U37575; AAC59999.1; -; Genomic_DNA.
EMBL; U37575; AAC60001.1; -; Genomic_DNA.
PIR; A02640; HSCH4.
PIR; JH0507; JH0507.
RefSeq; NP_001032932.1; NM_001037843.1.
RefSeq; NP_001032934.1; NM_001037845.1.
RefSeq; NP_001268414.1; NM_001281485.1.
RefSeq; XP_001233180.1; XM_001233179.4.
RefSeq; XP_003640418.1; XM_003640370.3.
RefSeq; XP_004937726.1; XM_004937669.2.
RefSeq; XP_425458.2; XM_425458.5.
UniGene; Gga.39882; -.
PDB; 1EQZ; X-ray; 2.50 A; D/H=1-103.
PDB; 1HIO; X-ray; 3.10 A; D=28-103.
PDB; 1HQ3; X-ray; 2.15 A; D/H=1-103.
PDB; 1TZY; X-ray; 1.90 A; D/H=1-103.
PDB; 2ARO; X-ray; 2.10 A; D/H=1-103.
PDB; 2HIO; X-ray; 3.10 A; D=1-103.
PDB; 3C9K; EM; 20.00 A; D/H=2-103.
PDBsum; 1EQZ; -.
PDBsum; 1HIO; -.
PDBsum; 1HQ3; -.
PDBsum; 1TZY; -.
PDBsum; 2ARO; -.
PDBsum; 2HIO; -.
PDBsum; 3C9K; -.
ProteinModelPortal; P62801; -.
SMR; P62801; -.
BioGrid; 679227; 7.
IntAct; P62801; 2.
STRING; 9031.ENSGALP00000037292; -.
PaxDb; P62801; -.
PRIDE; P62801; -.
Ensembl; ENSGALT00000046233; ENSGALP00000041526; ENSGALG00000025786.
Ensembl; ENSGALT00000049482; ENSGALP00000054690; ENSGALG00000032272.
Ensembl; ENSGALT00000053533; ENSGALP00000054121; ENSGALG00000032933.
Ensembl; ENSGALT00000066061; ENSGALP00000045681; ENSGALG00000032198.
Ensembl; ENSGALT00000067674; ENSGALP00000051551; ENSGALG00000035445.
Ensembl; ENSGALT00000070686; ENSGALP00000058410; ENSGALG00000037322.
Ensembl; ENSGALT00000079865; ENSGALP00000056887; ENSGALG00000041398.
Ensembl; ENSGALT00000080967; ENSGALP00000049875; ENSGALG00000042491.
GeneID; 100858049; -.
GeneID; 100858319; -.
GeneID; 417946; -.
GeneID; 417950; -.
GeneID; 427884; -.
GeneID; 770005; -.
GeneID; 770142; -.
KEGG; gga:100858049; -.
KEGG; gga:100858319; -.
KEGG; gga:417946; -.
KEGG; gga:417950; -.
KEGG; gga:427884; -.
KEGG; gga:770005; -.
KEGG; gga:770142; -.
CTD; 100858049; -.
CTD; 417946; -.
CTD; 554313; -.
CTD; 770142; -.
CTD; 8294; -.
CTD; 8360; -.
CTD; 8366; -.
eggNOG; KOG3467; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00760000119019; -.
HOVERGEN; HBG051878; -.
InParanoid; P62801; -.
KO; K11254; -.
OMA; HINGITK; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P62801; -.
EvolutionaryTrace; P62801; -.
Proteomes; UP000000539; Chromosome 1.
Bgee; ENSGALG00000025786; -.
GO; GO:0000788; C:nuclear nucleosome; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0042393; F:histone binding; IBA:GO_Central.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IEA:Ensembl.
GO; GO:0006336; P:DNA replication-independent nucleosome assembly; IEA:Ensembl.
GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IEA:Ensembl.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
GO; GO:0051290; P:protein heterotetramerization; IEA:Ensembl.
CDD; cd00076; H4; 1.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR035425; CENP-T/H4_C.
InterPro; IPR009072; Histone-fold.
InterPro; IPR001951; Histone_H4.
InterPro; IPR019809; Histone_H4_CS.
InterPro; IPR004823; TAF_TATA-bd.
Pfam; PF15511; CENP-T_C; 1.
PRINTS; PR00623; HISTONEH4.
SMART; SM00417; H4; 1.
SMART; SM00803; TAF; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00047; HISTONE_H4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Citrullination;
Complete proteome; DNA-binding; Hydroxylation; Isopeptide bond;
Methylation; Nucleosome core; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 103 Histone H4.
/FTId=PRO_0000158296.
DNA_BIND 17 21
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 4 4 Asymmetric dimethylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 4 4 Citrulline; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 4 4 Omega-N-methylarginine; by PRMT1;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 4 4 Symmetric dimethylarginine; by PRMT5 and
PRMT7; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 6 6 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 9 9 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 9 9 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 9 9 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 9 9 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 13 13 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 13 13 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 13 13 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 17 17 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 17 17 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 17 17 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 21 21 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 21 21 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 21 21 N6-methylated lysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 21 21 N6-methyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 32 32 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 32 32 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 32 32 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 32 32 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 32 32 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 45 45 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 45 45 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 45 45 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 48 48 Phosphoserine; by PAK2.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 52 52 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 60 60 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 60 60 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 78 78 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 78 78 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 78 78 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 78 78 N6-succinyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 80 80 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 80 80 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 80 80 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 80 80 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 92 92 N6-(2-hydroxyisobutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 92 92 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 92 92 N6-butyryllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 92 92 N6-propionyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
MOD_RES 92 92 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P62805}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P62805}.
HELIX 26 29 {ECO:0000244|PDB:1TZY}.
HELIX 32 41 {ECO:0000244|PDB:1TZY}.
HELIX 51 76 {ECO:0000244|PDB:1TZY}.
STRAND 80 82 {ECO:0000244|PDB:1TZY}.
HELIX 84 93 {ECO:0000244|PDB:1TZY}.
STRAND 97 100 {ECO:0000244|PDB:1TZY}.
SEQUENCE 103 AA; 11367 MW; A9E5DFD3F8B97598 CRC64;
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG


Related products :

Catalog number Product name Quantity
28-858 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
28-920 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP18 is a component of the histone 0.05 mg
28-857 Histone acetylation plays a key role in the regulation of eukaryotic gene expression. Histone acetylation and deacetylation are catalyzed by multisubunit complexes. SAP30 is a component of the histone 0.1 mg
25-522 UTX is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It demethylates trimethylated and dimethylated but not monomethylate 0.05 mg
orb61320 CI-994 CI-994 is a histone deacetylase (HDAC) inhibitor and induces histone hyperacetylation in living cells. CI-994 inhibited HDAC-1 and HDAC-2 but not the prototypical histone acetyltransferase GCN5 500 mg
29-186 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.1 mg
25-583 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.05 mg
27-131 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.05 mg
27-775 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.1 mg
25-113 CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complex 0.05 mg
bs-0931P Peptides: Histone H1b(Histone H1.4) Protein Length:12-25 amino acids. 200ug lyophilized
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 0.5mg
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 100ug
E0356h ELISA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
E0356h ELISA kit H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
U0356h CLIA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
303-35199 Anti_phospho Histone H3 (P_Ser10), monoclonal antibody Binds to Histone H3 phosphorylated at serine 10. 100 ul
30-333 DOT1L is a histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. 0.05 mg
ANTY021260 Polyclonal Antibodies: Histone H2A.X (Ab-139) ; Specificity: Histone H2A.X (Ab-139) ; Application: IHC 100ug
31-007 Histone H3, along with histone H4, plays a central role in nucleosome formation. 0.1 mg
ANTY021137 Polyclonal Antibodies: Histone H3.1 (Ab-10) ; Specificity: Histone H3.1 (Ab-10) ; Application: IHC 100ug
3623BP-50 Histone H3 Blocking Peptide target: Histone H3 50 μg
3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3621BP-50 Histone H2A Blocking Peptide target: Histone H2A 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

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