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Breast cancer anti-estrogen resistance protein 1 (CRK-associated substrate) (p130cas)

 BCAR1_MOUSE             Reviewed;         874 AA.
Q61140; Q60869; Q6PFF9;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 165.
RecName: Full=Breast cancer anti-estrogen resistance protein 1;
AltName: Full=CRK-associated substrate;
AltName: Full=p130cas;
Name=Bcar1; Synonyms=Cas, Crkas;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CAS-A AND CAS-B), AND INTERACTION
WITH PTK2/FAK1.
TISSUE=Embryo;
PubMed=7479864; DOI=10.1073/pnas.92.23.10678;
Polte T.R., Hanks S.K.;
"Interaction between focal adhesion kinase and Crk-associated tyrosine
kinase substrate p130Cas.";
Proc. Natl. Acad. Sci. U.S.A. 92:10678-10682(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH BCAR3.
PubMed=10438950;
Cai D., Clayton L.K., Smolyar A., Lerner A.;
"AND-34, a novel p130Cas-binding thymic stromal cell protein regulated
by adhesion and inflammatory cytokines.";
J. Immunol. 163:2104-2112(1999).
[5]
INTERACTION WITH NPHP1.
PubMed=10739664; DOI=10.1006/excr.2000.4822;
Donaldson J.C., Dempsey P.J., Reddy S., Bouton A.H., Coffey R.J.,
Hanks S.K.;
"Crk-associated substrate p130(Cas) interacts with nephrocystin and
both proteins localize to cell-cell contacts of polarized epithelial
cells.";
Exp. Cell Res. 256:168-178(2000).
[6]
INTERACTION WITH BCAR3.
PubMed=10896938; DOI=10.1074/jbc.M003074200;
Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
"p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-
Ras guanine nucleotide exchange factor.";
J. Biol. Chem. 275:30118-30123(2000).
[7]
INTERACTION WITH SH2D3C.
PubMed=10692442; DOI=10.1074/jbc.275.9.6404;
Sakakibara A., Hattori S.;
"Chat, a Cas/HEF1-associated adaptor protein that integrates multiple
signaling pathways.";
J. Biol. Chem. 275:6404-6410(2000).
[8]
INTERACTION WITH SH2D3C.
TISSUE=Spleen;
PubMed=12486027; DOI=10.1074/jbc.M207942200;
Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
"A novel hematopoietic adaptor protein, Chat-H, positively regulates T
cell receptor-mediated interleukin-2 production by Jurkat cells.";
J. Biol. Chem. 278:6012-6017(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132; TYR-366; TYR-376
AND TYR-414, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Docking protein which plays a central coordinating role
for tyrosine kinase-based signaling related to cell adhesion.
Implicated in induction of cell migration (By similarity). Has
been shown to be essential in cardiovascular development during
embryogenesis. {ECO:0000250}.
-!- SUBUNIT: Forms complexes in vivo with PTK2/FAK1, adapter protein
CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with
activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 (By
similarity). Part of a collagen stimulated complex involved in
cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas (By
similarity). Interacts with BCAR3, the interaction regulates
adhesion-dependent serine phosphorylation. Interacts with NPHP1,
PTK2B/PYK2 and SH2D3C. {ECO:0000250, ECO:0000269|PubMed:10438950,
ECO:0000269|PubMed:10692442, ECO:0000269|PubMed:10739664,
ECO:0000269|PubMed:10896938, ECO:0000269|PubMed:12486027,
ECO:0000269|PubMed:7479864}.
-!- INTERACTION:
Q9QY53:Nphp1; NbExp=2; IntAct=EBI-77088, EBI-77230;
P34152:Ptk2; NbExp=3; IntAct=EBI-77088, EBI-77070;
P18031:PTPN1 (xeno); NbExp=5; IntAct=EBI-77088, EBI-968788;
Q9QWI6:Srcin1; NbExp=2; IntAct=EBI-77088, EBI-775592;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
Cytoplasm {ECO:0000250}. 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=2;
Name=Cas-B;
IsoId=Q61140-1; Sequence=Displayed;
Name=Cas-A;
IsoId=Q61140-2; Sequence=VSP_004134;
-!- 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 ABL SH2 domains. The
HLH motif is absolutely required for the induction of pseudohyphal
growth in yeast and mediates heterodimerization with NEDD9.
-!- DOMAIN: A serine-rich region promotes activation of the serum
response element (SRE). {ECO:0000250}.
-!- DOMAIN: The SH3 domain is necessary for the localization of the
protein to focal adhesions and interacts with one proline-rich
region of PTK2/FAK1.
-!- 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 (By similarity). {ECO:0000250}.
-!- PTM: Dephosphorylated by PTPN14 at Tyr-132. {ECO:0000250}.
-!- SIMILARITY: Belongs to the CAS family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U48853; AAA93381.1; -; mRNA.
EMBL; U28151; AAA93248.1; -; mRNA.
EMBL; AK145863; BAE26705.1; -; mRNA.
EMBL; BC057578; AAH57578.1; -; mRNA.
CCDS; CCDS52675.1; -. [Q61140-1]
CCDS; CCDS85616.1; -. [Q61140-2]
RefSeq; NP_001185768.1; NM_001198839.1. [Q61140-2]
RefSeq; NP_034084.2; NM_009954.3. [Q61140-1]
UniGene; Mm.3758; -.
PDB; 5W93; X-ray; 2.00 A; A/B/C=738-874.
PDBsum; 5W93; -.
ProteinModelPortal; Q61140; -.
SMR; Q61140; -.
BioGrid; 198886; 8.
CORUM; Q61140; -.
IntAct; Q61140; 14.
MINT; MINT-100691; -.
STRING; 10090.ENSMUSP00000129584; -.
iPTMnet; Q61140; -.
PhosphoSitePlus; Q61140; -.
PaxDb; Q61140; -.
PRIDE; Q61140; -.
Ensembl; ENSMUST00000166232; ENSMUSP00000129584; ENSMUSG00000031955. [Q61140-1]
Ensembl; ENSMUST00000212349; ENSMUSP00000148364; ENSMUSG00000031955. [Q61140-2]
GeneID; 12927; -.
KEGG; mmu:12927; -.
UCSC; uc009nmt.2; mouse. [Q61140-2]
UCSC; uc009nmu.2; mouse. [Q61140-1]
CTD; 9564; -.
MGI; MGI:108091; Bcar1.
eggNOG; ENOG410IEDD; Eukaryota.
eggNOG; ENOG410ZSUM; LUCA.
GeneTree; ENSGT00490000043324; -.
HOGENOM; HOG000261698; -.
HOVERGEN; HBG004354; -.
InParanoid; Q61140; -.
KO; K05726; -.
OMA; LANMPDY; -.
OrthoDB; EOG091G0RVA; -.
TreeFam; TF328782; -.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
PRO; PR:Q61140; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031955; -.
CleanEx; MM_BCAR1; -.
Genevisible; Q61140; MM.
GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:MGI.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0050851; P:antigen receptor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
GO; GO:0016477; P:cell migration; IDA:MGI.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISO:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; ISO:MGI.
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.
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; Phosphoprotein;
Reference proteome; SH3 domain; SH3-binding.
CHAIN 1 874 Breast cancer anti-estrogen resistance
protein 1.
/FTId=PRO_0000064855.
DOMAIN 6 26 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 119 420 Substrate for kinases. {ECO:0000250}.
REGION 750 800 Divergent helix-loop-helix motif.
MOTIF 639 647 SH3-binding. {ECO:0000255}.
COMPBIAS 74 87 Pro-rich.
COMPBIAS 426 618 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 132 132 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 238 238 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 253 253 Phosphotyrosine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 273 273 Phosphothreonine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 366 366 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 376 376 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 414 414 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
MOD_RES 643 643 Phosphoserine.
{ECO:0000250|UniProtKB:P56945}.
VAR_SEQ 1 4 MTVP -> MKYL (in isoform Cas-A).
{ECO:0000303|PubMed:7479864}.
/FTId=VSP_004134.
CONFLICT 72 72 V -> A (in Ref. 1; AAA93381/AAA93248).
{ECO:0000305}.
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


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