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Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (Cas scaffolding protein family member 1) (p130cas)

 BCAR1_HUMAN             Reviewed;         870 AA.
P56945; B3KWD7; B4DEV4; B4DGB5; B4DIW5; B7Z7X7; E9PCL5; E9PCV2;
F5GXA2; F5GXV6; F5H7Z0; F8WA69; Q6QEF7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
09-FEB-2010, sequence version 2.
22-NOV-2017, entry version 179.
RecName: Full=Breast cancer anti-estrogen resistance protein 1;
AltName: Full=CRK-associated substrate;
AltName: Full=Cas scaffolding protein family member 1;
AltName: Full=p130cas;
Name=BCAR1; Synonyms=CAS, CASS1, CRKAS;
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 VARIANT SER-76.
TISSUE=Mammary cancer;
PubMed=10639512; DOI=10.1093/jnci/92.2.112;
Brinkman A., van der Flier S., Kok E.M., Dorssers L.C.J.;
"BCAR1, a human homologue of the adapter protein p130Cas, induces
anti-estrogen resistance in breast cancer cells.";
J. Natl. Cancer Inst. 92:112-120(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
TISSUE=Testis;
Otto E., Birnbaum S., Verbeek M., Hildebrandt F.;
"Interaction between human Crk-associated substrate (p130Cas) and
nephrocystin.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
TISSUE=Cornea;
Imoto Y., Ohguro N., Yoshida A., Tsujikawa M., Inoue Y., Tano Y.;
"The effects of growth factors on tyrosine phosphorylation of p130Cas
in corneal epithelial cell.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Lin L., Li H., Zhou G., Shen C., Ke R., Zhong G., Yang S.;
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7 AND
8), AND VARIANT SER-76.
TISSUE=Amygdala, Caudate nucleus, Cerebellum, Hippocampus,
Teratocarcinoma, and Testis;
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 GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
PROTEIN SEQUENCE OF 1-9; 380-391 AND 792-801, ACETYLATION AT MET-1,
AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lempens A., Norman J.C.;
Submitted (OCT-2009) to UniProtKB.
[8]
INTERACTION WITH CSPG4.
PubMed=10587647; DOI=10.1038/70302;
Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
"Melanoma chondroitin sulphate proteoglycan regulates cell spreading
through Cdc42, Ack-1 and p130cas.";
Nat. Cell Biol. 1:507-513(1999).
[9]
INTERACTION WITH INPPL1.
PubMed=11158326; DOI=10.1128/MCB.21.4.1416-1428.2001;
Prasad N., Topping R.S., Decker S.J.;
"SH2-containing inositol 5'-phosphatase SHIP2 associates with the
p130(Cas) adapter protein and regulates cellular adhesion and
spreading.";
Mol. Cell. Biol. 21:1416-1428(2001).
[10]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
BMX.
PubMed=12832404; DOI=10.1074/jbc.M306438200;
Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.;
"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the
actin cytoskeleton and cell migration.";
J. Biol. Chem. 278:35636-35643(2003).
[11]
FUNCTION IN CELL MIGRATION, AND INTERACTION WITH BCAR1; CDC42 AND CRK.
PubMed=17038317; DOI=10.1074/jbc.M604342200;
Modzelewska K., Newman L.P., Desai R., Keely P.J.;
"Ack1 mediates Cdc42-dependent cell migration and signaling to
p130Cas.";
J. Biol. Chem. 281:37527-37535(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-139; THR-269
AND SER-292, 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).
[13]
PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, AND INTERACTION WITH
BCAR3.
PubMed=19454314; DOI=10.1016/j.cellsig.2009.05.006;
Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A.,
Cai D., Costello C.E., Lerner A.;
"AND-34/BCAR3 regulates adhesion-dependent p130Cas serine
phosphorylation and breast cancer cell growth pattern.";
Cell. Signal. 21:1423-1435(2009).
[14]
INTERACTION WITH PTK2B/PYK2.
PubMed=19086031; DOI=10.1002/jcp.21649;
Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A.;
"Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and
regulates human glomerular mesangial cell adhesion and spreading.";
J. Cell. Physiol. 219:45-56(2009).
[15]
PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1.
PubMed=19147981; DOI=10.1172/JCI37160;
Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F.,
Giancotti F.G.;
"Ras- and PI3K-dependent breast tumorigenesis in mice and humans
requires focal adhesion kinase signaling.";
J. Clin. Invest. 119:252-266(2009).
[16]
INTERACTION WITH PEAK1.
PubMed=20534451; DOI=10.1073/pnas.0914776107;
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
Yates J.R. III, Klemke R.L.;
"Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton
and cancer progression.";
Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010).
[17]
ERRATUM.
Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
Yates J.R. III, Klemke R.L.;
Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-139, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-639, 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).
[21]
DEPHOSPHORYLATION AT TYR-128 BY PTPN14, AND PHOSPHORYLATION AT TYR-128
BY SRC.
PubMed=22710723; DOI=10.1038/onc.2012.220;
Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C.,
Markowitz S.D., Polakiewicz R.D., Wang Z.;
"Identification and functional characterization of p130Cas as a
substrate of protein tyrosine phosphatase nonreceptor 14.";
Oncogene 32:2087-2095(2013).
[22]
X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 3-71.
PubMed=15784259; DOI=10.1016/j.jmb.2005.02.017;
Wisniewska M., Bossenmaier B., Georges G., Hesse F., Dangl M.,
Kunkele K.P., Ioannidis I., Huber R., Engh R.A.;
"The 1.1 A resolution crystal structure of the p130cas SH3 domain and
ramifications for ligand selectivity.";
J. Mol. Biol. 347:1005-1014(2005).
[23]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 645-870 IN COMPLEX WITH
SH2D3C.
PubMed=22081014; DOI=10.1038/nsmb.2152;
Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H.,
Pasquale E.B., Riedl S.J.;
"NSP-Cas protein structures reveal a promiscuous interaction module in
cell signaling.";
Nat. Struct. Mol. Biol. 18:1381-1387(2011).
[24]
VARIANT [LARGE SCALE ANALYSIS] THR-407.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Docking protein which plays a central coordinating role
for tyrosine kinase-based signaling related to cell adhesion.
Implicated in induction of cell migration. Overexpression confers
antiestrogen resistance on breast cancer cells.
{ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:17038317}.
-!- SUBUNIT: Forms complexes in vivo with PTK2/FAK1, adapter protein
CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with
BCAR3, the interaction regulates adhesion-dependent serine
phosphorylation. Interacts with NPHP1 and SH2D3C. Interacts with
activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part
of a collagen-stimulated complex involved in cell migration made
of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3
domains. Interacts with PTK2B/PYK2. {ECO:0000269|PubMed:10587647,
ECO:0000269|PubMed:11158326, ECO:0000269|PubMed:12832404,
ECO:0000269|PubMed:17038317, ECO:0000269|PubMed:19086031,
ECO:0000269|PubMed:19454314, ECO:0000269|PubMed:20534451,
ECO:0000269|PubMed:22081014}.
-!- INTERACTION:
O75815-1:BCAR3; NbExp=3; IntAct=EBI-702093, EBI-15953103;
P53618:COPB1; NbExp=4; IntAct=EBI-702093, EBI-359063;
P46108:CRK; NbExp=5; IntAct=EBI-702093, EBI-886;
P06241:FYN; NbExp=3; IntAct=EBI-702093, EBI-515315;
O15357:INPPL1; NbExp=2; IntAct=EBI-702093, EBI-1384248;
P46940:IQGAP1; NbExp=4; IntAct=EBI-702093, EBI-297509;
P50281:MMP14; NbExp=3; IntAct=EBI-702093, EBI-992788;
Q9H792:PEAK1; NbExp=3; IntAct=EBI-702093, EBI-2609701;
Q05397:PTK2; NbExp=2; IntAct=EBI-702093, EBI-702142;
P18031:PTPN1; NbExp=5; IntAct=EBI-702093, EBI-968788;
Q05209:PTPN12; NbExp=4; IntAct=EBI-702093, EBI-2266035;
Q8N5H7-2:SH2D3C; NbExp=8; IntAct=EBI-702093, EBI-15952996;
P12931:SRC; NbExp=3; IntAct=EBI-702093, EBI-621482;
Q9C0H9:SRCIN1; NbExp=3; IntAct=EBI-702093, EBI-1393949;
Q9QWI6:Srcin1 (xeno); NbExp=3; IntAct=EBI-702093, EBI-775592;
Q07912:TNK2; NbExp=5; IntAct=EBI-702093, EBI-603457;
Q04205:TNS (xeno); NbExp=2; IntAct=EBI-702093, EBI-2607590;
Q68CZ2:TNS3; NbExp=8; IntAct=EBI-702093, EBI-1220488;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
{ECO:0000269|PubMed:12832404}. Cytoplasm
{ECO:0000269|PubMed:12832404}. Note=Unphosphorylated form
localizes in the cytoplasm and can move to the membrane upon
tyrosine phosphorylation. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1;
IsoId=P56945-1; Sequence=Displayed;
Name=2;
IsoId=P56945-2; Sequence=VSP_043559;
Note=No experimental confirmation available.;
Name=3;
IsoId=P56945-3; Sequence=VSP_045355;
Name=4;
IsoId=P56945-4; Sequence=VSP_046127, VSP_046128;
Note=No experimental confirmation available.;
Name=5;
IsoId=P56945-5; Sequence=VSP_046748;
Note=No experimental confirmation available.;
Name=6;
IsoId=P56945-6; Sequence=VSP_046749;
Note=No experimental confirmation available.;
Name=7;
IsoId=P56945-7; Sequence=VSP_046750;
Note=No experimental confirmation available.;
Name=8;
IsoId=P56945-8; Sequence=VSP_046751;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with an abundant expression
in the testis. Low level of expression seen in the liver, thymus,
and peripheral blood leukocytes. The protein has been detected in
a B-cell line.
-!- DOMAIN: Contains a central domain (substrate domain) containing
multiple potential SH2-binding sites and a C-terminal domain
containing a divergent helix-loop-helix (HLH) motif. The SH2-
binding sites putatively bind CRK, NCK and ABL1 SH2 domains. The
HLH motif is absolutely required for the induction of pseudohyphal
growth in yeast and mediates heterodimerization with NEDD9 (By
similarity). {ECO:0000250}.
-!- DOMAIN: A serine-rich region promotes activation of the serum
response element (SRE).
-!- DOMAIN: The SH3 domain is necessary for the localization of the
protein to focal adhesions and interacts with one proline-rich
region of PTK2/FAK11.
-!- PTM: PTK2/FAK1 activation mediates phosphorylation at the YDYVHL
motif; phosphorylation is most likely catalyzed by SRC family
members. SRC-family kinases are recruited to the phosphorylated
sites and can phosphorylate other tyrosine residues. Tyrosine
phosphorylation is triggered by integrin-mediated adhesion of
cells to the extracellular matrix. {ECO:0000269|PubMed:12832404,
ECO:0000269|PubMed:19147981, ECO:0000269|PubMed:19454314,
ECO:0000269|PubMed:22710723}.
-!- PTM: Dephosphorylated by PTPN14 at Tyr-128.
-!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/BCAR1ID761ch16q23.html";
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EMBL; AJ242987; CAB75875.2; -; mRNA.
EMBL; AF218451; AAF27527.1; -; mRNA.
EMBL; AB040024; BAA92711.1; -; mRNA.
EMBL; AY545071; AAS48631.1; -; mRNA.
EMBL; AK027608; BAB55230.1; -; mRNA.
EMBL; AK124815; BAG54099.1; -; mRNA.
EMBL; AK293808; BAG57215.1; -; mRNA.
EMBL; AK294513; BAG57726.1; -; mRNA.
EMBL; AK295809; BAG58627.1; -; mRNA.
EMBL; AK302617; BAH13763.1; -; mRNA.
EMBL; AC009078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS10915.1; -. [P56945-1]
CCDS; CCDS54037.1; -. [P56945-5]
CCDS; CCDS54038.1; -. [P56945-3]
CCDS; CCDS54039.1; -. [P56945-4]
CCDS; CCDS54040.1; -. [P56945-6]
CCDS; CCDS54041.1; -. [P56945-8]
CCDS; CCDS54042.1; -. [P56945-2]
CCDS; CCDS54043.1; -. [P56945-7]
RefSeq; NP_001164185.1; NM_001170714.1. [P56945-6]
RefSeq; NP_001164186.1; NM_001170715.1. [P56945-7]
RefSeq; NP_001164187.1; NM_001170716.1. [P56945-2]
RefSeq; NP_001164188.1; NM_001170717.1. [P56945-3]
RefSeq; NP_001164189.1; NM_001170718.1. [P56945-8]
RefSeq; NP_001164190.1; NM_001170719.1. [P56945-5]
RefSeq; NP_001164191.1; NM_001170720.1. [P56945-4]
RefSeq; NP_055382.2; NM_014567.3. [P56945-1]
RefSeq; XP_016879386.1; XM_017023897.1. [P56945-6]
UniGene; Hs.479747; -.
PDB; 1WYX; X-ray; 1.14 A; A/B=3-71.
PDB; 3T6G; X-ray; 2.50 A; B/D=645-870.
PDBsum; 1WYX; -.
PDBsum; 3T6G; -.
ProteinModelPortal; P56945; -.
SMR; P56945; -.
BioGrid; 114934; 68.
CORUM; P56945; -.
DIP; DIP-33855N; -.
ELM; P56945; -.
IntAct; P56945; 261.
MINT; MINT-1505539; -.
STRING; 9606.ENSP00000391669; -.
iPTMnet; P56945; -.
PhosphoSitePlus; P56945; -.
BioMuta; BCAR1; -.
DMDM; 288558806; -.
EPD; P56945; -.
MaxQB; P56945; -.
PaxDb; P56945; -.
PeptideAtlas; P56945; -.
PRIDE; P56945; -.
DNASU; 9564; -.
Ensembl; ENST00000162330; ENSP00000162330; ENSG00000050820. [P56945-1]
Ensembl; ENST00000393420; ENSP00000377072; ENSG00000050820. [P56945-3]
Ensembl; ENST00000393422; ENSP00000377074; ENSG00000050820. [P56945-7]
Ensembl; ENST00000418647; ENSP00000391669; ENSG00000050820. [P56945-6]
Ensembl; ENST00000420641; ENSP00000392708; ENSG00000050820. [P56945-2]
Ensembl; ENST00000535626; ENSP00000440370; ENSG00000050820. [P56945-4]
Ensembl; ENST00000538440; ENSP00000443841; ENSG00000050820. [P56945-8]
Ensembl; ENST00000542031; ENSP00000440415; ENSG00000050820. [P56945-5]
GeneID; 9564; -.
KEGG; hsa:9564; -.
UCSC; uc002fdv.4; human. [P56945-1]
CTD; 9564; -.
DisGeNET; 9564; -.
EuPathDB; HostDB:ENSG00000050820.16; -.
GeneCards; BCAR1; -.
H-InvDB; HIX0173293; -.
HGNC; HGNC:971; BCAR1.
HPA; CAB000443; -.
HPA; HPA042282; -.
MIM; 602941; gene.
neXtProt; NX_P56945; -.
OpenTargets; ENSG00000050820; -.
PharmGKB; PA25281; -.
eggNOG; ENOG410IEDD; Eukaryota.
eggNOG; ENOG410ZSUM; LUCA.
GeneTree; ENSGT00490000043324; -.
HOGENOM; HOG000261698; -.
HOVERGEN; HBG004354; -.
InParanoid; P56945; -.
KO; K05726; -.
OMA; LANMPDY; -.
OrthoDB; EOG091G0RVA; -.
PhylomeDB; P56945; -.
TreeFam; TF328782; -.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
SignaLink; P56945; -.
SIGNOR; P56945; -.
ChiTaRS; BCAR1; human.
EvolutionaryTrace; P56945; -.
GeneWiki; BCAR1; -.
GenomeRNAi; 9564; -.
PRO; PR:P56945; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000050820; -.
CleanEx; HS_BCAR1; -.
ExpressionAtlas; P56945; baseline and differential.
Genevisible; P56945; HS.
GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
GO; GO:0050851; P:antigen receptor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; IMP:BHF-UCL.
GO; GO:0051301; P:cell division; NAS:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:BHF-UCL.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; NAS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
CDD; cd12001; SH3_BCAR1; 1.
InterPro; IPR028848; BCAR1.
InterPro; IPR035745; BCAR1_SH3.
InterPro; IPR021901; CAS_C.
InterPro; IPR014928; Serine_rich.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR10654:SF15; PTHR10654:SF15; 1.
Pfam; PF12026; DUF3513; 1.
Pfam; PF08824; Serine_rich; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell adhesion;
Cell junction; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Polymorphism;
Reference proteome; SH3 domain; SH3-binding.
CHAIN 1 870 Breast cancer anti-estrogen resistance
protein 1.
/FTId=PRO_0000064854.
DOMAIN 3 65 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 115 416 Substrate for kinases. {ECO:0000250}.
REGION 746 796 Divergent helix-loop-helix motif.
MOTIF 635 643 SH3-binding. {ECO:0000255}.
COMPBIAS 74 87 Pro-rich.
COMPBIAS 422 614 Ser-rich.
MOD_RES 1 1 N-acetylmethionine. {ECO:0000269|Ref.7}.
MOD_RES 128 128 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:22710723}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19454314}.
MOD_RES 234 234 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 249 249 Phosphotyrosine; by ABL1.
{ECO:0000250|UniProtKB:Q63767}.
MOD_RES 269 269 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 292 292 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 362 362 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 372 372 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 410 410 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q61140}.
MOD_RES 428 428 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000269|PubMed:19454314}.
MOD_RES 639 639 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:19454314}.
VAR_SEQ 1 4 MNHL -> MLTHRPQEAEQRGRTPGPSFEW (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043559.
VAR_SEQ 1 4 MNHL -> MQGK (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046127.
VAR_SEQ 1 4 MNHL -> ME (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046748.
VAR_SEQ 1 4 MNHL -> MPAKPFLSSVLLSWKVLDFSGPGPQGTGQPCSC
GHWAEGQGGPPEPAGGP (in isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046749.
VAR_SEQ 1 4 MNHL -> MHCPGEAPLAAPRPTPKDPCLR (in
isoform 7).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046750.
VAR_SEQ 1 4 MNHL -> MSVP (in isoform 8).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046751.
VAR_SEQ 64 211 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046128.
VAR_SEQ 304 304 A -> AVSKCQGNARARLRLWGVW (in isoform 3).
{ECO:0000303|Ref.4}.
/FTId=VSP_045355.
VARIANT 76 76 P -> S (in dbSNP:rs1035539).
{ECO:0000269|PubMed:10639512,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_058970.
VARIANT 407 407 S -> T (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035798.
VARIANT 491 491 R -> L (in dbSNP:rs16957558).
/FTId=VAR_057820.
VARIANT 558 558 H -> R (in dbSNP:rs16957552).
/FTId=VAR_057821.
CONFLICT 63 63 L -> S (in Ref. 5; BAB55230).
{ECO:0000305}.
CONFLICT 236 236 I -> T (in Ref. 2; AAF27527).
{ECO:0000305}.
CONFLICT 254 254 V -> I (in Ref. 5; BAG54099).
{ECO:0000305}.
CONFLICT 349 349 A -> G (in Ref. 2; AAF27527).
{ECO:0000305}.
CONFLICT 363 363 D -> Y (in Ref. 2; AAF27527).
{ECO:0000305}.
CONFLICT 385 385 T -> A (in Ref. 4; AAS48631).
{ECO:0000305}.
CONFLICT 428 428 S -> P (in Ref. 5; BAB55230).
{ECO:0000305}.
CONFLICT 471 471 S -> G (in Ref. 5; BAB55230).
{ECO:0000305}.
CONFLICT 600 600 N -> S (in Ref. 4; AAS48631).
{ECO:0000305}.
CONFLICT 700 700 Q -> R (in Ref. 5; BAH13763).
{ECO:0000305}.
CONFLICT 714 714 P -> L (in Ref. 5; BAG54099).
{ECO:0000305}.
CONFLICT 740 740 D -> G (in Ref. 4; AAS48631).
{ECO:0000305}.
STRAND 5 12 {ECO:0000244|PDB:1WYX}.
STRAND 29 34 {ECO:0000244|PDB:1WYX}.
HELIX 37 39 {ECO:0000244|PDB:1WYX}.
STRAND 43 48 {ECO:0000244|PDB:1WYX}.
STRAND 51 56 {ECO:0000244|PDB:1WYX}.
HELIX 57 59 {ECO:0000244|PDB:1WYX}.
STRAND 60 68 {ECO:0000244|PDB:1WYX}.
HELIX 740 770 {ECO:0000244|PDB:3T6G}.
HELIX 775 801 {ECO:0000244|PDB:3T6G}.
HELIX 806 835 {ECO:0000244|PDB:3T6G}.
HELIX 840 870 {ECO:0000244|PDB:3T6G}.
SEQUENCE 870 AA; 93372 MW; B81EC3430049E795 CRC64;
MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG RQGIVPGNRL
KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT PMLPNTYQPQ PDSVYLVPTP
SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ
VPPSAGMGHD IYQVPPSMDT RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL
LAPGPQDIYD VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS
NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA PPPDSPPAED
VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA DGGVVDSGVY AVPPPAEREA
PAEGKRLSAS STGSTRSSQS ASSLEVAGPG REPLELEVAV EALARLQQGV SATVAHLLDL
AGSAGATGSW RSPSEPQEPL VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK
LSRQLQKMED VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN
ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD GQYENSEGGW
MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ LKQFERLEQE VSRPIDHDLA
NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ CEANLTTLTN AVDAFFTAVA TNQPPKIFVA
HSKFVILSAH KLVFIGDTLS RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP
SAAQDMVERV KELGHSTQQF RRVLGQLAAA


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