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P16277

- BLK_MOUSE

UniProt

P16277 - BLK_MOUSE

Protein

Tyrosine-protein kinase Blk

Gene

Blk

Organism
Mus musculus (Mouse)
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 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors. Binding of antigen to the B-cell antigen receptor (BCR) triggers signaling that ultimately leads to B-cell activation. Signaling through BLK plays an important role in transmitting signals through surface immunoglobulins and supports the pro-B to pre-B transition, as well as the signaling for growth arrest and apoptosis downstream of B-cell receptor. Specifically binds and phosphorylates CD79A at 'Tyr-188'and 'Tyr-199', as well as CD79B at 'Tyr-196' and 'Tyr-207'. Phosphorylates also the immunoglobulin G receptor FCGR2. With FYN and LYN, plays an essential role in pre-B-cell receptor (pre-BCR)-mediated NF-kappa-B activation. Contributes also to BTK activation by indirectly stimulating BTK intramolecular autophosphorylation. In pancreatic islets, acts as a modulator of beta-cells function through the up-regulation of PDX1 and NKX6-1 and consequent stimulation of insulin secretion in response to glucose.9 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

    Enzyme regulationi

    Antibody-mediated surface engagement of the B-cell antigen receptor (BCR) which results in the phosphorylation of BLK on tyrosine residues, stimulates the enzymatic activity.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei263 – 2631ATPPROSITE-ProRule annotation
    Active sitei354 – 3541Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi241 – 2499ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    3. protein binding Source: MGI

    GO - Biological processi

    1. B cell receptor signaling pathway Source: Ensembl
    2. positive regulation of insulin secretion Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Blk (EC:2.7.10.2)
    Alternative name(s):
    B lymphocyte kinase
    p55-Blk
    Gene namesi
    Name:Blk
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:88169. Blk.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchor By similarity
    Note: Present and active in lipid rafts By similarity. Membrane location is required for the phosphorylation of CD79A and CD79B.By similarity1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi145 – 1451R → K: Impairs the interaction with CD79A and CD79B. 1 Publication
    Mutagenesisi495 – 4951Y → F: Leads to constitutive activation of BLK. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 499498Tyrosine-protein kinase BlkPRO_0000088062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Modified residuei383 – 3831Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues after antibody-mediated surface engagement of the B-cell antigen receptor (BCR).
    Ubiquitination of activated BLK by the UBE3A ubiquitin protein ligase leads to its degradation by the ubiquitin-proteasome pathway.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP16277.
    PRIDEiP16277.

    PTM databases

    PhosphoSiteiP16277.

    Expressioni

    Tissue specificityi

    Specifically expressed in the B-cell lineage.2 Publications

    Inductioni

    Expression increases during B-cell differentiation and is under the control of the B-cell specific transcription factors PAX5 and NF-kappa-B.3 Publications

    Gene expression databases

    BgeeiP16277.
    CleanExiMM_BLK.
    GenevestigatoriP16277.

    Interactioni

    Subunit structurei

    Interacts with CBL (via SH2 domain) By similarity. Interacts with CD79A and CD79B (via SH2 domain).By similarity2 Publications

    Protein-protein interaction databases

    IntActiP16277. 3 interactions.
    STRINGi10090.ENSMUSP00000014597.

    Structurei

    Secondary structure

    1
    499
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi116 – 1194
    Helixi125 – 1328
    Beta strandi142 – 1443
    Beta strandi150 – 1523
    Beta strandi154 – 1585
    Beta strandi160 – 1623
    Turni163 – 1653
    Beta strandi171 – 1766
    Turni177 – 1793
    Beta strandi180 – 1845
    Beta strandi187 – 1915
    Helixi192 – 20110
    Beta strandi204 – 2085

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BLJNMR-A107-218[»]
    1BLKNMR-A107-218[»]
    ProteinModelPortaliP16277.
    SMRiP16277. Positions 57-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16277.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini52 – 11261SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini118 – 21497SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini235 – 488254Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00620000087866.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiQ8K2M8.
    KOiK08890.
    OMAiKNNMKVA.
    OrthoDBiEOG7GTT2V.
    TreeFamiTF351634.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P16277-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLLSSKRQV SEKGKGWSPV KIRTQDKAPP PLPPLVVFNH LAPPSPNQDP    50
    DEEERFVVAL FDYAAVNDRD LQVLKGEKLQ VLRSTGDWWL ARSLVTGREG 100
    YVPSNFVAPV ETLEVEKWFF RTISRKDAER QLLAPMNKAG SFLIRESESN 150
    KGAFSLSVKD ITTQGEVVKH YKIRSLDNGG YYISPRITFP TLQALVQHYS 200
    KKGDGLCQKL TLPCVNLAPK NLWAQDEWEI PRQSLKLVRK LGSGQFGEVW 250
    MGYYKNNMKV AIKTLKEGTM SPEAFLGEAN VMKTLQHERL VRLYAVVTRE 300
    PIYIVTEYMA RGCLLDFLKT DEGSRLSLPR LIDMSAQVAE GMAYIERMNS 350
    IHRDLRAANI LVSETLCCKI ADFGLARIID SEYTAQEGAK FPIKWTAPEA 400
    IHFGVFTIKA DVWSFGVLLM EIVTYGRVPY PGMSNPEVIR SLEHGYRMPC 450
    PETCPPELYN DIITECWRGR PEERPTFEFL QSVLEDFYTA TEGQYELQP 499
    Length:499
    Mass (Da):56,674
    Last modified:July 27, 2011 - v4
    Checksum:i14C607564BB4E66D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti421 – 4211E → V in AAA40453. (PubMed:2404338)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30903 mRNA. Translation: AAA40453.1.
    AK089888 mRNA. Translation: BAC40986.1.
    CT010240 mRNA. Translation: CAJ18448.1.
    AC090496 Genomic DNA. No translation available.
    BC030668 mRNA. Translation: AAH30668.1.
    CCDSiCCDS27200.1.
    PIRiA40092.
    RefSeqiNP_031575.2. NM_007549.2.
    UniGeneiMm.3962.

    Genome annotation databases

    EnsembliENSMUST00000014597; ENSMUSP00000014597; ENSMUSG00000014453.
    GeneIDi12143.
    KEGGimmu:12143.
    UCSCiuc007uhq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M30903 mRNA. Translation: AAA40453.1 .
    AK089888 mRNA. Translation: BAC40986.1 .
    CT010240 mRNA. Translation: CAJ18448.1 .
    AC090496 Genomic DNA. No translation available.
    BC030668 mRNA. Translation: AAH30668.1 .
    CCDSi CCDS27200.1.
    PIRi A40092.
    RefSeqi NP_031575.2. NM_007549.2.
    UniGenei Mm.3962.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BLJ NMR - A 107-218 [» ]
    1BLK NMR - A 107-218 [» ]
    ProteinModelPortali P16277.
    SMRi P16277. Positions 57-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P16277. 3 interactions.
    STRINGi 10090.ENSMUSP00000014597.

    Chemistry

    BindingDBi P16277.
    ChEMBLi CHEMBL3343.

    PTM databases

    PhosphoSitei P16277.

    Proteomic databases

    PaxDbi P16277.
    PRIDEi P16277.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000014597 ; ENSMUSP00000014597 ; ENSMUSG00000014453 .
    GeneIDi 12143.
    KEGGi mmu:12143.
    UCSCi uc007uhq.1. mouse.

    Organism-specific databases

    CTDi 640.
    MGIi MGI:88169. Blk.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00620000087866.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi Q8K2M8.
    KOi K08890.
    OMAi KNNMKVA.
    OrthoDBi EOG7GTT2V.
    TreeFami TF351634.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

    Miscellaneous databases

    EvolutionaryTracei P16277.
    NextBioi 280469.
    PROi P16277.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16277.
    CleanExi MM_BLK.
    Genevestigatori P16277.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR001452. SH3_domain.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 1 hit.
    SM00326. SH3. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Specific expression of a tyrosine kinase gene, blk, in B lymphoid cells."
      Dymecki S.M., Niederhuber J.E., Desiderio S.V.
      Science 247:332-336(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: B-cell.
    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: NOD.
    3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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: C57BL/6J.
      Tissue: Mammary gland.
    6. "Anti-immunoglobulin stimulation of B lymphocytes activates src-related protein-tyrosine kinases."
      Burkhardt A.L., Brunswick M., Bolen J.B., Mond J.J.
      Proc. Natl. Acad. Sci. U.S.A. 88:7410-7414(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "Structure and developmental regulation of the B-lymphoid tyrosine kinase gene blk."
      Dymecki S.M., Zwollo P., Zeller K., Kuhajda F.P., Desiderio S.V.
      J. Biol. Chem. 267:4815-4823(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "The MB-1/B29 heterodimer couples the B cell antigen receptor to multiple src family protein tyrosine kinases."
      Lin J., Justement L.B.
      J. Immunol. 149:1548-1555(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A AND CD79B.
    9. "Antisense oligodeoxynucleotides to the blk tyrosine kinase prevent anti-mu-chain-mediated growth inhibition and apoptosis in a B-cell lymphoma."
      Yao X.R., Scott D.W.
      Proc. Natl. Acad. Sci. U.S.A. 90:7946-7950(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Specific recognition of the blk promoter by the B-lymphoid transcription factor B-cell-specific activator protein."
      Zwollo P., Desiderio S.
      J. Biol. Chem. 269:15310-15317(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY PAX5.
    11. "Temporal differences in the activation of three classes of non-transmembrane protein tyrosine kinases following B-cell antigen receptor surface engagement."
      Saouaf S.J., Mahajan S., Rowley R.B., Kut S.A., Fargnoli J., Burkhardt A.L., Tsukada S., Witte O.N., Bolen J.B.
      Proc. Natl. Acad. Sci. U.S.A. 91:9524-9528(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    12. "Differential expression of the blk and ret tyrosine kinases during B lineage development is dependent on Ig rearrangement."
      Wasserman R., Li Y.S., Hardy R.R.
      J. Immunol. 155:644-651(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    13. "Reconstitution of the B cell antigen receptor signaling components in COS cells."
      Saouaf S.J., Kut S.A., Fargnoli J., Rowley R.B., Bolen J.B., Mahajan S.
      J. Biol. Chem. 270:27072-27078(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CD79A AND CD79B, INTERACTION WITH CD79A AND CD79B, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-145.
    14. "Src family protein tyrosine kinases induce autoactivation of Bruton's tyrosine kinase."
      Mahajan S., Fargnoli J., Burkhardt A.L., Kut S.A., Saouaf S.J., Bolen J.B.
      Mol. Cell. Biol. 15:5304-5311(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF BTK ACTIVITY.
    15. "Palmitylation of Src family tyrosine kinases regulates functional interaction with a B cell substrate."
      Saouaf S.J., Wolven A., Resh M.D., Bolen J.B.
      Biochem. Biophys. Res. Commun. 234:325-329(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CD79A.
    16. "The transcription factor NF-kappaB/p50 interacts with the blk gene during B cell activation."
      Zwollo P., Rao S., Wallin J.J., Gackstetter E.R., Koshland M.E.
      J. Biol. Chem. 273:18647-18655(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    17. "Malignant transformation of early lymphoid progenitors in mice expressing an activated Blk tyrosine kinase."
      Malek S.N., Dordai D.I., Reim J., Dintzis H., Desiderio S.
      Proc. Natl. Acad. Sci. U.S.A. 95:7351-7356(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-495.
    18. "Regulation of the Src family tyrosine kinase Blk through E6AP-mediated ubiquitination."
      Oda H., Kumar S., Howley P.M.
      Proc. Natl. Acad. Sci. U.S.A. 96:9557-9562(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    19. "Mimicry of pre-B-cell receptor signaling by activation of the tyrosine kinase Blk."
      Tretter T., Ross A.E., Dordai D.I., Desiderio S.
      J. Exp. Med. 198:1863-1873(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TYR-495.
    20. "Essential role of Src-family protein tyrosine kinases in NF-kappaB activation during B cell development."
      Saijo K., Schmedt C., Su I.H., Karasuyama H., Lowell C.A., Reth M., Adachi T., Patke A., Santana A., Tarakhovsky A.
      Nat. Immunol. 4:274-279(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "The three-dimensional solution structure of the SH2 domain from p55blk kinase."
      Metzler W.J., Leiting B., Pryor K., Mueller L., Farmer B.T. II
      Biochemistry 35:6201-6211(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF SH2 DOMAIN.

    Entry informationi

    Entry nameiBLK_MOUSE
    AccessioniPrimary (citable) accession number: P16277
    Secondary accession number(s): Q8K2M8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

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