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Q9QUN3

- BLNK_MOUSE

UniProt

Q9QUN3 - BLNK_MOUSE

Protein

B-cell linker protein

Gene

Blnk

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Functions as a central linker protein, downstream of the B-cell receptor (BCR), bridging the SYK kinase to a multitude of signaling pathways and regulating biological outcomes of B-cell function and development. Plays a role in the activation of ERK/EPHB2, MAP kinase p38 and JNK. Modulates AP1 activation. Important for the activation of NF-kappa-B and NFAT. Plays an important role in BCR-mediated PLCG1 and PLCG2 activation and Ca2+ mobilization and is required for trafficking of the BCR to late endosomes. However, does not seem to be required for pre-BCR-mediated activation of MAP kinase and phosphatidyl-inositol 3 (PI3) kinase signaling. May be required for the RAC1-JNK pathway. Plays a critical role in orchestrating the pro-B cell to pre-B cell transition. May play an important role in BCR-induced B-cell apoptosis.3 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. B cell activation Source: UniProtKB-KW
    2. intracellular signal transduction Source: Ensembl

    Keywords - Biological processi

    B-cell activation

    Enzyme and pathway databases

    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_198634. Regulation of signaling by CBL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    B-cell linker protein
    Alternative name(s):
    B-cell adapter containing a SH2 domain protein
    B-cell adapter containing a Src homology 2 domain protein
    Cytoplasmic adapter protein
    Lymphocyte antigen 57
    Src homology 2 domain-containing leukocyte protein of 65 kDa
    Short name:
    Slp-65
    Gene namesi
    Name:Blnk
    Synonyms:Bash, Ly57, Slp65
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 19

    Organism-specific databases

    MGIiMGI:96878. Blnk.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity
    Note: BCR activation results in the translocation to membrane fraction.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521Y → F: No effect on pre-BCR down-regulation. 1 Publication
    Mutagenesisi96 – 961Y → F: Fails to induce pre-BCR down-regulation, leading to splenomegaly and leukemia. 1 Publication
    Mutagenesisi373 – 3731R → L: Abolishes binding to CD79A and SYK. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 457457B-cell linker proteinPRO_0000064941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei72 – 721Phosphotyrosine; by SYKBy similarity
    Modified residuei84 – 841Phosphotyrosine; by SYKBy similarity
    Modified residuei96 – 961Phosphotyrosine; by SYKBy similarity
    Modified residuei178 – 1781Phosphotyrosine; by SYKBy similarity
    Modified residuei189 – 1891Phosphotyrosine; by SYKBy similarity

    Post-translational modificationi

    Following BCR activation, phosphorylated on tyrosine residues by SYK and LYN. When phosphorylated, serves as a scaffold to assemble downstream targets of antigen activation, including PLCG1, VAV1, GRB2 and NCK1. Phosphorylation of Tyr-84, Tyr-178 and Tyr-189 facilitates PLCG1 binding. Phosphorylation of Tyr-72 facilitates VAV1 and NCK1 binding. Phosphorylation is required for both Ca2+ and MAPK signaling pathways By similarity. Phosphorylation of Tyr-96 is required for the binding of BTK.By similarity1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9QUN3.
    PRIDEiQ9QUN3.

    PTM databases

    PhosphoSiteiQ9QUN3.

    Expressioni

    Tissue specificityi

    Expressed in the spleen and weakly in thymus, no expression was seen in liver, testis, or brain. Expressed in B-cell lines representing different developmental stages from the pre-B to the plasma cell stage, but not in a T-cell or a fibroblast cell line.1 Publication

    Gene expression databases

    ArrayExpressiQ9QUN3.
    BgeeiQ9QUN3.
    CleanExiMM_BLNK.
    GenevestigatoriQ9QUN3.

    Interactioni

    Subunit structurei

    Associates with PLCG1, VAV1 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with VAV3, PLCG2 and GRB2 By similarity. Interacts through its SH2 domain with CD79A. Interacts (via SH2 domain) with SYK; phosphorylated and activated by SYK. Interacts with SCIMP.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi201236. 5 interactions.
    IntActiQ9QUN3. 6 interactions.
    MINTiMINT-110328.

    Structurei

    Secondary structure

    1
    457
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi334 – 3407
    Turni341 – 3444
    Beta strandi346 – 3516
    Helixi354 – 36411
    Beta strandi372 – 3743
    Beta strandi383 – 3908
    Beta strandi393 – 3997
    Turni403 – 4064
    Beta strandi410 – 4123
    Beta strandi420 – 4223
    Helixi423 – 43210
    Beta strandi440 – 4423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EO6NMR-A330-457[»]
    ProteinModelPortaliQ9QUN3.
    SMRiQ9QUN3. Positions 328-457.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QUN3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini347 – 454108SH2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi130 – 330201Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG44661.
    GeneTreeiENSGT00530000063094.
    HOGENOMiHOG000088646.
    HOVERGENiHBG053147.
    InParanoidiQ9QUN3.
    KOiK07371.
    OMAiHRQENMQ.
    PhylomeDBiQ9QUN3.
    TreeFamiTF326567.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR000980. SH2.
    [Graphical view]
    PfamiPF00017. SH2. 1 hit.
    [Graphical view]
    SMARTiSM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QUN3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKLNKITVP ASQKLRQLQK MVHDIKNNEG GIMDKIKKLK VKGPPSVPRR    50
    DYALDSPADE EEQWSDDFDS DYENPDEHSD SEMYVMPAEE TGDDSYEPPP 100
    AEQQTRVVHP ALPFTRGEYV DNRSSQRHSP PFSKTLPSKP SWPSAKARLA 150
    STLPAPNSLQ KPQVPPKPKD LLEDEADYVV PVEDNDENYI HPRESSPPPA 200
    EKAPMVNRST KPNSSSKHMS PPGTVAGRNS GVWDSKSSLP AAPSPLPRAG 250
    KKPATPLKTT PVPPLPNASN VCEEKPVPAE RHRGSSHRQD TVQSPVFPPT 300
    QKPVHQKPVP LPRFPEAGSP AADGPFHSFP FNSTFADQEA ELLGKPWYAG 350
    ACDRKSAEEA LHRSNKDGSF LIRKSSGHDS KQPYTLVAFF NKRVYNIPVR 400
    FIEATKQYAL GKKKNGEEYF GSVVEIVNSH QHNPLVLIDS QNNTKDSTRL 450
    KYAVKVS 457
    Length:457
    Mass (Da):50,671
    Last modified:May 1, 2000 - v1
    Checksum:i66C93D4FDDF9D260
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti333 – 3331S → L in AAC40206. (PubMed:9697839)Curated
    Sequence conflicti340 – 3401A → G in AAC40206. (PubMed:9697839)Curated
    Sequence conflicti356 – 3561S → F in AAC40206. (PubMed:9697839)Curated
    Sequence conflicti376 – 3761S → F in AAC40206. (PubMed:9697839)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068182 mRNA. Translation: AAC40206.1.
    Y17159 mRNA. Translation: CAA76666.1.
    AB015290 mRNA. Translation: BAA34944.1.
    AJ298054 Genomic DNA. Translation: CAC18565.1.
    BC059785 mRNA. Translation: AAH59785.1.
    CCDSiCCDS37983.1.
    RefSeqiNP_032554.2. NM_008528.4.
    UniGeneiMm.9749.

    Genome annotation databases

    EnsembliENSMUST00000054769; ENSMUSP00000057844; ENSMUSG00000061132.
    GeneIDi17060.
    KEGGimmu:17060.
    UCSCiuc008hll.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF068182 mRNA. Translation: AAC40206.1 .
    Y17159 mRNA. Translation: CAA76666.1 .
    AB015290 mRNA. Translation: BAA34944.1 .
    AJ298054 Genomic DNA. Translation: CAC18565.1 .
    BC059785 mRNA. Translation: AAH59785.1 .
    CCDSi CCDS37983.1.
    RefSeqi NP_032554.2. NM_008528.4.
    UniGenei Mm.9749.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EO6 NMR - A 330-457 [» ]
    ProteinModelPortali Q9QUN3.
    SMRi Q9QUN3. Positions 328-457.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201236. 5 interactions.
    IntActi Q9QUN3. 6 interactions.
    MINTi MINT-110328.

    PTM databases

    PhosphoSitei Q9QUN3.

    Proteomic databases

    PaxDbi Q9QUN3.
    PRIDEi Q9QUN3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000054769 ; ENSMUSP00000057844 ; ENSMUSG00000061132 .
    GeneIDi 17060.
    KEGGi mmu:17060.
    UCSCi uc008hll.1. mouse.

    Organism-specific databases

    CTDi 29760.
    MGIi MGI:96878. Blnk.

    Phylogenomic databases

    eggNOGi NOG44661.
    GeneTreei ENSGT00530000063094.
    HOGENOMi HOG000088646.
    HOVERGENi HBG053147.
    InParanoidi Q9QUN3.
    KOi K07371.
    OMAi HRQENMQ.
    PhylomeDBi Q9QUN3.
    TreeFami TF326567.

    Enzyme and pathway databases

    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_198634. Regulation of signaling by CBL.

    Miscellaneous databases

    EvolutionaryTracei Q9QUN3.
    NextBioi 291162.
    PROi Q9QUN3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QUN3.
    Bgeei Q9QUN3.
    CleanExi MM_BLNK.
    Genevestigatori Q9QUN3.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR000980. SH2.
    [Graphical view ]
    Pfami PF00017. SH2. 1 hit.
    [Graphical view ]
    SMARTi SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "BLNK: a central linker protein in B cell activation."
      Fu C., Turck C.W., Kurosaki T., Chan A.C.
      Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "SLP-65: a new signaling component in B lymphocytes which requires expression of the antigen receptor for phosphorylation."
      Wienands J., Schweikert J., Wollschied B., Jumaa H., Nielsen P.J., Reth M.
      J. Exp. Med. 188:791-795(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-20; 147-161; 170-186; 356-366 AND 393-412, FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH VAV1 AND GRB2.
      Strain: BALB/c.
      Tissue: Lymphoid tissue.
    3. "BASH: B lymphocyte adaptor protein containing SH2 domain."
      Okamoto N., Hayashi K., Tsuji S., Goitsuka R., Kitamura D.
      Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "The murine SLP-65 gene."
      Nielsen P.J., Guenet J.-L.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "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: 129.
      Tissue: Mammary tumor.
    6. "Association of SLP-65/BLNK with the B cell antigen receptor through a non-ITAM tyrosine of Ig-alpha."
      Engels N., Wollscheid B., Wienands J.
      Eur. J. Immunol. 31:2126-2134(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A, MUTAGENESIS OF ARG-373.
    7. "Receptor-facilitated antigen presentation requires the recruitment of B cell linker protein to Igalpha."
      Siemasko K., Skaggs B.J., Kabak S., Williamson E., Brown B.K., Song W., Clark M.R.
      J. Immunol. 168:2127-2138(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A.
    8. "The direct recruitment of BLNK to immunoglobulin alpha couples the B-cell antigen receptor to distal signaling pathways."
      Kabak S., Skaggs B.J., Gold M.R., Affolter M., West K.L., Foster M.S., Siemasko K., Chan A.C., Aebersold R., Clark M.R.
      Mol. Cell. Biol. 22:2524-2535(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A.
    9. Cited for: FUNCTION IN PRO-B CELL TO PRE-B CELL TRANSITION, MUTAGENESIS OF TYR-52 AND TYR-96.
    10. "The kinase Syk as an adaptor controlling sustained calcium signalling and B-cell development."
      Kulathu Y., Hobeika E., Turchinovich G., Reth M.
      EMBO J. 27:1333-1344(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SYK ACTIVATION, INTERACTION WITH SYK, MUTAGENESIS OF ARG-373.
    11. "SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling."
      Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.
      Mol. Cell. Biol. 31:4550-4562(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCIMP.
    12. "Solution structure of the SH2 domain from mouse B-cell linker protein BLNK."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 328-457.

    Entry informationi

    Entry nameiBLNK_MOUSE
    AccessioniPrimary (citable) accession number: Q9QUN3
    Secondary accession number(s): O88504
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3