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Q61140

- BCAR1_MOUSE

UniProt

Q61140 - BCAR1_MOUSE

Protein

Breast cancer anti-estrogen resistance protein 1

Gene

Bcar1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 By similarity. Has been shown to be essential in cardiovascular development during embryogenesis.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. signal transducer activity Source: InterPro

    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. cell adhesion Source: UniProtKB-KW
    5. cell chemotaxis Source: Ensembl
    6. cell migration Source: UniProtKB
    7. cellular response to hepatocyte growth factor stimulus Source: Ensembl
    8. epidermal growth factor receptor signaling pathway Source: UniProtKB
    9. G-protein coupled receptor signaling pathway Source: UniProtKB
    10. hepatocyte growth factor receptor signaling pathway Source: Ensembl
    11. insulin receptor signaling pathway Source: UniProtKB
    12. integrin-mediated signaling pathway Source: UniProtKB
    13. neurotrophin TRK receptor signaling pathway Source: UniProtKB
    14. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    15. positive regulation of cell migration Source: UniProtKB
    16. positive regulation of endothelial cell migration Source: Ensembl
    17. vascular endothelial growth factor receptor signaling pathway Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Breast cancer anti-estrogen resistance protein 1
    Alternative name(s):
    CRK-associated substrate
    p130cas
    Gene namesi
    Name:Bcar1
    Synonyms:Cas, Crkas
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:108091. Bcar1.

    Subcellular locationi

    Cell junctionfocal adhesion By similarity. Cytoplasm By similarity
    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. focal adhesion Source: UniProtKB
    3. lamellipodium Source: MGI
    4. plasma membrane Source: Ensembl
    5. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 874874Breast cancer anti-estrogen resistance protein 1PRO_0000064855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei132 – 1321Phosphotyrosine1 Publication
    Modified residuei143 – 1431PhosphoserineBy similarity
    Modified residuei253 – 2531Phosphotyrosine; by ABL1By similarity
    Modified residuei273 – 2731PhosphothreonineBy similarity
    Modified residuei296 – 2961PhosphoserineBy similarity
    Modified residuei366 – 3661Phosphotyrosine1 Publication
    Modified residuei376 – 3761Phosphotyrosine1 Publication
    Modified residuei414 – 4141Phosphotyrosine1 Publication
    Modified residuei432 – 4321PhosphoserineBy similarity
    Modified residuei441 – 4411PhosphoserineBy similarity
    Modified residuei643 – 6431PhosphoserineBy similarity

    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 By similarity.By similarity
    Dephosphorylated by PTPN14 at Tyr-132.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ61140.
    PaxDbiQ61140.
    PRIDEiQ61140.

    PTM databases

    PhosphoSiteiQ61140.

    Expressioni

    Gene expression databases

    BgeeiQ61140.
    CleanExiMM_BCAR1.
    GenevestigatoriQ61140.

    Interactioni

    Subunit structurei

    Forms complexes in vivo with PTK2/FAK1, adapter protein CRKL and LYN kinase. Can heterodimerize with NEDD9. Interacts with activated CSPG4. Interacts with BMX, INPPL1/SHIP2 and PEAK1 By similarity. Part of a collagen stimulated complex involved in cell migration composed of CDC42, CRK, TNK2 and BCAR1/p130cas By similarity. Interacts with BCAR3, the interaction regulates adhesion-dependent serine phosphorylation. Interacts with NPHP1, PTK2B/PYK2 and SH2D3C.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Nphp1Q9QY532EBI-77088,EBI-77230
    Ptk2P341523EBI-77088,EBI-77070
    PTPN1P180315EBI-77088,EBI-968788From a different organism.
    Srcin1Q9QWI62EBI-77088,EBI-775592

    Protein-protein interaction databases

    BioGridi198886. 6 interactions.
    IntActiQ61140. 14 interactions.
    MINTiMINT-100691.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61140.
    SMRiQ61140. Positions 5-71, 454-614, 743-874.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini6 – 2621SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni119 – 420302Substrate for kinasesBy similarityAdd
    BLAST
    Regioni750 – 80051Divergent helix-loop-helix motifAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi639 – 6479SH3-bindingSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi74 – 8714Pro-richAdd
    BLAST
    Compositional biasi426 – 618193Ser-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 ABL SH2 domains. The HLH motif is absolutely required for the induction of pseudohyphal growth in yeast and mediates heterodimerization with NEDD9.
    A serine-rich region promotes activation of the serum response element (SRE).By similarity
    The SH3 domain is necessary for the localization of the protein to focal adhesions and interacts with one proline-rich region of PTK2/FAK1.

    Sequence similaritiesi

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

    Keywords - Domaini

    SH3 domain, SH3-binding

    Phylogenomic databases

    eggNOGiNOG82196.
    GeneTreeiENSGT00490000043324.
    HOGENOMiHOG000261698.
    HOVERGENiHBG004354.
    KOiK05726.
    OMAiFAKAKPF.
    OrthoDBiEOG7QRQTD.
    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 (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Cas-B (identifier: Q61140-1) [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

    MTVPNVLAKA LYDNVAESPD ELSFRKGDIM TVLERDTQGL DGWWLCSLHG    50
    RQGIVPGNRL KILVGMYDKK PVGPGPGPPA TPPQPQPSLP QGVHAPVPPA 100
    SQYSPMLPTA YQPQSDNVYL VPTPSKTQQG LYQAPGPNPQ FQSPPAKQTS 150
    TFSKQTPHHS FPSPATDLYQ VPPGPGSPAQ DIYQVPPSAG IGHDIYQVPP 200
    SLDTRGWEGT KPPAKVVVPT RVGQGYVYEA AQTEQDEYDT PRHLLAPGPQ 250
    DIYDVPPVRG LLPNQYGQEV YDTPPMAVKG PNGRDPLLDV YDVPPSVEKG 300
    LLSSSHHSVY DVPPSVSKDV PDGPLLREET YDVPPAFAKP KPFDPTRHPL 350
    ILAAPPPDSP AAEDVYDVPP PAPDLYDVPP GLRRPGPGTL YDVPRERVLP 400
    PEVADGSVVD DGVYAVPPPA EREAPTDGKR LSASSTGSTR SSQSASSLEV 450
    VVPGREPLEL EVAVESLARL QQGVSTTVAH LLDLVGSASG PGGWRGTSEP 500
    QEPPAQDLKA AVAAVHGAVH ELLEFARGAV SNATHTSDRT LHAKLSRQLQ 550
    KMEDVYQTLV VHGQVLDSGR GSPGFTPEDL DRLVACSRAV PEDAKQLASF 600
    LHGNASLLFR RTKAPGPGPE GSSSLHPNPT DKASSIQSRP LPSPPKFTSQ 650
    DSPDGQYENS EGGWMEDYDY VHLQGKEEFE KTQKELLERG NIMRQGKGQL 700
    ELQQLKQFER LEQEVSRPID HDLANWTPAQ PLVPGRTGGL GPSDRQLLLF 750
    YLEQCEANLT TLTDAVDAFF TAVATNQPPK IFVAHSKFVI LSAHKLVFIG 800
    DTLSRQAKAA DVRSQVTHYS NLLCDLLRGI VATTKAAALQ YPSPSAAQDM 850
    VDRVKELGHS TQQFRRVLGQ LAAA 874
    Length:874
    Mass (Da):94,285
    Last modified:July 27, 2011 - v2
    Checksum:i81E56BC7AD87B095
    GO
    Isoform Cas-A (identifier: Q61140-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:874
    Mass (Da):94,392
    Checksum:i25B8F5D1D61CC8B1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721V → A in AAA93381. (PubMed:7479864)Curated
    Sequence conflicti72 – 721V → A in AAA93248. (PubMed:7479864)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 44MTVP → MKYL in isoform Cas-A. 1 PublicationVSP_004134

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48853 mRNA. Translation: AAA93381.1.
    U28151 mRNA. Translation: AAA93248.1.
    AK145863 mRNA. Translation: BAE26705.1.
    BC057578 mRNA. Translation: AAH57578.1.
    CCDSiCCDS52675.1. [Q61140-1]
    RefSeqiNP_001185768.1. NM_001198839.1. [Q61140-2]
    NP_034084.2. NM_009954.3. [Q61140-1]
    UniGeneiMm.3758.

    Genome annotation databases

    EnsembliENSMUST00000166232; ENSMUSP00000129584; ENSMUSG00000031955. [Q61140-1]
    GeneIDi12927.
    KEGGimmu:12927.
    UCSCiuc009nmt.2. mouse. [Q61140-2]
    uc009nmu.2. mouse. [Q61140-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48853 mRNA. Translation: AAA93381.1 .
    U28151 mRNA. Translation: AAA93248.1 .
    AK145863 mRNA. Translation: BAE26705.1 .
    BC057578 mRNA. Translation: AAH57578.1 .
    CCDSi CCDS52675.1. [Q61140-1 ]
    RefSeqi NP_001185768.1. NM_001198839.1. [Q61140-2 ]
    NP_034084.2. NM_009954.3. [Q61140-1 ]
    UniGenei Mm.3758.

    3D structure databases

    ProteinModelPortali Q61140.
    SMRi Q61140. Positions 5-71, 454-614, 743-874.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198886. 6 interactions.
    IntActi Q61140. 14 interactions.
    MINTi MINT-100691.

    PTM databases

    PhosphoSitei Q61140.

    Proteomic databases

    MaxQBi Q61140.
    PaxDbi Q61140.
    PRIDEi Q61140.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000166232 ; ENSMUSP00000129584 ; ENSMUSG00000031955 . [Q61140-1 ]
    GeneIDi 12927.
    KEGGi mmu:12927.
    UCSCi uc009nmt.2. mouse. [Q61140-2 ]
    uc009nmu.2. mouse. [Q61140-1 ]

    Organism-specific databases

    CTDi 9564.
    MGIi MGI:108091. Bcar1.

    Phylogenomic databases

    eggNOGi NOG82196.
    GeneTreei ENSGT00490000043324.
    HOGENOMi HOG000261698.
    HOVERGENi HBG004354.
    KOi K05726.
    OMAi FAKAKPF.
    OrthoDBi EOG7QRQTD.
    TreeFami TF328782.

    Miscellaneous databases

    NextBioi 282588.
    PROi Q61140.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61140.
    CleanExi MM_BCAR1.
    Genevestigatori Q61140.

    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. "Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas."
      Polte T.R., Hanks S.K.
      Proc. Natl. Acad. Sci. U.S.A. 92:10678-10682(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CAS-A AND CAS-B), INTERACTION WITH PTK2/FAK1.
      Tissue: Embryo.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Placenta.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
    4. "AND-34, a novel p130Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines."
      Cai D., Clayton L.K., Smolyar A., Lerner A.
      J. Immunol. 163:2104-2112(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCAR3.
    5. "Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells."
      Donaldson J.C., Dempsey P.J., Reddy S., Bouton A.H., Coffey R.J., Hanks S.K.
      Exp. Cell Res. 256:168-178(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NPHP1.
    6. "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-Ras guanine nucleotide exchange factor."
      Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.
      J. Biol. Chem. 275:30118-30123(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BCAR3.
    7. "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways."
      Sakakibara A., Hattori S.
      J. Biol. Chem. 275:6404-6410(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2D3C.
    8. "A novel hematopoietic adaptor protein, Chat-H, positively regulates T cell receptor-mediated interleukin-2 production by Jurkat cells."
      Sakakibara A., Hattori S., Nakamura S., Katagiri T.
      J. Biol. Chem. 278:6012-6017(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SH2D3C.
      Tissue: Spleen.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132; TYR-366; TYR-376 AND TYR-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    11. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiBCAR1_MOUSE
    AccessioniPrimary (citable) accession number: Q61140
    Secondary accession number(s): Q60869, Q6PFF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3