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 (hVPS35) (Maternal-embryonic 3) (Vesicle protein sorting 35)

 VPS35_HUMAN             Reviewed;         796 AA.
Q96QK1; Q561W2; Q9H016; Q9H096; Q9H4P3; Q9H8J0; Q9NRS7; Q9NVG2;
Q9NX80; Q9NZK2;
25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
25-NOV-2002, sequence version 2.
25-OCT-2017, entry version 166.
RecName: Full=Vacuolar protein sorting-associated protein 35;
Short=hVPS35;
AltName: Full=Maternal-embryonic 3;
AltName: Full=Vesicle protein sorting 35;
Name=VPS35; Synonyms=MEM3; ORFNames=TCCCTA00141;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=11062004; DOI=10.1006/bbrc.2000.3727;
Edgar A.J., Polak J.M.;
"Human homologues of yeast vacuolar protein sorting 29 and 35.";
Biochem. Biophys. Res. Commun. 277:622-630(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
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 [MRNA], AND INTERACTION WITH VPS29; VPS26A; SNX1
AND SNX2.
TISSUE=Colon;
PubMed=11102511; DOI=10.1091/mbc.11.12.4105;
Renfrew Haft C., de la Luz Sierra M., Bafford R., Lesniak M.A.,
Barr V.A., Taylor S.I.;
"Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29,
and 35: assembly into multimeric complexes.";
Mol. Biol. Cell 11:4105-4116(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pheochromocytoma;
Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
"A novel gene expressed in human pheochromocytoma.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ileal mucosa, Placenta, and Teratocarcinoma;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Placenta, and Prostate;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-796.
TISSUE=Leukemia;
Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
Margolin J.F.;
"Pediatric leukemia cDNA sequencing project.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[9]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IGF2R.
PubMed=15078903; DOI=10.1083/jcb.200312055;
Arighi C.N., Hartnell L.M., Aguilar R.C., Haft C.R., Bonifacino J.S.;
"Role of the mammalian retromer in sorting of the cation-independent
mannose 6-phosphate receptor.";
J. Cell Biol. 165:123-133(2004).
[10]
FUNCTION.
PubMed=15247922; DOI=10.1038/ncb1153;
Verges M., Luton F., Gruber C., Tiemann F., Reinders L.G., Huang L.,
Burlingame A.L., Haft C.R., Mostov K.E.;
"The mammalian retromer regulates transcytosis of the polymeric
immunoglobulin receptor.";
Nat. Cell Biol. 6:763-769(2004).
[11]
INTERACTION WITH EHD1.
PubMed=17868075; DOI=10.1111/j.1600-0854.2007.00652.x;
Gokool S., Tattersall D., Seaman M.N.;
"EHD1 interacts with retromer to stabilize SNX1 tubules and facilitate
endosome-to-Golgi retrieval.";
Traffic 8:1873-1886(2007).
[12]
INTERACTION WITH RAB7A.
PubMed=19531583; DOI=10.1242/jcs.048686;
Seaman M.N., Harbour M.E., Tattersall D., Read E., Bright N.;
"Membrane recruitment of the cargo-selective retromer subcomplex is
catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP
TBC1D5.";
J. Cell Sci. 122:2371-2382(2009).
[13]
INTERACTION WITH GOLPH3.
PubMed=19553991; DOI=10.1038/nature08109;
Scott K.L., Kabbarah O., Liang M.C., Ivanova E., Anagnostou V., Wu J.,
Dhakal S., Wu M., Chen S., Feinberg T., Huang J., Saci A.,
Widlund H.R., Fisher D.E., Xiao Y., Rimm D.L., Protopopov A.,
Wong K.K., Chin L.;
"GOLPH3 modulates mTOR signalling and rapamycin sensitivity in
cancer.";
Nature 459:1085-1090(2009).
[14]
FUNCTION.
PubMed=20923837; DOI=10.1242/jcs.071472;
Harbour M.E., Breusegem S.Y., Antrobus R., Freeman C., Reid E.,
Seaman M.N.;
"The cargo-selective retromer complex is a recruiting hub for protein
complexes that regulate endosomal tubule dynamics.";
J. Cell Sci. 123:3703-3717(2010).
[15]
FUNCTION.
PubMed=20164305; DOI=10.1242/jcs.060574;
Tabuchi M., Yanatori I., Kawai Y., Kishi F.;
"Retromer-mediated direct sorting is required for proper endosomal
recycling of the mammalian iron transporter DMT1.";
J. Cell Sci. 123:756-766(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
FUNCTION OF THE SNX3-RETROMER, AND SUBUNIT.
PubMed=21725319; DOI=10.1038/ncb2281;
Harterink M., Port F., Lorenowicz M.J., McGough I.J., Silhankova M.,
Betist M.C., van Weering J.R., van Heesbeen R.G., Middelkoop T.C.,
Basler K., Cullen P.J., Korswagen H.C.;
"A SNX3-dependent retromer pathway mediates retrograde transport of
the Wnt sorting receptor Wntless and is required for Wnt secretion.";
Nat. Cell Biol. 13:914-923(2011).
[19]
FUNCTION, AND INTERACTION WITH WASHC2C; FKBP15 AND WASHC1.
PubMed=22070227; DOI=10.1042/BJ20111761;
Harbour M.E., Breusegem S.Y., Seaman M.N.;
"Recruitment of the endosomal WASH complex is mediated by the extended
'tail' of Fam21 binding to the retromer protein Vps35.";
Biochem. J. 442:209-220(2012).
[20]
FUNCTION, AND INTERACTION WITH WASHC2C.
PubMed=22513087; DOI=10.1091/mbc.E11-12-1059;
Jia D., Gomez T.S., Billadeau D.D., Rosen M.K.;
"Multiple repeat elements within the FAM21 tail link the WASH actin
regulatory complex to the retromer.";
Mol. Biol. Cell 23:2352-2361(2012).
[21]
INTERACTION WITH VPS29 AND VPS26, AND MUTAGENESIS OF LEU-108 AND
HIS-675.
PubMed=23331060; DOI=10.1111/boc.201200038;
Helfer E., Harbour M.E., Henriot V., Lakisic G., Sousa-Blin C.,
Volceanov L., Seaman M.N., Gautreau A.;
"Endosomal recruitment of the WASH complex: active sequences and
mutations impairing interaction with the retromer.";
Biol. Cell 105:191-207(2013).
[22]
INTERACTION WITH MAGEL2.
PubMed=23452853; DOI=10.1016/j.cell.2013.01.051;
Hao Y.H., Doyle J.M., Ramanathan S., Gomez T.S., Jia D., Xu M.,
Chen Z.J., Billadeau D.D., Rosen M.K., Potts P.R.;
"Regulation of WASH-dependent actin polymerization and protein
trafficking by ubiquitination.";
Cell 152:1051-1064(2013).
[23]
FUNCTION OF THE SNX27-RETROMER, SUBUNIT, AND INTERACTION WITH SNX27
AND WASHC5.
PubMed=23563491; DOI=10.1038/ncb2721;
Steinberg F., Gallon M., Winfield M., Thomas E.C., Bell A.J.,
Heesom K.J., Tavare J.M., Cullen P.J.;
"A global analysis of SNX27-retromer assembly and cargo specificity
reveals a function in glucose and metal ion transport.";
Nat. Cell Biol. 15:461-471(2013).
[24]
FUNCTION IN RETROGRADE TRANSPORT, INTERACTION WITH LRRK2, AND
CHARACTERIZATION OF VARIANT PARK17 ASN-620.
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).
[25]
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).
[26]
INTERACTION WITH SNX3 AND SLC11A2.
PubMed=24344282; DOI=10.1073/pnas.1316482111;
Harrison M.S., Hung C.S., Liu T.T., Christiano R., Walther T.C.,
Burd C.G.;
"A mechanism for retromer endosomal coat complex assembly with
cargo.";
Proc. Natl. Acad. Sci. U.S.A. 111:267-272(2014).
[27]
FUNCTION, INTERACTION WITH WASHC2C, AND CHARACTERIZATION OF VARIANT
PARK17 ASN-620.
PubMed=24980502; DOI=10.1016/j.cub.2014.06.024;
McGough I.J., Steinberg F., Jia D., Barbuti P.A., McMillan K.J.,
Heesom K.J., Whone A.L., Caldwell M.A., Billadeau D.D., Rosen M.K.,
Cullen P.J.;
"Retromer binding to FAM21 and the WASH complex is perturbed by the
Parkinson disease-linked VPS35(D620N) mutation.";
Curr. Biol. 24:1670-1676(2014).
[28]
FUNCTION, AND CHARACTERIZATION OF VARIANT PARK17 ASN-620.
PubMed=24819384; DOI=10.1038/ncomms4828;
Zavodszky E., Seaman M.N., Moreau K., Jimenez-Sanchez M.,
Breusegem S.Y., Harbour M.E., Rubinsztein D.C.;
"Mutation in VPS35 associated with Parkinson's disease impairs WASH
complex association and inhibits autophagy.";
Nat. Commun. 5:3828-3828(2014).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[30]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 483-780 IN COMPLEX WITH
VPS29, AND ELECTRON MICROSCOPY OF THE RETROMER COMPLEX CONTAINING
VPS29; VPS35 AND VPS26.
PubMed=17891154; DOI=10.1038/nature06216;
Hierro A., Rojas A.L., Rojas R., Murthy N., Effantin G., Kajava A.V.,
Steven A.C., Bonifacino J.S., Hurley J.H.;
"Functional architecture of the retromer cargo-recognition complex.";
Nature 449:1063-1067(2007).
[31]
VARIANT PARK17 ASN-620, AND VARIANTS SER-316 AND VAL-737.
PubMed=21763482; DOI=10.1016/j.ajhg.2011.06.001;
Vilarino-Guell C., Wider C., Ross O.A., Dachsel J.C., Kachergus J.M.,
Lincoln S.J., Soto-Ortolaza A.I., Cobb S.A., Wilhoite G.J.,
Bacon J.A., Behrouz B., Melrose H.L., Hentati E., Puschmann A.,
Evans D.M., Conibear E., Wasserman W.W., Aasly J.O., Burkhard P.R.,
Djaldetti R., Ghika J., Hentati F., Krygowska-Wajs A., Lynch T.,
Melamed E., Rajput A., Rajput A.H., Solida A., Wu R.M., Uitti R.J.,
Wszolek Z.K., Vingerhoets F., Farrer M.J.;
"VPS35 mutations in Parkinson disease.";
Am. J. Hum. Genet. 89:162-167(2011).
[32]
VARIANT PARK17 ASN-620, AND VARIANTS SER-51; ILE-57; ARG-82; MET-241;
TRP-524 AND MET-774.
PubMed=21763483; DOI=10.1016/j.ajhg.2011.06.008;
Zimprich A., Benet-Pages A., Struhal W., Graf E., Eck S.H.,
Offman M.N., Haubenberger D., Spielberger S., Schulte E.C.,
Lichtner P., Rossle S.C., Klopp N., Wolf E., Seppi K., Pirker W.,
Reinthaler E., Harutyunyan A., Kralovics R., Peters A., Zimprich F.,
Brucke T., Poewe W., Auff E., Trenkwalder C., Rost B., Ransmayr G.,
Winkelmann J., Meitinger T., Strom T.M.;
"A mutation in VPS35, encoding a subunit of the retromer complex,
causes late-onset Parkinson disease.";
Am. J. Hum. Genet. 89:168-175(2011).
[33]
VARIANT PARK17 ASN-620.
PubMed=22517097; DOI=10.1212/WNL.0b013e318253d5f2;
Lesage S., Condroyer C., Klebe S., Honore A., Tison F.,
Brefel-Courbon C., Durr A., Brice A.;
"Identification of VPS35 mutations replicated in French families with
Parkinson disease.";
Neurology 78:1449-1450(2012).
-!- 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 endosome-to-TGN 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)
(PubMed:15078903, PubMed:15247922, PubMed:20164305). Required for
endosomal localization of WASHC2C (PubMed:22070227). Mediates the
association of the CSC with the WASH complex via WASHC2
(PubMed:22070227, PubMed:24980502, PubMed:24819384). Required for
the endosomal localization of TBC1D5 (PubMed:20923837).
{ECO:0000269|PubMed:15078903, ECO:0000269|PubMed:15247922,
ECO:0000269|PubMed:20164305, ECO:0000269|PubMed:20923837,
ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:23395371,
ECO:0000269|PubMed:24819384, ECO:0000269|PubMed:24980502,
ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:22070227,
ECO:0000303|PubMed:22513087, ECO:0000303|PubMed:23563491}.
-!- SUBUNIT: Component of the heterotrimeric retromer cargo-selective
complex (CSC), also decribed as vacuolar protein sorting
subcomplex (VPS), formed by VPS26 (VPS26A or VPS26B), VPS29 and
VPS35 (PubMed:11102511). The CSC has a highly elongated structure
with VPS26 and VPS29 binding independently at opposite distal ends
of VPS35 as central platform (By similarity). 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 respective CSC and SNX-BAR
subcomplexes associate with low affinity. 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, VPS26B,
VPS29, SNX1, SNX2, IGF2R, SNX3, GOLPH3, LRRK2, SLC11A2, WASHC2A,
WASHC2C, FKBP15, WASHC1, RAB7A, SNX27, WASHC5, EHD1
(PubMed:11102511, PubMed:15078903, PubMed:17868075PubMed:22070227,
PubMed:19553991, PubMed:21725319, PubMed:22070227,
PubMed:22513087, PubMed:23331060, PubMed:23563491,
PubMed:23395371, PubMed:24344282, PubMed:24980502,
PubMed:17891154, PubMed:19531583). Interacts with MAGEL2; leading
to recruitment of the TRIM27:MAGEL2 E3 ubiquitin ligase complex
retromer-containing endosomes (PubMed:23452853). {ECO:0000250,
ECO:0000269|PubMed:11102511, ECO:0000269|PubMed:15078903,
ECO:0000269|PubMed:17868075, ECO:0000269|PubMed:17891154,
ECO:0000269|PubMed:19553991, ECO:0000269|PubMed:21725319,
ECO:0000269|PubMed:22070227, ECO:0000269|PubMed:22513087,
ECO:0000269|PubMed:23331060, ECO:0000269|PubMed:23395371,
ECO:0000269|PubMed:23452853, ECO:0000269|PubMed:23563491,
ECO:0000269|PubMed:24344282, ECO:0000269|PubMed:24980502,
ECO:0000303|PubMed:21725319, ECO:0000303|PubMed:23563491}.
-!- INTERACTION:
Q13596:SNX1; NbExp=2; IntAct=EBI-1054634, EBI-2822329;
Q92609:TBC1D5; NbExp=3; IntAct=EBI-1054634, EBI-742381;
O75436:VPS26A; NbExp=17; IntAct=EBI-1054634, EBI-1043891;
Q4G0F5:VPS26B; NbExp=4; IntAct=EBI-1054634, EBI-6151831;
Q9UBQ0:VPS29; NbExp=11; IntAct=EBI-1054634, EBI-718596;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
protein. Endosome {ECO:0000269|PubMed:15078903}. Early endosome
{ECO:0000305}. Late endosome {ECO:0000305}. Note=Localizes to
tubular profiles adjacent to endosomes.
{ECO:0000269|PubMed:15078903}.
-!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, brain,
placenta, skeletal muscle, spleen, thymus, testis, ovary, small
intestine, kidney and colon.
-!- DISEASE: Parkinson disease 17 (PARK17) [MIM:614203]: An autosomal
dominant, adult-onset form of Parkinson disease. Parkinson disease
is a complex neurodegenerative disorder characterized by
bradykinesia, resting tremor, muscular rigidity and postural
instability, as well as by a clinically significant response to
treatment with levodopa. The pathology involves the loss of
dopaminergic neurons in the substantia nigra and the presence of
Lewy bodies (intraneuronal accumulations of aggregated proteins),
in surviving neurons in various areas of the brain.
{ECO:0000269|PubMed:21763482, ECO:0000269|PubMed:21763483,
ECO:0000269|PubMed:22517097, ECO:0000269|PubMed:23395371,
ECO:0000269|PubMed:24819384, ECO:0000269|PubMed:24980502}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the VPS35 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG01989.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA91137.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB14626.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF191298; AAF02778.2; -; mRNA.
EMBL; AF186382; AAG40619.1; -; mRNA.
EMBL; AF175265; AAF89953.1; -; mRNA.
EMBL; AF183418; AAG09687.1; -; mRNA.
EMBL; AK001614; BAA91790.1; -; mRNA.
EMBL; AK023650; BAB14626.1; ALT_INIT; mRNA.
EMBL; AK000395; BAA91137.1; ALT_INIT; mRNA.
EMBL; AL136888; CAB66822.1; -; mRNA.
EMBL; AL512769; CAC21686.1; -; mRNA.
EMBL; BC002414; AAH02414.1; -; mRNA.
EMBL; BC010362; AAH10362.1; -; mRNA.
EMBL; BC093036; AAH93036.1; -; mRNA.
EMBL; AY007112; AAG01989.1; ALT_INIT; mRNA.
CCDS; CCDS10721.1; -.
PIR; JC7516; JC7516.
RefSeq; NP_060676.2; NM_018206.5.
UniGene; Hs.454528; -.
UniGene; Hs.595143; -.
PDB; 2R17; X-ray; 2.80 A; C/D=483-780.
PDB; 5F0J; X-ray; 2.70 A; A=14-470.
PDB; 5F0K; X-ray; 3.07 A; A/B/C/D/E=14-470.
PDB; 5F0L; X-ray; 3.20 A; A=14-470.
PDB; 5F0M; X-ray; 3.10 A; A=14-470.
PDB; 5F0P; X-ray; 2.78 A; A=14-470.
PDBsum; 2R17; -.
PDBsum; 5F0J; -.
PDBsum; 5F0K; -.
PDBsum; 5F0L; -.
PDBsum; 5F0M; -.
PDBsum; 5F0P; -.
ProteinModelPortal; Q96QK1; -.
SMR; Q96QK1; -.
BioGrid; 120855; 77.
CORUM; Q96QK1; -.
DIP; DIP-29076N; -.
IntAct; Q96QK1; 34.
MINT; MINT-5001902; -.
STRING; 9606.ENSP00000299138; -.
ChEMBL; CHEMBL2216744; -.
iPTMnet; Q96QK1; -.
PhosphoSitePlus; Q96QK1; -.
SwissPalm; Q96QK1; -.
BioMuta; VPS35; -.
DMDM; 25453321; -.
EPD; Q96QK1; -.
MaxQB; Q96QK1; -.
PaxDb; Q96QK1; -.
PeptideAtlas; Q96QK1; -.
PRIDE; Q96QK1; -.
DNASU; 55737; -.
Ensembl; ENST00000299138; ENSP00000299138; ENSG00000069329.
GeneID; 55737; -.
KEGG; hsa:55737; -.
UCSC; uc002eef.5; human.
CTD; 55737; -.
DisGeNET; 55737; -.
EuPathDB; HostDB:ENSG00000069329.15; -.
GeneCards; VPS35; -.
GeneReviews; VPS35; -.
HGNC; HGNC:13487; VPS35.
HPA; HPA040802; -.
MalaCards; VPS35; -.
MIM; 601501; gene.
MIM; 614203; phenotype.
neXtProt; NX_Q96QK1; -.
OpenTargets; ENSG00000069329; -.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA37783; -.
eggNOG; KOG1107; Eukaryota.
eggNOG; ENOG410XNXC; LUCA.
GeneTree; ENSGT00390000007315; -.
HOVERGEN; HBG054277; -.
InParanoid; Q96QK1; -.
KO; K18468; -.
OMA; RVADSCM; -.
OrthoDB; EOG091G0OHF; -.
PhylomeDB; Q96QK1; -.
TreeFam; TF105659; -.
Reactome; R-HSA-3238698; WNT ligand biogenesis and trafficking.
ChiTaRS; VPS35; human.
EvolutionaryTrace; Q96QK1; -.
GeneWiki; VPS35; -.
GenomeRNAi; 55737; -.
PRO; PR:Q96QK1; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000069329; -.
ExpressionAtlas; Q96QK1; baseline and differential.
Genevisible; Q96QK1; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0010008; C:endosome membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IBA:GO_Central.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; IDA:HPA.
GO; GO:0099073; C:mitochondrion-derived vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0030904; C:retromer complex; IDA:ParkinsonsUK-UCL.
GO; GO:0030906; C:retromer, cargo-selective complex; IDA:ParkinsonsUK-UCL.
GO; GO:0097422; C:tubular endosome; IDA: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; IEA:Ensembl.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:ParkinsonsUK-UCL.
GO; GO:0099074; P:mitochondrion to lysosome transport; IMP:ParkinsonsUK-UCL.
GO; GO:0060548; P:negative regulation of cell death; IGI:ParkinsonsUK-UCL.
GO; GO:1903828; P:negative regulation of cellular protein localization; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IGI:ParkinsonsUK-UCL.
GO; GO:1902823; P:negative regulation of late endosome to lysosome transport; IMP:UniProtKB.
GO; GO:1905166; P:negative regulation of lysosomal protein catabolic process; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0032463; P:negative regulation of protein homooligomerization; IEA:Ensembl.
GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IGI:ParkinsonsUK-UCL.
GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IEA:Ensembl.
GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IDA:ParkinsonsUK-UCL.
GO; GO:0090326; P:positive regulation of locomotion involved in locomotory behavior; IEA:Ensembl.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:ParkinsonsUK-UCL.
GO; GO:0061357; P:positive regulation of Wnt protein secretion; IEA:Ensembl.
GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
GO; GO:0033365; P:protein localization to organelle; IEA:Ensembl.
GO; GO:0032268; P:regulation of cellular protein metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:1902950; P:regulation of dendritic spine maintenance; IMP:ParkinsonsUK-UCL.
GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0010821; P:regulation of mitochondrion organization; IGI:ParkinsonsUK-UCL.
GO; GO:1905606; P:regulation of presynapse assembly; ISS:ParkinsonsUK-UCL.
GO; GO:0031647; P:regulation of protein stability; IMP:ParkinsonsUK-UCL.
GO; GO:2000331; P:regulation of terminal button organization; IMP:ParkinsonsUK-UCL.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
GO; GO:1990126; P:retrograde transport, endosome to plasma membrane; IMP:UniProtKB.
GO; GO:0045056; P:transcytosis; IDA:UniProtKB.
GO; GO:0050882; P:voluntary musculoskeletal movement; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
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; 3.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Endosome; Membrane;
Neurodegeneration; Parkinson disease; Parkinsonism; Phosphoprotein;
Polymorphism; Protein transport; Reference proteome; Transport.
CHAIN 1 796 Vacuolar protein sorting-associated
protein 35.
/FTId=PRO_0000065896.
REGION 25 44 Interaction with SNX3.
{ECO:0000269|PubMed:24344282}.
REGION 205 215 Interaction with SNX3.
{ECO:0000269|PubMed:24344282}.
REGION 438 796 Interaction with SLC11A2.
{ECO:0000269|PubMed:24344282}.
REGION 500 693 Interaction with IGF2R cytoplasmic
domain. {ECO:0000269|PubMed:15078903}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EQH3}.
MOD_RES 791 791 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9EQH3}.
VARIANT 51 51 G -> S (in dbSNP:rs193077277).
{ECO:0000269|PubMed:21763483}.
/FTId=VAR_066653.
VARIANT 57 57 M -> I (in dbSNP:rs183554824).
{ECO:0000269|PubMed:21763483}.
/FTId=VAR_066654.
VARIANT 82 82 T -> R (in dbSNP:rs188245364).
{ECO:0000269|PubMed:21763483}.
/FTId=VAR_066655.
VARIANT 241 241 I -> M (found in a patient with Parkinson
disease; dbSNP:rs192783364).
{ECO:0000269|PubMed:21763483}.
/FTId=VAR_066656.
VARIANT 316 316 P -> S (found in a patient with Parkinson
disease; dbSNP:rs770029606).
{ECO:0000269|PubMed:21763482}.
/FTId=VAR_066657.
VARIANT 524 524 R -> W (found in a patient with Parkinson
disease; dbSNP:rs184277092).
{ECO:0000269|PubMed:21763483}.
/FTId=VAR_066658.
VARIANT 602 602 V -> D (in dbSNP:rs34687100).
/FTId=VAR_054046.
VARIANT 620 620 D -> N (in PARK17; decreases interaction
with WASHC2C, FKBP15 and the WASH
complex; impairs recruitment of the WASH
complex to endosomes; shows reduced
retrograde transport of selective cargo
between lysosomes and the Golgi
apparatus; shows a progressive reduction
in neurite length and branching;
dbSNP:rs188286943).
{ECO:0000269|PubMed:21763482,
ECO:0000269|PubMed:21763483,
ECO:0000269|PubMed:22517097,
ECO:0000269|PubMed:23395371,
ECO:0000269|PubMed:24819384,
ECO:0000269|PubMed:24980502}.
/FTId=VAR_066659.
VARIANT 737 737 A -> V (in dbSNP:rs749516404).
{ECO:0000269|PubMed:21763482}.
/FTId=VAR_066660.
VARIANT 774 774 L -> M (in dbSNP:rs192419029).
{ECO:0000269|PubMed:21763483}.
/FTId=VAR_066661.
MUTAGEN 108 108 L->P: Disrupts interaction with VPS26; no
effect on interaction with VPS29.
{ECO:0000269|PubMed:23331060}.
MUTAGEN 675 675 H->R: Disrupts interaction with VPS29.
Does not effect interaction with VPS26.
{ECO:0000269|PubMed:23331060}.
CONFLICT 42 42 A -> S (in Ref. 6; CAB66822).
{ECO:0000305}.
CONFLICT 160 160 I -> T (in Ref. 5; BAB14626).
{ECO:0000305}.
CONFLICT 168 168 T -> P (in Ref. 3; AAF89953).
{ECO:0000305}.
CONFLICT 453 453 S -> F (in Ref. 7; AAH10362).
{ECO:0000305}.
CONFLICT 526 526 R -> G (in Ref. 5; BAA91790).
{ECO:0000305}.
CONFLICT 694 694 K -> E (in Ref. 5; BAA91790).
{ECO:0000305}.
CONFLICT 796 796 L -> H (in Ref. 5; BAA91137).
{ECO:0000305}.
HELIX 14 35 {ECO:0000244|PDB:5F0J}.
HELIX 39 50 {ECO:0000244|PDB:5F0J}.
HELIX 51 54 {ECO:0000244|PDB:5F0J}.
STRAND 56 58 {ECO:0000244|PDB:5F0J}.
HELIX 60 86 {ECO:0000244|PDB:5F0J}.
HELIX 94 97 {ECO:0000244|PDB:5F0J}.
HELIX 98 100 {ECO:0000244|PDB:5F0J}.
HELIX 104 121 {ECO:0000244|PDB:5F0J}.
HELIX 123 125 {ECO:0000244|PDB:5F0J}.
HELIX 126 136 {ECO:0000244|PDB:5F0J}.
HELIX 137 139 {ECO:0000244|PDB:5F0J}.
HELIX 143 156 {ECO:0000244|PDB:5F0J}.
TURN 157 160 {ECO:0000244|PDB:5F0J}.
HELIX 176 196 {ECO:0000244|PDB:5F0J}.
HELIX 197 199 {ECO:0000244|PDB:5F0J}.
HELIX 206 229 {ECO:0000244|PDB:5F0J}.
HELIX 235 240 {ECO:0000244|PDB:5F0J}.
HELIX 242 252 {ECO:0000244|PDB:5F0J}.
HELIX 256 269 {ECO:0000244|PDB:5F0J}.
HELIX 272 277 {ECO:0000244|PDB:5F0J}.
HELIX 279 286 {ECO:0000244|PDB:5F0J}.
HELIX 295 310 {ECO:0000244|PDB:5F0J}.
STRAND 313 315 {ECO:0000244|PDB:5F0J}.
STRAND 320 322 {ECO:0000244|PDB:5F0J}.
HELIX 324 338 {ECO:0000244|PDB:5F0J}.
HELIX 344 361 {ECO:0000244|PDB:5F0J}.
HELIX 366 382 {ECO:0000244|PDB:5F0J}.
STRAND 390 392 {ECO:0000244|PDB:5F0P}.
HELIX 393 408 {ECO:0000244|PDB:5F0J}.
HELIX 413 416 {ECO:0000244|PDB:5F0J}.
TURN 419 422 {ECO:0000244|PDB:5F0P}.
HELIX 423 427 {ECO:0000244|PDB:5F0J}.
HELIX 430 446 {ECO:0000244|PDB:5F0J}.
HELIX 454 468 {ECO:0000244|PDB:5F0J}.
TURN 484 487 {ECO:0000244|PDB:2R17}.
HELIX 488 498 {ECO:0000244|PDB:2R17}.
HELIX 503 518 {ECO:0000244|PDB:2R17}.
STRAND 522 524 {ECO:0000244|PDB:2R17}.
HELIX 525 544 {ECO:0000244|PDB:2R17}.
TURN 545 549 {ECO:0000244|PDB:2R17}.
HELIX 553 573 {ECO:0000244|PDB:2R17}.
HELIX 578 594 {ECO:0000244|PDB:2R17}.
HELIX 599 617 {ECO:0000244|PDB:2R17}.
HELIX 621 635 {ECO:0000244|PDB:2R17}.
HELIX 643 658 {ECO:0000244|PDB:2R17}.
HELIX 663 672 {ECO:0000244|PDB:2R17}.
HELIX 674 678 {ECO:0000244|PDB:2R17}.
TURN 683 687 {ECO:0000244|PDB:2R17}.
HELIX 693 709 {ECO:0000244|PDB:2R17}.
HELIX 713 731 {ECO:0000244|PDB:2R17}.
TURN 732 734 {ECO:0000244|PDB:2R17}.
HELIX 740 751 {ECO:0000244|PDB:2R17}.
TURN 752 755 {ECO:0000244|PDB:2R17}.
HELIX 761 776 {ECO:0000244|PDB:2R17}.
SEQUENCE 796 AA; 91707 MW; 28D2DD1C6B920A0A 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 DIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL QVSLINLAMK
CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR LLKIPVDTYN NILTVLKLKH
FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE IVSQDQVDSI MNLVSTLIQD QPDQPVEDPD
PEDFADEQSL VGRFIHLLRS EDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA
FRYKENSKVD DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE
TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR TQCALAASKL
LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL KKALKIANQC MDPSLQVQLF
IEILNRYIYF YEKENDAVTI QVLNQLIQKI REDLPNLESS EETEQINKHF HNTLEHLRLR
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