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

AP-4 complex subunit beta-1 (AP-4 adaptor complex subunit beta) (Adaptor-related protein complex 4 subunit beta-1) (Beta subunit of AP-4) (Beta4-adaptin)

 AP4B1_HUMAN             Reviewed;         739 AA.
Q9Y6B7; B7Z4X3; Q59EJ4; Q96CL6;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 2.
28-MAR-2018, entry version 151.
RecName: Full=AP-4 complex subunit beta-1 {ECO:0000305};
AltName: Full=AP-4 adaptor complex subunit beta;
AltName: Full=Adaptor-related protein complex 4 subunit beta-1;
AltName: Full=Beta subunit of AP-4;
AltName: Full=Beta4-adaptin;
Name=AP4B1 {ECO:0000312|HGNC:HGNC:572};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, TOPOLOGY, AND VARIANT SER-480.
TISSUE=Skeletal muscle;
PubMed=10066790; DOI=10.1074/jbc.274.11.7278;
Dell'Angelica E.C., Mullins C., Bonifacino J.S.;
"AP-4, a novel protein complex related to clathrin adaptors.";
J. Biol. Chem. 274:7278-7285(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-480.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10436028; DOI=10.1091/mbc.10.8.2787;
Hirst J., Bright N.A., Rous B., Robinson M.S.;
"Characterization of a fourth adaptor-related protein complex.";
Mol. Biol. Cell 10:2787-2802(1999).
[7]
INVOLVEMENT IN SPG47.
PubMed=21620353; DOI=10.1016/j.ajhg.2011.04.019;
Abou Jamra R., Philippe O., Raas-Rothschild A., Eck S.H., Graf E.,
Buchert R., Borck G., Ekici A., Brockschmidt F.F., Nothen M.M.,
Munnich A., Strom T.M., Reis A., Colleaux L.;
"Adaptor protein complex 4 deficiency causes severe autosomal-
recessive intellectual disability, progressive spastic paraplegia, shy
character, and short stature.";
Am. J. Hum. Genet. 88:788-795(2011).
[8]
INTERACTION WITH TEPSIN, AND SUBCELLULAR LOCATION.
PubMed=22472443; DOI=10.1083/jcb.201111049;
Borner G.H., Antrobus R., Hirst J., Bhumbra G.S., Kozik P.,
Jackson L.P., Sahlender D.A., Robinson M.S.;
"Multivariate proteomic profiling identifies novel accessory proteins
of coated vesicles.";
J. Cell Biol. 197:141-160(2012).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
INTERACTION WITH TEPSIN, REGION, AND MUTAGENESIS OF TRP-635 AND
TYR-682.
PubMed=26542808; DOI=10.1074/jbc.M115.683409;
Mattera R., Guardia C.M., Sidhu S.S., Bonifacino J.S.;
"Bivalent motif-ear interactions mediate the association of the
accessory protein tepsin with the AP-4 adaptor complex.";
J. Biol. Chem. 290:30736-30749(2015).
[11]
INTERACTION WITH TEPSIN, AND MUTAGENESIS OF ILE-669; ALA-670 AND
TYR-682.
PubMed=26756312; DOI=10.1111/tra.12375;
Frazier M.N., Davies A.K., Voehler M., Kendall A.K., Borner G.H.,
Chazin W.J., Robinson M.S., Jackson L.P.;
"Molecular basis for the interaction between AP4 beta4 and its
accessory protein, tepsin.";
Traffic 17:400-415(2016).
[12]
STRUCTURE BY NMR OF 610-739.
Northeast structural genomics consortium (NESG);
"Solution NMR structure of beta-adaptin appendage domain of human
adapter protein complex 4 subunit beta, Northeast structural genomics
consortium (NESG) target HR8998C.";
Submitted (JAN-2014) to the PDB data bank.
-!- FUNCTION: Component of the adaptor protein complex 4 (AP-4).
Adaptor protein complexes are vesicle coat components involved
both in vesicle formation and cargo selection. They control the
vesicular transport of proteins in different trafficking pathways
(PubMed:10066790, PubMed:10436028). AP-4 forms a non clathrin-
associated coat on vesicles departing the trans-Golgi network
(TGN) and may be involved in the targeting of proteins from the
trans-Golgi network (TGN) to the endosomal-lysosomal system. It is
also involved in protein sorting to the basolateral membrane in
epithelial cells and the proper asymmetric localization of
somatodendritic proteins in neurons. AP-4 is involved in the
recognition and binding of tyrosine-based sorting signals found in
the cytoplasmic part of cargos, but may also recognize other types
of sorting signal (Probable). {ECO:0000269|PubMed:10066790,
ECO:0000269|PubMed:10436028, ECO:0000305|PubMed:10066790,
ECO:0000305|PubMed:10436028}.
-!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer
composed of two large adaptins (epsilon-type subunit AP4E1 and
beta-type subunit AP4B1), a medium adaptin (mu-type subunit AP4M1)
and a small adaptin (sigma-type AP4S1) (PubMed:10066790,
PubMed:10436028). Interacts with TEPSIN; this interaction requires
the presence of a functional AP-4 complex (PubMed:22472443,
PubMed:26542808, PubMed:26756312). Interacts with GRIA2; probably
indirect it mediates the somatodendritic localization of GRIA2 in
neurons (By similarity). {ECO:0000250|UniProtKB:Q9WV76,
ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028,
ECO:0000269|PubMed:22472443, ECO:0000269|PubMed:26542808,
ECO:0000269|PubMed:26756312}.
-!- INTERACTION:
Q9H609:ZNF576; NbExp=7; IntAct=EBI-1047606, EBI-3921014;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
membrane {ECO:0000269|PubMed:10066790,
ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:22472443};
Peripheral membrane protein {ECO:0000269|PubMed:10066790}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y6B7-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y6B7-2; Sequence=VSP_055787, VSP_055788, VSP_055789;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10436028}.
-!- DISEASE: Spastic paraplegia 47, autosomal recessive (SPG47)
[MIM:614066]: A form of spastic paraplegia, a neurodegenerative
disorder characterized by a slow, gradual, progressive weakness
and spasticity of the lower limbs. SPG47 is characterized by
neonatal hypotonia that progresses to hypertonia and spasticity,
and severe mental retardation with poor or absent speech
development. {ECO:0000269|PubMed:21620353}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93054.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF092094; AAD20448.1; -; mRNA.
EMBL; AK298037; BAH12709.1; -; mRNA.
EMBL; AB209817; BAD93054.1; ALT_INIT; mRNA.
EMBL; AL137856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC014146; AAH14146.1; -; mRNA.
CCDS; CCDS865.1; -. [Q9Y6B7-1]
RefSeq; NP_001240781.1; NM_001253852.2. [Q9Y6B7-1]
RefSeq; NP_001240782.1; NM_001253853.2.
RefSeq; NP_001295241.1; NM_001308312.1.
RefSeq; NP_006585.2; NM_006594.4. [Q9Y6B7-1]
UniGene; Hs.515048; -.
UniGene; Hs.736555; -.
PDB; 2MJ7; NMR; -; A=610-739.
PDBsum; 2MJ7; -.
ProteinModelPortal; Q9Y6B7; -.
SMR; Q9Y6B7; -.
BioGrid; 115943; 10.
CORUM; Q9Y6B7; -.
DIP; DIP-24209N; -.
IntAct; Q9Y6B7; 9.
STRING; 9606.ENSP00000256658; -.
iPTMnet; Q9Y6B7; -.
PhosphoSitePlus; Q9Y6B7; -.
BioMuta; AP4B1; -.
DMDM; 126302520; -.
EPD; Q9Y6B7; -.
PaxDb; Q9Y6B7; -.
PeptideAtlas; Q9Y6B7; -.
PRIDE; Q9Y6B7; -.
DNASU; 10717; -.
Ensembl; ENST00000256658; ENSP00000256658; ENSG00000134262. [Q9Y6B7-1]
Ensembl; ENST00000369569; ENSP00000358582; ENSG00000134262. [Q9Y6B7-1]
GeneID; 10717; -.
KEGG; hsa:10717; -.
UCSC; uc001eeb.4; human. [Q9Y6B7-1]
CTD; 10717; -.
DisGeNET; 10717; -.
EuPathDB; HostDB:ENSG00000134262.12; -.
GeneCards; AP4B1; -.
HGNC; HGNC:572; AP4B1.
HPA; HPA028162; -.
HPA; HPA028652; -.
MalaCards; AP4B1; -.
MIM; 607245; gene.
MIM; 614066; phenotype.
neXtProt; NX_Q9Y6B7; -.
OpenTargets; ENSG00000134262; -.
Orphanet; 280763; Severe intellectual disability and progressive spastic paraplegia.
PharmGKB; PA24864; -.
eggNOG; KOG1061; Eukaryota.
eggNOG; COG5096; LUCA.
GeneTree; ENSGT00530000063138; -.
HOGENOM; HOG000294128; -.
HOVERGEN; HBG050521; -.
InParanoid; Q9Y6B7; -.
KO; K12401; -.
OMA; MSNNDMV; -.
OrthoDB; EOG091G058E; -.
PhylomeDB; Q9Y6B7; -.
TreeFam; TF354235; -.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
GeneWiki; AP4B1; -.
GenomeRNAi; 10717; -.
PRO; PR:Q9Y6B7; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134262; -.
CleanEx; HS_AP4B1; -.
ExpressionAtlas; Q9Y6B7; baseline and differential.
Genevisible; Q9Y6B7; HS.
GO; GO:0030124; C:AP-4 adaptor complex; IDA:UniProtKB.
GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0031904; C:endosome lumen; TAS:Reactome.
GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0030276; F:clathrin binding; IEA:InterPro.
GO; GO:0008104; P:protein localization; IC:UniProtKB.
GO; GO:0006605; P:protein targeting; IC:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.30.310.10; -; 1.
InterPro; IPR026739; AP_beta.
InterPro; IPR016342; AP_complex_bsu_1_2_4.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR015151; B-adaptin_app_sub_C.
InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
InterPro; IPR012295; TBP_dom_sf.
PANTHER; PTHR11134; PTHR11134; 1.
Pfam; PF01602; Adaptin_N; 1.
Pfam; PF09066; B2-adapt-app_C; 1.
PIRSF; PIRSF002291; AP_complex_beta; 1.
SMART; SM01020; B2-adapt-app_C; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Golgi apparatus; Hereditary spastic paraplegia; Membrane;
Neurodegeneration; Polymorphism; Protein transport;
Reference proteome; Transport.
CHAIN 1 739 AP-4 complex subunit beta-1.
/FTId=PRO_0000193750.
REGION 534 600 Hinge. {ECO:0000305|PubMed:26542808}.
REGION 601 739 Ear; mediates interaction with TEPSIN.
{ECO:0000269|PubMed:26542808}.
VAR_SEQ 113 205 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055787.
VAR_SEQ 373 395 GIARTYTDQCVQILTELLGLRQE -> RCLLLFLLENLDQP
ARKLWLEEP (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055788.
VAR_SEQ 396 739 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055789.
VARIANT 480 480 L -> S (in dbSNP:rs1217401).
{ECO:0000269|PubMed:10066790,
ECO:0000269|Ref.3}.
/FTId=VAR_030804.
MUTAGEN 635 635 W->A: Decreased interaction with TEPSIN.
{ECO:0000269|PubMed:26542808}.
MUTAGEN 669 669 I->A: Decreased interaction with TEPSIN;
when associated with S-670.
{ECO:0000269|PubMed:26756312}.
MUTAGEN 670 670 A->S: Decreased interaction with TEPSIN;
when associated with A-669.
{ECO:0000269|PubMed:26756312}.
MUTAGEN 682 682 Y->A,V: Decreased interaction with
TEPSIN. {ECO:0000269|PubMed:26542808,
ECO:0000269|PubMed:26756312}.
CONFLICT 140 140 A -> V (in Ref. 1; AAD20448).
{ECO:0000305}.
HELIX 628 637 {ECO:0000244|PDB:2MJ7}.
STRAND 641 647 {ECO:0000244|PDB:2MJ7}.
HELIX 654 663 {ECO:0000244|PDB:2MJ7}.
STRAND 667 671 {ECO:0000244|PDB:2MJ7}.
STRAND 677 687 {ECO:0000244|PDB:2MJ7}.
STRAND 692 699 {ECO:0000244|PDB:2MJ7}.
STRAND 701 703 {ECO:0000244|PDB:2MJ7}.
STRAND 705 714 {ECO:0000244|PDB:2MJ7}.
HELIX 717 735 {ECO:0000244|PDB:2MJ7}.
SEQUENCE 739 AA; 83260 MW; B6FC92215BDA5EDC CRC64;
MPYLGSEDVV KELKKALCNP HIQADRLRYR NVIQRVIRYM TQGLDMSGVF MEMVKASATV
DIVQKKLVYL YMCTYAPLKP DLALLAINTL CKDCSDPNPM VRGLALRSMC SLRMPGVQEY
IQQPILNGLR DKASYVRRVA VLGCAKMHNL HGDSEVDGAL VNELYSLLRD QDPIVVVNCL
RSLEEILKQE GGVVINKPIA HHLLNRMSKL DQWGQAEVLN FLLRYQPRSE EELFDILNLL
DSFLKSSSPG VVMGATKLFL ILAKMFPHVQ TDVLVRVKGP LLAACSSESR ELCFVALCHV
RQILHSLPGH FSSHYKKFFC SYSEPHYIKL QKVEVLCELV NDENVQQVLE ELRGYCTDVS
ADFAQAAIFA IGGIARTYTD QCVQILTELL GLRQEHITTV VVQTFRDLVW LCPQCTEAVC
QALPGCEENI QDSEGKQALI WLLGVHGERI PNAPYVLEDF VENVKSETFP AVKMELLTAL
LRLFLSRPAE CQDMLGRLLY YCIEEEKDMA VRDRGLFYYR LLLVGIDEVK RILCSPKSDP
TLGLLEDPAE RPVNSWASDF NTLVPVYGKA HWATISKCQG AERCDPELPK TSSFAASGPL
IPEENKERVQ ELPDSGALML VPNRQLTADY FEKTWLSLKV AHQQVLPWRG EFHPDTLQMA
LQVVNIQTIA MSRAGSRPWK AYLSAQDDTG CLFLTELLLE PGNSEMQISV KQNEARTETL
NSFISVLETV IGTIEEIKS


Related products :

Catalog number Product name Quantity


 

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