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Breakpoint cluster region protein (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-26)

 BCR_HUMAN               Reviewed;        1271 AA.
P11274; P78501; Q12842; Q4LE80; Q6NZI3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
22-NOV-2017, entry version 209.
RecName: Full=Breakpoint cluster region protein;
EC=2.7.11.1;
AltName: Full=Renal carcinoma antigen NY-REN-26;
Name=BCR; Synonyms=BCR1, D22S11;
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 2), AND VARIANT SER-796.
PubMed=3285291;
Lifshitz B., Fainstein E., Marcelle C., Shtivelman E., Amson R.,
Gale R.P., Canaani E.;
"bcr genes and transcripts.";
Oncogene 2:113-117(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHROMOSOMAL TRANSLOCATION.
PubMed=7665185; DOI=10.1006/geno.1995.1008;
Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D.,
Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y.,
McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G.,
Heisterkamp N., Groffen J., Roe B.A.;
"Sequence and analysis of the human ABL gene, the BCR gene, and
regions involved in the Philadelphia chromosomal translocation.";
Genomics 27:67-82(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-796.
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-872, CHROMOSOMAL TRANSLOCATION,
INVOLVEMENT IN CML, AND VARIANT SER-796.
PubMed=3107980;
Hariharan I.K., Adams J.M.;
"cDNA sequence for human bcr, the gene that translocates to the abl
oncogene in chronic myeloid leukaemia.";
EMBO J. 6:115-119(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-693, AND INVOLVEMENT IN CML.
PubMed=3540951; DOI=10.1073/pnas.83.24.9768;
Mes-Masson A.-M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.;
"Overlapping cDNA clones define the complete coding region for the
P210c-abl gene product associated with chronic myelogenous leukemia
cells containing the Philadelphia chromosome.";
Proc. Natl. Acad. Sci. U.S.A. 83:9768-9772(1986).
[6]
ERRATUM, AND SEQUENCE REVISION.
Mes-Masson A.M., McLaughlin J., Daley G.Q., Paskind M., Witte O.N.;
Proc. Natl. Acad. Sci. U.S.A. 84:2507-2507(1987).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 683-1271 (ISOFORM 1).
PubMed=2989703; DOI=10.1038/315758a0;
Heisterkamp N., Stam K., Groffen J., de Klein A., Grosveld G.;
"Structural organization of the bcr gene and its role in the Ph'
translocation.";
Nature 315:758-761(1985).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-46 AND 275-426.
PubMed=2263470; DOI=10.1093/nar/18.23.7119;
Zhu Q.S., Heisterkamp N., Groffen J.;
"Unique organization of the human BCR gene promoter.";
Nucleic Acids Res. 18:7119-7125(1990).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 56-426.
PubMed=2825022; DOI=10.1038/330386a0;
Fainstein E., Marcelle C., Rosner A., Canaani E., Gale R.P.,
Dreazen O., Smith S.D., Croce C.M.;
"A new fused transcript in Philadelphia chromosome positive acute
lymphocytic leukaemia.";
Nature 330:386-388(1987).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 362-438, AND ALTERNATIVE SPLICING.
PubMed=2915904;
Romero P., Beran M., Shtalrid M., Andersson B., Talpaz M., Blick M.;
"Alternative 5' end of the bcr-abl transcript in chronic myelogenous
leukemia.";
Oncogene 4:93-98(1989).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 670-842, INVOLVEMENT IN CML, AND
VARIANT SER-796.
PubMed=2407300;
Selleri L., von Lindern M., Hermans A., Meijer D., Torelli G.,
Grosveld G.;
"Chronic myeloid leukemia may be associated with several bcr-abl
transcripts including the acute lymphoid leukemia-type 7 kb
transcript.";
Blood 75:1146-1153(1990).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-4.
PubMed=1900918; DOI=10.1128/MCB.11.4.1854;
Shah N.P., Witte O.N., Denny C.T.;
"Characterization of the BCR promoter in Philadelphia chromosome-
positive and -negative cell lines.";
Mol. Cell. Biol. 11:1854-1860(1991).
[13]
FUNCTION.
PubMed=1903516; DOI=10.1038/351400a0;
Diekmann D., Brill S., Garrett M.D., Totty N., Hsuan J., Monfries C.,
Hall C., Lim L., Hall A.;
"Bcr encodes a GTPase-activating protein for p21rac.";
Nature 351:400-402(1991).
[14]
INTERACTION WITH ABL1 SH2-DOMAIN.
PubMed=1712671; DOI=10.1016/0092-8674(91)90148-R;
Pendergast A.M., Muller A.J., Havlik M.H., Maru Y., Witte O.N.;
"BCR sequences essential for transformation by the BCR-ABL oncogene
bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-
dependent manner.";
Cell 66:161-171(1991).
[15]
FUNCTION AS PROTEIN KINASE.
PubMed=1657398; DOI=10.1016/0092-8674(91)90521-Y;
Maru Y., Witte O.N.;
"The BCR gene encodes a novel serine/threonine kinase activity within
a single exon.";
Cell 67:459-468(1991).
[16]
PHOSPHORYLATION AT TYR-177 BY HCK, MUTAGENESIS OF TYR-177, AND
INTERACTION WITH HCK AND GRB2.
PubMed=9407116; DOI=10.1074/jbc.272.52.33260;
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B.,
Hallek M.;
"The Src family kinase Hck interacts with Bcr-Abl by a kinase-
independent mechanism and phosphorylates the Grb2-binding site of
Bcr.";
J. Biol. Chem. 272:33260-33270(1997).
[17]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1264, 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).
[19]
INTERACTION WITH FES/FPS; ABL1; PIK3R1 AND GRB2, MUTAGENESIS OF
TYR-177, AND PHOSPHORYLATION AT TYR-246.
PubMed=15302586; DOI=10.1016/j.yexcr.2004.05.010;
Laurent C.E., Smithgall T.E.;
"The c-Fes tyrosine kinase cooperates with the breakpoint cluster
region protein (Bcr) to induce neurite extension in a Rac- and Cdc42-
dependent manner.";
Exp. Cell Res. 299:188-198(2004).
[20]
INTERACTION WITH PDZK1, AND MUTAGENESIS OF 1269-THR--GLU-1271 AND
VAL-1271.
PubMed=15494376; DOI=10.1242/jcs.01472;
Malmberg E.K., Andersson C.X., Gentzsch M., Chen J.H., Mengos A.,
Cui L., Hansson G.C., Riordan J.R.;
"Bcr (breakpoint cluster region) protein binds to PDZ-domains of
scaffold protein PDZK1 and vesicle coat protein Mint3.";
J. Cell Sci. 117:5535-5541(2004).
[21]
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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177; SER-459 AND
SER-1264, 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).
[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-122; SER-215 AND
SER-459, 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]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-139; SER-202;
SER-215; SER-222; SER-356; SER-377; SER-459; SER-463; SER-473;
SER-488; TYR-554; THR-641; TYR-644; THR-693 AND SER-894, 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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, 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).
[30]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 3-72, AND
HOMOTETRAMERIZATION.
PubMed=11780146; DOI=10.1038/nsb747;
Zhao X., Ghaffari S., Lodish H., Malashkevich V.N., Kim P.S.;
"Structure of the Bcr-Abl oncoprotein oligomerization domain.";
Nat. Struct. Biol. 9:117-120(2002).
[31]
INTERACTION WITH SH2D5.
PubMed=25331951; DOI=10.1074/jbc.M114.615112;
Gray E.J., Petsalaki E., James D.A., Bagshaw R.D., Stacey M.M.,
Rocks O., Gingras A.C., Pawson T.;
"src homology 2 domain containing protein 5 (sh2d5) binds the
breakpoint cluster region protein, BCR, and regulates levels of Rac1-
GTP.";
J. Biol. Chem. 289:35397-35408(2014).
[32]
VARIANTS [LARGE SCALE ANALYSIS] PRO-400; MET-413; GLU-752; SER-796;
CYS-910; ILE-949; LYS-1037; MET-1091; ALA-1096; GLY-1104; ASN-1106;
THR-1149; LYS-1161; GLU-1187; MET-1189; GLY-1204 AND ARG-1235.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes
the exchange of RAC or CDC42-bound GDP by GTP, thereby activating
them. Displays serine/threonine kinase activity.
{ECO:0000269|PubMed:1657398, ECO:0000269|PubMed:1903516}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Homotetramer. Interacts with PDZK1. May interact with
CCPG1 (By similarity). Interacts with FES/FPS, ABL1, PIK3R1 and
GRB2. Interacts with HCK. Interacts with SH2D5 (PubMed:25331951).
{ECO:0000250|UniProtKB:Q6PAJ1, ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:15494376, ECO:0000269|PubMed:1712671,
ECO:0000269|PubMed:25331951, ECO:0000269|PubMed:9407116}.
-!- INTERACTION:
P62993:GRB2; NbExp=8; IntAct=EBI-712838, EBI-401755;
P18031:PTPN1; NbExp=3; IntAct=EBI-8658094, EBI-968788;
Q6ZV89-1:SH2D5; NbExp=2; IntAct=EBI-712838, EBI-15101685;
A2AM67:Sh2d5 (xeno); NbExp=7; IntAct=EBI-712838, EBI-15101945;
Q8JZW5:Sh2d5 (xeno); NbExp=2; IntAct=EBI-712838, EBI-15101675;
Q9H2K2:TNKS2; NbExp=3; IntAct=EBI-712838, EBI-4398527;
P04637:TP53; NbExp=2; IntAct=EBI-712838, EBI-366083;
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane, postsynaptic density {ECO:0000250|UniProtKB:Q6PAJ1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P11274-1; Sequence=Displayed;
Name=2;
IsoId=P11274-2; Sequence=VSP_024352;
Note=No experimental confirmation available.;
-!- DOMAIN: The region involved in binding to ABL1 SH2-domain is rich
in serine residues and needs to be Ser/Thr phosphorylated prior to
SH2 binding. This region is essential for the activation of the
ABL1 tyrosine kinase and transforming potential of the chimeric
BCR-ABL oncogene.
-!- DOMAIN: The DH domain is involved in interaction with CCPG1.
{ECO:0000250}.
-!- PTM: Autophosphorylated. Phosphorylated by FES/FPS on tyrosine
residues, leading to down-regulation of the BCR kinase activity.
Phosphorylation at Tyr-177 by HCK is important for interaction
with GRB2. {ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:9407116}.
-!- DISEASE: Leukemia, chronic myeloid (CML) [MIM:608232]: A clonal
myeloproliferative disorder of a pluripotent stem cell with a
specific cytogenetic abnormality, the Philadelphia chromosome
(Ph), involving myeloid, erythroid, megakaryocytic, B-lymphoid,
and sometimes T-lymphoid cells, but not marrow fibroblasts.
{ECO:0000269|PubMed:2407300, ECO:0000269|PubMed:3107980,
ECO:0000269|PubMed:3540951}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Note=A chromosomal aberration involving BCR has been
found in patients with chronic myeloid leukemia. Translocation
t(9;22)(q34;q11) with ABL1. The translocation produces a BCR-ABL
found also in acute myeloid leukemia (AML) and acute lymphoblastic
leukemia (ALL). {ECO:0000269|PubMed:3107980,
ECO:0000269|PubMed:7665185}.
-!- SEQUENCE CAUTION:
Sequence=BAE06073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCRID55.html";
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EMBL; Y00661; CAA68676.1; -; mRNA.
EMBL; U07000; AAB60388.1; -; Genomic_DNA.
EMBL; AB209991; BAE06073.1; ALT_INIT; mRNA.
EMBL; X02596; CAA26441.1; -; mRNA.
EMBL; M15025; AAA35594.1; -; Genomic_DNA.
EMBL; X52828; CAA37010.1; -; Genomic_DNA.
EMBL; X52829; CAA37011.1; -; Genomic_DNA.
EMBL; X14676; CAA32806.1; -; mRNA.
EMBL; M64437; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS13806.1; -. [P11274-1]
CCDS; CCDS13807.1; -. [P11274-2]
PIR; A26664; TVHUA2.
PIR; A91064; TVHUBR.
RefSeq; NP_004318.3; NM_004327.3. [P11274-1]
RefSeq; NP_067585.2; NM_021574.2. [P11274-2]
UniGene; Hs.517461; -.
UniGene; Hs.715409; -.
PDB; 1K1F; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-72.
PDB; 2AIN; NMR; -; B=1266-1271.
PDBsum; 1K1F; -.
PDBsum; 2AIN; -.
ProteinModelPortal; P11274; -.
SMR; P11274; -.
BioGrid; 107083; 77.
ELM; P11274; -.
IntAct; P11274; 33.
MINT; MINT-1207264; -.
STRING; 9606.ENSP00000303507; -.
BindingDB; P11274; -.
ChEMBL; CHEMBL5146; -.
DrugBank; DB06616; Bosutinib.
DrugBank; DB08901; Ponatinib.
iPTMnet; P11274; -.
PhosphoSitePlus; P11274; -.
BioMuta; BCR; -.
DMDM; 143811366; -.
EPD; P11274; -.
MaxQB; P11274; -.
PaxDb; P11274; -.
PeptideAtlas; P11274; -.
PRIDE; P11274; -.
Ensembl; ENST00000305877; ENSP00000303507; ENSG00000186716. [P11274-1]
Ensembl; ENST00000359540; ENSP00000352535; ENSG00000186716. [P11274-2]
GeneID; 613; -.
KEGG; hsa:613; -.
UCSC; uc002zww.4; human. [P11274-1]
CTD; 613; -.
DisGeNET; 613; -.
EuPathDB; HostDB:ENSG00000186716.19; -.
GeneCards; BCR; -.
H-InvDB; HIX0016226; -.
H-InvDB; HIX0016271; -.
H-InvDB; HIX0027936; -.
H-InvDB; HIX0041406; -.
HGNC; HGNC:1014; BCR.
HPA; CAB010421; -.
HPA; CAB018545; -.
HPA; HPA038337; -.
MalaCards; BCR; -.
MIM; 151410; gene.
MIM; 608232; phenotype.
neXtProt; NX_P11274; -.
OpenTargets; ENSG00000186716; -.
Orphanet; 521; Chronic myeloid leukemia.
Orphanet; 261330; Distal 22q11.2 microdeletion syndrome.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
PharmGKB; PA25321; -.
eggNOG; KOG4269; Eukaryota.
eggNOG; ENOG410XPGZ; LUCA.
GeneTree; ENSGT00890000139322; -.
HOGENOM; HOG000006779; -.
HOVERGEN; HBG004165; -.
InParanoid; P11274; -.
KO; K08878; -.
OMA; DRIMGKG; -.
OrthoDB; EOG091G03M3; -.
PhylomeDB; P11274; -.
TreeFam; TF105082; -.
Reactome; R-HSA-1839117; Signaling by cytosolic FGFR1 fusion mutants.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
SignaLink; P11274; -.
SIGNOR; P11274; -.
ChiTaRS; BCR; human.
EvolutionaryTrace; P11274; -.
GeneWiki; BCR_(gene); -.
GenomeRNAi; 613; -.
PRO; PR:P11274; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000186716; -.
CleanEx; HS_BCR; -.
ExpressionAtlas; P11274; baseline and differential.
Genevisible; P11274; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:ProtInc.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0060313; P:negative regulation of blood vessel remodeling; IEA:Ensembl.
GO; GO:0002692; P:negative regulation of cellular extravasation; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043314; P:negative regulation of neutrophil degranulation; IEA:Ensembl.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:0060268; P:negative regulation of respiratory burst; IEA:Ensembl.
GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:Ensembl.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0043114; P:regulation of vascular permeability; IEA:Ensembl.
GO; GO:0003014; P:renal system process; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
InterPro; IPR036481; Bcr-Abl_oncoprot_oligo_sf.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
Pfam; PF09036; Bcr-Abl_Oligo; 1.
Pfam; PF00168; C2; 1.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00239; C2; 1.
SMART; SM00233; PH; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF48350; SSF48350; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF69036; SSF69036; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50238; RHOGAP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Cell junction; Cell membrane; Chromosomal rearrangement;
Complete proteome; GTPase activation;
Guanine-nucleotide releasing factor; Kinase; Membrane; Methylation;
Nucleotide-binding; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Proto-oncogene; Reference proteome;
Serine/threonine-protein kinase; Synapse; Transferase.
CHAIN 1 1271 Breakpoint cluster region protein.
/FTId=PRO_0000080933.
DOMAIN 498 691 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 708 866 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 870 1002 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 1054 1248 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
REGION 1 426 Kinase.
REGION 197 385 Binding to ABL SH2-domain.
COMPBIAS 824 827 Poly-Leu.
SITE 426 427 Breakpoint for translocation to form BCR-
ABL oncogene.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 177 177 Phosphotyrosine; by HCK.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:9407116}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 222 222 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 236 236 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 246 246 Phosphotyrosine; by FES.
{ECO:0000269|PubMed:15302586}.
MOD_RES 356 356 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 382 382 Phosphoserine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 385 385 Phosphothreonine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 471 471 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q6PAJ1}.
MOD_RES 473 473 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 554 554 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 641 641 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 644 644 Phosphotyrosine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 693 693 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 894 894 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1264 1264 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
VAR_SEQ 961 1004 Missing (in isoform 2).
{ECO:0000303|PubMed:3285291}.
/FTId=VSP_024352.
VARIANT 400 400 S -> P (in a bladder transitional cell
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041883.
VARIANT 413 413 I -> M (in dbSNP:rs56321828).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041884.
VARIANT 558 558 K -> T (in dbSNP:rs4437065).
/FTId=VAR_051983.
VARIANT 752 752 D -> E (in dbSNP:rs12484731).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041885.
VARIANT 796 796 N -> S (in dbSNP:rs140504).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:2407300,
ECO:0000269|PubMed:3107980,
ECO:0000269|PubMed:3285291,
ECO:0000269|Ref.3}.
/FTId=VAR_031552.
VARIANT 910 910 Y -> C (in dbSNP:rs35537221).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041886.
VARIANT 949 949 V -> I (in dbSNP:rs2229038).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041887.
VARIANT 1037 1037 E -> K (in dbSNP:rs16999516).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_031553.
VARIANT 1091 1091 V -> M (in dbSNP:rs778229520).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041888.
VARIANT 1096 1096 T -> A (in dbSNP:rs745459086).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041889.
VARIANT 1104 1104 A -> G (in dbSNP:rs11558696).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041890.
VARIANT 1106 1106 D -> N (in dbSNP:rs879255379).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041891.
VARIANT 1127 1127 T -> M (in dbSNP:rs35812689).
/FTId=VAR_031554.
VARIANT 1149 1149 A -> T (in dbSNP:rs200099830).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041892.
VARIANT 1161 1161 E -> K. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041893.
VARIANT 1187 1187 K -> E. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_041894.
VARIANT 1189 1189 V -> M (in dbSNP:rs55816482).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041895.
VARIANT 1204 1204 A -> G (in dbSNP:rs56265970).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041896.
VARIANT 1235 1235 W -> R (in dbSNP:rs55719322).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041897.
MUTAGEN 177 177 Y->F: Abolishes interaction with FES and
GRB2. {ECO:0000269|PubMed:15302586,
ECO:0000269|PubMed:9407116}.
MUTAGEN 1269 1271 Missing: Abolishes interaction with
PDZK1. {ECO:0000269|PubMed:15494376}.
MUTAGEN 1271 1271 V->A: Reduces interaction with PDZK1.
{ECO:0000269|PubMed:15494376}.
CONFLICT 287 287 M -> I (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 418 418 G -> D (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 483 483 E -> K (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 560 560 F -> S (in Ref. 1; CAA68676).
{ECO:0000305}.
CONFLICT 690 690 E -> D (in Ref. 11). {ECO:0000305}.
CONFLICT 733 733 D -> E (in Ref. 4; CAA26441).
{ECO:0000305}.
HELIX 4 14 {ECO:0000244|PDB:1K1F}.
HELIX 28 64 {ECO:0000244|PDB:1K1F}.
STRAND 1268 1271 {ECO:0000244|PDB:2AIN}.
SEQUENCE 1271 AA; 142819 MW; 4BF66FA1E9D205FE CRC64;
MVDPVGFAEA WKAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ
TLLAKEKKSY DRQRWGFRRA AQAPDGASEP RASASRPQPA PADGADPPPA EEPEARPDGE
GSPGKARPGT ARRPGAAASG ERDDRGPPAS VAALRSNFER IRKGHGQPGA DAEKPFYVNV
EFHHERGLVK VNDKEVSDRI SSLGSQAMQM ERKKSQHGAG SSVGDASRPP YRGRSSESSC
GVDGDYEDAE LNPRFLKDNL IDANGGSRPP WPPLEYQPYQ SIYVGGMMEG EGKGPLLRSQ
STSEQEKRLT WPRRSYSPRS FEDCGGGYTP DCSSNENLTS SEEDFSSGQS SRVSPSPTTY
RMFRDKSRSP SQNSQQSFDS SSPPTPQCHK RHRHCPVVVS EATIVGVRKT GQIWPNDGEG
AFHGDADGSF GTPPGYGCAA DRAEEQRRHQ DGLPYIDDSP SSSPHLSSKG RGSRDALVSG
ALESTKASEL DLEKGLEMRK WVLSGILASE ETYLSHLEAL LLPMKPLKAA ATTSQPVLTS
QQIETIFFKV PELYEIHKEF YDGLFPRVQQ WSHQQRVGDL FQKLASQLGV YRAFVDNYGV
AMEMAEKCCQ ANAQFAEISE NLRARSNKDA KDPTTKNSLE TLLYKPVDRV TRSTLVLHDL
LKHTPASHPD HPLLQDALRI SQNFLSSINE EITPRRQSMT VKKGEHRQLL KDSFMVELVE
GARKLRHVFL FTDLLLCTKL KKQSGGKTQQ YDCKWYIPLT DLSFQMVDEL EAVPNIPLVP
DEELDALKIK ISQIKNDIQR EKRANKGSKA TERLKKKLSE QESLLLLMSP SMAFRVHSRN
GKSYTFLISS DYERAEWREN IREQQKKCFR SFSLTSVELQ MLTNSCVKLQ TVHSIPLTIN
KEDDESPGLY GFLNVIVHSA TGFKQSSNLY CTLEVDSFGY FVNKAKTRVY RDTAEPNWNE
EFEIELEGSQ TLRILCYEKC YNKTKIPKED GESTDRLMGK GQVQLDPQAL QDRDWQRTVI
AMNGIEVKLS VKFNSREFSL KRMPSRKQTG VFGVKIAVVT KRERSKVPYI VRQCVEEIER
RGMEEVGIYR VSGVATDIQA LKAAFDVNNK DVSVMMSEMD VNAIAGTLKL YFRELPEPLF
TDEFYPNFAE GIALSDPVAK ESCMLNLLLS LPEANLLTFL FLLDHLKRVA EKEAVNKMSL
HNLATVFGPT LLRPSEKESK LPANPSQPIT MTDSWSLEVM SQVQVLLYFL QLEAIPAPDS
KRQSILFSTE V


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