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Dysbindin (Biogenesis of lysosome-related organelles complex 1 subunit 8) (BLOC-1 subunit 8) (Dysbindin-1) (Dystrobrevin-binding protein 1) (Hermansky-Pudlak syndrome 7 protein) (HPS7 protein)

 DTBP1_HUMAN             Reviewed;         351 AA.
Q96EV8; A8K3V3; Q5THY3; Q5THY4; Q96NV2; Q9H0U2; Q9H3J5;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=Dysbindin;
AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 8;
Short=BLOC-1 subunit 8;
AltName: Full=Dysbindin-1;
AltName: Full=Dystrobrevin-binding protein 1;
AltName: Full=Hermansky-Pudlak syndrome 7 protein;
Short=HPS7 protein;
Name=DTNBP1; Synonyms=BLOC1S8; ORFNames=My031;
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), AND INVOLVEMENT IN HPS7.
TISSUE=Placenta;
PubMed=12923531; DOI=10.1038/ng1229;
Li W., Zhang Q., Oiso N., Novak E.K., Gautam R., O'Brien E.P.,
Tinsley C.L., Blake D.J., Spritz R.A., Copeland N.G., Jenkins N.A.,
Amato D., Roe B.A., Starcevic M., Dell'Angelica E.C., Elliott R.W.,
Mishra V., Kingsmore S.F., Paylor R.E., Swank R.T.;
"Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant
dysbindin, a member of the biogenesis of lysosome-related organelles
complex 1 (BLOC-1).";
Nat. Genet. 35:84-89(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Jiang Y., Straub R.E., Sullivan P.F., Chen X., O'Neill F.A., Walsh D.,
Kendler K.S., Riley B.P.;
"Localization and identification of a human DTNBP1 gene from a
putative schizophrenia susceptibility locus on 6p22.3 by in silico
cloning.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Neuroblastoma;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 109-351 (ISOFORM 1).
TISSUE=Fetal brain;
Mao Y.M., Xie Y., Ying K.;
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[8]
ASSOCIATION WITH SCHIZOPHRENIA, AND FUNCTION.
PubMed=15345706; DOI=10.1093/hmg/ddh280;
Numakawa T., Yagasaki Y., Ishimoto T., Okada T., Suzuki T., Iwata N.,
Ozaki N., Taguchi T., Tatsumi M., Kamijima K., Straub R.E.,
Weinberger D.R., Kunugi H., Hashimoto R.;
"Evidence of novel neuronal functions of dysbindin, a susceptibility
gene for schizophrenia.";
Hum. Mol. Genet. 13:2699-2708(2004).
[9]
ASSOCIATION WITH SCHIZOPHRENIA, TISSUE SPECIFICITY (ISOFORMS 1 AND 2),
AND SUBCELLULAR LOCATION.
PubMed=15124027; DOI=10.1172/JCI200420425;
Talbot K., Eidem W.L., Tinsley C.L., Benson M.A., Thompson E.W.,
Smith R.J., Hahn C.G., Siegel S.J., Trojanowski J.Q., Gur R.E.,
Blake D.J., Arnold S.E.;
"Dysbindin-1 is reduced in intrinsic, glutamatergic terminals of the
hippocampal formation in schizophrenia.";
J. Clin. Invest. 113:1353-1363(2004).
[10]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16980328; DOI=10.1093/hmg/ddl246;
Talbot K., Cho D.S., Ong W.Y., Benson M.A., Han L.Y., Kazi H.A.,
Kamins J., Hahn C.G., Blake D.J., Arnold S.E.;
"Dysbindin-1 is a synaptic and microtubular protein that binds brain
snapin.";
Hum. Mol. Genet. 15:3041-3054(2006).
[11]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=16837549; DOI=10.1091/mbc.E06-05-0379;
Di Pietro S.M., Falcon-Perez J.M., Tenza D., Setty S.R., Marks M.S.,
Raposo G., Dell'Angelica E.C.;
"BLOC-1 interacts with BLOC-2 and the AP-3 complex to facilitate
protein trafficking on endosomes.";
Mol. Biol. Cell 17:4027-4038(2006).
[12]
IDENTIFICATION IN THE BLOC-1 COMPLEX, AND FUNCTION.
PubMed=17182842; DOI=10.1091/mbc.E06-12-1066;
Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V.,
Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
Dell'Angelica E.C., Raposo G., Marks M.S.;
"BLOC-1 is required for cargo-specific sorting from vacuolar early
endosomes toward lysosome-related organelles.";
Mol. Biol. Cell 18:768-780(2007).
[13]
FUNCTION.
PubMed=17989303; DOI=10.1523/JNEUROSCI.1689-07.2007;
Iizuka Y., Sei Y., Weinberger D.R., Straub R.E.;
"Evidence that the BLOC-1 protein dysbindin modulates dopamine D2
receptor internalization and signaling but not D1 internalization.";
J. Neurosci. 27:12390-12395(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
ASSOCIATION WITH SCHIZOPHRENIA.
PubMed=19617633; DOI=10.1093/hmg/ddp329;
Tang J., LeGros R.P., Louneva N., Yeh L., Cohen J.W., Hahn C.G.,
Blake D.J., Arnold S.E., Talbot K.;
"Dysbindin-1 in dorsolateral prefrontal cortex of schizophrenia cases
is reduced in an isoform-specific manner unrelated to dysbindin-1 mRNA
expression.";
Hum. Mol. Genet. 18:3851-3863(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
REVIEW.
Talbot K., Ong W.-Y., Blake D.J., Tang J., Louneva N., Carlson G.C.,
Arnold S.E.;
"Dysbindin-1 and its protein family with special attention to the
potential role of dysbindin-1 in neuronal functions and the
pathophysiology of schizophrenia.";
(In) Javitt D.C., Kantrowitz J. (eds.);
Handbook of neurochemistry and molecular neurobiology (3rd ed.),
pp.27:107-241, Springer Science, New York (2009).
[18]
FUNCTION.
PubMed=19094965; DOI=10.1016/j.bbrc.2008.12.017;
Kubota K., Kumamoto N., Matsuzaki S., Hashimoto R., Hattori T.,
Okuda H., Takamura H., Takeda M., Katayama T., Tohyama M.;
"Dysbindin engages in c-Jun N-terminal kinase activity and
cytoskeletal organization.";
Biochem. Biophys. Res. Commun. 379:191-195(2009).
[19]
INTERACTION WITH TRIM32, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=19349376; DOI=10.1093/hmg/ddp167;
Locke M., Tinsley C.L., Benson M.A., Blake D.J.;
"TRIM32 is an E3 ubiquitin ligase for dysbindin.";
Hum. Mol. Genet. 18:2344-2358(2009).
[20]
INTERACTION WITH AP3M1, AND MUTAGENESIS OF TYR-215.
PubMed=19428785; DOI=10.1016/j.neuint.2009.01.014;
Taneichi-Kuroda S., Taya S., Hikita T., Fujino Y., Kaibuchi K.;
"Direct interaction of dysbindin with the AP-3 complex via its mu
subunit.";
Neurochem. Int. 54:431-438(2009).
[21]
SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3),
INTERACTION WITH AP3B2; XRCC5 AND XRCC6 IN THE DNA-DEPENDENT PROTEIN
KINASE COMPLEX DNA-PK, AND PHOSPHORYLATION.
PubMed=19142223; DOI=10.1371/journal.pone.0004199;
Oyama S., Yamakawa H., Sasagawa N., Hosoi Y., Futai E., Ishiura S.;
"Dysbindin-1, a schizophrenia-related protein, functionally interacts
with the DNA-dependent protein kinase complex in an isoform-dependent
manner.";
PLoS ONE 4:E4199-E4199(2009).
[22]
ASSOCIATION WITH SCHIZOPHRENIA, AND FUNCTION.
PubMed=20180862; DOI=10.1111/j.1601-183X.2010.00574.x;
Fallgatter A.J., Ehlis A.C., Herrmann M.J., Hohoff C., Reif A.,
Freitag C.M., Deckert J.;
"DTNBP1 (dysbindin) gene variants modulate prefrontal brain function
in schizophrenic patients--support for the glutamate hypothesis of
schizophrenias.";
Genes Brain Behav. 9:489-497(2010).
[23]
SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH XPO1, AND MUTAGENESIS
OF 243-LEU--LEU-256.
PubMed=20921223; DOI=10.1074/jbc.M110.107912;
Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.;
"Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related
protein, regulates synapsin I expression.";
J. Biol. Chem. 285:38630-38640(2010).
[24]
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).
[25]
ASSOCIATION WITH SCHIZOPHRENIA, TISSUE SPECIFICITY (ISOFORMS 1; 2 AND
3), AND SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
PubMed=21390302; DOI=10.1371/journal.pone.0016886;
Talbot K., Louneva N., Cohen J.W., Kazi H., Blake D.J., Arnold S.E.;
"Synaptic dysbindin-1 reductions in schizophrenia occur in an isoform-
specific manner indicating their subsynaptic location.";
PLoS ONE 6:E16886-E16886(2011).
[26]
IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
COMPLEX.
PubMed=22203680; DOI=10.1074/jbc.M111.325746;
Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R.,
Steven A.C., Bonifacino J.S., Hurley J.H.;
"Assembly and architecture of biogenesis of lysosome-related
organelles complex-1 (BLOC-1).";
J. Biol. Chem. 287:5882-5890(2012).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-321, 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).
-!- FUNCTION: Component of the BLOC-1 complex, a complex that is
required for normal biogenesis of lysosome-related organelles
(LRO), such as platelet dense granules and melanosomes. In concert
with the AP-3 complex, the BLOC-1 complex is required to target
membrane protein cargos into vesicles assembled at cell bodies for
delivery into neurites and nerve terminals. The BLOC-1 complex, in
association with SNARE proteins, is also proposed to be involved
in neurite extension. Associates with the BLOC-2 complex to
facilitate the transport of TYRP1 independent of AP-3 function.
Plays a role in synaptic vesicle trafficking and in
neurotransmitter release. Plays a role in the regulation of cell
surface exposure of DRD2. May play a role in actin cytoskeleton
reorganization and neurite outgrowth. May modulate MAPK8
phosphorylation. Appears to promote neuronal transmission and
viability through regulating the expression of SNAP25 and SYN1,
modulating PI3-kinase-Akt signaling and influencing glutamatergic
release. Regulates the expression of SYN1 through binding to its
promoter. Modulates prefrontal cortical activity via the
dopamine/D2 pathway. {ECO:0000269|PubMed:15345706,
ECO:0000269|PubMed:16837549, ECO:0000269|PubMed:17182842,
ECO:0000269|PubMed:17989303, ECO:0000269|PubMed:19094965,
ECO:0000269|PubMed:20180862, ECO:0000269|PubMed:20921223}.
-!- SUBUNIT: Interacts (via its coiled coil domain) with KXD1.
Interacts with CMYA5, PI4K2 and RNF151 (By similarity). Component
of the biogenesis of lysosome-related organelles complex 1 (BLOC-
1) composed of at least BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Interacts
directly in the complex with BLOC1S5, BLOC1S6 and SNAPIN/BLOC1S8.
The BLOC-1 complex associates with the AP-3 protein complex and
membrane protein cargos. This BLOC-1 complex also associates with
the BLOC-2 complex in endosomes. Binds to DTNA and DTNB but may
not be a physiological binding partner (PubMed:16980328).
Interacts (isoform 1 and isoform 2 only) with the DNA-dependent
protein kinase complex DNA-PK; the interaction phosphorylates
DTNBP1 in vitro. Interacts directly in this complex with XRCC5 and
XRCC6. Interacts with AP3M1, AP3B2 and TRIM32. Interacts with
XPO1; the interaction exports DTNBP1 out of the nucleus.
{ECO:0000250, ECO:0000269|PubMed:16837549,
ECO:0000269|PubMed:16980328, ECO:0000269|PubMed:17182842,
ECO:0000269|PubMed:19142223, ECO:0000269|PubMed:19349376,
ECO:0000269|PubMed:19428785, ECO:0000269|PubMed:20921223,
ECO:0000269|PubMed:22203680}.
-!- INTERACTION:
P78537:BLOC1S1; NbExp=3; IntAct=EBI-465804, EBI-348630;
Q6QNY1:BLOC1S2; NbExp=6; IntAct=EBI-465804, EBI-465872;
Q6QNY0:BLOC1S3; NbExp=3; IntAct=EBI-465804, EBI-465930;
Q8TDH9:BLOC1S5; NbExp=3; IntAct=EBI-465804, EBI-465861;
Q9UL45:BLOC1S6; NbExp=6; IntAct=EBI-465804, EBI-465781;
Q8WUW1:BRK1; NbExp=3; IntAct=EBI-465804, EBI-2837444;
Q8IYE0-2:CCDC146; NbExp=3; IntAct=EBI-465804, EBI-10247802;
Q494R4:CCDC153; NbExp=3; IntAct=EBI-465804, EBI-10241443;
Q8TD31-3:CCHCR1; NbExp=3; IntAct=EBI-465804, EBI-10175300;
O60941:DTNB; NbExp=3; IntAct=EBI-465804, EBI-740402;
A1L3X0:ELOVL7; NbExp=3; IntAct=EBI-465804, EBI-10285373;
Q96CS2:HAUS1; NbExp=3; IntAct=EBI-465804, EBI-2514791;
Q8IY31:IFT20; NbExp=3; IntAct=EBI-465804, EBI-744203;
Q7Z3B3:KANSL1; NbExp=3; IntAct=EBI-465804, EBI-740244;
Q9BVG8:KIFC3; NbExp=3; IntAct=EBI-465804, EBI-2125614;
Q7Z6G3:NECAB2; NbExp=4; IntAct=EBI-465804, EBI-950070;
Q7Z4N8:P4HA3; NbExp=3; IntAct=EBI-465804, EBI-10181968;
Q9NUL5:RYDEN; NbExp=3; IntAct=EBI-465804, EBI-10313866;
O00560:SDCBP; NbExp=3; IntAct=EBI-465804, EBI-727004;
O95295:SNAPIN; NbExp=4; IntAct=EBI-465804, EBI-296723;
A1L4H1:SSC5D; NbExp=3; IntAct=EBI-465804, EBI-10172867;
P14373:TRIM27; NbExp=3; IntAct=EBI-465804, EBI-719493;
Q8N3L3:TXLNB; NbExp=4; IntAct=EBI-465804, EBI-6116822;
Q9Y3C0:WASHC3; NbExp=3; IntAct=EBI-465804, EBI-712969;
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm
{ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Endosome membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Melanosome membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density
{ECO:0000269|PubMed:21390302}. Endoplasmic reticulum
{ECO:0000250}. Nucleus {ECO:0000269|PubMed:21390302}. Note=Mainly
cytoplasmic but shuttles between the cytoplasm and nucleus.
Exported out of the nucleus via its NES in a XPO1-dependent
manner. Nuclear localization is required for regulation of the
expression of genes such as SYN1. Detected in neuron cell bodies,
axons and dendrites. Mainly located to the postsynaptic density.
Detected at tubulovesicular elements in the vicinity of the Golgi
apparatus and of melanosomes. Occasionally detected at the
membrane of pigmented melanosomes in cultured melanoma cells. The
BLOC-1 complex associates with the BLOC-2 complex in early
endosome-associated tubules.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm
{ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:21390302};
Peripheral membrane protein {ECO:0000269|PubMed:21390302};
Cytoplasmic side {ECO:0000269|PubMed:21390302}. Endosome membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Melanosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:21390302}. Endoplasmic reticulum
{ECO:0000250}. Nucleus {ECO:0000269|PubMed:21390302}.
Note=Shuttles between the cytoplasm and nucleus. Exported out of
the nucleus via its NES in a XPO1-dependent manner. Nuclear
localization is required for regulation of the expression of genes
such as SYN1. Mainly expressed in the dendritic spine.
Predominantly a synaptic vesicle isoform but also highly expressed
in the nucleus. The BLOC-1 complex associates with the BLOC-2
complex in early endosome-associated tubules. Associated with the
AP-3 complex at presynaptic terminals.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm
{ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:21390302};
Peripheral membrane protein {ECO:0000269|PubMed:21390302};
Cytoplasmic side {ECO:0000269|PubMed:21390302}. Endosome membrane
{ECO:0000269|PubMed:21390302}; Peripheral membrane protein
{ECO:0000269|PubMed:21390302}; Cytoplasmic side
{ECO:0000269|PubMed:21390302}. Melanosome membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
{ECO:0000250}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:21390302}. Endoplasmic reticulum
{ECO:0000250}. Note=Exclusivley cytoplasmic. Predominantly found
in the postsynaptic density (PSD). Little association with
synaptic vesicles. The BLOC-1 complex associates with the BLOC-2
complex in early endosome-associated tubules. Associated with the
AP-3 complex at presynaptic terminals.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=3;
Name=1; Synonyms=Dysbindin 1-A;
IsoId=Q96EV8-1; Sequence=Displayed;
Note=Major isoform.;
Name=2;
IsoId=Q96EV8-2; Sequence=VSP_009023;
Note=May be due to intron retention.;
Name=3; Synonyms=Dysbindin 1-B;
IsoId=Q96EV8-3; Sequence=VSP_046062;
-!- TISSUE SPECIFICITY: Detected in brain, in neurons and in neuropil.
Isoform 1 is expressed in the cerebral cortex, and hippocampal
frontal (HF). Specific expression in the posterior half of the
superior temporal gyrus (pSTG). Higher expression of isoform 2 and
3 in the HF than in the pSTG while isoform 1 shows no difference
in expression in these areas. In the HF, detected in dentate gyrus
(DG) and in pyramidal cells of hippocampus CA2 and CA3 (at protein
level). Expressed in all principal neuronal populations of the HF,
namely pyramidal neurons in the subiculum and CA1-3, granule cells
in the dense cell layer of the DG (DGg), and polymorph cells in
the hilus of the DG (DGh). Maximal levels in CA2, CA3, and DGh.
Isoform 2 not expressed in the cerebral cortex.
{ECO:0000269|PubMed:16980328}.
-!- PTM: Ubiquitinated by TRIM32. Ubiquitination leads to DTNBP1
degradation. {ECO:0000269|PubMed:19349376}.
-!- PTM: Isoforms 1 and 2 highly phosphorylated by PRKDC in vitro.
Isoform 3 only weakly phosphorylated by PRKDC in vitro.
{ECO:0000269|PubMed:19142223}.
-!- DISEASE: Hermansky-Pudlak syndrome 7 (HPS7) [MIM:614076]: A form
of Hermansky-Pudlak syndrome, a genetically heterogeneous
autosomal recessive disorder characterized by oculocutaneous
albinism, bleeding due to platelet storage pool deficiency, and
lysosomal storage defects. This syndrome results from defects of
diverse cytoplasmic organelles including melanosomes, platelet
dense granules and lysosomes. Ceroid storage in the lungs is
associated with pulmonary fibrosis, a common cause of premature
death in individuals with HPS. {ECO:0000269|PubMed:12923531}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Note=Defects in DTNBP1 are associated with susceptibility
to schizophrenia, a mental disorder characterized by a breakdown
of thought processes and by poor emotional responsiveness. Genetic
mutations lead to alterations in the glutamatergic transmission in
the brain and modified Akt signaling (PubMed:15345706). Protein
levels and expression are reduced in nerve terminals of the
hippocampus and there is an increased release of glutamate in
schizophrenic patients (PubMed:15124027). Levels of isoform 1 are
reduced in the pSTG, but not in HF, by about 48% in 92% of
schizophrenic patients. In the HF, there is an average of 33%
reduction in synaptic expression of isoform 2 in 67% of cases, and
of isoform 3, an average reduction of 35% in 80% of cases. In the
dorsolateral prefrontal cortex (DLPFC), significant reductions in
levels of isoform 3 are observed about 71% of schizophrenic
patients showed an average reduction of this isoform of about 60%
(PubMed:19617633). {ECO:0000269|PubMed:15124027,
ECO:0000269|PubMed:15345706, ECO:0000269|PubMed:19617633}.
-!- SIMILARITY: Belongs to the dysbindin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG43145.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY265460; AAP91870.1; -; mRNA.
EMBL; AF394226; AAL46636.1; -; mRNA.
EMBL; AL136637; CAB66572.1; -; mRNA.
EMBL; AK054593; BAB70770.1; -; mRNA.
EMBL; AK290718; BAF83407.1; -; mRNA.
EMBL; AL022343; CAI21976.1; -; Genomic_DNA.
EMBL; AL021978; CAI21976.1; JOINED; Genomic_DNA.
EMBL; AL022343; CAI21977.1; -; Genomic_DNA.
EMBL; AL021978; CAI21977.1; JOINED; Genomic_DNA.
EMBL; AL021978; CAI42339.1; -; Genomic_DNA.
EMBL; AL022343; CAI42339.1; JOINED; Genomic_DNA.
EMBL; AL021978; CAI42340.1; -; Genomic_DNA.
EMBL; AL022343; CAI42340.1; JOINED; Genomic_DNA.
EMBL; BC011912; AAH11912.1; -; mRNA.
EMBL; AF061734; AAG43145.1; ALT_INIT; mRNA.
CCDS; CCDS4534.1; -. [Q96EV8-1]
CCDS; CCDS4535.1; -. [Q96EV8-2]
RefSeq; NP_001258596.1; NM_001271667.1. [Q96EV8-3]
RefSeq; NP_001258597.1; NM_001271668.1.
RefSeq; NP_001258598.1; NM_001271669.1.
RefSeq; NP_115498.2; NM_032122.4. [Q96EV8-1]
RefSeq; NP_898861.1; NM_183040.2. [Q96EV8-2]
UniGene; Hs.571148; -.
ProteinModelPortal; Q96EV8; -.
SMR; Q96EV8; -.
BioGrid; 123857; 134.
CORUM; Q96EV8; -.
IntAct; Q96EV8; 54.
MINT; MINT-1438666; -.
STRING; 9606.ENSP00000341680; -.
iPTMnet; Q96EV8; -.
PhosphoSitePlus; Q96EV8; -.
BioMuta; DTNBP1; -.
DMDM; 38604971; -.
EPD; Q96EV8; -.
MaxQB; Q96EV8; -.
PaxDb; Q96EV8; -.
PeptideAtlas; Q96EV8; -.
PRIDE; Q96EV8; -.
DNASU; 84062; -.
Ensembl; ENST00000338950; ENSP00000344718; ENSG00000047579. [Q96EV8-2]
Ensembl; ENST00000344537; ENSP00000341680; ENSG00000047579. [Q96EV8-1]
GeneID; 84062; -.
KEGG; hsa:84062; -.
UCSC; uc003nbm.4; human. [Q96EV8-1]
CTD; 84062; -.
DisGeNET; 84062; -.
EuPathDB; HostDB:ENSG00000047579.19; -.
GeneCards; DTNBP1; -.
GeneReviews; DTNBP1; -.
HGNC; HGNC:17328; DTNBP1.
HPA; HPA028053; -.
HPA; HPA029615; -.
HPA; HPA029616; -.
MalaCards; DTNBP1; -.
MIM; 607145; gene.
MIM; 614076; phenotype.
neXtProt; NX_Q96EV8; -.
OpenTargets; ENSG00000047579; -.
Orphanet; 231531; Hermansky-Pudlak syndrome type 7.
PharmGKB; PA27512; -.
eggNOG; ENOG410IF9S; Eukaryota.
eggNOG; ENOG4111YM1; LUCA.
GeneTree; ENSGT00390000010667; -.
HOGENOM; HOG000272621; -.
HOVERGEN; HBG051416; -.
InParanoid; Q96EV8; -.
KO; K20189; -.
OMA; NYNAGAD; -.
OrthoDB; EOG091G0ZXL; -.
PhylomeDB; Q96EV8; -.
TreeFam; TF332997; -.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
GeneWiki; Dysbindin; -.
GenomeRNAi; 84062; -.
PRO; PR:Q96EV8; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000047579; -.
CleanEx; HS_DTNBP1; -.
ExpressionAtlas; Q96EV8; baseline and differential.
Genevisible; Q96EV8; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0030426; C:growth cone; ISS:UniProtKB.
GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0030496; C:midbody; IDA:HPA.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
GO; GO:0016528; C:sarcoplasm; IEA:Ensembl.
GO; GO:0030672; C:synaptic vesicle membrane; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
GO; GO:0007596; P:blood coagulation; IEA:Ensembl.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0060155; P:platelet dense granule organization; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; ISS:UniProtKB.
GO; GO:0060159; P:regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
GO; GO:0014059; P:regulation of dopamine secretion; ISS:UniProtKB.
GO; GO:0043506; P:regulation of JUN kinase activity; IEA:Ensembl.
InterPro; IPR007531; Dysbindin.
PANTHER; PTHR16294; PTHR16294; 1.
Pfam; PF04440; Dysbindin; 1.
1: Evidence at protein level;
Albinism; Alternative initiation; Alternative splicing; Cell junction;
Cell membrane; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Endoplasmic reticulum; Endosome;
Hermansky-Pudlak syndrome; Membrane; Nucleus; Phosphoprotein;
Polymorphism; Postsynaptic cell membrane; Reference proteome;
Schizophrenia; Sensory transduction; Synapse; Ubl conjugation.
CHAIN 1 351 Dysbindin.
/FTId=PRO_0000191001.
REGION 173 331 Dysbindin.
COILED 88 181 {ECO:0000255}.
MOTIF 243 256 Nuclear export signal.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 349 349 Phosphoserine.
{ECO:0000250|UniProtKB:Q91WZ8}.
VAR_SEQ 1 81 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_046062.
VAR_SEQ 272 351 PESSTCQNEITLQVPNPSELRAKPPSSSSTCTDSATRDISE
GGESPVVQSDEEEVQVDTALATSHTDREATPDGGEDSDS
-> RVDKLALAEPGQYRCHSPPKVRRENHLPVTYA (in
isoform 2). {ECO:0000303|PubMed:11230166,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_009023.
VARIANT 214 214 G -> D (in dbSNP:rs16876589).
/FTId=VAR_053069.
VARIANT 272 272 P -> S (in dbSNP:rs17470454).
/FTId=VAR_029644.
MUTAGEN 215 215 Y->A: Reduced interaction with AP3M1.
{ECO:0000269|PubMed:19428785}.
MUTAGEN 243 256 LMDISDQEALDVFL->AMDASDQEAADVFA: Abolishes
cytoplasmic location. Increased
expression of SYN1.
{ECO:0000269|PubMed:20921223}.
CONFLICT 242 242 D -> V (in Ref. 3; CAB66572).
{ECO:0000305}.
SEQUENCE 351 AA; 39493 MW; 0504C86E12B66C08 CRC64;
MLETLRERLL SVQQDFTSGL KTLSDKSREA KVKSKPRTVP FLPKYSAGLE LLSRYEDTWA
ALHRRAKDCA SAGELVDSEV VMLSAHWEKK KTSLVELQEQ LQQLPALIAD LESMTANLTH
LEASFEEVEN NLLHLEDLCG QCELERCKHM QSQQLENYKK NKRKELETFK AELDAEHAQK
VLEMEHTQQM KLKERQKFFE EAFQQDMEQY LSTGYLQIAE RREPIGSMSS MEVNVDMLEQ
MDLMDISDQE ALDVFLNSGG EENTVLSPAL GPESSTCQNE ITLQVPNPSE LRAKPPSSSS
TCTDSATRDI SEGGESPVVQ SDEEEVQVDT ALATSHTDRE ATPDGGEDSD S


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