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Disabled homolog 2 (Adaptor molecule disabled-2) (Differentially expressed in ovarian carcinoma 2) (DOC-2) (Mitogen-responsive phosphoprotein)

 DAB2_MOUSE              Reviewed;         766 AA.
P98078; Q3U3K1; Q91W56; Q923E1;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
10-JAN-2006, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Disabled homolog 2;
AltName: Full=Adaptor molecule disabled-2;
AltName: Full=Differentially expressed in ovarian carcinoma 2;
Short=DOC-2;
AltName: Full=Mitogen-responsive phosphoprotein;
Name=Dab2; Synonyms=Doc2;
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] (ISOFORMS P67; P93 AND P96).
STRAIN=BALB/cJ; TISSUE=Macrophage;
PubMed=7775479; DOI=10.1074/jbc.270.23.14184;
Xu X.-X., Yang W., Jackowski S., Rock C.O.;
"Cloning of a novel phosphoprotein regulated by colony-stimulating
factor 1 shares a domain with the Drosophila disabled gene product.";
J. Biol. Chem. 270:14184-14191(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
P96).
STRAIN=129/Sv;
PubMed=11368898; DOI=10.1016/S0378-1119(01)00401-2;
Sheng Z., Smith E.R., He J., Tuppen J.A., Martin W.D., Dong F.B.,
Xu X.X.;
"Chromosomal location of murine disabled-2 gene and structural
comparison with its human ortholog.";
Gene 268:31-39(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P96).
STRAIN=NOD; TISSUE=Dendritic cell;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM P67).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH GRB2.
PubMed=9569023; DOI=10.1038/sj.onc.1201678;
Xu X.X., Yi T., Tang B., Lambeth J.D.;
"Disabled-2 (Dab2) is an SH3 domain-binding partner of Grb2.";
Oncogene 16:1561-1569(1998).
[6]
FUNCTION (ISOFORM P67), SUBCELLULAR LOCATION (ISOFORM P67), AND
INTERACTION WITH PIAS2.
PubMed=11104669; DOI=10.1042/bj3520645;
Cho S.-Y., Jeon J.W., Lee S.H., Park S.-S.;
"p67 isoform of mouse disabled 2 protein acts as a transcriptional
activator during the differentiation of F9 cells.";
Biochem. J. 352:645-650(2000).
[7]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LDLR; APP; APLP;
APLP2; INPP5D; LRP1 AND AP2A2, AND DOMAIN.
PubMed=11247302; DOI=10.1034/j.1600-0854.2001.020206.x;
Morris S.M., Cooper J.A.;
"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and
interacts with AP-2.";
Traffic 2:111-123(2001).
[8]
INTERACTION WITH MYO6.
PubMed=11906161; DOI=10.1006/bbrc.2002.6636;
Inoue A., Sato O., Homma K., Ikebe M.;
"DOC-2/DAB2 is the binding partner of myosin VI.";
Biochem. Biophys. Res. Commun. 292:300-307(2002).
[9]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=12413896; DOI=10.1006/dbio.2002.0810;
Yang D.H., Smith E.R., Roland I.H., Sheng Z., He J., Martin W.D.,
Hamilton T.C., Lambeth J.D., Xu X.X.;
"Disabled-2 is essential for endodermal cell positioning and structure
formation during mouse embryogenesis.";
Dev. Biol. 251:27-44(2002).
[10]
FUNCTION.
PubMed=11823414; DOI=10.1093/emboj/21.3.211;
Rosenbauer F., Kallies A., Scheller M., Knobeloch K.P., Rock C.O.,
Schwieger M., Stocking C., Horak I.;
"Disabled-2 is transcriptionally regulated by ICSBP and augments
macrophage spreading and adhesion.";
EMBO J. 21:211-220(2002).
[11]
FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=11927540; DOI=10.1093/emboj/21.7.1555;
Morris S.M., Tallquist M.D., Rock C.O., Cooper J.A.;
"Dual roles for the Dab2 adaptor protein in embryonic development and
kidney transport.";
EMBO J. 21:1555-1564(2002).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CLATHRIN AND
PHOSPHATIDYLINOSITIDES, AND DOMAIN.
PubMed=12234931; DOI=10.1093/emboj/cdf487;
Mishra S.K., Keyel P.A., Hawryluk M.J., Agostinelli N.R.,
Watkins S.C., Traub L.M.;
"Disabled-2 exhibits the properties of a cargo-selective endocytic
clathrin adaptor.";
EMBO J. 21:4915-4926(2002).
[13]
INTERACTION WITH DAB2IP.
PubMed=12877983; DOI=10.1016/S0169-328X(03)00176-1;
Homayouni R., Magdaleno S., Keshvara L., Rice D.S., Curran T.;
"Interaction of Disabled-1 and the GTPase activating protein Dab2IP in
mouse brain.";
Brain Res. Mol. Brain Res. 115:121-129(2003).
[14]
INTERACTION WITH SH3KBP1.
PubMed=14596919; DOI=10.1016/S0014-5793(03)01111-6;
Kowanetz K., Terzic J., Dikic I.;
"Dab2 links CIN85 with clathrin-mediated receptor internalization.";
FEBS Lett. 554:81-87(2003).
[15]
INTERACTION WITH ITGB3 AND ITGB5.
PubMed=12606711; DOI=10.1073/pnas.262791999;
Calderwood D.A., Fujioka Y., de Pereda J.M., Garcia-Alvarez B.,
Nakamoto T., Margolis B., McGlade C.J., Liddington R.C.,
Ginsberg M.H.;
"Integrin beta cytoplasmic domain interactions with phosphotyrosine-
binding domains: a structural prototype for diversity in integrin
signaling.";
Proc. Natl. Acad. Sci. U.S.A. 100:2272-2277(2003).
[16]
INTERACTION WITH NOSTRIN.
PubMed=15596140; DOI=10.1016/j.bbrc.2004.11.079;
Choi Y.-J., Cho S.-Y., Kim H.-W., Kim J.-A., Bae S.-H., Park S.-S.;
"Cloning and characterization of mouse disabled 2-interacting protein
2, a mouse orthologue of human NOSTRIN.";
Biochem. Biophys. Res. Commun. 326:594-599(2005).
[17]
FUNCTION, AND INTERACTION WITH ITGB1.
PubMed=15734730; DOI=10.1074/jbc.M500974200;
Prunier C., Howe P.H.;
"Disabled-2 (Dab2) is required for transforming growth factor beta-
induced epithelial to mesenchymal transition (EMT).";
J. Biol. Chem. 280:17540-17548(2005).
[18]
FUNCTION, AND INTERACTION WITH MAP3K7.
PubMed=15894542; DOI=10.1074/jbc.M501150200;
Hocevar B.A., Prunier C., Howe P.H.;
"Disabled-2 (Dab2) mediates transforming growth factor beta (TGFbeta)-
stimulated fibronectin synthesis through TGFbeta-activated kinase 1
and activation of the JNK pathway.";
J. Biol. Chem. 280:25920-25927(2005).
[19]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16263760; DOI=10.1242/jcs.02650;
Maurer M.E., Cooper J.A.;
"Endocytosis of megalin by visceral endoderm cells requires the Dab2
adaptor protein.";
J. Cell Sci. 118:5345-5355(2005).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[21]
FUNCTION, AND MUTAGENESIS OF LYS-53 AND SER-122.
PubMed=16984970; DOI=10.1242/jcs.03217;
Maurer M.E., Cooper J.A.;
"The adaptor protein Dab2 sorts LDL receptors into coated pits
independently of AP-2 and ARH.";
J. Cell Sci. 119:4235-4246(2006).
[22]
FUNCTION, AND MUTAGENESIS OF SER-122.
PubMed=16870701; DOI=10.1091/mbc.E06-05-0421;
Keyel P.A., Mishra S.K., Roth R., Heuser J.E., Watkins S.C.,
Traub L.M.;
"A single common portal for clathrin-mediated endocytosis of distinct
cargo governed by cargo-selective adaptors.";
Mol. Biol. Cell 17:4300-4317(2006).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323 AND SER-727, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[24]
FUNCTION, AND INTERACTION WITH AXIN1 AND PPP1CA.
PubMed=19581931; DOI=10.1038/onc.2009.157;
Jiang Y., Luo W., Howe P.H.;
"Dab2 stabilizes Axin and attenuates Wnt/beta-catenin signaling by
preventing protein phosphatase 1 (PP1)-Axin interactions.";
Oncogene 28:2999-3007(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-170; SER-193; THR-671;
SER-727 AND SER-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, 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).
[26]
FUNCTION.
PubMed=20881059; DOI=10.1091/mbc.E09-12-1019;
Penheiter S.G., Singh R.D., Repellin C.E., Wilkes M.C., Edens M.,
Howe P.H., Pagano R.E., Leof E.B.;
"Type II transforming growth factor-beta receptor recycling is
dependent upon the clathrin adaptor protein Dab2.";
Mol. Biol. Cell 21:4009-4019(2010).
[27]
INTERACTION WITH FCHO2, AND MUTAGENESIS OF PRO-294 AND PRO-299.
PubMed=22323290; DOI=10.1091/mbc.E11-09-0812;
Mulkearns E.E., Cooper J.A.;
"FCH domain only-2 organizes clathrin-coated structures and interacts
with Disabled-2 for low-density lipoprotein receptor endocytosis.";
Mol. Biol. Cell 23:1330-1342(2012).
[28]
INTERACTION WITH EPS15, EPS15L1 AND ITSN1, AND MUTAGENESIS OF PHE-255;
PHE-398; PHE-589; PHE-736 AND PHE-765.
PubMed=22648170; DOI=10.1091/mbc.E11-12-1007;
Teckchandani A., Mulkearns E.E., Randolph T.W., Toida N., Cooper J.A.;
"The clathrin adaptor Dab2 recruits EH domain scaffold proteins to
regulate integrin beta1 endocytosis.";
Mol. Biol. Cell 23:2905-2916(2012).
[29]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 33-191, AND MUTAGENESIS OF
LYS-53 AND LYS-90.
PubMed=12826668; DOI=10.1074/jbc.M304384200;
Yun M., Keshvara L., Park C.G., Zhang Y.M., Dickerson J.B., Zheng J.,
Rock C.O., Curran T., Park H.W.;
"Crystal structures of the Dab homology domains of mouse disabled 1
and 2.";
J. Biol. Chem. 278:36572-36581(2003).
-!- FUNCTION: Adapter protein that functions as clathrin-associated
sorting protein (CLASP) required for clathrin-mediated endocytosis
of selected cargo proteins. Can bind and assemble clathrin, and
binds simultaneously to phosphatidylinositol 4,5-bisphosphate
(PtdIns(4,5)P2) and cargos containing non-phosphorylated NPXY
internalization motifs, such as the LDL receptor, to recruit them
to clathrin-coated pits. Can function in clathrin-mediated
endocytosis independently of the AP-2 complex. Involved in
endocytosis of integrin beta-1; this function seems to redundant
with the AP-2 complex and seems to require DAB2 binding to
endocytosis accessory EH domain-containing proteins such as EPS15,
EPS15L1 and ITSN1. Involved in endocytosis of cystic fibrosis
transmembrane conductance regulator/CFTR. Isoform p96 is involved
in endocytosis of megalin/LRP2 lipoprotein receptor during
embryonal development. Required for recycling of the TGF-beta
receptor. Isoform p67 is not involved in LDL receptor endocytosis.
Involved in CFTR trafficking to the late endosome. Involved in
several receptor-mediated signaling pathways. Involved in TGF-beta
receptor signaling and facilitates phosphorylation of the signal
transducer SMAD2. Mediates TFG-beta-stimulated JNK activation. May
inhibit the canoniocal Wnt/beta-catenin signaling pathway by
stabilizing the beta-catenin destruction complex through a
competing association with axin preventing its dephosphorylation
through protein phosphatase 1 (PP1). Sequesters LRP6 towards
clathrin-mediated endocytosis, leading to inhibition of Wnt/beta-
catenin signaling. May activate non-canonical Wnt signaling. In
cell surface growth factor/Ras signaling pathways proposed to
inhibit ERK activation by interrupting the binding of GRB2 to SOS1
and to inhibit SRC by preventing its activating phosphorylation at
'Tyr-419'. Proposed to be involved in modulation of androgen
receptor (AR) signaling mediated by SRC activation; seems to
compete with AR for interaction with SRC. Plays a role in the CSF-
1 signal transduction pathway. Plays a role in cellular
differentiation. Involved in cell positioning and formation of
visceral endoderm (VE) during embryogenesis and proposed to be
required in the VE to respond to Nodal signaling coming from the
epiblast. Required for the epithelial to mesenchymal transition, a
process necessary for proper embryonic development. May be
involved in myeloid cell differentiation and can induce macrophage
adhesion and spreading. Isoform p67 may be involved in
transcriptional regulation. May act as a tumor suppressor.
{ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11823414,
ECO:0000269|PubMed:11927540, ECO:0000269|PubMed:12234931,
ECO:0000269|PubMed:12413896, ECO:0000269|PubMed:15734730,
ECO:0000269|PubMed:15894542, ECO:0000269|PubMed:16263760,
ECO:0000269|PubMed:16870701, ECO:0000269|PubMed:16984970,
ECO:0000269|PubMed:19581931, ECO:0000269|PubMed:20881059}.
-!- SUBUNIT: Interacts (via NPXY motif) with DAB2 (via PID domain).
Can interact (via PID domain) with LDLR, APP, APLP1 and APLP2, and
weakly with INPP5D (via NPXY motifs); the interaction is impaired
by tyrosine phosphorylation of the respective NPXY motifs. Can
weakly interact (via PID domain) with LRP1 (via NPXY motif); the
interaction is enhanced by tyrosine phosphorylation of the NPXY
motif. Interacts with LRP2 (via NPXY motif); the interaction is
not affected by tyrosine phosphorylation of the NPXY motif.
Interacts with clathrin; in vitro can assemble clathrin triskelia
into polyhedral coats. Interacts with AP2A2, ITGB1, ITGB3, ITGB5,
PIAS2, DAB2IP, NOSTRIN, FCHO1, DVL3 and EPS15L1. Interacts with
SH3KBP1 (via SH3 domains). Interacts with GRB2; competes with SOS1
for binding to GRB2 and the interaction is enhanced by EGF and NT-
3 stimulation. Isoform p96 interacts with EPS15 and ITSN1; isoform
p67 does not interact with EPS15 and only weakly interacts with
ITSN1. Interacts with MAP3K7; the interaction is induced by TGF-
beta stimulation and may mediate TGF-beta stimulated JNK
activation. Interacts with AXIN1 and PPP1CA; the interactions are
mutually exclusive. Interacts with the globular tail of MYO6.
Interacts (via DPF motifs) with FCHO2; the interaction is direct
and required for DAB2-mediated LDLR endocytosis. Interacts with
LRP6; the interaction involves LRP6 phosphorylation by CK2 and
sequesters LRP6 towards clathrin-mediated endocytosis. Associates
with the TGF-beta receptor complex (Probable). Interacts with
SMAD2 and SMAD3; the interactions are enhanced upon TGF-beta
stimulation. Interacts with GRB2; the interaction is enhanced by
EGF and NT-3 stimulation. Interacts with SRC; the interaction is
enhanced by EGF stimulation. {ECO:0000269|PubMed:11104669,
ECO:0000269|PubMed:11247302, ECO:0000269|PubMed:11906161,
ECO:0000269|PubMed:12234931, ECO:0000269|PubMed:12606711,
ECO:0000269|PubMed:12877983, ECO:0000269|PubMed:14596919,
ECO:0000269|PubMed:15596140, ECO:0000269|PubMed:15734730,
ECO:0000269|PubMed:15894542, ECO:0000269|PubMed:19581931,
ECO:0000269|PubMed:22323290, ECO:0000269|PubMed:22648170,
ECO:0000269|PubMed:9569023, ECO:0000305}.
-!- INTERACTION:
O94973:AP2A2 (xeno); NbExp=2; IntAct=EBI-1391846, EBI-1642835;
O35625:Axin1; NbExp=4; IntAct=EBI-1391846, EBI-2365912;
Q92997:DVL3 (xeno); NbExp=2; IntAct=EBI-1391846, EBI-739789;
P42567:Eps15; NbExp=2; IntAct=EBI-1391846, EBI-443923;
Q60902:Eps15l1; NbExp=2; IntAct=EBI-1391846, EBI-443931;
Q0JRZ9:FCHO2 (xeno); NbExp=4; IntAct=EBI-1391846, EBI-2609756;
P35917:Flt4; NbExp=3; IntAct=EBI-1391846, EBI-7845747;
P62993:GRB2 (xeno); NbExp=4; IntAct=EBI-1391846, EBI-401755;
Q60631:Grb2; NbExp=4; IntAct=EBI-1391846, EBI-1688;
Q9I8D1:MYO6 (xeno); NbExp=2; IntAct=EBI-1391846, EBI-6307292;
Q9UM54:MYO6 (xeno); NbExp=4; IntAct=EBI-1391846, EBI-350606;
Q9CR95:Necap1; NbExp=2; IntAct=EBI-1391846, EBI-7592476;
Q6WKZ7:Nostrin; NbExp=2; IntAct=EBI-1391846, EBI-1391878;
Q99NH2-1:Pard3; NbExp=2; IntAct=EBI-1391846, EBI-15946047;
Q8C5D8:Pias2; NbExp=3; IntAct=EBI-6305891, EBI-6305825;
Q96B97:SH3KBP1 (xeno); NbExp=9; IntAct=EBI-1391846, EBI-346595;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
membrane. Membrane, clathrin-coated pit. Note=Colocalizes with
large insert-containing isoforms of MYO6 at clathrin-coated
pits/vesicles. During mitosis is progressively displaced from the
membrane and translocated to the cytoplasm (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform p96: Membrane, clathrin-coated pit.
Note=Colocalizes with LDLR at clathrin-coated pits.
-!- SUBCELLULAR LOCATION: Isoform p67: Cytoplasm
{ECO:0000269|PubMed:11104669}. Nucleus
{ECO:0000269|PubMed:11104669}. Note=Diffuse localization in the
cytoplasm; does not localize to clathrin-coated pits.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=p96;
IsoId=P98078-1; Sequence=Displayed;
Name=p93;
IsoId=P98078-2; Sequence=VSP_004182;
Name=p67;
IsoId=P98078-3; Sequence=VSP_004183;
-!- TISSUE SPECIFICITY: Isoform p96 and isoform p67 are expressed in
adult kidney and fibroblasts with isoform p96 being the
predominant form. Isoform p67 is the predominant isoform expressed
in embryonic visceral endoderm. {ECO:0000269|PubMed:16263760}.
-!- DEVELOPMENTAL STAGE: At E6.5 specifically expressed in the cells
of the visceral endoderm. {ECO:0000269|PubMed:11927540,
ECO:0000269|PubMed:12413896}.
-!- DOMAIN: The PID domain binds to predominantly non-phosphorylated
NPXY internalization motifs present in members of the LDLR and APP
family; it also mediates simultaneous binding to
phosphatidylinositol 4,5-bisphosphate (PubMed:11247302,
PubMed:12234931). {ECO:0000269|PubMed:11247302,
ECO:0000269|PubMed:12234931}.
-!- DOMAIN: The Asn-Pro-Phe (NPF) motifs, which are found in proteins
involved in the endocytic pathway, mediate the interaction with
the EH domain of EPS15, EPS15R and ITSN1.
{ECO:0000269|PubMed:22648170}.
-!- PTM: Phosphorylated on serine residues in response to mitogenic
growth-factor stimulation. Phosphorylation during mitosis is
leading to membrane displacement (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal; embryos arrest prior to
gastrulation and show lack of endodermal organization, failure to
thin the distal tip visceral endoderm (VE), elongate the extra-
embryonic portion of the egg cylinder and properly organize the
epiblast. Loss of the specific megalin/LRP2 lipoprotein receptor
distribution at the brush border at the apical cell edge in
presumptive VE cells. Conditionally mutant mice are overtly
normal, but have reduced clathrin-coated pits in kidney proximal
tubule cells and excrete specific plasma proteins in the urine,
consistent with reduced transport by LRP2 in the proximal tubule.
{ECO:0000269|PubMed:11927540, ECO:0000269|PubMed:12413896}.
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EMBL; U18869; AAB02646.1; -; mRNA.
EMBL; U18869; AAB02647.1; -; mRNA.
EMBL; U18869; AAB02645.1; -; mRNA.
EMBL; AF260580; AAG44669.1; -; Genomic_DNA.
EMBL; AK154716; BAE32784.1; -; mRNA.
EMBL; BC016887; AAH16887.1; -; mRNA.
EMBL; BC006588; AAH06588.1; -; mRNA.
CCDS; CCDS37029.1; -. [P98078-1]
CCDS; CCDS37030.1; -. [P98078-3]
CCDS; CCDS79357.1; -. [P98078-2]
RefSeq; NP_001008702.1; NM_001008702.2.
RefSeq; NP_001032994.1; NM_001037905.3.
RefSeq; NP_075607.2; NM_023118.5.
RefSeq; XP_011243626.1; XM_011245324.1.
RefSeq; XP_017171913.1; XM_017316424.1.
UniGene; Mm.240830; -.
PDB; 1M7E; X-ray; 2.45 A; A/B/C=33-191.
PDB; 1P3R; X-ray; 2.10 A; A/B/C=32-191.
PDBsum; 1M7E; -.
PDBsum; 1P3R; -.
ProteinModelPortal; P98078; -.
SMR; P98078; -.
BioGrid; 199043; 11.
DIP; DIP-39422N; -.
IntAct; P98078; 55.
MINT; MINT-259116; -.
STRING; 10090.ENSMUSP00000079689; -.
iPTMnet; P98078; -.
PhosphoSitePlus; P98078; -.
SwissPalm; P98078; -.
MaxQB; P98078; -.
PaxDb; P98078; -.
PeptideAtlas; P98078; -.
PRIDE; P98078; -.
GeneID; 13132; -.
KEGG; mmu:13132; -.
UCSC; uc007vde.1; mouse. [P98078-1]
CTD; 1601; -.
MGI; MGI:109175; Dab2.
eggNOG; KOG3535; Eukaryota.
eggNOG; ENOG410XZ1H; LUCA.
HOGENOM; HOG000060158; -.
HOVERGEN; HBG018945; -.
InParanoid; P98078; -.
KO; K12475; -.
PhylomeDB; P98078; -.
TreeFam; TF316724; -.
ChiTaRS; Dab2; mouse.
EvolutionaryTrace; P98078; -.
PRO; PR:P98078; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_DAB2; -.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0030132; C:clathrin coat of coated pit; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; ISO:MGI.
GO; GO:0030136; C:clathrin-coated vesicle; ISO:MGI.
GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0001650; C:fibrillar center; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0035612; F:AP-2 adaptor complex binding; IDA:UniProtKB.
GO; GO:0038024; F:cargo receptor activity; IDA:UniProtKB.
GO; GO:0035615; F:clathrin adaptor activity; IDA:UniProtKB.
GO; GO:0030276; F:clathrin binding; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0007257; P:activation of JUN kinase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
GO; GO:0048268; P:clathrin coat assembly; IDA:UniProtKB.
GO; GO:0007492; P:endoderm development; IMP:MGI.
GO; GO:0007588; P:excretion; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0035026; P:leading edge cell differentiation; ISO:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IEP:UniProtKB.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0006907; P:pinocytosis; IMP:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:2000370; P:positive regulation of clathrin-dependent endocytosis; IDA:UniProtKB.
GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:MGI.
GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0002092; P:positive regulation of receptor internalization; IMP:CACAO.
GO; GO:0001921; P:positive regulation of receptor recycling; IMP:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; ISO:MGI.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:2000096; P:positive regulation of Wnt signaling pathway, planar cell polarity pathway; ISO:MGI.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR006020; PTB/PI_dom.
Pfam; PF00640; PID; 1.
SMART; SM00462; PTB; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS01179; PID; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Apoptosis;
Coated pit; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Developmental protein; Differentiation; Endocytosis; Membrane;
Nucleus; Phosphoprotein; Protein transport; Reference proteome;
Transport; Wnt signaling pathway.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P98082}.
CHAIN 2 766 Disabled homolog 2.
/FTId=PRO_0000079771.
DOMAIN 45 196 PID. {ECO:0000255|PROSITE-
ProRule:PRU00148}.
REGION 230 447 Required for localization to clathrin-
coated pits.
REGION 600 730 Sufficient for interaction with GRB2.
{ECO:0000269|PubMed:9569023}.
REGION 617 625 Required for interaction with CSK.
{ECO:0000250}.
REGION 647 766 Required for interaction with MYO6.
{ECO:0000269|PubMed:11906161}.
REGION 661 669 Required for interaction with GRB2 and
CSK. {ECO:0000250}.
REGION 707 723 Sufficient for interaction with SH3KBP1
SH3 domain.
MOTIF 293 295 DPF 1.
MOTIF 298 300 DPF 2.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P98082}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:O88797}.
MOD_RES 170 170 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 326 326 Phosphoserine; in mitosis. {ECO:0000250}.
MOD_RES 328 328 Phosphoserine; in mitosis. {ECO:0000250}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000250|UniProtKB:P98082}.
MOD_RES 671 671 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 759 759 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 209 229 Missing (in isoform p93).
{ECO:0000303|PubMed:7775479}.
/FTId=VSP_004182.
VAR_SEQ 230 447 Missing (in isoform p67).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7775479}.
/FTId=VSP_004183.
MUTAGEN 53 53 K->A: Abolishes binding to PtdIns(4,5)P2.
{ECO:0000269|PubMed:12826668,
ECO:0000269|PubMed:16984970}.
MUTAGEN 53 53 K->Q: Abolishes LDLR endocytosis.
{ECO:0000269|PubMed:12826668,
ECO:0000269|PubMed:16984970}.
MUTAGEN 90 90 K->A: Abolishes binding to PtdIns(4,5)P2.
{ECO:0000269|PubMed:12826668}.
MUTAGEN 122 122 S->T: Abolishes LDLR endocytosis.
{ECO:0000269|PubMed:16870701,
ECO:0000269|PubMed:16984970}.
MUTAGEN 122 122 S->Y: Impairs LDLR endocytosis.
{ECO:0000269|PubMed:16870701,
ECO:0000269|PubMed:16984970}.
MUTAGEN 255 255 F->V: Abolishes interaction with ITSN1,
fails to internalize integrin beta-1;
when associated with V-398, V-589, V-736
and V-765. {ECO:0000269|PubMed:22648170}.
MUTAGEN 294 294 P->A: Loss of interaction with FCHO2;
when associated with A-299.
{ECO:0000269|PubMed:22323290}.
MUTAGEN 299 299 P->A: Loss of interaction with FCHO2;
when associated with A-294.
{ECO:0000269|PubMed:22323290}.
MUTAGEN 398 398 F->V: Abolishes interaction with ITSN1,
fails to internalize integrin beta-1;
when associated with V-255, V-589, V-736
and V-765. {ECO:0000269|PubMed:22648170}.
MUTAGEN 589 589 F->V: Abolishes interaction with EPS15
and impairs interaction with ITSN1, fails
to internalize integrin beta-1; when
associated with V-736 and V-765.
Abolishes interaction with ITSN1; when
associated with V-255, V-398, V-736 and
V-765. {ECO:0000269|PubMed:22648170}.
MUTAGEN 736 736 F->V: Abolishes interaction with EPS15
and impairs interaction with ITSN1, fails
to internalize integrin beta-1; when
associated with V-589 and V-765.
Abolishes interaction with ITSN1; when
associated with V-255, V-398, V-589, and
V-765. {ECO:0000269|PubMed:22648170}.
MUTAGEN 765 765 F->V: Abolishes interaction with EPS15
and impairs interaction with ITSN1, fails
to internalize integrin beta-1; when
associated with V-589 and V-736.
Abolishes interaction with ITSN1; when
associated with V-255, V-398, V-589 and
V-736. {ECO:0000269|PubMed:22648170}.
CONFLICT 10 10 T -> A (in Ref. 4; AAH06588).
{ECO:0000305}.
CONFLICT 224 224 D -> G (in Ref. 4; AAH06588).
{ECO:0000305}.
CONFLICT 338 338 G -> V (in Ref. 1; AAB02646/AAB02645).
{ECO:0000305}.
CONFLICT 454 454 L -> P (in Ref. 1; AAB02645/AAB02646/
AAB02647 and 2; AAG44669). {ECO:0000305}.
CONFLICT 490 490 A -> P (in Ref. 1; AAB02645/AAB02646/
AAB02647 and 2; AAG44669). {ECO:0000305}.
CONFLICT 536 536 R -> G (in Ref. 3; BAE32784 and 4;
AAH16887/AAH06588). {ECO:0000305}.
CONFLICT 553 553 S -> P (in Ref. 4; AAH06588).
{ECO:0000305}.
HELIX 36 43 {ECO:0000244|PDB:1P3R}.
STRAND 48 63 {ECO:0000244|PDB:1P3R}.
HELIX 66 84 {ECO:0000244|PDB:1P3R}.
TURN 85 87 {ECO:0000244|PDB:1P3R}.
STRAND 91 98 {ECO:0000244|PDB:1P3R}.
STRAND 101 106 {ECO:0000244|PDB:1P3R}.
TURN 107 109 {ECO:0000244|PDB:1P3R}.
STRAND 112 116 {ECO:0000244|PDB:1P3R}.
HELIX 118 120 {ECO:0000244|PDB:1P3R}.
STRAND 121 126 {ECO:0000244|PDB:1P3R}.
STRAND 133 140 {ECO:0000244|PDB:1P3R}.
STRAND 144 153 {ECO:0000244|PDB:1P3R}.
HELIX 156 177 {ECO:0000244|PDB:1P3R}.
SEQUENCE 766 AA; 82312 MW; 856C946BD43C4B07 CRC64;
MSNEVETSTT NGQPDQQAAP KAPSKKEKKK GSEKTDEYLL ARFKGDGVKY KAKLIGIDDV
PDARGDKMSQ DSMMKLKGMA AAGRSQGQHK QRIWVNISLS GIKIIDEKTG VIEHEHPVNK
ISFIARDVTD NRAFGYVCGG EGQHQFFAIK TGQQAEPLVV DLKDLFQVIY NVKKKEEDKK
KVEEANKAEE NGSEALMTLD DQANKLKLGV DQMDLFGDMS TPPDLNSPTE SKDILLVDLN
SEIDTNQNSL RENPFLTNGV TSCSLPRPKP QASFLPENAF SANLNFFPTP NPDPFRDDPF
AQPDQSAPSS FDSLTSPDQK KASLSSSSTP QSKGPLNGDT DYFGQQFDQL SNRTGKPEAQ
GGPWPYPSSQ TQQAVRTQNG VSEREQNGFH IKSSPNPFVG SPPKGLSVPN GVKQDLESSV
QSSAHDSIAI IPPPQSTKPG RGRRTAKSSA NDLLASDIFA SEPPGQMSPT GQPAVPQSNF
LDLFKGNAPA PVGPLVGLGT VPVTPPQAGP WTPVVYSPST TVVPGAIISG QPPSFRQPLV
FGTTPAVQVW NQSPSFATPA SPPPPTVWCP TTSVAPNAWS STSPLGNPFQ SNNIFPPPTM
STQSSPQPMM SSVLATPPQP PPRNGPLKDI PSDAFTGLDP LGDKEVKEVK EMFKDFQLRQ
PPLVPSRKGE TPPSGTSSAF SSYFNNKVGI PQEHVDHDDF DANQLLNKIN EPPKPAPRQG
VLLGTKSADN SLENPFSKGF SSSNPSVVSQ PASSDPHRSP FGNPFA


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