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P25911

- LYN_MOUSE

UniProt

P25911 - LYN_MOUSE

Protein

Tyrosine-protein kinase Lyn

Gene

Lyn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 162 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'.36 Publications

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.4 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Subject to autoinhibition, mediated by intramolecular interactions between the SH2 domain and the C-terminal phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508 inhibits kinase activity. Kinase activity is modulated by dephosphorylation by PTPRC/CD45. Inhibited by dasatinib, PP2, and SU6656.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei275 – 2751ATPCurated
    Active sitei367 – 3671Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi253 – 2619ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. erythropoietin receptor binding Source: UniProtKB
    3. glycosphingolipid binding Source: Ensembl
    4. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
    5. protein binding Source: UniProtKB
    6. protein complex binding Source: MGI
    7. protein kinase activity Source: MGI
    8. protein tyrosine kinase activity Source: UniProtKB
    9. SH3 domain binding Source: MGI

    GO - Biological processi

    1. apoptotic nuclear changes Source: Ensembl
    2. B cell homeostasis Source: UniProtKB
    3. B cell receptor signaling pathway Source: MGI
    4. cellular response to DNA damage stimulus Source: Ensembl
    5. cellular response to extracellular stimulus Source: Ensembl
    6. cellular response to heat Source: Ensembl
    7. cellular response to retinoic acid Source: Ensembl
    8. cytokine secretion Source: Ensembl
    9. dendritic cell differentiation Source: UniProtKB
    10. erythrocyte differentiation Source: UniProtKB
    11. Fc receptor mediated inhibitory signaling pathway Source: UniProtKB
    12. Fc receptor mediated stimulatory signaling pathway Source: UniProtKB
    13. hemoglobin biosynthetic process Source: UniProtKB
    14. hemopoiesis Source: UniProtKB
    15. histamine secretion by mast cell Source: Ensembl
    16. immune response-regulating cell surface receptor signaling pathway Source: UniProtKB
    17. innate immune response Source: UniProtKB-KW
    18. intracellular signal transduction Source: MGI
    19. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
    20. negative regulation of B cell proliferation Source: UniProtKB
    21. negative regulation of cell proliferation Source: UniProtKB
    22. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    23. negative regulation of intracellular signal transduction Source: UniProtKB
    24. negative regulation of MAP kinase activity Source: UniProtKB
    25. negative regulation of mast cell proliferation Source: UniProtKB
    26. negative regulation of myeloid leukocyte differentiation Source: UniProtKB
    27. negative regulation of protein phosphorylation Source: UniProtKB
    28. negative regulation of toll-like receptor 2 signaling pathway Source: UniProtKB
    29. negative regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
    30. neuron projection development Source: MGI
    31. oligodendrocyte development Source: Ensembl
    32. peptidyl-tyrosine phosphorylation Source: UniProtKB
    33. platelet degranulation Source: UniProtKB
    34. positive regulation of B cell receptor signaling pathway Source: MGI
    35. positive regulation of cell migration Source: UniProtKB
    36. positive regulation of cell proliferation Source: UniProtKB
    37. positive regulation of dendritic cell apoptotic process Source: UniProtKB
    38. positive regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
    39. positive regulation of glial cell proliferation Source: Ensembl
    40. positive regulation of mast cell proliferation Source: Ensembl
    41. positive regulation of neuron projection development Source: Ensembl
    42. positive regulation of oligodendrocyte progenitor proliferation Source: Ensembl
    43. positive regulation of peptidyl-tyrosine phosphorylation Source: MGI
    44. positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    45. positive regulation of stress-activated protein kinase signaling cascade Source: Ensembl
    46. positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
    47. protein autophosphorylation Source: UniProtKB
    48. regulation of B cell apoptotic process Source: UniProtKB
    49. regulation of B cell receptor signaling pathway Source: UniProtKB
    50. regulation of cell adhesion mediated by integrin Source: Ensembl
    51. regulation of cytokine production Source: UniProtKB
    52. regulation of cytokine secretion Source: UniProtKB
    53. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    54. regulation of erythrocyte differentiation Source: UniProtKB
    55. regulation of inflammatory response Source: UniProtKB
    56. regulation of mast cell activation Source: UniProtKB
    57. regulation of mast cell degranulation Source: UniProtKB
    58. regulation of monocyte chemotaxis Source: Ensembl
    59. regulation of platelet aggregation Source: UniProtKB
    60. regulation of release of sequestered calcium ion into cytosol Source: MGI
    61. response to amino acid Source: Ensembl
    62. response to axon injury Source: Ensembl
    63. response to carbohydrate Source: Ensembl
    64. response to drug Source: Ensembl
    65. response to hormone Source: UniProtKB
    66. response to insulin Source: Ensembl
    67. response to organic cyclic compound Source: Ensembl
    68. response to sterol depletion Source: Ensembl
    69. response to toxic substance Source: Ensembl
    70. signal transduction Source: UniProtKB
    71. tolerance induction to self antigen Source: UniProtKB
    72. transmembrane receptor protein tyrosine kinase signaling pathway Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Immunity, Inflammatory response, Innate immunity

    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.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188204. Fc epsilon receptor (FCERI) signaling.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196487. FCGR activation.
    REACT_198614. Growth hormone receptor signaling.
    REACT_204081. CD28 co-stimulation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225107. Platelet Adhesion to exposed collagen.
    REACT_225233. Cell surface interactions at the vascular wall.
    REACT_227425. Regulation of KIT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Lyn (EC:2.7.10.2)
    Alternative name(s):
    V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
    p53Lyn
    p56Lyn
    Gene namesi
    Name:Lyn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:96892. Lyn.

    Subcellular locationi

    Cell membrane By similarity. Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Golgi apparatus By similarity
    Note: Accumulates in the nucleus by inhibition of Crm1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activity. The trafficking from the Golgi apparatus to the cell membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. integrin alpha2-beta1 complex Source: Ensembl
    5. mast cell granule Source: GOC
    6. membrane raft Source: Ensembl
    7. mitochondrial crista Source: Ensembl
    8. mitochondrial intermembrane space Source: Ensembl
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    11. plasma membrane Source: MGI
    12. postsynaptic density Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype at birth. B-cell development in the bone marrow proceeds normally, but mice have reduced numbers of peripheral B-cells, with a greater proportion of immature cells and an increased turnover rate. Dendritic cells also have a more immature phenotype. Mice develop severe asthma upon exposure to airborne antigen. Mice display elevated levels of serum IgM. Aging mice display strongly increased levels of myeloid cells, severe extramedullary hematoipoiesis and tend to develop monocyte/macrophage tumors. After about 16 weeks, mice begin to develop splenomegaly and glomerulonephritis, and display autoimmune antibodies. Their B-cells are hypersensitive to stimulation of the B-cell receptor, and display enhanced activation of the MAP kinase signaling pathway. Mice do not display an allergic response upon IgE receptor engagement.7 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi508 – 5081Y → F: Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 512511Tyrosine-protein kinase LynPRO_0000088130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycineBy similarity
    Lipidationi3 – 31S-palmitoyl cysteineBy similarity
    Modified residuei6 – 61PhosphoserineBy similarity
    Modified residuei19 – 191Phosphoserine2 Publications
    Modified residuei30 – 301PhosphothreonineBy similarity
    Modified residuei32 – 321PhosphotyrosineBy similarity
    Modified residuei37 – 371PhosphothreonineBy similarity
    Modified residuei193 – 1931PhosphotyrosineBy similarity
    Modified residuei194 – 1941PhosphotyrosineBy similarity
    Modified residuei228 – 2281PhosphoserineBy similarity
    Modified residuei265 – 2651PhosphotyrosineBy similarity
    Modified residuei306 – 3061PhosphotyrosineBy similarity
    Modified residuei316 – 3161PhosphotyrosineBy similarity
    Modified residuei397 – 3971Phosphotyrosine; by autocatalysis4 Publications
    Modified residuei460 – 4601PhosphotyrosineBy similarity
    Modified residuei473 – 4731PhosphotyrosineBy similarity
    Modified residuei489 – 4891PhosphothreonineBy similarity
    Modified residuei502 – 5021PhosphothreonineBy similarity
    Modified residuei508 – 5081Phosphotyrosine; by autocatalysis, CSK and MATK4 Publications

    Post-translational modificationi

    Ubiquitinated by CBL, leading to its degradation.1 Publication
    Phosphorylated on tyrosine residues in response to KIT signaling By similarity. Autophosphorylated. Phosphorylation at Tyr-397 is required for optimal activity. Phosphorylation at Tyr-508 inhibits kinase activity. Phosphorylated at Tyr-508 by CSK. Dephosphorylated by PTPRC/CD45. Becomes rapidly phosphorylated upon activation of the B-cell receptor and the immunoglobulin receptor FCGR1A.By similarity5 Publications

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP25911.
    PaxDbiP25911.
    PRIDEiP25911.

    PTM databases

    PhosphoSiteiP25911.

    Expressioni

    Tissue specificityi

    Detected in bone marrow-derived monocytes (at protein level). Expressed predominantly in B-lymphoid and myeloid cells.1 Publication

    Gene expression databases

    ArrayExpressiP25911.
    BgeeiP25911.
    GenevestigatoriP25911.

    Interactioni

    Subunit structurei

    Interacts with TEC. Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon activation of the B-cell antigen receptor. Interacts with the B-cell receptor complex. Interacts with phosphorylated THEMIS2. Interacts with EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3 domains) with MUC1 is stimulated by IL7 and the subsequent phosphorylation increases the binding between MUC1 and CTNNB1/beta-catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1. Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase; this interaction enhances phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1; identified in a complex with PAG1 and STAT3. Interacts with ABL1. Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via proline-rich region). Interacts with LPXN (via LD motif 3) and the interaction is induced upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-domain) with ANKRD54 (via ankyrin repeat region) in an activation-independent status of LYN. Forms a multiprotein complex with ANKRD54 and HCLS1. Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hcls1P4971010EBI-643537,EBI-924601
    Plcg2Q8CIH52EBI-643537,EBI-617954

    Protein-protein interaction databases

    BioGridi201256. 10 interactions.
    DIPiDIP-37806N.
    IntActiP25911. 13 interactions.
    MINTiMINT-100482.

    Structurei

    Secondary structure

    1
    512
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi244 – 2463
    Beta strandi247 – 2548
    Beta strandi257 – 26610
    Turni267 – 2693
    Beta strandi270 – 2778
    Helixi284 – 29411
    Beta strandi305 – 3095
    Beta strandi311 – 3144
    Beta strandi316 – 3205
    Helixi327 – 3326
    Helixi336 – 3383
    Helixi341 – 36020
    Helixi370 – 3723
    Beta strandi373 – 3753
    Beta strandi381 – 3833
    Helixi407 – 4093
    Helixi412 – 4176
    Helixi422 – 43817
    Helixi449 – 4557
    Helixi456 – 4583
    Helixi470 – 47910
    Helixi484 – 4863
    Helixi490 – 4989

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2ZV7X-ray2.50A239-512[»]
    2ZV8X-ray2.70A239-512[»]
    2ZV9X-ray2.76A239-512[»]
    2ZVAX-ray2.60A239-512[»]
    ProteinModelPortaliP25911.
    SMRiP25911. Positions 64-512.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25911.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 12361SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini129 – 22698SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini247 – 501255Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The protein kinase domain plays an important role in its localization in the cell membrane.By similarity

    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.
    HOGENOMiHOG000233858.
    HOVERGENiHBG008761.
    InParanoidiP25911.
    KOiK05854.
    OMAiWWRAKSL.
    OrthoDBiEOG7GTT2V.
    PhylomeDBiP25911.
    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.
    IPR008266. Tyr_kinase_AS.
    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.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P25911-1) [UniParc]FASTAAdd to Basket

    Also known as: LYN A, p56

    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

    MGCIKSKRKD NLNDDEVDSK TQPVRNTDRT IYVRDPTSNK QQRPVPEFHL    50
    LPGQRFQTKD PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW 100
    KAKSLSSKRE GFIPSNYVAK VNTLETEEWF FKDITRKDAE RQLLAPGNSA 150
    GAFLIRESET LKGSFSLSVR DYDPMHGDVI KHYKIRSLDN GGYYISPRIT 200
    FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW EIPRESIKLV 250
    KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD 300
    KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ 350
    IAEGMAYIER KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR 400
    EGAKFPIKWT APEAINFGCF TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA 450
    DVMSALSQGY RMPRMENCPD ELYDIMKMCW KEKAEERPTF DYLQSVLDDF 500
    YTATEGQYQQ QP 512
    Length:512
    Mass (Da):58,812
    Last modified:January 23, 2007 - v4
    Checksum:iFDA1D21CC90C50EC
    GO
    Isoform 2 (identifier: P25911-2) [UniParc]FASTAAdd to Basket

    Also known as: LYN B, p53

    The sequence of this isoform differs from the canonical sequence as follows:
         25-45: Missing.

    Show »
    Length:491
    Mass (Da):56,285
    Checksum:i2C82015D510B1F59
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771I → F in AAA39471. (PubMed:2017160)Curated
    Sequence conflicti77 – 771I → F in AAA39472. (PubMed:2017160)Curated
    Sequence conflicti161 – 1611L → I in AAA39471. (PubMed:2017160)Curated
    Sequence conflicti161 – 1611L → I in AAA39472. (PubMed:2017160)Curated
    Sequence conflicti279 – 2791P → L in AAA39471. (PubMed:2017160)Curated
    Sequence conflicti279 – 2791P → L in AAA39472. (PubMed:2017160)Curated
    Sequence conflicti391 – 3911V → I in AAA39471. (PubMed:2017160)Curated
    Sequence conflicti391 – 3911V → I in AAA39472. (PubMed:2017160)Curated
    Sequence conflicti415 – 4151I → F in AAA40017. (PubMed:2482828)Curated
    Sequence conflicti425 – 4251D → N in AAA39470. (PubMed:1710766)Curated
    Sequence conflicti432 – 4321L → P in AAA40017. (PubMed:2482828)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei25 – 4521Missing in isoform 2. 1 PublicationVSP_005003Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64608 mRNA. Translation: AAA39470.1.
    M57696 mRNA. Translation: AAA39471.1.
    M57697 mRNA. Translation: AAA39472.1.
    BC031547 mRNA. Translation: AAH31547.1.
    M33426 mRNA. Translation: AAA40017.1.
    CCDSiCCDS17939.1. [P25911-2]
    CCDS51109.1. [P25911-1]
    PIRiA39719.
    RefSeqiNP_001104566.1. NM_001111096.1. [P25911-1]
    UniGeneiMm.317331.

    Genome annotation databases

    EnsembliENSMUST00000041377; ENSMUSP00000038838; ENSMUSG00000042228. [P25911-1]
    ENSMUST00000103010; ENSMUSP00000100075; ENSMUSG00000042228. [P25911-2]
    GeneIDi17096.
    KEGGimmu:17096.
    UCSCiuc008rwm.2. mouse. [P25911-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64608 mRNA. Translation: AAA39470.1 .
    M57696 mRNA. Translation: AAA39471.1 .
    M57697 mRNA. Translation: AAA39472.1 .
    BC031547 mRNA. Translation: AAH31547.1 .
    M33426 mRNA. Translation: AAA40017.1 .
    CCDSi CCDS17939.1. [P25911-2 ]
    CCDS51109.1. [P25911-1 ]
    PIRi A39719.
    RefSeqi NP_001104566.1. NM_001111096.1. [P25911-1 ]
    UniGenei Mm.317331.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2ZV7 X-ray 2.50 A 239-512 [» ]
    2ZV8 X-ray 2.70 A 239-512 [» ]
    2ZV9 X-ray 2.76 A 239-512 [» ]
    2ZVA X-ray 2.60 A 239-512 [» ]
    ProteinModelPortali P25911.
    SMRi P25911. Positions 64-512.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201256. 10 interactions.
    DIPi DIP-37806N.
    IntActi P25911. 13 interactions.
    MINTi MINT-100482.

    Chemistry

    ChEMBLi CHEMBL2258.

    PTM databases

    PhosphoSitei P25911.

    Proteomic databases

    MaxQBi P25911.
    PaxDbi P25911.
    PRIDEi P25911.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000041377 ; ENSMUSP00000038838 ; ENSMUSG00000042228 . [P25911-1 ]
    ENSMUST00000103010 ; ENSMUSP00000100075 ; ENSMUSG00000042228 . [P25911-2 ]
    GeneIDi 17096.
    KEGGi mmu:17096.
    UCSCi uc008rwm.2. mouse. [P25911-1 ]

    Organism-specific databases

    CTDi 4067.
    MGIi MGI:96892. Lyn.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233858.
    HOVERGENi HBG008761.
    InParanoidi P25911.
    KOi K05854.
    OMAi WWRAKSL.
    OrthoDBi EOG7GTT2V.
    PhylomeDBi P25911.
    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.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188204. Fc epsilon receptor (FCERI) signaling.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196487. FCGR activation.
    REACT_198614. Growth hormone receptor signaling.
    REACT_204081. CD28 co-stimulation.
    REACT_205561. FCERI mediated NF-kB activation.
    REACT_213364. Role of LAT2/NTAL/LAB on calcium mobilization.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225107. Platelet Adhesion to exposed collagen.
    REACT_225233. Cell surface interactions at the vascular wall.
    REACT_227425. Regulation of KIT signaling.

    Miscellaneous databases

    EvolutionaryTracei P25911.
    NextBioi 291240.
    PROi P25911.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25911.
    Bgeei P25911.
    Genevestigatori P25911.

    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.
    IPR008266. Tyr_kinase_AS.
    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.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Alternatively spliced murine lyn mRNAs encode distinct proteins."
      Stanley E., Ralph S.J., McEwen S., Boulet I., Holtzman D.A., Lock P., Dunn A.R.
      Mol. Cell. Biol. 11:3399-3406(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
    2. "Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus."
      Yi T., Bolen J.B., Ihle J.N.
      Mol. Cell. Biol. 11:2391-2398(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
    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] (ISOFORM 1).
      Strain: Czech II.
      Tissue: Mammary gland.
    4. "The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
      Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
      Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-432.
    5. "Association of B cell antigen receptor with protein tyrosine kinase Lyn."
      Yamanashi Y., Kakiuchi T., Mizuguchi J., Yamamoto T., Toyoshima K.
      Science 251:192-194(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH B CELL RECEPTOR, AUTOPHOSPHORYLATION.
    6. "Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity."
      Clark M.R., Johnson S.A., Cambier J.C.
      EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A.
    7. "B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn."
      Law D.A., Chan V.W., Datta S.K., DeFranco A.L.
      Curr. Biol. 3:645-657(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A AND CD79B, FUNCTION IN PHOSPHORYLATION OF CD79A AND CD79B.
    8. "Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling."
      Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T., Yamamoto T., Yamamura H.
      J. Exp. Med. 179:1725-1729(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SYK PHOSPHORYLATION.
    9. "Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha."
      Pleiman C.M., Abrams C., Gauen L.T., Bedzyk W., Jongstra J., Shaw A.S., Cambier J.C.
      Proc. Natl. Acad. Sci. U.S.A. 91:4268-4272(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD79A.
    10. "Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit."
      Pleiman C.M., Hertz W.M., Cambier J.C.
      Science 263:1609-1612(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PIK3R1 ACTIVATION, INTERACTION WITH PIK3R1.
    11. "Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease."
      Hibbs M.L., Tarlinton D.M., Armes J., Grail D., Hodgson G., Maglitto R., Stacker S.A., Dunn A.R.
      Cell 83:301-311(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    12. "Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice."
      Nishizumi H., Taniuchi I., Yamanashi Y., Kitamura D., Ilic D., Mori S., Watanabe T., Yamamoto T.
      Immunity 3:549-560(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B CELLS AND IN PHOSPHORYLATION OF CBL AND HCLS1.
    13. "Tyrosine phosphorylation and translocation of the c-cbl protein after activation of tyrosine kinase signaling pathways."
      Tanaka S., Neff L., Baron R., Levy J.B.
      J. Biol. Chem. 270:14347-14351(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL.
    14. "Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase."
      Sotirellis N., Johnson T.M., Hibbs M.L., Stanley I.J., Stanley E., Dunn A.R., Cheng H.C.
      J. Biol. Chem. 270:29773-29780(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION.
    15. "Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase."
      Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.
      FASEB J. 10:637-642(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TEC PHOSPHORYLATION, INTERACTION WITH TEC.
    16. "Altered antigen receptor signaling and impaired Fas-mediated apoptosis of B cells in Lyn-deficient mice."
      Wang J., Koizumi T., Watanabe T.
      J. Exp. Med. 184:831-838(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    17. "Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases."
      Rawlings D.J., Scharenberg A.M., Park H., Wahl M.I., Lin S., Kato R.M., Fluckiger A.C., Witte O.N., Kinet J.P.
      Science 271:822-825(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BTK.
    18. "Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation."
      Chan V.W., Meng F., Soriano P., DeFranco A.L., Lowell C.A.
      Immunity 7:69-81(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, ALTERNATIVE SPLICING, PHOSPHORYLATION.
    19. "Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells."
      Nishizumi H., Yamamoto T.
      J. Immunol. 158:2350-2355(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAST CELLS AND IN SIGNALING DOWN-STREAM OF FCER1.
    20. "Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway."
      Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.
      Blood 91:3734-3745(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPOR AND JAK2, FUNCTION.
    21. "Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes."
      Chan V.W., Lowell C.A., DeFranco A.L.
      Curr. Biol. 8:545-553(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION AND ACTIVATION OF MAPK1/ERK2; MAPK8/JNK1 AND MAPK9/JNK2.
    22. "Inhibition of the B cell by CD22: a requirement for Lyn."
      Smith K.G., Tarlinton D.M., Doody G.M., Hibbs M.L., Fearon D.T.
      J. Exp. Med. 187:807-811(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CD22 PHOSPHORYLATION.
    23. "A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals."
      Nishizumi H., Horikawa K., Mlinaric-Rascan I., Yamamoto T.
      J. Exp. Med. 187:1343-1348(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION.
    24. "Fc epsilon receptor I-associated lyn-dependent phosphorylation of Fc gamma receptor IIB during negative regulation of mast cell activation."
      Malbec O., Fong D.C., Turner M., Tybulewicz V.L., Cambier J.C., Fridman W.H., Daeron M.
      J. Immunol. 160:1647-1658(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FCGR2 PHOSPHORYLATION, INTERACTION WITH FCGR2.
    25. "The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1 upon tyrosine phosphorylation."
      Adachi T., Flaswinkel H., Yakura H., Reth M., Tsubata T.
      J. Immunol. 160:4662-4665(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CD72 PHOSPHORYLATION.
    26. "Regulation of B-1 cell activation and its autoantibody production by Lyn kinase-regulated signallings."
      Ochi H., Takeshita H., Suda T., Nisitani S., Honjo T., Watanabe T.
      Immunology 98:595-603(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN ERYTHROPOIESIS.
    27. "CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells."
      Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H.
      J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, DEPHOSPHORYLATION BY PTPRC/CD45, ENZYME REGULATION.
    28. "Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1."
      Maeda A., Scharenberg A.M., Tsukada S., Bolen J.B., Kinet J.P., Kurosaki T.
      Oncogene 18:2291-2297(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LILRB3/PIR-B.
    29. "Association of Lyn tyrosine kinase to the GM-CSF and IL-3 receptor common betac subunit and role of Src tyrosine kinases in DNA synthesis and anti-apoptosis."
      Dahl M.E., Arai K.I., Watanabe S.
      Genes Cells 5:143-153(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CSF2RB, INTERACTION WITH CSF2RB.
    30. "Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling."
      Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H., Yamamoto T., Baltimore D.
      Genes Dev. 14:11-16(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF DOK1.
    31. "Negative regulation of B cell receptor-mediated signaling in B-1 cells through CD5 and Ly49 co-receptors via Lyn kinase activity."
      Ochi H., Watanabe T.
      Int. Immunol. 12:1417-1423(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN CD5 PHOSPHORYLATION.
    32. "Lyn is required for normal stem cell factor-induced proliferation and chemotaxis of primary hematopoietic cells."
      O'Laughlin-Bunner B., Radosevic N., Taylor M.L., Shivakrupa R., DeBerry C., Metcalfe D.D., Zhou M., Lowell C., Linnekin D.
      Blood 98:343-350(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION AND MIGRATION IN RESPONSE TO KITLG.
    33. "Gain- and loss-of-function Lyn mutant mice define a critical inhibitory role for Lyn in the myeloid lineage."
      Harder K.W., Parsons L.M., Armes J., Evans N., Kountouri N., Clark R., Quilici C., Grail D., Hodgson G.S., Dunn A.R., Hibbs M.L.
      Immunity 15:603-615(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF SIRPA; PTPN6/SHP-1; PTPN11/SHP-2 AND INPP5D/SHIP-1, MUTAGENESIS OF TYR-508.
    34. "Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis."
      Grishin A.V., Azhipa O., Semenov I., Corey S.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PPP1R15A.
    35. "Sustained activation of Lyn tyrosine kinase in vivo leads to autoimmunity."
      Hibbs M.L., Harder K.W., Armes J., Kountouri N., Quilici C., Casagranda F., Dunn A.R., Tarlinton D.M.
      J. Exp. Med. 196:1593-1604(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IN REGULATION OF IMMUNE RESPONSE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF TYR-508.
    36. "Regulation of signaling in B cells through the phosphorylation of Syk on linker region tyrosines. A mechanism for negative signaling by the Lyn tyrosine kinase."
      Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.
      J. Biol. Chem. 277:31703-31714(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATING SYK.
    37. "The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling."
      Pereira S., Lowell C.
      J. Immunol. 171:1319-1327(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    38. "Lyn tyrosine kinase regulates thrombopoietin-induced proliferation of hematopoietic cell lines and primary megakaryocytic progenitors."
      Lannutti B.J., Drachman J.G.
      Blood 103:3736-3743(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DOWN-REGULATION OF THPO-MEDIATED CELL PROLIFERATION AND IN DOWN-REGULATION OF MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
    39. "Differential regulation of the B cell receptor-mediated signaling by the E3 ubiquitin ligase Cbl."
      Shao Y., Yang C., Elly C., Liu Y.C.
      J. Biol. Chem. 279:43646-43653(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    40. "The Src kinase Lyn is a negative regulator of mast cell proliferation."
      Hernandez-Hansen V., Mackay G.A., Lowell C.A., Wilson B.S., Oliver J.M.
      J. Leukoc. Biol. 75:143-151(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MAST CELL PROLIFERATION AND IN DOWN-REGULATION OF AKT1; MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
    41. "The Lyn tyrosine kinase differentially regulates dendritic cell generation and maturation."
      Chu C.L., Lowell C.A.
      J. Immunol. 175:2880-2889(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS NEGATIVE REGULATOR OF DENDRITIC CELL DIFFERENTIATION; PROLIFERATION AND SURVIVAL.
    42. "Lyn-deficient mice develop severe, persistent asthma: Lyn is a critical negative regulator of Th2 immunity."
      Beavitt S.J., Harder K.W., Kemp J.M., Jones J., Quilici C., Casagranda F., Lam E., Turner D., Brennan S., Sly P.D., Tarlinton D.M., Anderson G.P., Hibbs M.L.
      J. Immunol. 175:1867-1875(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MATURATION OF DENDRITIC CELLS AND IN INFLAMMATORY RESPONSE.
    43. "Positive and negative regulation of mast cell activation by Lyn via the FcepsilonRI."
      Xiao W., Nishimoto H., Hong H., Kitaura J., Nunomura S., Maeda-Yamamoto M., Kawakami Y., Lowell C.A., Ra C., Kawakami T.
      J. Immunol. 175:6885-6892(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN FCER1 SIGNALING; PHOSPHORYLATION OF SYK; MS4A2/FCER1B; INPP5D/SHIP AND PTPN6/SHP-1; ACTIVATION OF AKT1; MAPK1/ERK2 AND MAPK3/ERK1, PHOSPHORYLATION AT TYR-397, INTERACTION WITH MS4A2/FCER1B.
    44. "LIME acts as a transmembrane adapter mediating BCR-dependent B-cell activation."
      Ahn E., Lee H., Yun Y.
      Blood 107:1521-1527(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIME1, FUNCTION IN PHOSPHORYLATION OF LIME1.
    45. "Identification of Y589 and Y599 in the juxtamembrane domain of Flt3 as ligand-induced autophosphorylation sites involved in binding of Src family kinases and the protein tyrosine phosphatase SHP2."
      Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
      Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLT3.
    46. "Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
      Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
      J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    47. "Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets."
      Rathore V.B., Okada M., Newman P.J., Newman D.K.
      Biochem. J. 403:275-281(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1I1.
    48. "Leupaxin negatively regulates B cell receptor signaling."
      Chew V., Lam K.P.
      J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF LPXN, INTERACTION WITH LPXN.
    49. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    50. "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
      Samuels A.L., Klinken S.P., Ingley E.
      Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD54.
    51. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; TYR-397 AND TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    52. "Erythropoietin down-regulates stem cell factor receptor (Kit) expression in the leukemic proerythroblast: role of Lyn kinase."
      Kosmider O., Buet D., Gallais I., Denis N., Moreau-Gachelin F.
      PLoS ONE 4:E5721-E5721(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    53. "Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
      Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
      PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THEMIS2.
    54. "An important role of the SRC family kinase Lyn in stimulating platelet granule secretion."
      Li Z., Zhang G., Liu J., Stojanovic A., Ruan C., Lowell C.A., Du X.
      J. Biol. Chem. 285:12559-12570(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PLATELET GRANULE SECRETION AND PLATELET AGGREGATION.
    55. "Activation of murine macrophages via TLR2 and TLR4 is negatively regulated by a Lyn/PI3K module and promoted by SHIP1."
      Keck S., Freudenberg M., Huber M.
      J. Immunol. 184:5809-5818(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DOWN-REGULATION OF TLR2 AND TLR4 SIGNALING; CYTOKINE RELEASE AND THE INFLAMMATORY RESPONSE TO LIPOPOLYSACCHARIDE.
    56. "Src-family kinases in B-cell development and signaling."
      Gauld S.B., Cambier J.C.
      Oncogene 23:8001-8006(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN B CELLS.
    57. "Lyn tyrosine kinase: accentuating the positive and the negative."
      Xu Y., Harder K.W., Huntington N.D., Hibbs M.L., Tarlinton D.M.
      Immunity 22:9-18(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON ROLE IN B CELLS.
    58. "Src-family kinases: rheostats of immune cell signaling."
      Lowell C.A.
      Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    59. "Multiple roles of Lyn kinase in myeloid cell signaling and function."
      Scapini P., Pereira S., Zhang H., Lowell C.A.
      Immunol. Rev. 228:23-40(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    60. "Crystal structures of the Lyn protein tyrosine kinase domain in its Apo- and inhibitor-bound state."
      Williams N.K., Lucet I.S., Klinken S.P., Ingley E., Rossjohn J.
      J. Biol. Chem. 284:284-291(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 239-512 IN COMPLEXES WITH DASATINIB; PP2 AND AMP-PNP, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiLYN_MOUSE
    AccessioniPrimary (citable) accession number: P25911
    Secondary accession number(s): Q62127
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 162 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

    Dasty 3