BCAR1_MOUSE
ID BCAR1_MOUSE Reviewed; 874 AA.
AC Q61140; Q60869; Q6PFF9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Breast cancer anti-estrogen resistance protein 1;
DE AltName: Full=CRK-associated substrate;
DE AltName: Full=p130cas;
GN Name=Bcar1; Synonyms=Cas, Crkas;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CAS-A AND CAS-B), AND INTERACTION WITH
RP PTK2/FAK1.
RC TISSUE=Embryo;
RX PubMed=7479864; DOI=10.1073/pnas.92.23.10678;
RA Polte T.R., Hanks S.K.;
RT "Interaction between focal adhesion kinase and Crk-associated tyrosine
RT kinase substrate p130Cas.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10678-10682(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH BCAR3.
RX PubMed=10438950;
RA Cai D., Clayton L.K., Smolyar A., Lerner A.;
RT "AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by
RT adhesion and inflammatory cytokines.";
RL J. Immunol. 163:2104-2112(1999).
RN [5]
RP INTERACTION WITH NPHP1.
RX PubMed=10739664; DOI=10.1006/excr.2000.4822;
RA Donaldson J.C., Dempsey P.J., Reddy S., Bouton A.H., Coffey R.J.,
RA Hanks S.K.;
RT "Crk-associated substrate p130(Cas) interacts with nephrocystin and both
RT proteins localize to cell-cell contacts of polarized epithelial cells.";
RL Exp. Cell Res. 256:168-178(2000).
RN [6]
RP INTERACTION WITH BCAR3.
RX PubMed=10896938; DOI=10.1074/jbc.m003074200;
RA Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
RT "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras
RT guanine nucleotide exchange factor.";
RL J. Biol. Chem. 275:30118-30123(2000).
RN [7]
RP INTERACTION WITH SH2D3C.
RX PubMed=10692442; DOI=10.1074/jbc.275.9.6404;
RA Sakakibara A., Hattori S.;
RT "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple
RT signaling pathways.";
RL J. Biol. Chem. 275:6404-6410(2000).
RN [8]
RP INTERACTION WITH SH2D3C.
RC TISSUE=Spleen;
RX PubMed=12486027; DOI=10.1074/jbc.m207942200;
RA Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
RT "A novel hematopoietic adaptor protein, Chat-H, positively regulates T cell
RT receptor-mediated interleukin-2 production by Jurkat cells.";
RL J. Biol. Chem. 278:6012-6017(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132; TYR-366; TYR-376 AND
RP TYR-414, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [10]
RP INTERACTION WITH SH2D3C.
RX PubMed=17174122; DOI=10.1016/j.immuni.2006.09.014;
RA Regelmann A.G., Danzl N.M., Wanjalla C., Alexandropoulos K.;
RT "The hematopoietic isoform of Cas-Hef1-associated signal transducer
RT regulates chemokine-induced inside-out signaling and T cell trafficking.";
RL Immunity 25:907-918(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=19365570;
RA Near R.I., Smith R.S., Toselli P.A., Freddo T.F., Bloom A.B.,
RA Vanden Borre P., Seldin D.C., Lerner A.;
RT "Loss of AND-34/BCAR3 expression in mice results in rupture of the adult
RT lens.";
RL Mol. Vis. 15:685-699(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [15]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20881139; DOI=10.1523/jneurosci.3289-10.2010;
RA Wang L., Vervoort V., Wallez Y., Core N., Cremer H., Pasquale E.B.;
RT "The SRC homology 2 domain protein Shep1 plays an important role in the
RT penetration of olfactory sensory axons into the forebrain.";
RL J. Neurosci. 30:13201-13210(2010).
RN [16]
RP IDENTIFICATION IN A COMPLEX WITH PTPRA; BCAR3 AND SRC, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22801373; DOI=10.1128/mcb.00214-12;
RA Sun G., Cheng S.Y., Chen M., Lim C.J., Pallen C.J.;
RT "Protein tyrosine phosphatase alpha phosphotyrosyl-789 binds BCAR3 to
RT position Cas for activation at integrin-mediated focal adhesions.";
RL Mol. Cell. Biol. 32:3776-3789(2012).
RN [17]
RP FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3.
RX PubMed=25499443; DOI=10.1186/s13058-014-0476-9;
RA Guo J., Canaff L., Rajadurai C.V., Fils-Aime N., Tian J., Dai M., Korah J.,
RA Villatoro M., Park M., Ali S., Lebrun J.J.;
RT "Breast cancer anti-estrogen resistance 3 inhibits transforming growth
RT factor beta/Smad signaling and associates with favorable breast cancer
RT disease outcomes.";
RL Breast Cancer Res. 16:476-476(2014).
CC -!- FUNCTION: Docking protein which plays a central coordinating role for
CC tyrosine kinase-based signaling related to cell adhesion (By
CC similarity). Implicated in induction of cell migration and cell
CC branching (PubMed:25499443). Involved in the BCAR3-mediated inhibition
CC of TGFB signaling (PubMed:25499443). {ECO:0000250|UniProtKB:P56945,
CC ECO:0000269|PubMed:25499443}.
CC -!- SUBUNIT: Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL
CC and LYN kinase. Can heterodimerize with NEDD9. Component of a complex
CC comprised of SH2D3C, BCAR1/CAS, and CRK (By similarity). Within the
CC complex, interacts with SH2D3C (via C-terminus), and CRK (By
CC similarity). Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via
CC SH2 domain) and SRC; the formation of the complex is dependent on
CC intergrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373).
CC Interacts with BCAR3 (via Ras-GEF domain); the interaction regulates
CC adhesion-dependent serine phosphorylation (PubMed:10896938,
CC PubMed:22801373). Interacts with SMAD2 and SMAD3 (PubMed:25499443).
CC Interacts with NPHP1 (PubMed:10739664). Interacts with PTK2B/PYK2 (By
CC similarity). Interacts (via C-terminus) with SH2D3C/CHAT isoform 2 (via
CC C-terminus) (PubMed:10692442, PubMed:12486027, PubMed:17174122).
CC Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and
CC PEAK1 (By similarity). Part of a collagen stimulated complex involved
CC in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By
CC similarity). Interacts with TNK2 via SH3 domains. {ECO:0000250,
CC ECO:0000250|UniProtKB:P56945, ECO:0000269|PubMed:10438950,
CC ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:10739664,
CC ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12486027,
CC ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:22801373,
CC ECO:0000269|PubMed:25499443, ECO:0000269|PubMed:7479864}.
CC -!- INTERACTION:
CC Q61140; Q9QY53: Nphp1; NbExp=2; IntAct=EBI-77088, EBI-77230;
CC Q61140; P34152: Ptk2; NbExp=3; IntAct=EBI-77088, EBI-77070;
CC Q61140; Q9QWI6: Srcin1; NbExp=2; IntAct=EBI-77088, EBI-775592;
CC Q61140; P18031: PTPN1; Xeno; NbExp=5; IntAct=EBI-77088, EBI-968788;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:22801373}. Cytoplasm {ECO:0000269|PubMed:22801373}.
CC Cell projection, axon {ECO:0000269|PubMed:20881139}.
CC Note=Unphosphorylated form localizes in the cytoplasm
CC (PubMed:22801373). Localizes to focal adhesion sites following integrin
CC engagement (PubMed:22801373). {ECO:0000269|PubMed:22801373}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Cas-B;
CC IsoId=Q61140-1; Sequence=Displayed;
CC Name=Cas-A;
CC IsoId=Q61140-2; Sequence=VSP_004134;
CC -!- TISSUE SPECIFICITY: Expressed in olfactory sensory neurons (at protein
CC level) (PubMed:20881139). Expressed abundantly in the liver, lung,
CC brain, and at lower levels in the heart (at protein level)
CC (PubMed:19365570). {ECO:0000269|PubMed:19365570,
CC ECO:0000269|PubMed:20881139}.
CC -!- DOMAIN: Contains a central domain (substrate domain) containing
CC multiple potential SH2-binding sites and a C-terminal domain containing
CC a divergent helix-loop-helix (HLH) motif. The SH2-binding sites
CC putatively bind CRK, NCK and ABL SH2 domains. The HLH motif is
CC absolutely required for the induction of pseudohyphal growth in yeast
CC and mediates heterodimerization with NEDD9.
CC -!- DOMAIN: A serine-rich region promotes activation of the serum response
CC element (SRE). {ECO:0000250}.
CC -!- DOMAIN: The SH3 domain is necessary for the localization of the protein
CC to focal adhesions and interacts with one proline-rich region of
CC PTK2/FAK1.
CC -!- PTM: PTK2/FAK1 activation mediates phosphorylation at the YDYVHL motif;
CC phosphorylation is most likely catalyzed by SRC family members. SRC-
CC family kinases are recruited to the phosphorylated sites and can
CC phosphorylate other tyrosine residues. Tyrosine phosphorylation is
CC triggered by integrin mediated adhesion of cells to the extracellular
CC matrix (By similarity). {ECO:0000250}.
CC -!- PTM: Dephosphorylated by PTPN14 at Tyr-132. {ECO:0000250}.
CC -!- PTM: Phosphorylated by SRC kinase in a EDN1- and PTK2B-mediated manner;
CC phosphorylation strengthens its interaction with BCAR3 as part of the
CC PTK2B/BCAR1/BCAR3/RAP1 signaling pathway.
CC {ECO:0000250|UniProtKB:P56945}.
CC -!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
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DR EMBL; U48853; AAA93381.1; -; mRNA.
DR EMBL; U28151; AAA93248.1; -; mRNA.
DR EMBL; AK145863; BAE26705.1; -; mRNA.
DR EMBL; BC057578; AAH57578.1; -; mRNA.
DR CCDS; CCDS52675.1; -. [Q61140-1]
DR CCDS; CCDS85616.1; -. [Q61140-2]
DR RefSeq; NP_001185768.1; NM_001198839.1. [Q61140-2]
DR RefSeq; NP_034084.2; NM_009954.3. [Q61140-1]
DR PDB; 5W93; X-ray; 2.00 A; A/B/C=738-874.
DR PDBsum; 5W93; -.
DR AlphaFoldDB; Q61140; -.
DR SMR; Q61140; -.
DR BioGRID; 198886; 16.
DR CORUM; Q61140; -.
DR IntAct; Q61140; 13.
DR MINT; Q61140; -.
DR STRING; 10090.ENSMUSP00000129584; -.
DR iPTMnet; Q61140; -.
DR PhosphoSitePlus; Q61140; -.
DR MaxQB; Q61140; -.
DR PaxDb; Q61140; -.
DR PRIDE; Q61140; -.
DR ProteomicsDB; 273441; -. [Q61140-1]
DR ProteomicsDB; 273442; -. [Q61140-2]
DR Antibodypedia; 3607; 847 antibodies from 41 providers.
DR DNASU; 12927; -.
DR Ensembl; ENSMUST00000166232; ENSMUSP00000129584; ENSMUSG00000031955. [Q61140-1]
DR Ensembl; ENSMUST00000212349; ENSMUSP00000148364; ENSMUSG00000031955. [Q61140-2]
DR GeneID; 12927; -.
DR KEGG; mmu:12927; -.
DR UCSC; uc009nmt.2; mouse. [Q61140-2]
DR UCSC; uc009nmu.2; mouse. [Q61140-1]
DR CTD; 9564; -.
DR MGI; MGI:108091; Bcar1.
DR VEuPathDB; HostDB:ENSMUSG00000031955; -.
DR eggNOG; ENOG502QQHE; Eukaryota.
DR GeneTree; ENSGT00950000183008; -.
DR HOGENOM; CLU_017000_1_0_1; -.
DR InParanoid; Q61140; -.
DR OMA; AQDVRHK; -.
DR OrthoDB; 1086228at2759; -.
DR PhylomeDB; Q61140; -.
DR TreeFam; TF328782; -.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR BioGRID-ORCS; 12927; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Bcar1; mouse.
DR PRO; PR:Q61140; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q61140; protein.
DR Bgee; ENSMUSG00000031955; Expressed in endothelial cell of lymphatic vessel and 257 other tissues.
DR Genevisible; Q61140; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0016020; C:membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR GO; GO:0016477; P:cell migration; IDA:MGI.
DR GO; GO:1990859; P:cellular response to endothelin; ISO:MGI.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:MGI.
DR GO; GO:0071732; P:cellular response to nitric oxide; ISO:MGI.
DR GO; GO:0086100; P:endothelin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; ISO:MGI.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
DR CDD; cd12001; SH3_BCAR1; 1.
DR Gene3D; 1.20.120.830; -; 1.
DR InterPro; IPR028848; BCAR1.
DR InterPro; IPR035745; BCAR1_SH3.
DR InterPro; IPR021901; CAS_C.
DR InterPro; IPR037362; CAS_fam.
DR InterPro; IPR014928; Serine_rich_dom.
DR InterPro; IPR038319; Serine_rich_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10654; PTHR10654; 1.
DR PANTHER; PTHR10654:SF15; PTHR10654:SF15; 1.
DR Pfam; PF12026; CAS_C; 1.
DR Pfam; PF08824; Serine_rich; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell adhesion;
KW Cell junction; Cell projection; Cytoplasm; Phosphoprotein;
KW Reference proteome; SH3 domain; SH3-binding.
FT CHAIN 1..874
FT /note="Breast cancer anti-estrogen resistance protein 1"
FT /id="PRO_0000064855"
FT DOMAIN 3..65
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 71..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..420
FT /note="Substrate for kinases"
FT /evidence="ECO:0000250"
FT REGION 374..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 750..800
FT /note="Divergent helix-loop-helix motif"
FT MOTIF 639..647
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT MOD_RES 132
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT MOD_RES 238
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 273
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT MOD_RES 366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 376
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 414
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56945"
FT VAR_SEQ 1..4
FT /note="MTVP -> MKYL (in isoform Cas-A)"
FT /evidence="ECO:0000303|PubMed:7479864"
FT /id="VSP_004134"
FT CONFLICT 72
FT /note="V -> A (in Ref. 1; AAA93381/AAA93248)"
FT /evidence="ECO:0000305"
FT HELIX 742..774
FT /evidence="ECO:0007829|PDB:5W93"
FT HELIX 779..806
FT /evidence="ECO:0007829|PDB:5W93"
FT HELIX 810..839
FT /evidence="ECO:0007829|PDB:5W93"
FT HELIX 844..872
FT /evidence="ECO:0007829|PDB:5W93"
SQ SEQUENCE 874 AA; 94285 MW; 81E56BC7AD87B095 CRC64;
MTVPNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG RQGIVPGNRL
KILVGMYDKK PVGPGPGPPA TPPQPQPSLP QGVHAPVPPA SQYSPMLPTA YQPQSDNVYL
VPTPSKTQQG LYQAPGPNPQ FQSPPAKQTS TFSKQTPHHS FPSPATDLYQ VPPGPGSPAQ
DIYQVPPSAG IGHDIYQVPP SLDTRGWEGT KPPAKVVVPT RVGQGYVYEA AQTEQDEYDT
PRHLLAPGPQ DIYDVPPVRG LLPNQYGQEV YDTPPMAVKG PNGRDPLLDV YDVPPSVEKG
LLSSSHHSVY DVPPSVSKDV PDGPLLREET YDVPPAFAKP KPFDPTRHPL ILAAPPPDSP
AAEDVYDVPP PAPDLYDVPP GLRRPGPGTL YDVPRERVLP PEVADGSVVD DGVYAVPPPA
EREAPTDGKR LSASSTGSTR SSQSASSLEV VVPGREPLEL EVAVESLARL QQGVSTTVAH
LLDLVGSASG PGGWRGTSEP QEPPAQDLKA AVAAVHGAVH ELLEFARGAV SNATHTSDRT
LHAKLSRQLQ KMEDVYQTLV VHGQVLDSGR GSPGFTPEDL DRLVACSRAV PEDAKQLASF
LHGNASLLFR RTKAPGPGPE GSSSLHPNPT DKASSIQSRP LPSPPKFTSQ DSPDGQYENS
EGGWMEDYDY VHLQGKEEFE KTQKELLERG NIMRQGKGQL ELQQLKQFER LEQEVSRPID
HDLANWTPAQ PLVPGRTGGL GPSDRQLLLF YLEQCEANLT TLTDAVDAFF TAVATNQPPK
IFVAHSKFVI LSAHKLVFIG DTLSRQAKAA DVRSQVTHYS NLLCDLLRGI VATTKAAALQ
YPSPSAAQDM VDRVKELGHS TQQFRRVLGQ LAAA
