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 24-JAN-2024, entry version 202. 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. Interacts (when CC tyrosine-phosphorylated) with tensin TNS1; the interaction is increased CC by phosphorylation of TNS1 (By similarity). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 17. 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; 10090-ENSMUSP00000129584; -. DR ProteomicsDB; 273441; -. [Q61140-1] DR ProteomicsDB; 273442; -. [Q61140-2] DR Pumba; Q61140; -. DR Antibodypedia; 3607; 968 antibodies from 41 providers. DR DNASU; 12927; -. DR Ensembl; ENSMUST00000166232.4; ENSMUSP00000129584.3; ENSMUSG00000031955.11. [Q61140-1] DR Ensembl; ENSMUST00000212349.2; ENSMUSP00000148364.2; ENSMUSG00000031955.11. [Q61140-2] DR GeneID; 12927; -. DR KEGG; mmu:12927; -. DR UCSC; uc009nmt.2; mouse. [Q61140-2] DR UCSC; uc009nmu.2; mouse. [Q61140-1] DR AGR; MGI:108091; -. 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; THAIDAF; -. DR OrthoDB; 2902504at2759; -. 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 78 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 261 other cell types or tissues. 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; IEA:Ensembl. 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: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; cd11569; FAT-like_BCAR1_C; 1. DR CDD; cd11552; Serine_rich_BCAR1; 1. DR CDD; cd12001; SH3_BCAR1; 1. DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 1. DR Gene3D; 1.20.120.830; Serine-rich domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR046976; BCAR1_C. 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:SF15; BREAST CANCER ANTI-ESTROGEN RESISTANCE PROTEIN 1; 1. DR PANTHER; PTHR10654; CAS SCAFFOLDING PROTEIN; 1. DR Pfam; PF12026; CAS_C; 1. DR Pfam; PF08824; Serine_rich; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR PRINTS; PR01887; SPECTRNALPHA. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q61140; MM. 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 //