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

Vacuolar protein sorting-associated protein 72 homolog (Protein YL-1) (Transcription factor-like 1)

 VPS72_HUMAN             Reviewed;         364 AA.
Q15906; A6NLK9; A6PW55; Q53GJ2; Q5U0R4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
27-SEP-2017, entry version 156.
RecName: Full=Vacuolar protein sorting-associated protein 72 homolog;
AltName: Full=Protein YL-1;
AltName: Full=Transcription factor-like 1;
Name=VPS72; Synonyms=TCFL1, YL1;
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).
TISSUE=Fibroblast;
PubMed=7702631; DOI=10.1006/bbrc.1995.1433;
Horikawa I., Tanaka H., Yuasa Y., Suzuki M., Oshimura M.;
"Molecular cloning of a novel human cDNA on chromosome 1q21 and its
mouse homolog encoding a nuclear protein with DNA-binding ability.";
Biochem. Biophys. Res. Commun. 208:999-1007(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-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 GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-258 (ISOFORM 2).
TISSUE=Embryonic stem cell, and Kidney;
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).
[7]
IDENTIFICATION IN A NUA4-RELATED COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[8]
SUBUNIT.
PubMed=15647280; DOI=10.1074/jbc.M500001200;
Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B.,
Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W.;
"The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60
histone acetyltransferase and SRCAP complexes.";
J. Biol. Chem. 280:13665-13670(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-129, AND
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-115, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[12]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 6-69 IN COMPLEX WITH H2AFZ
AND HIST1H2BJ, FUNCTION, INTERACTION WITH H2AFZ AND HIST1H2BJ,
MUTAGENESIS OF 29-PHE--PHE-37 AND 43-ASP--TYR-46, AND SUBCELLULAR
LOCATION.
PubMed=26974126; DOI=10.1038/NSMB.3189;
Latrick C.M., Marek M., Ouararhni K., Papin C., Stoll I.,
Ignatyeva M., Obri A., Ennifar E., Dimitrov S., Romier C., Hamiche A.;
"Molecular basis and specificity of H2A.Z-H2B recognition and
deposition by the histone chaperone YL1.";
Nat. Struct. Mol. Biol. 23:309-316(2016).
[13]
VARIANT [LARGE SCALE ANALYSIS] VAL-318.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Deposition-and-exchange histone chaperone specific for
H2AFZ, specifically chaperones H2AFZ and deposits it into
nucleosomes. As component of the SRCAP complex, mediates the ATP-
dependent exchange of histone H2AFZ/H2B dimers for nucleosomal
H2A/H2B, leading to transcriptional regulation of selected genes
by chromatin remodeling. {ECO:0000269|PubMed:26974126}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5/TIP60 and the subunits
EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
MRGBP, YEATS4/GAS41 and VPS72/YL1. Component of a NuA4-related
complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP,
EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A,
VPS72 and YEATS4/GAS41. Also part of a multiprotein complex which
contains SRCAP and which binds to H2AFZ/H2AZ. Interacts (via N-
terminal domain) with heterodimer HIST1H2BJ and H2AFZ
(PubMed:26974126). {ECO:0000269|PubMed:14966270,
ECO:0000269|PubMed:15647280, ECO:0000269|PubMed:26974126}.
-!- INTERACTION:
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-399189, EBI-2549423;
Q99750:MDFI; NbExp=4; IntAct=EBI-399189, EBI-724076;
Q9Y265:RUVBL1; NbExp=6; IntAct=EBI-399189, EBI-353675;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:26974126}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15906-1; Sequence=Displayed;
Name=2;
IsoId=Q15906-2; Sequence=VSP_047566;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the VPS72/YL1 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; D43642; BAA07757.1; -; mRNA.
EMBL; BT019356; AAV38163.1; -; mRNA.
EMBL; BT019357; AAV38164.1; -; mRNA.
EMBL; AK222935; BAD96655.1; -; mRNA.
EMBL; AK222939; BAD96659.1; -; mRNA.
EMBL; AL592424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471121; EAW53462.1; -; Genomic_DNA.
EMBL; BC003151; AAH03151.1; -; mRNA.
EMBL; CX163016; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS59201.1; -. [Q15906-2]
CCDS; CCDS989.1; -. [Q15906-1]
PIR; JC4140; JC4140.
RefSeq; NP_001258016.1; NM_001271087.1. [Q15906-2]
RefSeq; NP_005988.1; NM_005997.2. [Q15906-1]
UniGene; Hs.2430; -.
PDB; 5FUG; X-ray; 2.70 A; C/F/I/L=6-69.
PDBsum; 5FUG; -.
ProteinModelPortal; Q15906; -.
SMR; Q15906; -.
BioGrid; 112804; 47.
CORUM; Q15906; -.
DIP; DIP-31767N; -.
IntAct; Q15906; 32.
MINT; MINT-1444540; -.
STRING; 9606.ENSP00000357887; -.
iPTMnet; Q15906; -.
PhosphoSitePlus; Q15906; -.
DMDM; 2499159; -.
EPD; Q15906; -.
MaxQB; Q15906; -.
PaxDb; Q15906; -.
PeptideAtlas; Q15906; -.
PRIDE; Q15906; -.
DNASU; 6944; -.
Ensembl; ENST00000354473; ENSP00000346464; ENSG00000163159. [Q15906-2]
Ensembl; ENST00000368892; ENSP00000357887; ENSG00000163159. [Q15906-1]
GeneID; 6944; -.
KEGG; hsa:6944; -.
UCSC; uc001exe.3; human. [Q15906-1]
CTD; 6944; -.
DisGeNET; 6944; -.
EuPathDB; HostDB:ENSG00000163159.11; -.
GeneCards; VPS72; -.
HGNC; HGNC:11644; VPS72.
HPA; HPA065709; -.
MIM; 600607; gene.
neXtProt; NX_Q15906; -.
OpenTargets; ENSG00000163159; -.
PharmGKB; PA36396; -.
eggNOG; KOG2897; Eukaryota.
eggNOG; ENOG41119RU; LUCA.
GeneTree; ENSGT00390000017503; -.
HOGENOM; HOG000033695; -.
HOVERGEN; HBG083244; -.
InParanoid; Q15906; -.
KO; K11664; -.
OMA; CERTFVT; -.
OrthoDB; EOG091G0BQW; -.
PhylomeDB; Q15906; -.
TreeFam; TF314532; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
ChiTaRS; VPS72; human.
GeneWiki; VPS72; -.
GenomeRNAi; 6944; -.
PRO; PR:Q15906; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163159; -.
CleanEx; HS_VPS72; -.
Genevisible; Q15906; HS.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0043486; P:histone exchange; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR008895; Vps72/YL1.
InterPro; IPR013272; Vps72/YL1_C.
PANTHER; PTHR13275; PTHR13275; 1.
Pfam; PF08265; YL1_C; 1.
SMART; SM00993; YL1_C; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 364 Vacuolar protein sorting-associated
protein 72 homolog.
/FTId=PRO_0000066283.
DNA_BIND 156 206 {ECO:0000255}.
COMPBIAS 22 77 Asp/Glu-rich (acidic).
COMPBIAS 333 354 Pro-rich.
COMPBIAS 341 350 Poly-Pro.
MOD_RES 127 127 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 236 236 G -> GSLCFSLSFVLR (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047566.
VARIANT 318 318 I -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035803.
MUTAGEN 29 37 FYQTTYGGF->AAQTTAGGA: Highly decreases
interation with H2AFZ and HIST1H2BJ.
Abolishes interaction with H2AFZ and
HIST1H2BJ and exchange of H2A for H2AFZ
in nucleosomes; when associated with A-
43--46-A. {ECO:0000269|PubMed:26974126}.
MUTAGEN 43 46 DDEY->ADAA: Almost abolishes interation
with H2AFZ and HIST1H2BJ. Abolishes
interaction with H2AFZ and HIST1H2BJ and
exchange of H2A for H2AFZ in nucleosomes;
when associated with A-29--37-A.
{ECO:0000269|PubMed:26974126}.
CONFLICT 30 30 Y -> H (in Ref. 3; BAD96655/BAD96659).
{ECO:0000305}.
CONFLICT 53 53 T -> I (in Ref. 3; BAD96655/BAD96659).
{ECO:0000305}.
TURN 11 16 {ECO:0000244|PDB:5FUG}.
HELIX 17 22 {ECO:0000244|PDB:5FUG}.
HELIX 29 32 {ECO:0000244|PDB:5FUG}.
HELIX 33 35 {ECO:0000244|PDB:5FUG}.
STRAND 54 57 {ECO:0000244|PDB:5FUG}.
SEQUENCE 364 AA; 40594 MW; 0AEB90B62B2BCA4A CRC64;
MSLAGGRAPR KTAGNRLSGL LEAEEEDEFY QTTYGGFTEE SGDDEYQGDQ SDTEDEVDSD
FDIDEGDEPS SDGEAEEPRR KRRVVTKAYK EPLKSLRPRK VNTPAGSSQK AREEKALLPL
ELQDDGSDSR KSMRQSTAEH TRQTFLRVQE RQGQSRRRKG PHCERPLTQE ELLREAKITE
ELNLRSLETY ERLEADKKKQ VHKKRKCPGP IITYHSVTVP LVGEPGPKEE NVDIEGLDPA
PSVSALTPHA GTGPVNPPAR CSRTFITFSD DATFEEWFPQ GRPPKVPVRE VCPVTHRPAL
YRDPVTDIPY ATARAFKIIR EAYKKYITAH GLPPTASALG PGPPPPEPLP GSGPRALRQK
IVIK


Related products :

Catalog number Product name Quantity
EIAAB45972 Mouse,Mus musculus,Protein YL-1,Tcfl1,Transcription factor-like 1,Vacuolar protein sorting-associated protein 72 homolog,Vps72,Yl1
18-003-42469 Vacuolar protein sorting protein 72 homolog - Transcription factor-like 1; Protein YL-1 Polyclonal 0.05 mg Aff Pur
EIAAB45971 Homo sapiens,Human,Protein YL-1,TCFL1,Transcription factor-like 1,Vacuolar protein sorting-associated protein 72 homolog,VPS72,YL1
EIAAB45973 Bos taurus,Bovine,TCFL1,Transcription factor-like 1,Vacuolar protein sorting-associated protein 72 homolog,VPS72
EIAAB45937 DC15,DC7,Homo sapiens,Human,hVPS29,MDS007,PEP11 homolog,Vacuolar protein sorting-associated protein 29,Vesicle protein sorting 29,VPS29
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
EIAAB45877 Coh1,Cohen syndrome protein 1 homolog,Kiaa0532,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 13B,Vps13b
EIAAB45876 Chac,Chorea-acanthocytosis protein homolog,Chorein,Kiaa0986,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 13A,Vps13a
EIAAB45950 Mouse,Mus musculus,mVAM2,Vacuolar protein sorting-associated protein 41 homolog,VAM2 homolog,Vps41
EIAAB45961 Are1,Rat,Rattus norvegicus,SAC2 suppressor of actin mutations 2-like protein,Sacm2l,Vacuolar protein sorting-associated protein 52 homolog,Vps52
EIAAB45962 Homo sapiens,Human,SAC2 suppressor of actin mutations 2-like protein,SACM2L,Vacuolar protein sorting-associated protein 52 homolog,VPS52
EIAAB45921 Homo sapiens,Human,hVPS11,PP3476,RING finger protein 108,RNF108,Vacuolar protein sorting-associated protein 11 homolog,VPS11
EIAAB07223 CGI-149,Charged multivesicular body protein 3,CHMP3,Chromatin-modifying protein 3,Homo sapiens,Human,hVps24,NEDF,Neuroendocrine differentiation factor,Vacuolar protein sorting-associated protein 24,VP
EIAAB45923 Bos taurus,Bovine,Vacuolar protein sorting-associated protein 16 homolog,VPS16
CSB-EL025900RA Rat Vacuolar protein sorting-associated protein 28 homolog(VPS28) ELISA kit SpeciesRat 96T
I1837 Vacuolar protein sorting-associated protein 28 homolog (VPS28), Human, ELISA Kit 96T
CSB-EL025917HU Human Vacuolar protein sorting-associated protein 53 homolog(VPS53) ELISA kit 96T
CSB-EL025916RA Rat Vacuolar protein sorting-associated protein 52 homolog(VPS52) ELISA kit SpeciesRat 96T
EIAAB45935 Rat,Rattus norvegicus,Vacuolar protein sorting-associated protein 28 homolog,Vps28
EIAAB45967 Mouse,Mus musculus,Vacuolar protein sorting-associated protein 53 homolog,Vps53
EIAAB45964 Mouse,Mus musculus,Vacuolar protein sorting-associated protein 52 homolog,Vps52
CSB-EL025894HU Human Vacuolar protein sorting-associated protein 16 homolog(VPS16) ELISA kit 96T
I1863 Vacuolar protein sorting-associated protein 41 homolog (VPS41), Human, ELISA Kit 96T
CSB-EL025895MO Mouse Vacuolar protein sorting-associated protein 18 homolog(VPS18) ELISA kit 96T
CSB-EL025894MO Mouse Vacuolar protein sorting-associated protein 16 homolog(VPS16) ELISA kit 96T


 

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