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 35 (Maternal-embryonic 3) (Vesicle protein sorting 35)

 VPS35_MOUSE             Reviewed;         796 AA.
Q9EQH3; Q61123;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 137.
RecName: Full=Vacuolar protein sorting-associated protein 35;
AltName: Full=Maternal-embryonic 3;
AltName: Full=Vesicle protein sorting 35;
Name=Vps35; Synonyms=Mem3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo, and Embryonic carcinoma;
PubMed=8678978; DOI=10.1007/s003359900174;
Hwang S.-Y., Benjamin L.E., Oh B., Rothstein J.L., Ackerman S.L.,
Beddington R.S.P., Solter D., Knowles B.B.;
"Genetic mapping and embryonic expression of a novel, maternally
transcribed gene Mem3.";
Mamm. Genome 7:586-590(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11112353; DOI=10.1006/geno.2000.6380;
Zhang P., Yu L., Gao J., Fu Q., Dai F., Zhao Y., Zheng L., Zhao S.;
"Cloning and characterization of human VPS35 and mouse Vps35 and
mapping of VPS35 to human chromosome 16q13-q21.";
Genomics 70:253-257(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
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).
[4]
PROTEIN SEQUENCE OF 91-107; 218-226; 297-305; 313-323; 372-382;
404-417 AND 574-582, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
INTERACTION WITH VPS26B.
PubMed=16190980; DOI=10.1111/j.1600-0854.2005.00328.x;
Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C.,
Gleeson P.A., Wicking C., Teasdale R.D.;
"A novel mammalian retromer component, Vps26B.";
Traffic 6:991-1001(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[8]
SUBUNIT.
PubMed=21040701; DOI=10.1016/j.bbrc.2010.10.121;
Kim E., Lee Y., Lee H.J., Kim J.S., Song B.S., Huh J.W., Lee S.R.,
Kim S.U., Kim S.H., Hong Y., Shim I., Chang K.T.;
"Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin
trafficking.";
Biochem. Biophys. Res. Commun. 403:167-171(2010).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
SUBUNIT.
PubMed=20875039; DOI=10.1111/j.1600-0854.2010.01124.x;
Norwood S.J., Shaw D.J., Cowieson N.P., Owen D.J., Teasdale R.D.,
Collins B.M.;
"Assembly and solution structure of the core retromer protein
complex.";
Traffic 12:56-71(2011).
[11]
SUBUNIT.
PubMed=21920005; DOI=10.1111/j.1600-0854.2011.01284.x;
Bugarcic A., Zhe Y., Kerr M.C., Griffin J., Collins B.M.,
Teasdale R.D.;
"Vps26A and Vps26B subunits define distinct retromer complexes.";
Traffic 12:1759-1773(2011).
[12]
INTERACTION WITH LRRK2.
PubMed=23395371; DOI=10.1016/j.neuron.2012.11.033;
MacLeod D.A., Rhinn H., Kuwahara T., Zolin A., Di Paolo G.,
McCabe B.D., MacCabe B.D., Marder K.S., Honig L.S., Clark L.N.,
Small S.A., Abeliovich A.;
"RAB7L1 interacts with LRRK2 to modify intraneuronal protein sorting
and Parkinson's disease risk.";
Neuron 77:425-439(2013).
-!- FUNCTION: Acts as component of the retromer cargo-selective
complex (CSC). The CSC is believed to be the core functional
component of retromer or respective retromer complex variants
acting to prevent missorting of selected transmembrane cargo
proteins into the lysosomal degradation pathway. The recruitment
of the CSC to the endosomal membrane involves RAB7A and SNX3. The
CSC seems to associate with the cytoplasmic domain of cargo
proteins predominantly via VPS35; however, these interactions seem
to be of low affinity and retromer SNX proteins may also
contribute to cargo selectivity thus questioning the classical
function of the CSC. The SNX-BAR retromer mediates retrograde
transport of cargo proteins from endosomes to the trans-Golgi
network (TGN) and is involved in endosome-to-plasma membrane
transport for cargo protein recycling. The SNX3-retromer mediates
the retrograde transport of WLS distinct from the SNX-BAR retromer
pathway. The SNX27-retromer is believed to be involved in
endosome-to-plasma membrane trafficking and recycling of a broad
spectrum of cargo proteins. The CSC seems to act as recruitment
hub for other proteins, such as the WASH complex and TBC1D5
(Probable). Required for retrograde transport of lysosomal enzyme
receptor IGF2R and SLC11A2. Required to regulate transcytosis of
the polymeric immunoglobulin receptor (pIgR-pIgA). Required for
endosomal localization of WASHC2 and mediates the association of
the CSC with the WASH complex (By similarity).
{ECO:0000250|UniProtKB:Q96QK1}.
-!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
complex (CSC), also described as vacuolar protein sorting
subcomplex (VPS) formed by VPS26 (VPS26A or VPS26B), VPS29 and
VPS35. The CSC has a highly elongated structure with VPS26 and
VPS29 binding independently at opposite distal ends of VPS35 as
central platform (PubMed:21040701, PubMed:20875039,
PubMed:21920005). The CSC is believed to associate with variable
sorting nexins to form functionally distinct retromer complex
variants. The originally described retromer complex (also called
SNX-BAR retromer) is a pentamer containing the CSC and a
heterodimeric membrane-deforming subcomplex formed between SNX1 or
SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the
affinity between the respective CSC and SNX-BAR subcomplexes is
low. The CSC associates with SNX3 to form a SNX3-retromer complex.
The CSC associates with SNX27, the WASH complex and the SNX-BAR
subcomplex to form the SNX27-retromer complex (Probable).
Interacts with VPS26A, VPS29, VPS26B and LRRK2 (PubMed:16190980,
PubMed:21040701, PubMed:20875039, PubMed:21920005,
PubMed:23395371). Interacts with SNX1, SNX2, IGF2R, SNX3, GOLPH3,
SLC11A2, WASHC2, FKBP15, WASHC1, EHD1. Interacts with MAGEL2;
leading to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase
complex retromer-containing endosomes (By similarity).
{ECO:0000250|UniProtKB:Q96QK1, ECO:0000269|PubMed:16190980,
ECO:0000269|PubMed:20875039, ECO:0000269|PubMed:21040701,
ECO:0000269|PubMed:21920005, ECO:0000269|PubMed:23395371}.
-!- INTERACTION:
Q5T1M5:FKBP15 (xeno); NbExp=3; IntAct=EBI-775825, EBI-5235934;
O88307:Sorl1; NbExp=2; IntAct=EBI-775825, EBI-7540114;
Q6PHU5:Sort1; NbExp=3; IntAct=EBI-775825, EBI-6985663;
P40336-1:Vps26a; NbExp=2; IntAct=EBI-775825, EBI-15553779;
Q9QZ88:Vps29; NbExp=5; IntAct=EBI-775825, EBI-8334188;
Q9QZ88-1:Vps29; NbExp=3; IntAct=EBI-775825, EBI-15553808;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane
{ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Endosome
{ECO:0000250|UniProtKB:Q96QK1}. Early endosome {ECO:0000305}. Late
endosome {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fat tissue,
testis, brain, kidney, thymus, liver and pancreas, and at lower
levels in heart, intestine and skeletal muscle. Detected in
oocytes, pre-implantation embryos and at E6.5-E12.5.
-!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB18153.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U47024; AAB18153.1; ALT_FRAME; mRNA.
EMBL; AF226323; AAG40621.1; -; mRNA.
EMBL; BC005469; AAH05469.1; -; mRNA.
EMBL; BC006637; AAH06637.1; -; mRNA.
CCDS; CCDS40421.1; -.
RefSeq; NP_075373.1; NM_022997.4.
UniGene; Mm.296520; -.
UniGene; Mm.391632; -.
ProteinModelPortal; Q9EQH3; -.
SMR; Q9EQH3; -.
BioGrid; 211137; 7.
CORUM; Q9EQH3; -.
DIP; DIP-32210N; -.
IntAct; Q9EQH3; 36.
MINT; MINT-1870050; -.
STRING; 10090.ENSMUSP00000034131; -.
iPTMnet; Q9EQH3; -.
PhosphoSitePlus; Q9EQH3; -.
SwissPalm; Q9EQH3; -.
EPD; Q9EQH3; -.
MaxQB; Q9EQH3; -.
PaxDb; Q9EQH3; -.
PRIDE; Q9EQH3; -.
Ensembl; ENSMUST00000034131; ENSMUSP00000034131; ENSMUSG00000031696.
GeneID; 65114; -.
KEGG; mmu:65114; -.
UCSC; uc009mpo.1; mouse.
CTD; 55737; -.
MGI; MGI:1890467; Vps35.
eggNOG; KOG1107; Eukaryota.
eggNOG; ENOG410XNXC; LUCA.
GeneTree; ENSGT00390000007315; -.
HOGENOM; HOG000196946; -.
HOVERGEN; HBG054277; -.
InParanoid; Q9EQH3; -.
KO; K18468; -.
OMA; RVADSCM; -.
OrthoDB; EOG091G0OHF; -.
PhylomeDB; Q9EQH3; -.
TreeFam; TF105659; -.
Reactome; R-MMU-3238698; WNT ligand biogenesis and trafficking.
ChiTaRS; Vps35; mouse.
PRO; PR:Q9EQH3; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031696; -.
CleanEx; MM_VPS35; -.
ExpressionAtlas; Q9EQH3; baseline and differential.
Genevisible; Q9EQH3; MM.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; ISO:MGI.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0010008; C:endosome membrane; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISA:MGI.
GO; GO:0005770; C:late endosome; IBA:GO_Central.
GO; GO:0005765; C:lysosomal membrane; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0099073; C:mitochondrion-derived vesicle; ISO:MGI.
GO; GO:0043005; C:neuron projection; IMP:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:ParkinsonsUK-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0030904; C:retromer complex; IDA:UniProtKB.
GO; GO:0030906; C:retromer, cargo-selective complex; ISO:MGI.
GO; GO:0097422; C:tubular endosome; ISS:UniProtKB.
GO; GO:0031748; F:D1 dopamine receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0008565; F:protein transporter activity; IBA:GO_Central.
GO; GO:0007040; P:lysosome organization; IMP:ParkinsonsUK-UCL.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; ISO:MGI.
GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:MGI.
GO; GO:1903828; P:negative regulation of cellular protein localization; IMP:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:1902823; P:negative regulation of late endosome to lysosome transport; ISO:MGI.
GO; GO:1905166; P:negative regulation of lysosomal protein catabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IMP:ParkinsonsUK-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IMP:ParkinsonsUK-UCL.
GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; IMP:ParkinsonsUK-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:1903364; P:positive regulation of cellular protein catabolic process; ISO:MGI.
GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IMP:ParkinsonsUK-UCL.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IMP:ParkinsonsUK-UCL.
GO; GO:0090141; P:positive regulation of mitochondrial fission; ISO:MGI.
GO; GO:0061357; P:positive regulation of Wnt protein secretion; IMP:ParkinsonsUK-UCL.
GO; GO:0031648; P:protein destabilization; IMP:ParkinsonsUK-UCL.
GO; GO:0033365; P:protein localization to organelle; IMP:ParkinsonsUK-UCL.
GO; GO:0032268; P:regulation of cellular protein metabolic process; ISO:MGI.
GO; GO:1902950; P:regulation of dendritic spine maintenance; ISO:MGI.
GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:2000331; P:regulation of terminal button organization; ISO:MGI.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; ISS:UniProtKB.
GO; GO:0045056; P:transcytosis; ISS:UniProtKB.
GO; GO:0006624; P:vacuolar protein processing; ISA:MGI.
GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:ParkinsonsUK-UCL.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR005378; Vps35.
PANTHER; PTHR11099; PTHR11099; 1.
Pfam; PF03635; Vps35; 1.
PIRSF; PIRSF009375; Retromer_Vps35; 1.
SUPFAM; SSF48371; SSF48371; 2.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Direct protein sequencing; Endosome;
Membrane; Phosphoprotein; Protein transport; Reference proteome;
Transport.
CHAIN 1 796 Vacuolar protein sorting-associated
protein 35.
/FTId=PRO_0000065897.
REGION 25 44 Interaction with SNX3.
{ECO:0000250|UniProtKB:Q96QK1}.
REGION 205 215 Interaction with SNX3.
{ECO:0000250|UniProtKB:Q96QK1}.
REGION 438 796 Interaction with SLC11A2.
{ECO:0000250|UniProtKB:Q96QK1}.
REGION 500 693 Interaction with IGF2R cytoplasmic
domain. {ECO:0000250|UniProtKB:Q96QK1}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:Q96QK1}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 791 791 Phosphotyrosine.
{ECO:0000244|PubMed:17947660,
ECO:0000244|PubMed:19131326}.
SEQUENCE 796 AA; 91713 MW; 2ABD338111D641CC CRC64;
MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP
KSYYELYMAI SDELHYLEVY LTDEFAKGRK VADLYELVQY AGNIIPRLYL LITVGVVYVK
SFPQSRKDIL KDLVEMCRGV QHPLRGLFLR NYLLQCTRNI LPDEGEPTDE ETTGDISDSM
DFVLLNFAEM NKLWVRMQHQ GHSRDREKRE RERQELRILV GTNLVRLSQL EGVNVERYKQ
IVLTGILEQV VNCRDALAQE YLMECIIQVF PDEFHLQTLN PFLRACAELH QNVNVKNIII
ALIDRLALFA HREDGPGIPA EIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL QVSLINLAMK
CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR LLKIPVDTYN NILTVLKLKH
FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE IVSQDQVDSI MNLVSTLIQD QPDQPVEDPD
PEDFADEQSL VGRFIHLLRS DDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA
FRYKENSQMD DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE
TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR TQCALAASKL
LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL KKALKIANQC MDPSLQVQLF
IEILNRYIYF YEKENDAVTI QVLNQLIQKI REDLPNLESS EETEQINKHF HNTLEHLRSR
RESPESEGPI YEGLIL


Related products :

Catalog number Product name Quantity
EIAAB45941 Homo sapiens,Human,hVPS35,Maternal-embryonic 3,MEM3,TCCCTA00141,Vacuolar protein sorting-associated protein 35,Vesicle protein sorting 35,VPS35
EIAAB45942 Maternal-embryonic 3,Mem3,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 35,Vesicle protein sorting 35,Vps35
EIAAB45937 DC15,DC7,Homo sapiens,Human,hVPS29,MDS007,PEP11 homolog,Vacuolar protein sorting-associated protein 29,Vesicle protein sorting 29,VPS29
EIAAB45885 Homo sapiens,Human,hVPS26,Vacuolar protein sorting-associated protein 26A,Vesicle protein sorting 26A,VPS26,VPS26A
EIAAB45887 Homo sapiens,Human,Vacuolar protein sorting-associated protein 26B,Vesicle protein sorting 26B,VPS26B
EIAAB45882 Rat,Rattus norvegicus,Vacuolar protein sorting-associated protein 26A,Vesicle protein sorting 26A,Vps26,Vps26a
EIAAB45943 Bos taurus,Bovine,Vacuolar protein sorting-associated protein 35,Vesicle protein sorting 35,VPS35
EIAAB45939 Mouse,Mus musculus,Vacuolar protein sorting-associated protein 29,Vesicle protein sorting 29,Vps29
EIAAB45886 Mouse,Mus musculus,Vacuolar protein sorting-associated protein 26B,Vesicle protein sorting 26B,Vps26b
EIAAB45940 Rat,Rattus norvegicus,Vacuolar protein sorting-associated protein 29,Vesicle protein sorting 29,Vps29
EIAAB45883 Bos taurus,Bovine,Vacuolar protein sorting-associated protein 26A,Vesicle protein sorting 26A,VPS26A
EIAAB45938 Bos taurus,Bovine,Vacuolar protein sorting-associated protein 29,Vesicle protein sorting 29,VPS29
EIAAB45884 H beta 58,H<beta>58 protein,Mouse,Mus musculus,mVPS26,Vacuolar protein sorting-associated protein 26A,Vesicle protein sorting 26A,Vps26,Vps26a
EIAAB45936 Chicken,Gallus gallus,RCJMB04_25e21,Vacuolar protein sorting-associated protein 29,Vesicle protein sorting 29,VPS29
EIAAB07222 Charged multivesicular body protein 3,Chmp3,Chromatin-modifying protein 3,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 24,Vps24
EIAAB07221 Bos taurus,Bovine,Charged multivesicular body protein 3,CHMP3,Chromatin-modifying protein 3,Vacuolar protein sorting-associated protein 24,VPS24
EIAAB07220 Charged multivesicular body protein 3,Chmp3,Chromatin-modifying protein 3,Rat,Rattus norvegicus,rVps24p,Vacuolar protein sorting-associated protein 24,Vps24
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
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
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
EIAAB45877 Coh1,Cohen syndrome protein 1 homolog,Kiaa0532,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 13B,Vps13b
EIAAB45875 CHAC,Chorea-acanthocytosis protein,Chorein,Homo sapiens,Human,KIAA0986,Vacuolar protein sorting-associated protein 13A,VPS13A
EIAAB45876 Chac,Chorea-acanthocytosis protein homolog,Chorein,Kiaa0986,Mouse,Mus musculus,Vacuolar protein sorting-associated protein 13A,Vps13a


 

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