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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.10 Ref.11
Subunit structure	Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1 and SH2D3C. 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.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.16
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.10
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.10 Ref.13 Ref.15 Ref.20 Dephosphorylated by PTPN14 at Tyr-128. Ref.10 Ref.13 Ref.15 Ref.20
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	Alternative splicing 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 PubMed 9020138. 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 PubMed 9295052. Source: UniProtKB actin filament organization Inferred from direct assay PubMed 16105984. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell chemotaxis Inferred from mutant phenotype PubMed 21245381. Source: BHF-UCL cell division Non-traceable author statement PubMed 10675905. Source: UniProtKB cell proliferation Traceable author statement Ref.1. Source: ProtInc cellular response to hepatocyte growth factor stimulus Inferred from mutant phenotype PubMed 21245381. 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 PubMed 21245381. Source: BHF-UCL insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB integrin-mediated signaling pathway Inferred from direct assay PubMed 8649368. Source: UniProtKB neurotrophin TRK receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet-derived growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of endothelial cell migration Inferred from direct assay PubMed 21245381. Source: BHF-UCL regulation of apoptotic process Traceable author statement PubMed 11607844. Source: UniProtKB regulation of cell growth Traceable author statement PubMed 11607844. Source: UniProtKB vascular endothelial growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 21245381. Source: BHF-UCL
Cellular_component	cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from sequence or structural similarity. Source: UniProtKB ruffle Inferred from direct assay PubMed 9472046. Source: UniProtKB
Molecular_function	signal transducer activity Traceable author statement PubMed 8070403. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	2	EBI-702093,EBI-886
INPPL1	O15357	2	EBI-702093,EBI-1384248
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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P56945-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P56945-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → MLTHRPQEAEQRGRTPGPSFEW

Note: No experimental confirmation available.

Isoform 3 (identifier: P56945-3)

The sequence of this isoform differs from the canonical sequence as follows:
     304-304: A → AVSKCQGNARARLRLWGVW

Isoform 4 (identifier: P56945-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → MQGK
     64-211: Missing.

Note: No experimental confirmation available.

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.7

Modified residue

128

1

Phosphotyrosine; by SRC

Modified residue

134

1

Phosphoserine Ref.12 Ref.18

Modified residue

139

1

Phosphoserine Ref.12 Ref.13 Ref.18

Modified residue

224

1

Phosphotyrosine By similarity

Modified residue

234

1

Phosphotyrosine By similarity

Modified residue

249

1

Phosphotyrosine; by ABL1

Modified residue

269

1

Phosphothreonine Ref.12

Modified residue

292

1

Phosphoserine Ref.12

Modified residue

327

1

Phosphotyrosine By similarity

Modified residue

362

1

Phosphotyrosine By similarity

Modified residue

410

1

Phosphotyrosine By similarity

Modified residue

428

1

Phosphoserine Ref.19

Modified residue

437

1

Phosphoserine Ref.13

Modified residue

639

1

Phosphoserine Ref.13

Natural variations

Alternative sequence

1 – 4

4

MNHL → MLTHRPQEAEQRGRTPGPSF EW in isoform 2.

VSP_043559

Alternative sequence

1 – 4

4

MNHL → MQGK in isoform 4.

VSP_046127

Alternative sequence

64 – 211

148

Missing in isoform 4.

VSP_046128

Alternative sequence

304

1

A → AVSKCQGNARARLRLWGVW in isoform 3.

VSP_045355

Natural variant

76

1

P → S. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs1035539 [ dbSNP | Ensembl ].

VAR_058970

Natural variant

407

1

S → T in a breast cancer sample; somatic mutation. Ref.23

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.5

Sequence conflict

63

1

L → S in BAB55230. Ref.5

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

385

1

T → A in AAS48631. Ref.4

Sequence conflict

428

1

S → P in BAB55230. Ref.5

Sequence conflict

471

1

S → G in BAB55230. Ref.5

Sequence conflict

600

1

N → S in AAS48631. Ref.4

Sequence conflict

700

1

Q → R in BAH13763. Ref.5

Sequence conflict

740

1

D → G in AAS48631. 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

Helix

740 – 770

31

Helix

775 – 801

27

Helix

806 – 835

30

Helix

840 – 870

31

Sequences

	Sequence		Length	Mass (Da)
	Isoform 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
	Isoform 2 [UniParc]. Checksum: 4CA6EC5C8EFE3DA6	FASTA	888	95,469
	10 20 30 40 50 60 MLTHRPQEAE QRGRTPGPSF EWNVLAKALY DNVAESPDEL SFRKGDIMTV LEQDTQGLDG 70 80 90 100 110 120 WWLCSLHGRQ GIVPGNRLKI LVGMYDKKPA GPGPGPPATP AQPQPGLHAP APPASQYTPM 130 140 150 160 170 180 LPNTYQPQPD SVYLVPTPSK AQQGLYQVPG PSPQFQSPPA KQTSTFSKQT PHHPFPSPAT 190 200 210 220 230 240 DLYQVPPGPG GPAQDIYQVP PSAGMGHDIY QVPPSMDTRS WEGTKPPAKV VVPTRVGQGY 250 260 270 280 290 300 VYEAAQPEQD EYDIPRHLLA PGPQDIYDVP PVRGLLPSQY GQEVYDTPPM AVKGPNGRDP 310 320 330 340 350 360 LLEVYDVPPS VEKGLPPSNH HAVYDVPPSV SKDVPDGPLL REETYDVPPA FAKAKPFDPA 370 380 390 400 410 420 RTPLVLAAPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG 430 440 450 460 470 480 GVVDSGVYAV PPPAEREAPA EGKRLSASST GSTRSSQSAS SLEVAGPGRE PLELEVAVEA 490 500 510 520 530 540 LARLQQGVSA TVAHLLDLAG SAGATGSWRS PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA 550 560 570 580 590 600 RSAVGNAAHT SDRALHAKLS RQLQKMEDVH QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC 610 620 630 640 650 660 SRAVPEDAKQ LASFLHGNAS LLFRRTKATA PGPEGGGTLH PNPTDKTSSI QSRPLPSPPK 670 680 690 700 710 720 FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL LEKGSITRQG KSQLELQQLK 730 740 750 760 770 780 QFERLEQEVS RPIDHDLANW TPAQPLAPGR TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV 790 800 810 820 830 840 DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCDL 850 860 870 880 LRGIVATTKA AALQYPSPSA AQDMVERVKE LGHSTQQFRR VLGQLAAA
	Isoform 3 [UniParc]. Checksum: FF81642D11EB93AC	FASTA	888	95,454
	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 NHHAVSKCQG NARARLRLWG VWVYDVPPSV SKDVPDGPLL REETYDVPPA FAKAKPFDPA 370 380 390 400 410 420 RTPLVLAAPP PDSPPAEDVY DVPPPAPDLY DVPPGLRRPG PGTLYDVPRE RVLPPEVADG 430 440 450 460 470 480 GVVDSGVYAV PPPAEREAPA EGKRLSASST GSTRSSQSAS SLEVAGPGRE PLELEVAVEA 490 500 510 520 530 540 LARLQQGVSA TVAHLLDLAG SAGATGSWRS PSEPQEPLVQ DLQAAVAAVQ SAVHELLEFA 550 560 570 580 590 600 RSAVGNAAHT SDRALHAKLS RQLQKMEDVH QTLVAHGQAL DAGRGGSGAT LEDLDRLVAC 610 620 630 640 650 660 SRAVPEDAKQ LASFLHGNAS LLFRRTKATA PGPEGGGTLH PNPTDKTSSI QSRPLPSPPK 670 680 690 700 710 720 FTSQDSPDGQ YENSEGGWME DYDYVHLQGK EEFEKTQKEL LEKGSITRQG KSQLELQQLK 730 740 750 760 770 780 QFERLEQEVS RPIDHDLANW TPAQPLAPGR TGGLGPSDRQ LLLFYLEQCE ANLTTLTNAV 790 800 810 820 830 840 DAFFTAVATN QPPKIFVAHS KFVILSAHKL VFIGDTLSRQ AKAADVRSQV THYSNLLCDL 850 860 870 880 LRGIVATTKA AALQYPSPSA AQDMVERVKE LGHSTQQFRR VLGQLAAA
	Isoform 4 [UniParc]. Checksum: 2537ED6C3BEBE512	FASTA	722	77,731
	10 20 30 40 50 60 MQGKNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG RQGIVPGNRL 70 80 90 100 110 120 KILVVVPTRV GQGYVYEAAQ PEQDEYDIPR HLLAPGPQDI YDVPPVRGLL PSQYGQEVYD 130 140 150 160 170 180 TPPMAVKGPN GRDPLLEVYD VPPSVEKGLP PSNHHAVYDV PPSVSKDVPD GPLLREETYD 190 200 210 220 230 240 VPPAFAKAKP FDPARTPLVL AAPPPDSPPA EDVYDVPPPA PDLYDVPPGL RRPGPGTLYD 250 260 270 280 290 300 VPRERVLPPE VADGGVVDSG VYAVPPPAER EAPAEGKRLS ASSTGSTRSS QSASSLEVAG 310 320 330 340 350 360 PGREPLELEV AVEALARLQQ GVSATVAHLL DLAGSAGATG SWRSPSEPQE PLVQDLQAAV 370 380 390 400 410 420 AAVQSAVHEL LEFARSAVGN AAHTSDRALH AKLSRQLQKM EDVHQTLVAH GQALDAGRGG 430 440 450 460 470 480 SGATLEDLDR LVACSRAVPE DAKQLASFLH GNASLLFRRT KATAPGPEGG GTLHPNPTDK 490 500 510 520 530 540 TSSIQSRPLP SPPKFTSQDS PDGQYENSEG GWMEDYDYVH LQGKEEFEKT QKELLEKGSI 550 560 570 580 590 600 TRQGKSQLEL QQLKQFERLE QEVSRPIDHD LANWTPAQPL APGRTGGLGP SDRQLLLFYL 610 620 630 640 650 660 EQCEANLTTL TNAVDAFFTA VATNQPPKIF VAHSKFVILS AHKLVFIGDT LSRQAKAADV 670 680 690 700 710 720 RSQVTHYSNL LCDLLRGIVA TTKAAALQYP SPSAAQDMVE RVKELGHSTQ QFRRVLGQLA AA

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1), 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] (ISOFORM 1), VARIANT SER-76. Tissue: Cornea.
[4]	Lin L., Li H., Zhou G., Shen C., Ke R., Zhong G., Yang S. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), VARIANT SER-76. Tissue: Hippocampus, Teratocarcinoma and Testis.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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.
[8]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSPG4.
[9]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INPPL1.
[10]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, INTERACTION WITH BMX.
[11]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH BCAR1; CDC42 AND CRK.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-139; THR-269 AND SER-292, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"AND-34/BCAR3 regulates adhesion-dependent p130Cas serine phosphorylation and breast cancer cell growth pattern." Makkinje A., Near R.I., Infusini G., Vanden Borre P., Bloom A., Cai D., Costello C.E., Lerner A. Cell. Signal. 21:1423-1435(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-139; SER-437 AND SER-639, INTERACTION WITH BCAR3.
[14]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PTK2B/PYK2.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY SRC UPON ACTIVATION OF PTK2/FAK1.
[16]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PEAK1.
[17]	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)
[18]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-139, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, MASS SPECTROMETRY.
[20]	"Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14." Zhang P., Guo A., Possemato A., Wang C., Beard L., Carlin C., Markowitz S.D., Polakiewicz R.D., Wang Z. Oncogene 0:0-0(2012) [PubMed] [Europe PMC] [Abstract] Cited for: DEPHOSPHORYLATION BY PTPN14 AT TYR-128.
[21]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS) OF 3-71.
[22]	"NSP-Cas protein structures reveal a promiscuous interaction module in cell signaling." Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H., Pasquale E.B., Riedl S.J. Nat. Struct. Mol. Biol. 18:1381-1387(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 645-870 IN COMPLEX WITH SH2D3C.
[23]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-407.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ242987 mRNA. Translation: CAB75875.2.
AF218451 mRNA. Translation: AAF27527.1.
AB040024 mRNA. Translation: BAA92711.1.
AY545071 mRNA. Translation: AAS48631.1.
AK027608 mRNA. Translation: BAB55230.1.
AK295809 mRNA. Translation: BAG58627.1.
AK302617 mRNA. Translation: BAH13763.1.
AC009078 Genomic DNA. No translation available.

IPI

IPI00011998.
IPI00872386.
IPI00954799.
IPI00954889.

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, 739-870.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33855N.

IntAct

P56945. 22 interactions.

MINT

MINT-1505539.

STRING

9606.ENSP00000162330.

PTM databases

PhosphoSite

P56945.

Polymorphism databases

DMDM

288558806.

Proteomic databases

PaxDb

P56945.

PRIDE

P56945.

Protocols and materials databases

DNASU

9564.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000162330; ENSP00000162330; ENSG00000050820.
ENST00000393420; ENSP00000377072; ENSG00000050820.
ENST00000420641; ENSP00000392708; ENSG00000050820.
ENST00000535626; ENSP00000440370; ENSG00000050820.

GeneID

9564.

KEGG

hsa:9564.

UCSC

uc002fdv.3. human.
uc010cgu.3. human.
uc010vnc.2. human.
uc010vnd.2. human.

Organism-specific databases

CTD

9564.

GeneCards

GC16M075262.

H-InvDB

HIX0173293.

HGNC

HGNC:971. BCAR1.

HPA

CAB000443.

MIM

602941. gene.

neXtProt

NX_P56945.

PharmGKB

PA25281.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG82196.

HOGENOM

HOG000261698.

HOVERGEN

HBG004354.

KO

K05726.

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.

SignaLink

P56945.

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]

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

Search...

Other

ChEMBL

CHEMBL5559.

ChiTaRS

BCAR1. human.

EvolutionaryTrace

P56945.

GenomeRNAi

9564.

NextBio

35871.

SOURCE

Search...

Entry information

Entry name

BCAR1_HUMAN

Accession

Primary (citable) accession number: P56945
Secondary accession number(s): B4DIW5 , B7Z7X7, F5GXV6, F8WA69, Q6QEF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 9, 2010
Last modified:	May 29, 2013
This is version 132 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.