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Lyn  Protein, Antibody, ELISA Kit, cDNA Clone

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    Lyn Summary & Protein Information

    Lyn Background

    Catalytic activity: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:7682714, ECO:0000269|PubMed:8064233}.
    Enzyme regulation: ENZYME REGULATION: 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. {ECO:0000269|PubMed:16920712, ECO:0000269|PubMed:7935444}.
    Subunit structure: 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 with Epstein-Barr virus LMP2A. Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip). Interacts (via SH2 and SH3 domains) with UNC119; leading to LYN activation. Interacts with CD36. {ECO:0000269|PubMed:10362357, ECO:0000269|PubMed:10574931, ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:11306681, ECO:0000269|PubMed:11517336, ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:11955060, ECO:0000269|PubMed:12496276, ECO:0000269|PubMed:12750561, ECO:0000269|PubMed:16155203, ECO:0000269|PubMed:16912036, ECO:0000269|PubMed:16920712, ECO:0000269|PubMed:17233630, ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:17977829, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18235045, ECO:0000269|PubMed:19718658, ECO:0000269|PubMed:19807924, ECO:0000269|PubMed:19857964, ECO:0000269|PubMed:20037584, ECO:0000269|PubMed:20534535, ECO:0000269|PubMed:21930792, ECO:0000269|PubMed:7682714, ECO:0000269|PubMed:7687428, ECO:0000269|PubMed:7895172, ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:9232445, ECO:0000269|PubMed:9341198}.
    Domain: The protein kinase domain plays an important role in its localization in the cell membrane. {ECO:0000269|PubMed:15173188}.
    Subcellular location: Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. 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 plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts.
    Tissue specificity: Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors. {ECO:0000269|PubMed:3561390, ECO:0000269|PubMed:8064233}.
    Post-translational: Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent. {ECO:0000269|PubMed:16920712, ECO:0000269|PubMed:20534535}.; Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. 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. {ECO:0000269|PubMed:18056483, ECO:0000269|PubMed:18070987, ECO:0000269|PubMed:18577747, ECO:0000269|PubMed:7935444, ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:9171348, ECO:0000269|PubMed:9341198}.
    Involvement in disease: DISEASE: Note=Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells.
    Sequence similarity: Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 protein kinase domain. {ECO:0000255|PROSITE-ProRule:PRU00159}.; Contains 1 SH2 domain. {ECO:0000255|PROSITE-ProRule:PRU00191}.; Contains 1 SH3 domain. {ECO:0000255|PROSITE-ProRule:PRU00192}.
    General information above from UniProt

    Tyrosine-protein kinase Lyn is a member of the Src family of protein tyrosine kinases, which is mainly expressed in hematopoietic cells, in neural tissues liver, and adipose tissue. Tyrosine-protein kinase Lyn has many functions. Lyn kinase may down regulate expression of stem cell growth factor receptor (KIT). Lyn kinase Acts as an effector of EpoR (erythropoietin receptor) in controlling KIT expression and may play a central role in erythroid differentiation during the switch between proliferation and maturation. Lyn kinase also acts as a positive regulator of cell movement while negatively regulating adhesion to stromal cells by inhibiting the ICAM-1-binding activity of beta-2 integrins. Lyn kinase relays suppressing signals from the chemokine receptor CXCR4 to beta-2 integrin LFA-1 in hematopoietic precursors. This kinase is Involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. In a word, Lyn kinase functions primarily as negative regulator, but can also function as activator, depending on the context. Tyrosine-protein kinase Lyn Required for the initiation of the B-cell response, but also for its down-regulation and termination. It also Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. It has been reported that Lyn kinase plays a role in the inflammatory response to bacterial lipopolysaccharide. Lyn kinase 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.

    Lyn Alternative Name

    JTK8,p53Lyn,p56Lyn, [homo-sapiens]
    p53Lyn,p56Lyn, [Human]
    p53Lyn,p56Lyn, [Mouse]
    Hck-2,p53Lyn,p56Lyn,AA407514, [mus-musculus]

    Lyn Related Studies

  • Grishin A V, et al. (2001) Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis. Proc Natl Acad Sci U.S.A. 98 (18): 10172-7.
  • Hayashi T, et al. (1999) The AMPA receptor interacts with and signals through the protein tyrosine kinase Lyn. Nature. 397(6714): 72-6.
  • Ptasznik A, et al. (2004) Short interfering RNA (siRNA) targeting the Lyn kinase induces apoptosis in primary, and drug-resistant, BCR-ABL1(+) leukemia cells. Nat Med. 10(11): 1187-9.