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Drebrin-like protein (Cervical SH3P7) (Cervical mucin-associated protein) (Drebrin-F) (HPK1-interacting protein of 55 kDa) (HIP-55) (SH3 domain-containing protein 7)

 DBNL_HUMAN              Reviewed;         430 AA.
Q9UJU6; A4D2I9; B4DDP6; B4DEM2; C9J7P1; P84070; Q6IAI8; Q96F30;
Q96K74; Q9HBN8; Q9NR72;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 172.
RecName: Full=Drebrin-like protein;
AltName: Full=Cervical SH3P7;
AltName: Full=Cervical mucin-associated protein;
AltName: Full=Drebrin-F;
AltName: Full=HPK1-interacting protein of 55 kDa;
Short=HIP-55;
AltName: Full=SH3 domain-containing protein 7;
Name=DBNL; Synonyms=CMAP, SH3P7; ORFNames=PP5423;
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 INTERACTION WITH MAP4K1.
PubMed=10567356; DOI=10.1074/jbc.274.48.33945;
Ensenat D., Yao Z., Wang X.-S., Kori R., Zhou G., Lee S.C., Tan T.-H.;
"A novel src homology 3 domain-containing adaptor protein, HIP-55,
that interacts with hematopoietic progenitor kinase 1.";
J. Biol. Chem. 274:33945-33950(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zhang W., Yuan Z., Wan T., He L., Cao X.;
"Molecular cloning of cDNA encoding drebrin F.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cervix;
Toribara N.W., Ho S.B., Wang R., Arthur M., Shekels L.L.,
Spurr-Michaud S., Keutmann H.T., Hill J.A., Gipson I.K.;
"Expression cloning of a novel cervical mucin-associated protein
(CMAP).";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 5 AND 6).
TISSUE=Cerebellum, and Mammary gland;
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] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Eye;
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).
[11]
IDENTIFICATION.
PubMed=9891087; DOI=10.1128/MCB.19.2.1539;
Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J.,
Wienands J.;
"SH3P7 is a cytoskeleton adapter protein and is coupled to signal
transduction from lymphocyte antigen receptors.";
Mol. Cell. Biol. 19:1539-1546(1999).
[12]
DEGRADATION BY CASPASES.
PubMed=11689006; DOI=10.1006/bbrc.2001.5862;
Chen Y.-R., Kori R., John B., Tan T.-H.;
"Caspase-mediated cleavage of actin-binding and SH3-domain-containing
proteins cortactin, HS1, and HIP-55 during apoptosis.";
Biochem. Biophys. Res. Commun. 288:981-989(2001).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14729663; DOI=10.1074/jbc.M312659200;
Le Bras S., Foucault I., Foussat A., Brignone C., Acuto O.,
Deckert M.;
"Recruitment of the actin-binding protein HIP-55 to the immunological
synapse regulates T cell receptor signaling and endocytosis.";
J. Biol. Chem. 279:15550-15560(2004).
[15]
INTERACTION WITH PRAM1, CLEAVAGE BY CASPASES, AND MUTAGENESIS OF
ASP-361.
PubMed=15637062; DOI=10.1074/jbc.M413564200;
Denis F.M., Benecke A., Di Gioia Y., Touw I.P., Cayre Y.E., Lutz P.G.;
"PRAM-1 potentiates arsenic trioxide-induced JNK activation.";
J. Biol. Chem. 280:9043-9048(2005).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-232 (ISOFORMS 2 AND 3), PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 4), PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-183 (ISOFORM 6), AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, 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).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269, 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).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176 AND LYS-288, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-269,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 (ISOFORMS 2 AND 3),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 (ISOFORM 4),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 (ISOFORM 6), 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).
[25]
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-232; SER-269;
SER-272; SER-275; SER-283 AND THR-291, 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-269 AND SER-275, 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).
[29]
STRUCTURE BY NMR OF 1-133.
PubMed=19768801; DOI=10.1002/pro.248;
Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M.,
Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.;
"NMR solution structures of actin depolymerizing factor homology
domains.";
Protein Sci. 18:2384-2392(2009).
-!- FUNCTION: Adapter protein that binds F-actin and DNM1, and thereby
plays a role in receptor-mediated endocytosis. Plays a role in the
reorganization of the actin cytoskeleton, formation of cell
projections, such as neurites, in neuron morphogenesis and synapse
formation via its interaction with WASL and COBL. Does not bind G-
actin and promote actin polymerization by itself. Required for the
formation of organized podosome rosettes (By similarity). May act
as a common effector of antigen receptor-signaling pathways in
leukocytes. Acts as a key component of the immunological synapse
that regulates T-cell activation by bridging TCRs and the actin
cytoskeleton to gene activation and endocytic processes.
{ECO:0000250, ECO:0000269|PubMed:14729663}.
-!- SUBUNIT: Interacts with SHANK2, SHANK3 and SYN1. Interacts with
FGD1 and DNM1. Interacts with ANKRD54. Interacts with COBL.
Interacts with WASL and WIPF1 (By similarity). Interacts with
MAP4K1 and PRAM1. {ECO:0000250, ECO:0000269|PubMed:10567356,
ECO:0000269|PubMed:15637062}.
-!- INTERACTION:
Q96AP0:ACD; NbExp=2; IntAct=EBI-751783, EBI-717666;
Q9H788:SH2D4A; NbExp=6; IntAct=EBI-751783, EBI-747035;
Q9H788-2:SH2D4A; NbExp=3; IntAct=EBI-751783, EBI-10308083;
P78314:SH3BP2; NbExp=7; IntAct=EBI-751783, EBI-727062;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q62418}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:Q62418}. Cell projection, ruffle
{ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:Q62418}. Cytoplasm, cytosol
{ECO:0000250|UniProtKB:Q62418}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q62418}. Cell projection
{ECO:0000250|UniProtKB:Q62418}. Cell membrane
{ECO:0000269|PubMed:14729663}; Peripheral membrane protein;
Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, clathrin-
coated vesicle membrane {ECO:0000250|UniProtKB:Q62418}; Peripheral
membrane protein; Cytoplasmic side. Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q62418}; Peripheral membrane protein;
Cytoplasmic side. Cell projection, podosome
{ECO:0000250|UniProtKB:Q62418}. Early endosome
{ECO:0000269|PubMed:14729663}. Note=Detected in neuron cell body
and cell projections, such as neurites. Colocalizes with cytosolic
dynamin in hippocampus neurons (By similarity). Cortical actin
cytoskeleton. Associates with lamellipodial actin and membrane
ruffles. Colocalizes with actin and cortactin at podosome dots and
podosome rosettes (By similarity). {ECO:0000250|UniProtKB:Q62418}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q9UJU6-1; Sequence=Displayed;
Name=2;
IsoId=Q9UJU6-2; Sequence=VSP_011398;
Note=No experimental confirmation available. Contains a
phosphoserine at position 232. {ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231};
Name=3;
IsoId=Q9UJU6-3; Sequence=VSP_011398, VSP_011399;
Note=No experimental confirmation available. Contains a
phosphoserine at position 232. {ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231};
Name=4;
IsoId=Q9UJU6-4; Sequence=VSP_054779, VSP_011398;
Note=Contains a phosphoserine at position 137.
{ECO:0000244|PubMed:16964243, ECO:0000244|PubMed:20068231};
Name=5;
IsoId=Q9UJU6-5; Sequence=VSP_054780;
Name=6;
IsoId=Q9UJU6-6; Sequence=VSP_057346, VSP_011398;
Note=No experimental confirmation available. Contains a
phosphoserine at position 183. {ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231};
-!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3
and PRAM1.
-!- PTM: Degraded by caspases during apoptosis.
-!- SIMILARITY: Belongs to the ABP1 family. {ECO:0000305}.
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EMBL; AF197060; AAF13701.1; -; mRNA.
EMBL; AF077353; AAF80228.1; -; mRNA.
EMBL; AF250287; AAF81273.1; -; mRNA.
EMBL; AF151364; AAG13120.1; -; mRNA.
EMBL; AF218020; AAG17262.2; -; mRNA.
EMBL; AK027367; BAB55065.1; -; mRNA.
EMBL; AK293279; BAG56807.1; -; mRNA.
EMBL; AK293698; BAG57133.1; -; mRNA.
EMBL; CR457167; CAG33448.1; -; mRNA.
EMBL; AC017116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236960; EAL23770.1; -; Genomic_DNA.
EMBL; CH471128; EAW61132.1; -; Genomic_DNA.
EMBL; BC011677; AAH11677.1; -; mRNA.
EMBL; BC031687; AAH31687.1; -; mRNA.
CCDS; CCDS34622.1; -. [Q9UJU6-2]
CCDS; CCDS34623.1; -. [Q9UJU6-1]
CCDS; CCDS47579.1; -. [Q9UJU6-3]
CCDS; CCDS64633.1; -. [Q9UJU6-4]
CCDS; CCDS64634.1; -. [Q9UJU6-5]
RefSeq; NP_001014436.1; NM_001014436.2. [Q9UJU6-1]
RefSeq; NP_001116428.1; NM_001122956.1. [Q9UJU6-3]
RefSeq; NP_001271242.1; NM_001284313.1. [Q9UJU6-5]
RefSeq; NP_001271244.1; NM_001284315.1. [Q9UJU6-4]
RefSeq; NP_054782.2; NM_014063.6. [Q9UJU6-2]
UniGene; Hs.436500; -.
PDB; 1X67; NMR; -; A=1-133.
PDBsum; 1X67; -.
ProteinModelPortal; Q9UJU6; -.
SMR; Q9UJU6; -.
BioGrid; 118809; 63.
IntAct; Q9UJU6; 11.
MINT; Q9UJU6; -.
STRING; 9606.ENSP00000417653; -.
iPTMnet; Q9UJU6; -.
PhosphoSitePlus; Q9UJU6; -.
BioMuta; DBNL; -.
DMDM; 51316115; -.
OGP; Q9UJU6; -.
EPD; Q9UJU6; -.
PaxDb; Q9UJU6; -.
PeptideAtlas; Q9UJU6; -.
PRIDE; Q9UJU6; -.
ProteomicsDB; 84659; -.
ProteomicsDB; 84660; -. [Q9UJU6-2]
ProteomicsDB; 84661; -. [Q9UJU6-3]
TopDownProteomics; Q9UJU6-2; -. [Q9UJU6-2]
DNASU; 28988; -.
Ensembl; ENST00000440166; ENSP00000415173; ENSG00000136279. [Q9UJU6-5]
Ensembl; ENST00000448521; ENSP00000411701; ENSG00000136279. [Q9UJU6-1]
Ensembl; ENST00000456905; ENSP00000416421; ENSG00000136279. [Q9UJU6-6]
Ensembl; ENST00000468694; ENSP00000417653; ENSG00000136279. [Q9UJU6-3]
Ensembl; ENST00000490734; ENSP00000417749; ENSG00000136279. [Q9UJU6-4]
Ensembl; ENST00000494774; ENSP00000419992; ENSG00000136279. [Q9UJU6-2]
GeneID; 28988; -.
KEGG; hsa:28988; -.
UCSC; uc003tjo.5; human. [Q9UJU6-1]
CTD; 28988; -.
DisGeNET; 28988; -.
EuPathDB; HostDB:ENSG00000136279.18; -.
GeneCards; DBNL; -.
HGNC; HGNC:2696; DBNL.
HPA; HPA020265; -.
HPA; HPA027735; -.
MIM; 610106; gene.
neXtProt; NX_Q9UJU6; -.
OpenTargets; ENSG00000136279; -.
PharmGKB; PA27164; -.
eggNOG; KOG3655; Eukaryota.
eggNOG; ENOG410XRVX; LUCA.
GeneTree; ENSGT00940000156732; -.
HOGENOM; HOG000008567; -.
HOVERGEN; HBG051316; -.
InParanoid; Q9UJU6; -.
KO; K20520; -.
OMA; GYEGQTN; -.
OrthoDB; EOG091G05KP; -.
PhylomeDB; Q9UJU6; -.
TreeFam; TF318935; -.
Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-HSA-6794361; Neurexins and neuroligins.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; Q9UJU6; -.
SIGNOR; Q9UJU6; -.
ChiTaRS; DBNL; human.
EvolutionaryTrace; Q9UJU6; -.
GeneWiki; Drebrin-like; -.
GenomeRNAi; 28988; -.
PMAP-CutDB; Q9UJU6; -.
PRO; PR:Q9UJU6; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000136279; Expressed in 182 organ(s), highest expression level in lower esophagus mucosa.
CleanEx; HS_DBNL; -.
ExpressionAtlas; Q9UJU6; baseline and differential.
Genevisible; Q9UJU6; HS.
GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0002102; C:podosome; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0003779; F:actin binding; ISS:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0007257; P:activation of JUN kinase activity; TAS:ProtInc.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0071800; P:podosome assembly; ISS:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; IEA:InterPro.
GO; GO:0097178; P:ruffle assembly; IEA:InterPro.
GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
CDD; cd11960; SH3_Abp1_eu; 1.
Gene3D; 3.40.20.10; -; 1.
InterPro; IPR002108; ADF-H.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR029923; Dbnl.
InterPro; IPR035717; Drebrin-like_SH3.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10829:SF12; PTHR10829:SF12; 1.
Pfam; PF00241; Cofilin_ADF; 1.
Pfam; PF14604; SH3_9; 1.
SMART; SM00102; ADF; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS51263; ADF_H; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; Adaptive immunity;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Cytoskeleton; Endocytosis; Endosome; Golgi apparatus; Immunity;
Membrane; Phosphoprotein; Reference proteome; SH3 domain; Synapse;
Transport.
CHAIN 1 430 Drebrin-like protein.
/FTId=PRO_0000079793.
DOMAIN 4 133 ADF-H. {ECO:0000255|PROSITE-
ProRule:PRU00599}.
DOMAIN 371 430 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
COILED 176 231 {ECO:0000255}.
SITE 361 362 Cleavage; by caspase-3.
MOD_RES 26 26 Phosphothreonine.
{ECO:0000250|UniProtKB:Q62418}.
MOD_RES 160 160 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 176 176 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 269 269 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:23186163}.
MOD_RES 288 288 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 291 291 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 334 334 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62418}.
MOD_RES 344 344 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q62418}.
VAR_SEQ 1 109 MAANLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIR
VAGTGEGGLEEMVEELNSGKVMYAFCRVKDPNSGLPKFVLI
NWTGEGVNDVRKGACASHVSTMASFLK -> MKATAMTSAW
LAQG (in isoform 4). {ECO:0000305}.
/FTId=VSP_054779.
VAR_SEQ 1 103 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054780.
VAR_SEQ 110 158 Missing (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057346.
VAR_SEQ 234 234 Q -> QS (in isoform 2, isoform 3, isoform
4 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011398.
VAR_SEQ 251 251 Q -> QGSTCASLQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_011399.
MUTAGEN 361 361 D->A: Abolishes cleavage by caspase-3.
{ECO:0000269|PubMed:15637062}.
CONFLICT 8 8 N -> K (in Ref. 4; AAG17262).
{ECO:0000305}.
CONFLICT 98 98 A -> S (in Ref. 3; AAF81273/AAG13120).
{ECO:0000305}.
CONFLICT 235 235 R -> S (in Ref. 3; AAF81273/AAG13120).
{ECO:0000305}.
CONFLICT 430 430 E -> D (in Ref. 6; CAG33448).
{ECO:0000305}.
HELIX 9 20 {ECO:0000244|PDB:1X67}.
STRAND 22 25 {ECO:0000244|PDB:1X67}.
STRAND 27 38 {ECO:0000244|PDB:1X67}.
STRAND 40 48 {ECO:0000244|PDB:1X67}.
HELIX 50 56 {ECO:0000244|PDB:1X67}.
STRAND 61 70 {ECO:0000244|PDB:1X67}.
STRAND 72 74 {ECO:0000244|PDB:1X67}.
STRAND 76 85 {ECO:0000244|PDB:1X67}.
HELIX 91 107 {ECO:0000244|PDB:1X67}.
TURN 108 110 {ECO:0000244|PDB:1X67}.
STRAND 111 115 {ECO:0000244|PDB:1X67}.
HELIX 120 123 {ECO:0000244|PDB:1X67}.
HELIX 125 133 {ECO:0000244|PDB:1X67}.
SEQUENCE 430 AA; 48207 MW; 7E8C42ED047257AE CRC64;
MAANLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EEMVEELNSG
KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACASH VSTMASFLKG AHVTINARAE
EDVEPECIME KVAKASGANY SFHKESGRFQ DVGPQAPVGS VYQKTNAVSE IKRVGKDSFW
AKAEKEEENR RLEEKRRAEE AQRQLEQERR ERELREAARR EQRYQEQGGE ASPQRTWEQQ
QEVVSRNRNE QESAVHPREI FKQKERAMST TSISSPQPGK LRSPFLQKQL TQPETHFGRE
PAAAISRPRA DLPAEEPAPS TPPCLVQAEE EAVYEEPPEQ ETFYEQPPLV QQQGAGSEHI
DHHIQGQGLS GQGLCARALY DYQAADDTEI SFDPENLITG IEVIDEGWWR GYGPDGHFGM
FPANYVELIE


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