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P56945 (BCAR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length870 AA.
Sequence statusComplete.
Protein existenceEvidence 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 junctionfocal 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 processCell adhesion
   Cellular componentCell junction
Cytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3 domain
SH3-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB 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

antigen receptor-mediated signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

blood coagulation

Traceable author statement. Source: Reactome

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 migration

Inferred from direct assay PubMed 9425168. 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 cell migration

Inferred from direct assay PubMed 9472046. 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_componentcytoplasm

Inferred from direct assay PubMed 8070403. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

ruffle

Inferred from direct assay PubMed 9472046. Source: UniProtKB

   Molecular_functionprotein kinase binding

Inferred from physical interaction PubMed 10026197PubMed 8070403PubMed 8649368PubMed 9020138PubMed 9472046. Source: UniProtKB

signal transducer activity

Traceable author statement PubMed 8070403. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 8 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.
Isoform 5 (identifier: P56945-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → ME
Note: No experimental confirmation available.
Isoform 6 (identifier: P56945-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → MPAKPFLSSVLLSWKVLDFSGPGPQGTGQPCSCGHWAEGQGGPPEPAGGP
Note: No experimental confirmation available.
Isoform 7 (identifier: P56945-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → MHCPGEAPLAAPRPTPKDPCLR
Note: No experimental confirmation available.
Isoform 8 (identifier: P56945-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MNHL → MSVP
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 870870Breast cancer anti-estrogen resistance protein 1
PRO_0000064854

Regions

Domain3 – 6563SH3
Region115 – 416302Substrate for kinases By similarity
Region746 – 79651Divergent helix-loop-helix motif
Motif635 – 6439SH3-binding Potential
Compositional bias74 – 8714Pro-rich
Compositional bias422 – 614193Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7
Modified residue1281Phosphotyrosine; by SRC
Modified residue1341Phosphoserine Ref.12 Ref.18
Modified residue1391Phosphoserine Ref.12 Ref.13 Ref.18
Modified residue2491Phosphotyrosine; by ABL1
Modified residue2691Phosphothreonine Ref.12
Modified residue2921Phosphoserine Ref.12
Modified residue3621Phosphotyrosine By similarity
Modified residue3721Phosphotyrosine By similarity
Modified residue4101Phosphotyrosine By similarity
Modified residue4281Phosphoserine Ref.19
Modified residue4371Phosphoserine Ref.13
Modified residue6391Phosphoserine Ref.13

Natural variations

Alternative sequence1 – 44MNHL → MLTHRPQEAEQRGRTPGPSF EW in isoform 2.
VSP_043559
Alternative sequence1 – 44MNHL → MQGK in isoform 4.
VSP_046127
Alternative sequence1 – 44MNHL → ME in isoform 5.
VSP_046748
Alternative sequence1 – 44MNHL → MPAKPFLSSVLLSWKVLDFS GPGPQGTGQPCSCGHWAEGQ GGPPEPAGGP in isoform 6.
VSP_046749
Alternative sequence1 – 44MNHL → MHCPGEAPLAAPRPTPKDPC LR in isoform 7.
VSP_046750
Alternative sequence1 – 44MNHL → MSVP in isoform 8.
VSP_046751
Alternative sequence64 – 211148Missing in isoform 4.
VSP_046128
Alternative sequence3041A → AVSKCQGNARARLRLWGVW in isoform 3.
VSP_045355
Natural variant761P → S. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs1035539 [ dbSNP | Ensembl ].
VAR_058970
Natural variant4071S → T in a breast cancer sample; somatic mutation. Ref.23
VAR_035798
Natural variant4911R → L.
Corresponds to variant rs16957558 [ dbSNP | Ensembl ].
VAR_057820
Natural variant5581H → R.
Corresponds to variant rs16957552 [ dbSNP | Ensembl ].
VAR_057821

Experimental info

Sequence conflict631L → S in BAB55230. Ref.5
Sequence conflict2361I → T in AAF27527. Ref.2
Sequence conflict2541V → I in BAG54099. Ref.5
Sequence conflict3491A → G in AAF27527. Ref.2
Sequence conflict3631D → Y in AAF27527. Ref.2
Sequence conflict3851T → A in AAS48631. Ref.4
Sequence conflict4281S → P in BAB55230. Ref.5
Sequence conflict4711S → G in BAB55230. Ref.5
Sequence conflict6001N → S in AAS48631. Ref.4
Sequence conflict7001Q → R in BAH13763. Ref.5
Sequence conflict7141P → L in BAG54099. Ref.5
Sequence conflict7401D → G in AAS48631. Ref.4

Secondary structure

.................... 870
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 9, 2010. Version 2.
Checksum: B81EC3430049E795

FASTA87093,372
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 4CA6EC5C8EFE3DA6
Show »

FASTA88895,469
Isoform 3 [UniParc].

Checksum: FF81642D11EB93AC
Show »

FASTA88895,454
Isoform 4 [UniParc].

Checksum: 2537ED6C3BEBE512
Show »

FASTA72277,731
Isoform 5 [UniParc].

Checksum: DB6B70B2AB1926CD
Show »

FASTA86893,137
Isoform 6 [UniParc].

Checksum: 3A5FDEB4BA15527B
Show »

FASTA91697,877
Isoform 7 [UniParc].

Checksum: CD3BA8494536FC76
Show »

FASTA88895,216
Isoform 8 [UniParc].

Checksum: 2262F3718326A675
Show »

FASTA87093,291

References

« Hide '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. expand/collapse author list , 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; 4; 5; 6; 7 AND 8), VARIANT SER-76.
Tissue: Amygdala, Caudate nucleus, Cerebellum, 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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 32:2087-2095(2013) [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. expand/collapse author list , 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.

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.
AK124815 mRNA. Translation: BAG54099.1.
AK293808 mRNA. Translation: BAG57215.1.
AK294513 mRNA. Translation: BAG57726.1.
AK295809 mRNA. Translation: BAG58627.1.
AK302617 mRNA. Translation: BAH13763.1.
AC009078 Genomic DNA. No translation available.
RefSeqNP_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.
UniGeneHs.479747.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYXX-ray1.14A/B3-71[»]
3T6GX-ray2.50B/D645-870[»]
ProteinModelPortalP56945.
SMRP56945. Positions 3-71, 448-610, 739-870.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114934. 64 interactions.
DIPDIP-33855N.
IntActP56945. 32 interactions.
MINTMINT-1505539.
STRING9606.ENSP00000162330.

PTM databases

PhosphoSiteP56945.

Polymorphism databases

DMDM288558806.

Proteomic databases

PaxDbP56945.
PRIDEP56945.

Protocols and materials databases

DNASU9564.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000162330; ENSP00000162330; ENSG00000050820. [P56945-1]
ENST00000393420; ENSP00000377072; ENSG00000050820. [P56945-3]
ENST00000393422; ENSP00000377074; ENSG00000050820. [P56945-7]
ENST00000418647; ENSP00000391669; ENSG00000050820. [P56945-6]
ENST00000420641; ENSP00000392708; ENSG00000050820. [P56945-2]
ENST00000535626; ENSP00000440370; ENSG00000050820. [P56945-4]
ENST00000538440; ENSP00000443841; ENSG00000050820. [P56945-8]
ENST00000542031; ENSP00000440415; ENSG00000050820. [P56945-5]
GeneID9564.
KEGGhsa:9564.
UCSCuc002fdv.3. human. [P56945-1]
uc010vnd.2. human. [P56945-2]

Organism-specific databases

CTD9564.
GeneCardsGC16M075262.
H-InvDBHIX0173293.
HGNCHGNC:971. BCAR1.
HPACAB000443.
HPA042282.
MIM602941. gene.
neXtProtNX_P56945.
PharmGKBPA25281.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82196.
HOGENOMHOG000261698.
HOVERGENHBG004354.
KOK05726.
OMAFAKAKPF.
OrthoDBEOG7QRQTD.
PhylomeDBP56945.
TreeFamTF328782.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
SignaLinkP56945.

Gene expression databases

ArrayExpressP56945.
BgeeP56945.
CleanExHS_BCAR1.
GenevestigatorP56945.

Family and domain databases

InterProIPR028848. BCAR1.
IPR021901. CAS_DUF3513.
IPR014928. Serine_rich.
IPR001452. SH3_domain.
IPR013315. Spectrin_alpha_SH3.
[Graphical view]
PANTHERPTHR10654:SF5. PTHR10654:SF5. 1 hit.
PfamPF12026. DUF3513. 1 hit.
PF08824. Serine_rich. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00452. SH3DOMAIN.
PR01887. SPECTRNALPHA.
SMARTSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSBCAR1. human.
EvolutionaryTraceP56945.
GeneWikiBCAR1.
GenomeRNAi9564.
NextBio35471708.
PROP56945.
SOURCESearch...

Entry information

Entry nameBCAR1_HUMAN
AccessionPrimary (citable) accession number: P56945
Secondary accession number(s): B3KWD7 expand/collapse secondary AC list , B4DEV4, B4DGB5, B4DIW5, B7Z7X7, E9PCL5, E9PCV2, F5GXA2, F5GXV6, F5H7Z0, F8WA69, Q6QEF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: February 9, 2010
Last modified: April 16, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM