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P56945

- BCAR1_HUMAN

UniProt

P56945 - BCAR1_HUMAN

Protein

Breast cancer anti-estrogen resistance protein 1

Gene

BCAR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (09 Feb 2010)
      Previous versions | rss
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    Functioni

    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.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase binding Source: UniProtKB
    3. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. actin filament organization Source: UniProtKB
    2. antigen receptor-mediated signaling pathway Source: UniProtKB
    3. B cell receptor signaling pathway Source: UniProtKB
    4. blood coagulation Source: Reactome
    5. cell adhesion Source: UniProtKB-KW
    6. cell chemotaxis Source: BHF-UCL
    7. cell division Source: UniProtKB
    8. cell migration Source: UniProtKB
    9. cell proliferation Source: ProtInc
    10. cellular response to hepatocyte growth factor stimulus Source: BHF-UCL
    11. epidermal growth factor receptor signaling pathway Source: UniProtKB
    12. G-protein coupled receptor signaling pathway Source: UniProtKB
    13. hepatocyte growth factor receptor signaling pathway Source: BHF-UCL
    14. insulin receptor signaling pathway Source: UniProtKB
    15. integrin-mediated signaling pathway Source: UniProtKB
    16. neurotrophin TRK receptor signaling pathway Source: UniProtKB
    17. platelet activation Source: Reactome
    18. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    19. positive regulation of cell migration Source: UniProtKB
    20. positive regulation of endothelial cell migration Source: BHF-UCL
    21. regulation of apoptotic process Source: UniProtKB
    22. regulation of cell growth Source: UniProtKB
    23. T cell receptor signaling pathway Source: UniProtKB
    24. vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_17025. Downstream signal transduction.
    SignaLinkiP56945.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Breast cancer anti-estrogen resistance protein 1
    Alternative name(s):
    CRK-associated substrate
    Cas scaffolding protein family member 1
    p130cas
    Gene namesi
    Name:BCAR1
    Synonyms:CAS, CASS1, CRKAS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:971. BCAR1.

    Subcellular locationi

    Cell junctionfocal adhesion 1 Publication. Cytoplasm 1 Publication
    Note: Unphosphorylated form localizes in the cytoplasm and can move to the membrane upon tyrosine phosphorylation.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. focal adhesion Source: UniProtKB
    4. lamellipodium Source: Ensembl
    5. nucleolus Source: HPA
    6. plasma membrane Source: HPA
    7. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25281.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 870870Breast cancer anti-estrogen resistance protein 1PRO_0000064854Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei128 – 1281Phosphotyrosine; by SRC1 Publication
    Modified residuei134 – 1341Phosphoserine2 Publications
    Modified residuei139 – 1391Phosphoserine3 Publications
    Modified residuei249 – 2491Phosphotyrosine; by ABL1By similarity
    Modified residuei269 – 2691Phosphothreonine1 Publication
    Modified residuei292 – 2921Phosphoserine1 Publication
    Modified residuei362 – 3621PhosphotyrosineBy similarity
    Modified residuei372 – 3721PhosphotyrosineBy similarity
    Modified residuei410 – 4101PhosphotyrosineBy similarity
    Modified residuei428 – 4281Phosphoserine1 Publication
    Modified residuei437 – 4371Phosphoserine1 Publication
    Modified residuei639 – 6391Phosphoserine1 Publication

    Post-translational modificationi

    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.7 Publications
    Dephosphorylated by PTPN14 at Tyr-128.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP56945.
    PaxDbiP56945.
    PRIDEiP56945.

    PTM databases

    PhosphoSiteiP56945.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiP56945.
    BgeeiP56945.
    CleanExiHS_BCAR1.
    GenevestigatoriP56945.

    Organism-specific databases

    HPAiCAB000443.
    HPA042282.

    Interactioni

    Subunit structurei

    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/PYK2.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRKP461085EBI-702093,EBI-886
    FYNP062413EBI-702093,EBI-515315
    INPPL1O153572EBI-702093,EBI-1384248
    MMP14P502813EBI-702093,EBI-992788
    PTK2Q053972EBI-702093,EBI-702142
    PTPN1P180315EBI-702093,EBI-968788
    PTPN12Q052094EBI-702093,EBI-2266035
    SRCP129313EBI-702093,EBI-621482
    SRCIN1Q9C0H93EBI-702093,EBI-1393949
    Srcin1Q9QWI63EBI-702093,EBI-775592From a different organism.
    TNK2Q079125EBI-702093,EBI-603457
    TNSQ042052EBI-702093,EBI-2607590From a different organism.
    TNS3Q68CZ28EBI-702093,EBI-1220488

    Protein-protein interaction databases

    BioGridi114934. 64 interactions.
    DIPiDIP-33855N.
    IntActiP56945. 32 interactions.
    MINTiMINT-1505539.
    STRINGi9606.ENSP00000162330.

    Structurei

    Secondary structure

    1
    870
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Beta strandi29 – 346
    Helixi37 – 393
    Beta strandi43 – 486
    Beta strandi51 – 566
    Helixi57 – 593
    Beta strandi60 – 689
    Helixi740 – 77031
    Helixi775 – 80127
    Helixi806 – 83530
    Helixi840 – 87031

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WYXX-ray1.14A/B3-71[»]
    3T6GX-ray2.50B/D645-870[»]
    ProteinModelPortaliP56945.
    SMRiP56945. Positions 3-71, 448-610, 739-870.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56945.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 6563SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni115 – 416302Substrate for kinasesBy similarityAdd
    BLAST
    Regioni746 – 79651Divergent helix-loop-helix motifAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi635 – 6439SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi74 – 8714Pro-richAdd
    BLAST
    Compositional biasi422 – 614193Ser-richAdd
    BLAST

    Domaini

    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).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.

    Sequence similaritiesi

    Belongs to the CAS family.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain, SH3-binding

    Phylogenomic databases

    eggNOGiNOG82196.
    HOGENOMiHOG000261698.
    HOVERGENiHBG004354.
    KOiK05726.
    OMAiFAKAKPF.
    OrthoDBiEOG7QRQTD.
    PhylomeDBiP56945.
    TreeFamiTF328782.

    Family and domain databases

    InterProiIPR028848. BCAR1.
    IPR021901. CAS_DUF3513.
    IPR014928. Serine_rich.
    IPR001452. SH3_domain.
    IPR013315. Spectrin_alpha_SH3.
    [Graphical view]
    PANTHERiPTHR10654:SF5. PTHR10654:SF5. 1 hit.
    PfamiPF12026. DUF3513. 1 hit.
    PF08824. Serine_rich. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P56945-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MNHLNVLAKA LYDNVAESPD ELSFRKGDIM TVLEQDTQGL DGWWLCSLHG    50
    RQGIVPGNRL KILVGMYDKK PAGPGPGPPA TPAQPQPGLH APAPPASQYT 100
    PMLPNTYQPQ PDSVYLVPTP SKAQQGLYQV PGPSPQFQSP PAKQTSTFSK 150
    QTPHHPFPSP ATDLYQVPPG PGGPAQDIYQ VPPSAGMGHD IYQVPPSMDT 200
    RSWEGTKPPA KVVVPTRVGQ GYVYEAAQPE QDEYDIPRHL LAPGPQDIYD 250
    VPPVRGLLPS QYGQEVYDTP PMAVKGPNGR DPLLEVYDVP PSVEKGLPPS 300
    NHHAVYDVPP SVSKDVPDGP LLREETYDVP PAFAKAKPFD PARTPLVLAA 350
    PPPDSPPAED VYDVPPPAPD LYDVPPGLRR PGPGTLYDVP RERVLPPEVA 400
    DGGVVDSGVY AVPPPAEREA PAEGKRLSAS STGSTRSSQS ASSLEVAGPG 450
    REPLELEVAV EALARLQQGV SATVAHLLDL AGSAGATGSW RSPSEPQEPL 500
    VQDLQAAVAA VQSAVHELLE FARSAVGNAA HTSDRALHAK LSRQLQKMED 550
    VHQTLVAHGQ ALDAGRGGSG ATLEDLDRLV ACSRAVPEDA KQLASFLHGN 600
    ASLLFRRTKA TAPGPEGGGT LHPNPTDKTS SIQSRPLPSP PKFTSQDSPD 650
    GQYENSEGGW MEDYDYVHLQ GKEEFEKTQK ELLEKGSITR QGKSQLELQQ 700
    LKQFERLEQE VSRPIDHDLA NWTPAQPLAP GRTGGLGPSD RQLLLFYLEQ 750
    CEANLTTLTN AVDAFFTAVA TNQPPKIFVA HSKFVILSAH KLVFIGDTLS 800
    RQAKAADVRS QVTHYSNLLC DLLRGIVATT KAAALQYPSP SAAQDMVERV 850
    KELGHSTQQF RRVLGQLAAA 870
    Length:870
    Mass (Da):93,372
    Last modified:February 9, 2010 - v2
    Checksum:iB81EC3430049E795
    GO
    Isoform 2 (identifier: P56945-2) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:888
    Mass (Da):95,469
    Checksum:i4CA6EC5C8EFE3DA6
    GO
    Isoform 3 (identifier: P56945-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:888
    Mass (Da):95,454
    Checksum:iFF81642D11EB93AC
    GO
    Isoform 4 (identifier: P56945-4) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:722
    Mass (Da):77,731
    Checksum:i2537ED6C3BEBE512
    GO
    Isoform 5 (identifier: P56945-5) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:868
    Mass (Da):93,137
    Checksum:iDB6B70B2AB1926CD
    GO
    Isoform 6 (identifier: P56945-6) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:916
    Mass (Da):97,877
    Checksum:i3A5FDEB4BA15527B
    GO
    Isoform 7 (identifier: P56945-7) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:888
    Mass (Da):95,216
    Checksum:iCD3BA8494536FC76
    GO
    Isoform 8 (identifier: P56945-8) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:870
    Mass (Da):93,291
    Checksum:i2262F3718326A675
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti63 – 631L → S in BAB55230. (PubMed:14702039)Curated
    Sequence conflicti236 – 2361I → T in AAF27527. 1 PublicationCurated
    Sequence conflicti254 – 2541V → I in BAG54099. (PubMed:14702039)Curated
    Sequence conflicti349 – 3491A → G in AAF27527. 1 PublicationCurated
    Sequence conflicti363 – 3631D → Y in AAF27527. 1 PublicationCurated
    Sequence conflicti385 – 3851T → A in AAS48631. 1 PublicationCurated
    Sequence conflicti428 – 4281S → P in BAB55230. (PubMed:14702039)Curated
    Sequence conflicti471 – 4711S → G in BAB55230. (PubMed:14702039)Curated
    Sequence conflicti600 – 6001N → S in AAS48631. 1 PublicationCurated
    Sequence conflicti700 – 7001Q → R in BAH13763. (PubMed:14702039)Curated
    Sequence conflicti714 – 7141P → L in BAG54099. (PubMed:14702039)Curated
    Sequence conflicti740 – 7401D → G in AAS48631. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761P → S.4 Publications
    Corresponds to variant rs1035539 [ dbSNP | Ensembl ].
    VAR_058970
    Natural varianti407 – 4071S → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035798
    Natural varianti491 – 4911R → L.
    Corresponds to variant rs16957558 [ dbSNP | Ensembl ].
    VAR_057820
    Natural varianti558 – 5581H → R.
    Corresponds to variant rs16957552 [ dbSNP | Ensembl ].
    VAR_057821

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MNHL → MLTHRPQEAEQRGRTPGPSF EW in isoform 2. 1 PublicationVSP_043559
    Alternative sequencei1 – 44MNHL → MQGK in isoform 4. 1 PublicationVSP_046127
    Alternative sequencei1 – 44MNHL → ME in isoform 5. 1 PublicationVSP_046748
    Alternative sequencei1 – 44MNHL → MPAKPFLSSVLLSWKVLDFS GPGPQGTGQPCSCGHWAEGQ GGPPEPAGGP in isoform 6. 1 PublicationVSP_046749
    Alternative sequencei1 – 44MNHL → MHCPGEAPLAAPRPTPKDPC LR in isoform 7. 1 PublicationVSP_046750
    Alternative sequencei1 – 44MNHL → MSVP in isoform 8. 1 PublicationVSP_046751
    Alternative sequencei64 – 211148Missing in isoform 4. 1 PublicationVSP_046128Add
    BLAST
    Alternative sequencei304 – 3041A → AVSKCQGNARARLRLWGVW in isoform 3. 1 PublicationVSP_045355

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10915.1. [P56945-1]
    CCDS54037.1. [P56945-5]
    CCDS54038.1. [P56945-3]
    CCDS54039.1. [P56945-4]
    CCDS54040.1. [P56945-6]
    CCDS54041.1. [P56945-8]
    CCDS54042.1. [P56945-2]
    CCDS54043.1. [P56945-7]
    RefSeqiNP_001164185.1. NM_001170714.1. [P56945-6]
    NP_001164186.1. NM_001170715.1. [P56945-7]
    NP_001164187.1. NM_001170716.1. [P56945-2]
    NP_001164188.1. NM_001170717.1. [P56945-3]
    NP_001164189.1. NM_001170718.1. [P56945-8]
    NP_001164190.1. NM_001170719.1. [P56945-5]
    NP_001164191.1. NM_001170720.1. [P56945-4]
    NP_001164192.1. NM_001170721.1.
    NP_055382.2. NM_014567.3. [P56945-1]
    XP_006721411.1. XM_006721348.1. [P56945-6]
    UniGeneiHs.479747.

    Genome annotation databases

    EnsembliENST00000162330; 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]
    GeneIDi9564.
    KEGGihsa:9564.
    UCSCiuc002fdv.3. human. [P56945-1]
    uc010vnd.2. human. [P56945-2]

    Polymorphism databases

    DMDMi288558806.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS10915.1. [P56945-1 ]
    CCDS54037.1. [P56945-5 ]
    CCDS54038.1. [P56945-3 ]
    CCDS54039.1. [P56945-4 ]
    CCDS54040.1. [P56945-6 ]
    CCDS54041.1. [P56945-8 ]
    CCDS54042.1. [P56945-2 ]
    CCDS54043.1. [P56945-7 ]
    RefSeqi NP_001164185.1. NM_001170714.1. [P56945-6 ]
    NP_001164186.1. NM_001170715.1. [P56945-7 ]
    NP_001164187.1. NM_001170716.1. [P56945-2 ]
    NP_001164188.1. NM_001170717.1. [P56945-3 ]
    NP_001164189.1. NM_001170718.1. [P56945-8 ]
    NP_001164190.1. NM_001170719.1. [P56945-5 ]
    NP_001164191.1. NM_001170720.1. [P56945-4 ]
    NP_001164192.1. NM_001170721.1.
    NP_055382.2. NM_014567.3. [P56945-1 ]
    XP_006721411.1. XM_006721348.1. [P56945-6 ]
    UniGenei Hs.479747.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P56945.
    SMRi P56945. Positions 3-71, 448-610, 739-870.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114934. 64 interactions.
    DIPi DIP-33855N.
    IntActi P56945. 32 interactions.
    MINTi MINT-1505539.
    STRINGi 9606.ENSP00000162330.

    PTM databases

    PhosphoSitei P56945.

    Polymorphism databases

    DMDMi 288558806.

    Proteomic databases

    MaxQBi P56945.
    PaxDbi P56945.
    PRIDEi P56945.

    Protocols and materials databases

    DNASUi 9564.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000162330 ; 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 ]
    GeneIDi 9564.
    KEGGi hsa:9564.
    UCSCi uc002fdv.3. human. [P56945-1 ]
    uc010vnd.2. human. [P56945-2 ]

    Organism-specific databases

    CTDi 9564.
    GeneCardsi GC16M075262.
    H-InvDB HIX0173293.
    HGNCi HGNC:971. BCAR1.
    HPAi CAB000443.
    HPA042282.
    MIMi 602941. gene.
    neXtProti NX_P56945.
    PharmGKBi PA25281.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82196.
    HOGENOMi HOG000261698.
    HOVERGENi HBG004354.
    KOi K05726.
    OMAi FAKAKPF.
    OrthoDBi EOG7QRQTD.
    PhylomeDBi P56945.
    TreeFami TF328782.

    Enzyme and pathway databases

    Reactomei REACT_15381. p130Cas linkage to MAPK signaling for integrins.
    REACT_17025. Downstream signal transduction.
    SignaLinki P56945.

    Miscellaneous databases

    ChiTaRSi BCAR1. human.
    EvolutionaryTracei P56945.
    GeneWikii BCAR1.
    GenomeRNAii 9564.
    NextBioi 35471708.
    PROi P56945.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P56945.
    Bgeei P56945.
    CleanExi HS_BCAR1.
    Genevestigatori P56945.

    Family and domain databases

    InterProi IPR028848. BCAR1.
    IPR021901. CAS_DUF3513.
    IPR014928. Serine_rich.
    IPR001452. SH3_domain.
    IPR013315. Spectrin_alpha_SH3.
    [Graphical view ]
    PANTHERi PTHR10654:SF5. PTHR10654:SF5. 1 hit.
    Pfami PF12026. DUF3513. 1 hit.
    PF08824. Serine_rich. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00452. SH3DOMAIN.
    PR01887. SPECTRNALPHA.
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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; 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.
      , 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. 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. Cited for: INTERACTION WITH PEAK1.
    17. "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.
    18. "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].
    19. "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 AT TYR-128 BY PTPN14, PHOSPHORYLATION AT TYR-128 BY SRC.
    20. "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.
    21. "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.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-407.

    Entry informationi

    Entry nameiBCAR1_HUMAN
    AccessioniPrimary (citable) accession number: P56945
    Secondary accession number(s): B3KWD7
    , B4DEV4, B4DGB5, B4DIW5, B7Z7X7, E9PCL5, E9PCV2, F5GXA2, F5GXV6, F5H7Z0, F8WA69, Q6QEF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: February 9, 2010
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3