Reviewed, UniProtKB/Swiss-Prot P56945 (BCAR1_HUMAN)

Names and origin

Protein names

Recommended name:
    Breast cancer anti-estrogen resistance protein 1
Alternative name(s):
    CRK-associated substrate
    p130cas
    Cas scaffolding protein family member 1

Gene names

Name:	BCAR1
Synonyms:	CAS, CASS1, CRKAS

Organism

Homo sapiens (Human) [Complete proteome]

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.
Subunit structure	Forms complexes in vivo with focal adhesion kinase 1, adapter protein CRKL and LYN kinase. Can heterodimerize with CASL. Interacts with BCAR3, NPHP1, PTK2B and SH2D3C By similarity. Interacts with activated CSPG4. Interacts with INPPL1/SHIP2. Ref.7 Ref.8
Subcellular location	Cell junction › focal adhesion By similarity. Cytoplasm By similarity. Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation By similarity.
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 ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with CASL 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 focal adhesion kinase 1.
Post-translational modification	Focal adhesion kinase 1 phosphorylates the protein at the YDYVHL motif. 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.14 Ref.15 Ref.16
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
Gene Ontology (GO)
Biological process	B cell receptor signaling pathway Inferred from direct assay. Source: UniProtKB G-protein coupled receptor protein signaling pathway Non-traceable author statement. Source: UniProtKB T cell receptor signaling pathway Non-traceable author statement. Source: UniProtKB actin filament organization Inferred from direct assay. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell division Non-traceable author statement. Source: UniProtKB cell migration Inferred from direct assay. Source: UniProtKB cell proliferation Ref.1 Traceable author statement. Source: ProtInc epidermal growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB 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 apoptosis Traceable author statement. Source: UniProtKB regulation of cell growth Traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. 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	1	EBI-702093,EBI-886
FYN	P06241	1	EBI-702093,EBI-515315
P140	Q9C0H9	1	EBI-702093,EBI-1393949
P140	Q9QWI6	1	EBI-702093,EBI-775592	From a different organism.

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.9 Ref.14 Ref.16

Modified residue

134

1

Phosphoserine Ref.15

Modified residue

139

1

Phosphoserine Ref.13 Ref.15

Modified residue

222

1

Phosphotyrosine Ref.9

Modified residue

224

1

Phosphotyrosine Ref.9

Modified residue

234

1

Phosphotyrosine Ref.9 Ref.14 Ref.16

Modified residue

249

1

Phosphotyrosine Ref.9 Ref.10 Ref.14 Ref.16

Modified residue

267

1

Phosphotyrosine Ref.16

Modified residue

269

1

Phosphothreonine Ref.15

Modified residue

287

1

Phosphotyrosine Ref.16

Modified residue

292

1

Phosphoserine Ref.15

Modified residue

327

1

Phosphotyrosine Ref.10 Ref.11 Ref.16

Modified residue

362

1

Phosphotyrosine By similarity

Modified residue

387

1

Phosphotyrosine Ref.9 Ref.14 Ref.16

Modified residue

410

1

Phosphotyrosine By similarity

Modified residue

639

1

Phosphoserine Ref.12

Natural variations

Natural variant

76

1

P → S: dbSNP rs1035539.

VAR_058970

Natural variant

407

1

S → T in a breast cancer sample; somatic mutation. Ref.17

VAR_035798

Natural variant

491

1

R → L: dbSNP rs16957558.

VAR_057820

Natural variant

558

1

H → R: dbSNP rs16957552.

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)
	P56945-1 [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]	"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: Epithelium.
[10]	"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: Epithelium.
[11]	"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.
[12]	"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: Epithelium.
[13]	"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: Epithelium.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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_055382.2.

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	[»]

SMR

P56945. Positions 448-610.

ModBase

Search...

Protein-protein interaction databases

IntAct

P56945. 14 interactions.

STRING

P56945.

PTM databases

PhosphoSite

P56945.

Proteomic databases

PRIDE

P56945.

Genome annotation databases

Ensembl

ENST00000162330; ENSP00000162330; ENSG00000050820; Homo sapiens. [Genome view]

GeneID

9564.

KEGG

hsa:9564.

Organism-specific databases

CTD

9564.

GeneCards

GC16M073820.

H-InvDB

HIX0013243.

HGNC

HGNC:971. BCAR1.

HPA

CAB000443.

MIM

602941. gene.

PharmGKB

PA25281.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG15595.

HOVERGEN

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_13552. Integrin cell surface interactions.
REACT_16888. Signaling by PDGF.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P56945.

Bgee

P56945.

CleanEx

HS_BCAR1.

Genevestigator

P56945.

GermOnline

ENSG00000050820. Homo sapiens.

Family and domain databases

InterPro

IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR020473. SH3_region.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]

Pfam

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

PRINTS

PR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.

SMART

SM00326. SH3. 1 hit.
[Graphical view]

PROSITE

PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

35871.

SOURCE

Search...

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:	February 9, 2010
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.