P56945 (BCAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Breast cancer anti-estrogen resistance protein 1

Alternative name(s):
CRK-associated substrate
Cas scaffolding protein family member 1
p130cas

Gene names

Name:	BCAR1
Synonyms:	CAS, CASS1, CRKAS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	870 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Docking protein which plays a central coordinating role for tyrosine kinase-based signaling related to cell adhesion. Implicated in induction of cell migration. Overexpression confers antiestrogen resistance on breast cancer cells. Ref.9 Ref.14
Subunit structure	Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with BCAR3, NPHP1 and SH2D3C By similarity. Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1. Part of a collagen-stimulated complex involved in cell migration made of CDC42, CRK, TNK2 and BCAR1/p130cas. Interacts with TNK2 via SH3 domains. Interacts with PTK2B/PYK2. Ref.7 Ref.8 Ref.9 Ref.14 Ref.19 Ref.22
Subcellular location	Cell junction › focal adhesion. Cytoplasm. Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation By similarity. Ref.9
Tissue specificity	Widely expressed with an abundant expression in the testis. Low level of expression seen in the liver, thymus, and peripheral blood leukocytes. The protein has been detected in a B-cell line.
Domain	Contains a central domain (substrate domain) containing multiple potential SH2-binding sites and a C-terminal domain containing a divergent helix-loop-helix (HLH) motif. The SH2-binding sites putatively bind CRK, NCK and ABL1 SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9 By similarity. A serine-rich region promotes activation of the serum response element (SRE). The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK11.
Post-translational modification	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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.21
Sequence similarities	Belongs to the CAS family. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cytoplasm
Coding sequence diversity	Polymorphism
Domain	SH3 domain SH3-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	B cell receptor signaling pathway Inferred from direct assay. Source: UniProtKB G-protein coupled receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB T cell receptor signaling pathway Non-traceable author statement. Source: UniProtKB actin filament organization Inferred from direct assay. Source: UniProtKB blood coagulation Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell chemotaxis Inferred from mutant phenotype. Source: BHF-UCL cell division Non-traceable author statement. Source: UniProtKB cell proliferation Traceable author statement. Source: ProtInc cellular response to hepatocyte growth factor stimulus Inferred from mutant phenotype. Source: BHF-UCL epidermal growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB hepatocyte growth factor receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB integrin-mediated signaling pathway Inferred from direct assay. Source: UniProtKB nerve growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB platelet-derived growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell migration Inferred from direct assay. Source: UniProtKB regulation of apoptotic process Traceable author statement. Source: UniProtKB regulation of cell growth Traceable author statement. Source: UniProtKB vascular endothelial growth factor receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from sequence or structural similarity. Source: UniProtKB membrane fraction Inferred from direct assay. Source: UniProtKB ruffle Inferred from direct assay. Source: UniProtKB
Molecular function	SH3 domain binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase binding Inferred from physical interaction. Source: UniProtKB protein phosphatase binding Inferred from physical interaction. Source: UniProtKB signal transducer activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	2	EBI-702093,EBI-886
SRCIN1	Q9C0H9	3	EBI-702093,EBI-1393949
Srcin1	Q9QWI6	3	EBI-702093,EBI-775592	From a different organism.
TNS	Q04205	2	EBI-702093,EBI-2607590	From a different organism.
TNS3	Q68CZ2	8	EBI-702093,EBI-1220488

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 870

870

Breast cancer anti-estrogen resistance protein 1

PRO_0000064854

Regions

Domain

3 – 65

63

SH3

Region

115 – 416

302

Substrate for kinases By similarity

Region

746 – 796

51

Divergent helix-loop-helix motif

Motif

635 – 643

9

SH3-binding Potential

Compositional bias

74 – 87

14

Pro-rich

Compositional bias

422 – 614

193

Ser-rich

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6

Modified residue

128

1

Phosphotyrosine Ref.10 Ref.16 Ref.21

Modified residue

134

1

Phosphoserine Ref.18

Modified residue

139

1

Phosphoserine Ref.15 Ref.18

Modified residue

222

1

Phosphotyrosine Ref.10

Modified residue

224

1

Phosphotyrosine Ref.10

Modified residue

234

1

Phosphotyrosine Ref.10 Ref.16 Ref.17 Ref.21

Modified residue

249

1

Phosphotyrosine; by ABL1 Ref.10 Ref.11 Ref.16 Ref.21

Modified residue

267

1

Phosphotyrosine Ref.17 Ref.21

Modified residue

269

1

Phosphothreonine Ref.18

Modified residue

287

1

Phosphotyrosine Ref.21

Modified residue

292

1

Phosphoserine Ref.18

Modified residue

327

1

Phosphotyrosine Ref.11 Ref.12 Ref.17 Ref.21

Modified residue

362

1

Phosphotyrosine Ref.17

Modified residue

387

1

Phosphotyrosine Ref.10 Ref.16 Ref.17 Ref.21

Modified residue

410

1

Phosphotyrosine Ref.17

Modified residue

639

1

Phosphoserine Ref.13

Natural variations

Natural variant

76

1

P → S. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs1035539 [ dbSNP | Ensembl ].

VAR_058970

Natural variant

407

1

S → T in a breast cancer sample; somatic mutation. Ref.25

VAR_035798

Natural variant

491

1

R → L.
Corresponds to variant rs16957558 [ dbSNP | Ensembl ].

VAR_057820

Natural variant

558

1

H → R.
Corresponds to variant rs16957552 [ dbSNP | Ensembl ].

VAR_057821

Experimental info

Sequence conflict

2 – 4

3

NHL → SVP in BAB55230. Ref.4

Sequence conflict

63

1

L → S in BAB55230. Ref.4

Sequence conflict

236

1

I → T in AAF27527. Ref.2

Sequence conflict

349

1

A → G in AAF27527. Ref.2

Sequence conflict

363

1

D → Y in AAF27527. Ref.2

Sequence conflict

428

1

S → P in BAB55230. Ref.4

Sequence conflict

471

1

S → G in BAB55230. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

870

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

29 – 34

6

Helix

37 – 39

3

Beta strand

43 – 48

6

Beta strand

51 – 56

6

Helix

57 – 59

3

Beta strand

60 – 68

9

Sequences

	Sequence		Length	Mass (Da)
	P56945 [UniParc]. Last modified February 9, 2010. Version 2. Checksum: B81EC3430049E795	FASTA	870	93,372
	10 20 30 40 50 60 MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG RQGIVPGNRL 70 80 90 100 110 120 KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT PMLPNTYQPQ PDSVYLVPTP 130 140 150 160 170 180 SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ 190 200 210 220 230 240 VPPSAGMGHD IYQVPPSMDT RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL 250 260 270 280 290 300 LAPGPQDIYD VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS 310 320 330 340 350 360 NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA PPPDSPPAED 370 380 390 400 410 420 VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA DGGVVDSGVY AVPPPAEREA 430 440 450 460 470 480 PAEGKRLSAS STGSTRSSQS ASSLEVAGPG REPLELEVAV EALARLQQGV SATVAHLLDL 490 500 510 520 530 540 AGSAGATGSW RSPSEPQEPL VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK 550 560 570 580 590 600 LSRQLQKMED VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN 610 620 630 640 650 660 ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD GQYENSEGGW 670 680 690 700 710 720 MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ LKQFERLEQE VSRPIDHDLA 730 740 750 760 770 780 NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ CEANLTTLTN AVDAFFTAVA TNQPPKIFVA 790 800 810 820 830 840 HSKFVILSAH KLVFIGDTLS RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP 850 860 870 SAAQDMVERV KELGHSTQQF RRVLGQLAAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"BCAR1, a human homologue of the adapter protein p130Cas, induces anti-estrogen resistance in breast cancer cells." Brinkman A., van der Flier S., Kok E.M., Dorssers L.C.J. J. Natl. Cancer Inst. 92:112-120(2000) [PubMed: 10639512] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-76. Tissue: Mammary cancer.
[2]	"Interaction between human Crk-associated substrate (p130Cas) and nephrocystin." Otto E., Birnbaum S., Verbeek M., Hildebrandt F. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-76. Tissue: Testis.
[3]	"The effects of growth factors on tyrosine phosphorylation of p130Cas in corneal epithelial cell." Imoto Y., Ohguro N., Yoshida A., Tsujikawa M., Inoue Y., Tano Y. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-76. Tissue: Cornea.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-76. Tissue: Teratocarcinoma.
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed: 15616553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Bienvenut W.V., Lempens A., Norman J.C. Submitted (OCT-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-9; 380-391 AND 792-801, ACETYLATION AT MET-1, MASS SPECTROMETRY. Tissue: Ovarian carcinoma.
[7]	"Melanoma chondroitin sulphate proteoglycan regulates cell spreading through Cdc42, Ack-1 and p130cas." Eisenmann K.M., McCarthy J.B., Simpson M.A., Keely P.J., Guan J.-L., Tachibana K., Lim L., Manser E., Furcht L.T., Iida J. Nat. Cell Biol. 1:507-513(1999) [PubMed: 10587647] [Abstract] Cited for: INTERACTION WITH CSPG4.
[8]	"SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading." Prasad N., Topping R.S., Decker S.J. Mol. Cell. Biol. 21:1416-1428(2001) [PubMed: 11158326] [Abstract] Cited for: INTERACTION WITH INPPL1.
[9]	"p130Cas Couples the tyrosine kinase Bmx/Etk with regulation of the actin cytoskeleton and cell migration." Abassi Y.A., Rehn M., Ekman N., Alitalo K., Vuori K. J. Biol. Chem. 278:35636-35643(2003) [PubMed: 12832404] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX.
[10]	"Phosphoproteome analysis of HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC)." Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A. J. Proteome Res. 4:1661-1671(2005) [PubMed: 16212419] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128; TYR-222; TYR-224; TYR-234; TYR-249 AND TYR-387, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249 AND TYR-327, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-327, MASS SPECTROMETRY.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas." Modzelewska K., Newman L.P., Desai R., Keely P.J. J. Biol. Chem. 281:37527-37535(2006) [PubMed: 17038317] [Abstract] Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK.
[15]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128; TYR-234; TYR-249 AND TYR-387, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[17]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-234; TYR-267; TYR-327; TYR-362; TYR-387 AND TYR-410, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-139; THR-269 AND SER-292, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Pyk2 mediates endothelin-1 signaling via p130Cas/BCAR3 cascade and regulates human glomerular mesangial cell adhesion and spreading." Rufanova V.A., Alexanian A., Wakatsuki T., Lerner A., Sorokin A. J. Cell. Physiol. 219:45-56(2009) [PubMed: 19086031] [Abstract] Cited for: INTERACTION WITH PTK2B/PYK2.
[20]	"Ras- and PI3K-dependent breast tumorigenesis in mice and humans requires focal adhesion kinase signaling." Pylayeva Y., Gillen K.M., Gerald W., Beggs H.E., Reichardt L.F., Giancotti F.G. J. Clin. Invest. 119:252-266(2009) [PubMed: 19147981] [Abstract] Cited for: PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1.
[21]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-128; TYR-234; TYR-249; TYR-267; TYR-287; TYR-327 AND TYR-387, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[22]	"Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton and cancer progression." Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L. Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010) [PubMed: 20534451] [Abstract] Cited for: INTERACTION WITH PEAK1.
[23]	Erratum Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W., Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M., Yates J.R. III, Klemke R.L. Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010)
[24]	"The 1.1 A resolution crystal structure of the p130cas SH3 domain and ramifications for ligand selectivity." Wisniewska M., Bossenmaier B., Georges G., Hesse F., Dangl M., Kunkele K.P., Ioannidis I., Huber R., Engh R.A. J. Mol. Biol. 347:1005-1014(2005) [PubMed: 15784259] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 3-71.
[25]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-407.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ242987 mRNA. Translation: CAB75875.2.
AF218451 mRNA. Translation: AAF27527.1.
AB040024 mRNA. Translation: BAA92711.1.
AK027608 mRNA. Translation: BAB55230.1.
AC009078 Genomic DNA. No translation available.

IPI

IPI00872386.

RefSeq

NP_001164185.1. NM_001170714.1.
NP_001164186.1. NM_001170715.1.
NP_001164187.1. NM_001170716.1.
NP_001164188.1. NM_001170717.1.
NP_001164189.1. NM_001170718.1.
NP_001164190.1. NM_001170719.1.
NP_001164191.1. NM_001170720.1.
NP_001164192.1. NM_001170721.1.
NP_055382.2. NM_014567.3.

UniGene

Hs.479747.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WYX	X-ray	1.14	A/B	3-71	[»]
3T6G	X-ray	2.50	B/D	645-870	[»]

ProteinModelPortal

P56945.

SMR

P56945. Positions 3-71, 448-610.

ModBase

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Protein-protein interaction databases

IntAct

P56945. 17 interactions.

MINT

MINT-1505539.

STRING

P56945.

PTM databases

PhosphoSite

P56945.

Polymorphism databases

DMDM

288558806.

Proteomic databases

PRIDE

P56945.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000162330; ENSP00000162330; ENSG00000050820.

GeneID

9564.

KEGG

hsa:9564.

Organism-specific databases

CTD

9564.

GeneCards

GC16M075262.

H-InvDB

HIX0013243.

HGNC

HGNC:971. BCAR1.

HPA

CAB000443.

MIM

602941. gene.

neXtProt

NX_P56945.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG15595.

HOVERGEN

HBG004354.

PhylomeDB

P56945.

Enzyme and pathway databases

Pathway_Interaction_DB

endothelinpathway. Endothelins.
epha2_fwdpathway. EPHA2 forward signaling.
igf1_pathway. IGF1 pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
lysophospholipid_pathway. LPA receptor mediated events.
avb3_opn_pathway. Osteopontin-mediated events.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
pdgfrbpathway. PDGFR-beta signaling pathway.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.
prlsignalingeventspathway. Signaling events mediated by PRL.
ptp1bpathway. Signaling events mediated by PTP1B.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P56945.

Bgee

P56945.

CleanEx

HS_BCAR1.

Genevestigator

P56945.

GermOnline

ENSG00000050820. Homo sapiens.

Family and domain databases

InterPro

IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]

KO

K05726.

Pfam

PF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

35871.

SOURCE

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Entry information

Entry name

BCAR1_HUMAN

Accession

Primary (citable) accession number: P56945

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 9, 2010
Last modified:	January 25, 2012
This is version 118 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.