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Database: UniProt
Entry: P56945
LinkDB: P56945
Original site: P56945 
ID   BCAR1_HUMAN             Reviewed;         870 AA.
AC   P56945; B3KWD7; B4DEV4; B4DGB5; B4DIW5; B7Z7X7; E9PCL5; E9PCV2; F5GXA2;
AC   F5GXV6; F5H7Z0; F8WA69; Q6QEF7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 2.
DT   07-OCT-2020, entry version 202.
DE   RecName: Full=Breast cancer anti-estrogen resistance protein 1;
DE   AltName: Full=CRK-associated substrate;
DE   AltName: Full=Cas scaffolding protein family member 1;
DE   AltName: Full=p130cas;
GN   Name=BCAR1; Synonyms=CAS, CASS1, CRKAS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
RC   TISSUE=Mammary cancer;
RX   PubMed=10639512; DOI=10.1093/jnci/92.2.112;
RA   Brinkman A., van der Flier S., Kok E.M., Dorssers L.C.J.;
RT   "BCAR1, a human homologue of the adapter protein p130Cas, induces anti-
RT   estrogen resistance in breast cancer cells.";
RL   J. Natl. Cancer Inst. 92:112-120(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
RC   TISSUE=Testis;
RA   Otto E., Birnbaum S., Verbeek M., Hildebrandt F.;
RT   "Interaction between human Crk-associated substrate (p130Cas) and
RT   nephrocystin.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-76.
RC   TISSUE=Cornea;
RA   Imoto Y., Ohguro N., Yoshida A., Tsujikawa M., Inoue Y., Tano Y.;
RT   "The effects of growth factors on tyrosine phosphorylation of p130Cas in
RT   corneal epithelial cell.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Lin L., Li H., Zhou G., Shen C., Ke R., Zhong G., Yang S.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5; 6; 7 AND 8),
RP   AND VARIANT SER-76.
RC   TISSUE=Amygdala, Caudate nucleus, Cerebellum, Hippocampus, Teratocarcinoma,
RC   and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15616553; DOI=10.1038/nature03187;
RA   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA   Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA   Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA   Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA   Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA   Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA   Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA   Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA   Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA   Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA   Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA   Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA   Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA   Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA   Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA   Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA   Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA   Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA   DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA   Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA   Myers R.M., Rubin E.M., Pennacchio L.A.;
RT   "The sequence and analysis of duplication-rich human chromosome 16.";
RL   Nature 432:988-994(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-9; 380-391 AND 792-801, ACETYLATION AT MET-1, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Ovarian carcinoma;
RA   Bienvenut W.V., Lempens A., Norman J.C.;
RL   Submitted (OCT-2009) to UniProtKB.
RN   [8]
RP   INTERACTION WITH CSPG4.
RX   PubMed=10587647; DOI=10.1038/70302;
RA   Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L.,
RA   Tachibana K., Lim L., Manser E., Furcht L.T., Iida J.;
RT   "Melanoma chondroitin sulphate proteoglycan regulates cell spreading
RT   through Cdc42, Ack-1 and p130cas.";
RL   Nat. Cell Biol. 1:507-513(1999).
RN   [9]
RP   INTERACTION WITH INPPL1.
RX   PubMed=11158326; DOI=10.1128/mcb.21.4.1416-1428.2001;
RA   Prasad N., Topping R.S., Decker S.J.;
RT   "SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas)
RT   adapter protein and regulates cellular adhesion and spreading.";
RL   Mol. Cell. Biol. 21:1416-1428(2001).
RN   [10]
RP   FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH SH2D3C AND CRK.
RX   PubMed=12432078; DOI=10.1242/jcs.00207;
RA   Sakakibara A., Ohba Y., Kurokawa K., Matsuda M., Hattori S.;
RT   "Novel function of Chat in controlling cell adhesion via Cas-Crk-C3G-
RT   pathway-mediated Rap1 activation.";
RL   J. Cell Sci. 115:4915-4924(2002).
RN   [11]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH BMX.
RX   PubMed=12832404; DOI=10.1074/jbc.m306438200;
RA   Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K.;
RT   "p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin
RT   cytoskeleton and cell migration.";
RL   J. Biol. Chem. 278:35636-35643(2003).
RN   [12]
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   [13]
RP   FUNCTION IN CELL MIGRATION, AND INTERACTION WITH BCAR1; CDC42 AND CRK.
RX   PubMed=17038317; DOI=10.1074/jbc.m604342200;
RA   Modzelewska K., Newman L.P., Desai R., Keely P.J.;
RT   "Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas.";
RL   J. Biol. Chem. 281:37527-37535(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-139; THR-269 AND
RP   SER-292, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [15]
RP   PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, AND INTERACTION WITH
RP   BCAR3.
RX   PubMed=19454314; DOI=10.1016/j.cellsig.2009.05.006;
RA   Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A., Cai D.,
RA   Costello C.E., Lerner A.;
RT   "AND-34/BCAR3 regulates adhesion-dependent p130Cas serine phosphorylation
RT   and breast cancer cell growth pattern.";
RL   Cell. Signal. 21:1423-1435(2009).
RN   [16]
RP   INTERACTION WITH PTK2B/PYK2, AND PHOSPHORYLATION.
RX   PubMed=19086031; DOI=10.1002/jcp.21649;
RA   Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A.;
RT   "Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and
RT   regulates human glomerular mesangial cell adhesion and spreading.";
RL   J. Cell. Physiol. 219:45-56(2009).
RN   [17]
RP   PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1.
RX   PubMed=19147981; DOI=10.1172/jci37160;
RA   Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F.,
RA   Giancotti F.G.;
RT   "Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires
RT   focal adhesion kinase signaling.";
RL   J. Clin. Invest. 119:252-266(2009).
RN   [18]
RP   INTERACTION WITH PEAK1.
RX   PubMed=20534451; DOI=10.1073/pnas.0914776107;
RA   Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA   Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA   Yates J.R. III, Klemke R.L.;
RT   "Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and
RT   cancer progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010).
RN   [19]
RP   ERRATUM OF PUBMED:20534451.
RA   Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA   Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA   Yates J.R. III, Klemke R.L.;
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-139, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [22]
RP   IDENTIFICATION IN A COMPLEX WITH PTPRA; BCAR3 AND SRC.
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   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-639, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [24]
RP   DEPHOSPHORYLATION AT TYR-128 BY PTPN14, AND PHOSPHORYLATION AT TYR-128 BY
RP   SRC.
RX   PubMed=22710723; DOI=10.1038/onc.2012.220;
RA   Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C.,
RA   Markowitz S.D., Polakiewicz R.D., Wang Z.;
RT   "Identification and functional characterization of p130Cas as a substrate
RT   of protein tyrosine phosphatase nonreceptor 14.";
RL   Oncogene 32:2087-2095(2013).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 3-71.
RX   PubMed=15784259; DOI=10.1016/j.jmb.2005.02.017;
RA   Wisniewska M., Bossenmaier B., Georges G., Hesse F., Dangl M.,
RA   Kunkele K.P., Ioannidis I., Huber R., Engh R.A.;
RT   "The 1.1 A resolution crystal structure of the p130cas SH3 domain and
RT   ramifications for ligand selectivity.";
RL   J. Mol. Biol. 347:1005-1014(2005).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 645-870 IN COMPLEX WITH SH2D3C AND
RP   BCAR3, AND MUTAGENESIS OF LEU-787; PHE-794 AND ASP-797.
RX   PubMed=22081014; DOI=10.1038/nsmb.2152;
RA   Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H.,
RA   Pasquale E.B., Riedl S.J.;
RT   "NSP-Cas protein structures reveal a promiscuous interaction module in cell
RT   signaling.";
RL   Nat. Struct. Mol. Biol. 18:1381-1387(2011).
RN   [27]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-407.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Docking protein which plays a central coordinating role for
CC       tyrosine kinase-based signaling related to cell adhesion
CC       (PubMed:12832404, PubMed:12432078). Implicated in induction of cell
CC       migration and cell branching (PubMed:12432078, PubMed:12832404,
CC       PubMed:17038317). Involved in the BCAR3-mediated inhibition of TGFB
CC       signaling (By similarity). {ECO:0000250|UniProtKB:Q61140,
CC       ECO:0000269|PubMed:12432078, ECO:0000269|PubMed:12832404,
CC       ECO:0000269|PubMed:17038317}.
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 (PubMed:12432078). Within the
CC       complex, interacts with SH2D3C (via C-terminus), and CRK
CC       (PubMed:12432078, PubMed:17174122). Part of a complex comprised of
CC       PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the
CC       complex is dependent on intergrin mediated-tyrosine phosphorylation of
CC       PTPRA (PubMed:22801373). Interacts with BCAR3 (via Ras-GEF domain); the
CC       interaction regulates adhesion-dependent serine phosphorylation
CC       (PubMed:22081014). Interacts with SMAD2 and SMAD3 (By similarity).
CC       Interacts with NPHP1 (By similarity). Interacts with PTK2B/PYK2
CC       (PubMed:19086031). Interacts (via C-terminus) with SH2D3C/CHAT isoform
CC       2 (via C-terminus) (PubMed:17174122, PubMed:22081014). Interacts with
CC       activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part of a
CC       collagen-stimulated complex involved in cell migration made of CDC42,
CC       CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3 domains.
CC       {ECO:0000250|UniProtKB:Q61140, ECO:0000269|PubMed:10587647,
CC       ECO:0000269|PubMed:11158326, ECO:0000269|PubMed:12432078,
CC       ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:17038317,
CC       ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:19086031,
CC       ECO:0000269|PubMed:19454314, ECO:0000269|PubMed:20534451,
CC       ECO:0000269|PubMed:22081014, ECO:0000269|PubMed:22801373}.
CC   -!- INTERACTION:
CC       P56945; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-702093, EBI-11954519;
CC       P56945; O75815-1: BCAR3; NbExp=3; IntAct=EBI-702093, EBI-15953103;
CC       P56945; P53618: COPB1; NbExp=3; IntAct=EBI-702093, EBI-359063;
CC       P56945; P46108: CRK; NbExp=7; IntAct=EBI-702093, EBI-886;
CC       P56945; Q5T9C2-3: FAM102A; NbExp=3; IntAct=EBI-702093, EBI-11980989;
CC       P56945; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-702093, EBI-6658203;
CC       P56945; P06241: FYN; NbExp=4; IntAct=EBI-702093, EBI-515315;
CC       P56945; P06241-3: FYN; NbExp=3; IntAct=EBI-702093, EBI-10691738;
CC       P56945; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-702093, EBI-7251368;
CC       P56945; O15357: INPPL1; NbExp=2; IntAct=EBI-702093, EBI-1384248;
CC       P56945; P46940: IQGAP1; NbExp=4; IntAct=EBI-702093, EBI-297509;
CC       P56945; P50281: MMP14; NbExp=3; IntAct=EBI-702093, EBI-992788;
CC       P56945; O43639: NCK2; NbExp=3; IntAct=EBI-702093, EBI-713635;
CC       P56945; Q9H792: PEAK1; NbExp=3; IntAct=EBI-702093, EBI-2609701;
CC       P56945; Q96QH2: PRAM1; NbExp=3; IntAct=EBI-702093, EBI-2860740;
CC       P56945; Q05397: PTK2; NbExp=2; IntAct=EBI-702093, EBI-702142;
CC       P56945; P18031: PTPN1; NbExp=5; IntAct=EBI-702093, EBI-968788;
CC       P56945; Q05209: PTPN12; NbExp=4; IntAct=EBI-702093, EBI-2266035;
CC       P56945; Q8N5H7-2: SH2D3C; NbExp=8; IntAct=EBI-702093, EBI-15952996;
CC       P56945; P12931: SRC; NbExp=3; IntAct=EBI-702093, EBI-621482;
CC       P56945; Q9C0H9: SRCIN1; NbExp=3; IntAct=EBI-702093, EBI-1393949;
CC       P56945; Q07912: TNK2; NbExp=5; IntAct=EBI-702093, EBI-603457;
CC       P56945; Q68CZ2: TNS3; NbExp=8; IntAct=EBI-702093, EBI-1220488;
CC       P56945; O75604: USP2; NbExp=3; IntAct=EBI-702093, EBI-743272;
CC       P56945; P18206-2: VCL; NbExp=3; IntAct=EBI-702093, EBI-11027067;
CC       P56945; P07947: YES1; NbExp=3; IntAct=EBI-702093, EBI-515331;
CC       P56945; Q9QWI6: Srcin1; Xeno; NbExp=3; IntAct=EBI-702093, EBI-775592;
CC       P56945; Q04205: TNS; Xeno; NbExp=2; IntAct=EBI-702093, EBI-2607590;
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000269|PubMed:12832404}. Cytoplasm {ECO:0000269|PubMed:12832404}.
CC       Cell projection, axon {ECO:0000250|UniProtKB:Q61140}.
CC       Note=Unphosphorylated form localizes in the cytoplasm (By similarity).
CC       Localizes to focal adhesion sites following integrin engagement (By
CC       similarity). {ECO:0000250|UniProtKB:Q61140}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1;
CC         IsoId=P56945-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P56945-2; Sequence=VSP_043559;
CC       Name=3;
CC         IsoId=P56945-3; Sequence=VSP_045355;
CC       Name=4;
CC         IsoId=P56945-4; Sequence=VSP_046127, VSP_046128;
CC       Name=5;
CC         IsoId=P56945-5; Sequence=VSP_046748;
CC       Name=6;
CC         IsoId=P56945-6; Sequence=VSP_046749;
CC       Name=7;
CC         IsoId=P56945-7; Sequence=VSP_046750;
CC       Name=8;
CC         IsoId=P56945-8; Sequence=VSP_046751;
CC   -!- TISSUE SPECIFICITY: Widely expressed with an abundant expression in the
CC       testis. Low level of expression seen in the liver, thymus, and
CC       peripheral blood leukocytes. The protein has been detected in a B-cell
CC       line.
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 ABL1 SH2 domains. The HLH motif is
CC       absolutely required for the induction of pseudohyphal growth in yeast
CC       and mediates heterodimerization with NEDD9 (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: A serine-rich region promotes activation of the serum response
CC       element (SRE).
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/FAK11.
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. {ECO:0000269|PubMed:12832404, ECO:0000269|PubMed:19147981,
CC       ECO:0000269|PubMed:19454314, ECO:0000269|PubMed:22710723}.
CC   -!- PTM: Dephosphorylated by PTPN14 at Tyr-128.
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:0000269|PubMed:19086031}.
CC   -!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/BCAR1ID761ch16q23.html";
DR   EMBL; AJ242987; CAB75875.2; -; mRNA.
DR   EMBL; AF218451; AAF27527.1; -; mRNA.
DR   EMBL; AB040024; BAA92711.1; -; mRNA.
DR   EMBL; AY545071; AAS48631.1; -; mRNA.
DR   EMBL; AK027608; BAB55230.1; -; mRNA.
DR   EMBL; AK124815; BAG54099.1; -; mRNA.
DR   EMBL; AK293808; BAG57215.1; -; mRNA.
DR   EMBL; AK294513; BAG57726.1; -; mRNA.
DR   EMBL; AK295809; BAG58627.1; -; mRNA.
DR   EMBL; AK302617; BAH13763.1; -; mRNA.
DR   EMBL; AC009078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS10915.1; -. [P56945-1]
DR   CCDS; CCDS54037.1; -. [P56945-5]
DR   CCDS; CCDS54038.1; -. [P56945-3]
DR   CCDS; CCDS54039.1; -. [P56945-4]
DR   CCDS; CCDS54040.1; -. [P56945-6]
DR   CCDS; CCDS54041.1; -. [P56945-8]
DR   CCDS; CCDS54042.1; -. [P56945-2]
DR   CCDS; CCDS54043.1; -. [P56945-7]
DR   RefSeq; NP_001164185.1; NM_001170714.1. [P56945-6]
DR   RefSeq; NP_001164186.1; NM_001170715.1. [P56945-7]
DR   RefSeq; NP_001164187.1; NM_001170716.1. [P56945-2]
DR   RefSeq; NP_001164188.1; NM_001170717.1. [P56945-3]
DR   RefSeq; NP_001164189.1; NM_001170718.1. [P56945-8]
DR   RefSeq; NP_001164190.1; NM_001170719.1. [P56945-5]
DR   RefSeq; NP_001164191.1; NM_001170720.1. [P56945-4]
DR   RefSeq; NP_055382.2; NM_014567.3. [P56945-1]
DR   RefSeq; XP_016879386.1; XM_017023897.1.
DR   PDB; 1WYX; X-ray; 1.14 A; A/B=3-71.
DR   PDB; 3T6G; X-ray; 2.50 A; B/D=645-870.
DR   PDB; 5O2M; NMR; -; A=4-73.
DR   PDB; 5O2P; NMR; -; A=4-73.
DR   PDB; 5O2Q; NMR; -; A=4-73.
DR   PDBsum; 1WYX; -.
DR   PDBsum; 3T6G; -.
DR   PDBsum; 5O2M; -.
DR   PDBsum; 5O2P; -.
DR   PDBsum; 5O2Q; -.
DR   SMR; P56945; -.
DR   BioGRID; 114934; 93.
DR   CORUM; P56945; -.
DR   DIP; DIP-33855N; -.
DR   ELM; P56945; -.
DR   IntAct; P56945; 261.
DR   MINT; P56945; -.
DR   STRING; 9606.ENSP00000391669; -.
DR   iPTMnet; P56945; -.
DR   PhosphoSitePlus; P56945; -.
DR   BioMuta; BCAR1; -.
DR   DMDM; 288558806; -.
DR   EPD; P56945; -.
DR   jPOST; P56945; -.
DR   MassIVE; P56945; -.
DR   MaxQB; P56945; -.
DR   PaxDb; P56945; -.
DR   PeptideAtlas; P56945; -.
DR   PRIDE; P56945; -.
DR   ProteomicsDB; 19466; -.
DR   ProteomicsDB; 19521; -.
DR   ProteomicsDB; 24360; -.
DR   ProteomicsDB; 24539; -.
DR   ProteomicsDB; 27632; -.
DR   ProteomicsDB; 30445; -.
DR   ProteomicsDB; 56960; -. [P56945-1]
DR   ProteomicsDB; 56961; -. [P56945-2]
DR   ABCD; P56945; 2 sequenced antibodies.
DR   Antibodypedia; 3607; 774 antibodies.
DR   DNASU; 9564; -.
DR   Ensembl; ENST00000162330; ENSP00000162330; ENSG00000050820. [P56945-1]
DR   Ensembl; ENST00000393420; ENSP00000377072; ENSG00000050820. [P56945-3]
DR   Ensembl; ENST00000393422; ENSP00000377074; ENSG00000050820. [P56945-7]
DR   Ensembl; ENST00000418647; ENSP00000391669; ENSG00000050820. [P56945-6]
DR   Ensembl; ENST00000420641; ENSP00000392708; ENSG00000050820. [P56945-2]
DR   Ensembl; ENST00000535626; ENSP00000440370; ENSG00000050820. [P56945-4]
DR   Ensembl; ENST00000538440; ENSP00000443841; ENSG00000050820. [P56945-8]
DR   Ensembl; ENST00000542031; ENSP00000440415; ENSG00000050820. [P56945-5]
DR   GeneID; 9564; -.
DR   KEGG; hsa:9564; -.
DR   UCSC; uc002fdv.4; human. [P56945-1]
DR   CTD; 9564; -.
DR   DisGeNET; 9564; -.
DR   EuPathDB; HostDB:ENSG00000050820.16; -.
DR   GeneCards; BCAR1; -.
DR   HGNC; HGNC:971; BCAR1.
DR   HPA; ENSG00000050820; Low tissue specificity.
DR   MIM; 602941; gene.
DR   neXtProt; NX_P56945; -.
DR   OpenTargets; ENSG00000050820; -.
DR   PharmGKB; PA25281; -.
DR   eggNOG; ENOG502QQHE; Eukaryota.
DR   GeneTree; ENSGT00950000183008; -.
DR   HOGENOM; CLU_017000_1_0_1; -.
DR   InParanoid; P56945; -.
DR   KO; K05726; -.
DR   OMA; NYADTPD; -.
DR   OrthoDB; 1086228at2759; -.
DR   PhylomeDB; P56945; -.
DR   TreeFam; TF328782; -.
DR   PathwayCommons; P56945; -.
DR   Reactome; R-HSA-186763; Downstream signal transduction.
DR   Reactome; R-HSA-372708; p130Cas linkage to MAPK signaling for integrins.
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   SignaLink; P56945; -.
DR   SIGNOR; P56945; -.
DR   BioGRID-ORCS; 9564; 284 hits in 876 CRISPR screens.
DR   ChiTaRS; BCAR1; human.
DR   EvolutionaryTrace; P56945; -.
DR   GeneWiki; BCAR1; -.
DR   GenomeRNAi; 9564; -.
DR   Pharos; P56945; Tbio.
DR   PRO; PR:P56945; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P56945; protein.
DR   Bgee; ENSG00000050820; Expressed in cerebellum and 196 other tissues.
DR   ExpressionAtlas; P56945; baseline and differential.
DR   Genevisible; P56945; HS.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005925; C:focal adhesion; IDA:BHF-UCL.
DR   GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR   GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
DR   GO; GO:0090527; P:actin filament reorganization; IBA:GO_Central.
DR   GO; GO:0050851; P:antigen receptor-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0060326; P:cell chemotaxis; IMP:BHF-UCL.
DR   GO; GO:0051301; P:cell division; NAS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR   GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:BHF-UCL.
DR   GO; GO:0086100; P:endothelin receptor signaling pathway; IDA: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; ISS:UniProtKB.
DR   GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:UniProtKB.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:BHF-UCL.
DR   GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
DR   GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; NAS:UniProtKB.
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; IMP:BHF-UCL.
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; Diabetes mellitus;
KW   Direct protein sequencing; Phosphoprotein; Polymorphism;
KW   Reference proteome; SH3 domain; SH3-binding.
FT   CHAIN           1..870
FT                   /note="Breast cancer anti-estrogen resistance protein 1"
FT                   /id="PRO_0000064854"
FT   DOMAIN          3..65
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          115..416
FT                   /note="Substrate for kinases"
FT                   /evidence="ECO:0000250"
FT   REGION          746..796
FT                   /note="Divergent helix-loop-helix motif"
FT   MOTIF           635..643
FT                   /note="SH3-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        74..87
FT                   /note="Pro-rich"
FT   COMPBIAS        422..614
FT                   /note="Ser-rich"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|Ref.7"
FT   MOD_RES         128
FT                   /note="Phosphotyrosine; by SRC"
FT                   /evidence="ECO:0000269|PubMed:22710723"
FT   MOD_RES         134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         139
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:19454314"
FT   MOD_RES         234
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61140"
FT   MOD_RES         249
FT                   /note="Phosphotyrosine; by ABL1"
FT                   /evidence="ECO:0000250|UniProtKB:Q63767"
FT   MOD_RES         269
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648"
FT   MOD_RES         362
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61140"
FT   MOD_RES         372
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61140"
FT   MOD_RES         410
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61140"
FT   MOD_RES         428
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21406692"
FT   MOD_RES         437
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:19454314"
FT   MOD_RES         639
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163,
FT                   ECO:0000269|PubMed:19454314"
FT   VAR_SEQ         1..4
FT                   /note="MNHL -> MLTHRPQEAEQRGRTPGPSFEW (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_043559"
FT   VAR_SEQ         1..4
FT                   /note="MNHL -> MQGK (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046127"
FT   VAR_SEQ         1..4
FT                   /note="MNHL -> ME (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046748"
FT   VAR_SEQ         1..4
FT                   /note="MNHL -> MPAKPFLSSVLLSWKVLDFSGPGPQGTGQPCSCGHWAEGQGGPP
FT                   EPAGGP (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046749"
FT   VAR_SEQ         1..4
FT                   /note="MNHL -> MHCPGEAPLAAPRPTPKDPCLR (in isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046750"
FT   VAR_SEQ         1..4
FT                   /note="MNHL -> MSVP (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046751"
FT   VAR_SEQ         64..211
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046128"
FT   VAR_SEQ         304
FT                   /note="A -> AVSKCQGNARARLRLWGVW (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_045355"
FT   VARIANT         76
FT                   /note="P -> S (in dbSNP:rs1035539)"
FT                   /evidence="ECO:0000269|PubMed:10639512,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2,
FT                   ECO:0000269|Ref.3"
FT                   /id="VAR_058970"
FT   VARIANT         407
FT                   /note="S -> T (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs144989936)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035798"
FT   VARIANT         491
FT                   /note="R -> L (in dbSNP:rs16957558)"
FT                   /id="VAR_057820"
FT   VARIANT         558
FT                   /note="H -> R (in dbSNP:rs16957552)"
FT                   /id="VAR_057821"
FT   MUTAGEN         787
FT                   /note="L->E: Weakens interaction with SH2D3C."
FT                   /evidence="ECO:0000269|PubMed:22081014"
FT   MUTAGEN         794
FT                   /note="F->R: Weakens interaction with SH2D3C."
FT                   /evidence="ECO:0000269|PubMed:22081014"
FT   MUTAGEN         797
FT                   /note="D->R: Weakens interaction with SH2D3C."
FT                   /evidence="ECO:0000269|PubMed:22081014"
FT   CONFLICT        63
FT                   /note="L -> S (in Ref. 5; BAB55230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="I -> T (in Ref. 2; AAF27527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        254
FT                   /note="V -> I (in Ref. 5; BAG54099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        349
FT                   /note="A -> G (in Ref. 2; AAF27527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="D -> Y (in Ref. 2; AAF27527)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        385
FT                   /note="T -> A (in Ref. 4; AAS48631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        428
FT                   /note="S -> P (in Ref. 5; BAB55230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        471
FT                   /note="S -> G (in Ref. 5; BAB55230)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        600
FT                   /note="N -> S (in Ref. 4; AAS48631)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        700
FT                   /note="Q -> R (in Ref. 5; BAH13763)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        714
FT                   /note="P -> L (in Ref. 5; BAG54099)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        740
FT                   /note="D -> G (in Ref. 4; AAS48631)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..12
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   STRAND          29..34
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   HELIX           37..39
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   STRAND          43..48
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   STRAND          51..56
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   HELIX           57..59
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   STRAND          60..68
FT                   /evidence="ECO:0000244|PDB:1WYX"
FT   HELIX           740..770
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           775..801
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           806..835
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           840..870
FT                   /evidence="ECO:0000244|PDB:3T6G"
SQ   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
//
DBGET integrated database retrieval system