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Tyrosine-protein kinase Lyn (EC 2.7.10.2) (Lck/Yes-related novel protein tyrosine kinase) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)

 LYN_HUMAN               Reviewed;         512 AA.
P07948; A0AVQ5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 215.
RecName: Full=Tyrosine-protein kinase Lyn;
EC=2.7.10.2;
AltName: Full=Lck/Yes-related novel protein tyrosine kinase;
AltName: Full=V-yes-1 Yamaguchi sarcoma viral related oncogene homolog;
AltName: Full=p53Lyn;
AltName: Full=p56Lyn;
Name=LYN; Synonyms=JTK8;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=3561390; DOI=10.1128/MCB.7.1.237;
Yamanashi Y., Fukushige S., Semba K., Sukegawa J., Miyajima N.,
Matsubara K., Yamamoto T., Toyoshima K.;
"The yes-related cellular gene lyn encodes a possible tyrosine kinase
similar to p56lck.";
Mol. Cell. Biol. 7:237-243(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=8125304; DOI=10.1016/0378-1119(94)90811-7;
Rider L.G., Raben N., Miller L., Jelsema C.;
"The cDNAs encoding two forms of the LYN protein tyrosine kinase are
expressed in rat mast cells and human myeloid cells.";
Gene 138:219-222(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
PubMed=2247464; DOI=10.1073/pnas.87.22.8913;
Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K.;
"Putative tyrosine kinases expressed in K-562 human leukemia cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
PubMed=1510669; DOI=10.1016/S0006-291X(05)81562-1;
Bielke W., Ziemiecki A., Kappos L., Miescher G.C.;
"Expression of the B cell-associated tyrosine kinase gene Lyn in
primary neuroblastoma tumours and its modulation during the
differentiation of neuroblastoma cell lines.";
Biochem. Biophys. Res. Commun. 186:1403-1409(1992).
[6]
FUNCTION IN CD19 PHOSPHORYLATION, AND INTERACTION WITH CD19.
PubMed=7687428; DOI=10.1006/bbrc.1993.1807;
Roifman C.M., Ke S.;
"CD19 is a substrate of the antigen receptor-associated protein
tyrosine kinase in human B cells.";
Biochem. Biophys. Res. Commun. 194:222-225(1993).
[7]
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND INTERACTION WITH HCLS1.
PubMed=7682714; DOI=10.1073/pnas.90.8.3631;
Yamanashi Y., Okada M., Semba T., Yamori T., Umemori H., Tsunasawa S.,
Toyoshima K., Kitamura D., Watanabe T., Yamamoto T.;
"Identification of HS1 protein as a major substrate of protein-
tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling.";
Proc. Natl. Acad. Sci. U.S.A. 90:3631-3635(1993).
[8]
INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
PubMed=8064233; DOI=10.1084/jem.180.3.1165;
Wang A.V., Scholl P.R., Geha R.S.;
"Physical and functional association of the high affinity
immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and
Lyn.";
J. Exp. Med. 180:1165-1170(1994).
[9]
PHOSPHORYLATION AT TYR-397 AND TYR-508, AND ENZYME REGULATION.
PubMed=7935444; DOI=10.1128/MCB.14.11.7306;
Hata A., Sabe H., Kurosaki T., Takata M., Hanafusa H.;
"Functional analysis of Csk in signal transduction through the B-cell
antigen receptor.";
Mol. Cell. Biol. 14:7306-7313(1994).
[10]
INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
PubMed=7895172; DOI=10.1016/S1074-7613(95)80040-9;
Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R.,
Bolen J.B., Kieff E.;
"Integral membrane protein 2 of Epstein-Barr virus regulates
reactivation from latency through dominant negative effects on
protein-tyrosine kinases.";
Immunity 2:155-166(1995).
[11]
PHOSPHORYLATION AT TYR-508 BY MATK.
TISSUE=Platelet;
PubMed=9171348; DOI=10.1093/emboj/16.9.2342;
Hirao A., Hamaguchi I., Suda T., Yamaguchi N.;
"Translocation of the Csk homologous kinase (Chk/Hyl) controls
activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated
platelets.";
EMBO J. 16:2342-2351(1997).
[12]
INTERACTION WITH FCGR2B.
PubMed=9232445; DOI=10.1016/S0165-2478(97)00055-2;
Sarmay G., Koncz G., Pecht I., Gergely J.;
"Fc gamma receptor type IIb induced recruitment of inositol and
protein phosphatases to the signal transductory complex of human B-
cell.";
Immunol. Lett. 57:159-164(1997).
[13]
INTERACTION WITH KIT, AND PHOSPHORYLATION.
PubMed=9341198; DOI=10.1074/jbc.272.43.27450;
Linnekin D., DeBerry C.S., Mou S.;
"Lyn associates with the juxtamembrane region of c-Kit and is
activated by stem cell factor in hematopoietic cell lines and normal
progenitor cells.";
J. Biol. Chem. 272:27450-27455(1997).
[14]
FUNCTION IN DNA DAMAGE RESPONSE; APOPTOSIS AND PHOSPHORYLATION OF
PTPN6/SHPTP1, AND INTERACTION WITH PTPN6/SHPTP1.
PubMed=10574931; DOI=10.1074/jbc.274.49.34663;
Yoshida K., Kharbanda S., Kufe D.;
"Functional interaction between SHPTP1 and the Lyn tyrosine kinase in
the apoptotic response to DNA damage.";
J. Biol. Chem. 274:34663-34668(1999).
[15]
INTERACTION WITH CBLC.
PubMed=10362357; DOI=10.1038/sj.onc.1202753;
Keane M.M., Ettenberg S.A., Nau M.M., Banerjee P., Cuello M.,
Penninger J., Lipkowitz S.;
"cbl-3: a new mammalian cbl family protein.";
Oncogene 18:3365-3375(1999).
[16]
FUNCTION IN CD79A PHOSPHORYLATION, AND INTERACTION WITH CD79A.
PubMed=10748115; DOI=10.1074/jbc.M909044199;
Gaul B.S., Harrison M.L., Geahlen R.L., Burton R.A., Post C.B.;
"Substrate recognition by the Lyn protein-tyrosine kinase. NMR
structure of the immunoreceptor tyrosine-based activation motif
signaling region of the B cell antigen receptor.";
J. Biol. Chem. 275:16174-16182(2000).
[17]
FUNCTION IN REGULATION OF MAST CELL PROLIFERATION, AND MUTAGENESIS OF
LYS-275.
PubMed=11435302; DOI=10.1182/blood.V98.2.343;
O'Laughlin-Bunner B., Radosevic N., Taylor M.L., Shivakrupa R.,
DeBerry C., Metcalfe D.D., Zhou M., Lowell C., Linnekin D.;
"Lyn is required for normal stem cell factor-induced proliferation and
chemotaxis of primary hematopoietic cells.";
Blood 98:343-350(2001).
[18]
INTERACTION WITH PDE4A.
TISSUE=Brain;
PubMed=11306681;
Rena G., Begg F., Ross A., MacKenzie C., McPhee I., Campbell L.,
Huston E., Sullivan M., Houslay M.D.;
"Molecular cloning, genomic positioning, promoter identification, and
characterization of the novel cyclic AMP-specific phosphodiesterase
PDE4A10.";
Mol. Pharmacol. 59:996-1011(2001).
[19]
FUNCTION.
PubMed=10891478; DOI=10.1128/MCB.20.15.5370-5380.2000;
Yoshida K., Weichselbaum R., Kharbanda S., Kufe D.;
"Role for Lyn tyrosine kinase as a regulator of stress-activated
protein kinase activity in response to DNA damage.";
Mol. Cell. Biol. 20:5370-5380(2000).
[20]
FUNCTION IN DNA DAMAGE RESPONSE; APOPTOSIS AND PHOSPHORYLATION OF
PPP1R15A, INTERACTION WITH PPP1R15A, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF LYS-275.
PubMed=11517336; DOI=10.1073/pnas.191130798;
Grishin A.V., Azhipa O., Semenov I., Corey S.J.;
"Interaction between growth arrest-DNA damage protein 34 and Src
kinase Lyn negatively regulates genotoxic apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001).
[21]
FUNCTION IN PHOSPHORYLATION OF KIT AND DOK1, CATALYTIC ACTIVITY, AND
INTERACTION WITH KIT.
PubMed=11825908; DOI=10.1074/jbc.M200277200;
Liang X., Wisniewski D., Strife A., Shivakrupa R., Clarkson B.,
Resh M.D.;
"Phosphatidylinositol 3-kinase and Src family kinases are required for
phosphorylation and membrane recruitment of Dok-1 in c-Kit
signaling.";
J. Biol. Chem. 277:13732-13738(2002).
[22]
INTERACTION WITH MUC1.
PubMed=12750561; DOI=10.4161/cbt.2.2.282;
Li Y., Chen W., Ren J., Yu W.H., Li Q., Yoshida K., Kufe D.;
"DF3/MUC1 signaling in multiple myeloma cells is regulated by
interleukin-7.";
Cancer Biol. Ther. 2:187-193(2003).
[23]
INTERACTION WITH UNC119.
PubMed=12496276; DOI=10.1074/jbc.M208261200;
Cen O., Gorska M.M., Stafford S.J., Sur S., Alam R.;
"Identification of UNC119 as a novel activator of SRC-type tyrosine
kinases.";
J. Biol. Chem. 278:8837-8845(2003).
[24]
FUNCTION IN THPO-MEDIATED CELL PROLIFERATION.
PubMed=14726379; DOI=10.1182/blood-2003-10-3566;
Lannutti B.J., Drachman J.G.;
"Lyn tyrosine kinase regulates thrombopoietin-induced proliferation of
hematopoietic cell lines and primary megakaryocytic progenitors.";
Blood 103:3736-3743(2004).
[25]
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-275; ASP-346;
GLU-353; ASP-498 AND ASP-499.
PubMed=15173188; DOI=10.1083/jcb.200403011;
Kasahara K., Nakayama Y., Ikeda K., Fukushima Y., Matsuda D.,
Horimoto S., Yamaguchi N.;
"Trafficking of Lyn through the Golgi caveolin involves the charged
residues on alphaE and alphaI helices in the kinase domain.";
J. Cell Biol. 165:641-652(2004).
[26]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[27]
FUNCTION IN PHOSPHORYLATION OF HCLS1.
PubMed=15795233; DOI=10.1074/jbc.M412634200;
Brunati A.M., Deana R., Folda A., Massimino M.L., Marin O., Ledro S.,
Pinna L.A., Donella-Deana A.;
"Thrombin-induced tyrosine phosphorylation of HS1 in human platelets
is sequentially catalyzed by Syk and Lyn tyrosine kinases and
associated with the cellular migration of the protein.";
J. Biol. Chem. 280:21029-21035(2005).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[29]
FUNCTION.
PubMed=16467205; DOI=10.1182/blood-2005-08-3343;
Nakata Y., Tomkowicz B., Gewirtz A.M., Ptasznik A.;
"Integrin inhibition through Lyn-dependent cross talk from CXCR4
chemokine receptors in normal human CD34+ marrow cells.";
Blood 107:4234-4239(2006).
[30]
INTERACTION WITH ABL1.
PubMed=16912036; DOI=10.1074/jbc.M605902200;
Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P.,
Wu J., Hochrein J.M., Engen J.R., Smithgall T.E.;
"Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and
modulate Bcr-Abl transforming activity.";
J. Biol. Chem. 281:30907-30916(2006).
[31]
INTERACTION WITH PAG1, MUTAGENESIS OF TYR-397 AND TYR-508, ENZYME
REGULATION, AND UBIQUITINATION.
PubMed=16920712; DOI=10.1074/jbc.M602637200;
Ingley E., Schneider J.R., Payne C.J., McCarthy D.J., Harder K.W.,
Hibbs M.L., Klinken S.P.;
"Csk-binding protein mediates sequential enzymatic down-regulation and
degradation of Lyn in erythropoietin-stimulated cells.";
J. Biol. Chem. 281:31920-31929(2006).
[32]
INTERACTION WITH TGFB1I1.
PubMed=17233630; DOI=10.1042/BJ20061618;
Rathore V.B., Okada M., Newman P.J., Newman D.K.;
"Paxillin family members function as Csk-binding proteins that
regulate Lyn activity in human and murine platelets.";
Biochem. J. 403:275-281(2007).
[33]
FUNCTION IN PHOSPHORYLATION OF LPXN, AND INTERACTION WITH LPXN.
PubMed=17640867; DOI=10.1074/jbc.M704625200;
Chew V., Lam K.P.;
"Leupaxin negatively regulates B cell receptor signaling.";
J. Biol. Chem. 282:27181-27191(2007).
[34]
INTERACTION WITH TOM1L1, AND FUNCTION IN TOM1L1 PHOSPHORYLATION.
PubMed=17977829; DOI=10.1074/jbc.M705168200;
Zhang J., Suzuki K., Hitomi T., Siraganian R.P.;
"TOM1L1 is a Lyn substrate involved in FcepsilonRI signaling in mast
cells.";
J. Biol. Chem. 282:37669-37677(2007).
[35]
FUNCTION IN CELL PROLIFERATION AND SURVIVAL, PHOSPHORYLATION,
SUBCELLULAR LOCATION, AND ROLE IN DISEASE.
PubMed=18056483; DOI=10.1182/blood-2007-04-082099;
Dos Santos C., Demur C., Bardet V., Prade-Houdellier N., Payrastre B.,
Recher C.;
"A critical role for Lyn in acute myeloid leukemia.";
Blood 111:2269-2279(2008).
[36]
FUNCTION, PHOSPHORYLATION AT TYR-397 AND TYR-508, INTERACTION WITH
PAG1 AND STAT3, AND SUBCELLULAR LOCATION.
PubMed=18070987; DOI=10.1182/blood-2007-05-090985;
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D.,
van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U.,
Borisch B., Hoessli D.C.;
"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn
tyrosine kinase in human B-NHL rafts.";
Blood 111:2310-2320(2008).
[37]
INTERACTION WITH CBL AND BCR-ABL, FUNCTION IN PHOSPHORYLATION OF
BCR-ABL, AND ROLE IN DISEASE.
PubMed=18235045; DOI=10.1182/blood-2007-08-109330;
Wu J., Meng F., Lu H., Kong L., Bornmann W., Peng Z., Talpaz M.,
Donato N.J.;
"Lyn regulates BCR-ABL and Gab2 tyrosine phosphorylation and c-Cbl
protein stability in imatinib-resistant chronic myelogenous leukemia
cells.";
Blood 111:3821-3829(2008).
[38]
SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF
GLY-2; CYS-3 AND LYS-275.
PubMed=18817770; DOI=10.1016/j.yexcr.2008.08.019;
Ikeda K., Nakayama Y., Togashi Y., Obata Y., Kuga T., Kasahara K.,
Fukumoto Y., Yamaguchi N.;
"Nuclear localization of Lyn tyrosine kinase mediated by inhibition of
its kinase activity.";
Exp. Cell Res. 314:3392-3404(2008).
[39]
FUNCTION IN ADHESION AND CELL MIGRATION.
PubMed=18802065; DOI=10.4049/jimmunol.181.7.4632;
Malik M., Chen Y.-Y., Kienzle M.F., Tomkowicz B.E., Collman R.G.,
Ptasznik A.;
"Monocyte migration and LFA-1-mediated attachment to brain
microvascular endothelia is regulated by SDF-1 alpha through Lyn
kinase.";
J. Immunol. 181:4632-4637(2008).
[40]
PHOSPHORYLATION AT TYR-193 AND TYR-460, AND ROLE IN DISEASE.
PubMed=18577747; DOI=10.1093/jnci/djn188;
Wu J., Meng F., Kong L.Y., Peng Z., Ying Y., Bornmann W.G.,
Darnay B.G., Lamothe B., Sun H., Talpaz M., Donato N.J.;
"Association between imatinib-resistant BCR-ABL mutation-negative
leukemia and persistent activation of LYN kinase.";
J. Natl. Cancer Inst. 100:926-939(2008).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[42]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; TYR-473 AND
TYR-508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[44]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[45]
INTERACTION WITH ADAM15.
PubMed=19718658; DOI=10.1002/jcb.22317;
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
"Alternative splicing of ADAM15 regulates its interactions with
cellular SH3 proteins.";
J. Cell. Biochem. 108:877-885(2009).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-228;
TYR-306; TYR-316; TYR-473 AND TYR-508, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[47]
FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
PubMed=20028775; DOI=10.1189/jlb.0409227;
Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B.,
Houtman J.C.;
"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402
and 580 occurs via a distinct mechanism than other receptor systems.";
J. Leukoc. Biol. 87:691-701(2010).
[48]
FUNCTION IN LTR4 AND LTR6 HETERODIMERIZATION, AND INTERACTION WITH
CD36.
PubMed=20037584; DOI=10.1038/ni.1836;
Stewart C.R., Stuart L.M., Wilkinson K., van Gils J.M., Deng J.,
Halle A., Rayner K.J., Boyer L., Zhong R., Frazier W.A.,
Lacy-Hulbert A., El Khoury J., Golenbock D.T., Moore K.J.;
"CD36 ligands promote sterile inflammation through assembly of a Toll-
like receptor 4 and 6 heterodimer.";
Nat. Immunol. 11:155-161(2010).
[49]
INTERACTION WITH NDFIP1 AND NDFIP2, AND UBIQUITINATION.
PubMed=20534535; DOI=10.1073/pnas.0911714107;
Mund T., Pelham H.R.;
"Regulation of PTEN/Akt and MAP kinase signaling pathways by the
ubiquitin ligase activators Ndfip1 and Ndfip2.";
Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[51]
INTERACTION WITH SCIMP.
PubMed=21930792; DOI=10.1128/MCB.05817-11;
Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M.,
Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A.,
Brdicka T.;
"SCIMP, a transmembrane adapter protein involved in major
histocompatibility complex class II signaling.";
Mol. Cell. Biol. 31:4550-4562(2011).
[52]
REVIEW.
PubMed=15220000; DOI=10.1016/j.molimm.2004.04.010;
Lowell C.A.;
"Src-family kinases: rheostats of immune cell signaling.";
Mol. Immunol. 41:631-643(2004).
[53]
REVIEW ON ROLE IN B CELLS.
PubMed=15489917; DOI=10.1038/sj.onc.1208075;
Gauld S.B., Cambier J.C.;
"Src-family kinases in B-cell development and signaling.";
Oncogene 23:8001-8006(2004).
[54]
REVIEW ON ROLE IN B CELLS.
PubMed=15664155; DOI=10.1016/S1074-7613(04)00381-4;
Xu Y., Harder K.W., Huntington N.D., Hibbs M.L., Tarlinton D.M.;
"Lyn tyrosine kinase: accentuating the positive and the negative.";
Immunity 22:9-18(2005).
[55]
REVIEW ON ROLE IN GROWTH FACTOR SIGNALING.
PubMed=16801133; DOI=10.1080/08977190600581327;
Hibbs M.L., Harder K.W.;
"The duplicitous nature of the Lyn tyrosine kinase in growth factor
signaling.";
Growth Factors 24:137-149(2006).
[56]
REVIEW ON ROLE IN MAST CELLS.
PubMed=18772004; DOI=10.1016/S0065-2776(08)00403-3;
Rivera J., Fierro N.A., Olivera A., Suzuki R.;
"New insights on mast cell activation via the high affinity receptor
for IgE.";
Adv. Immunol. 98:85-120(2008).
[57]
ROLE IN MYELOID CELL FUNCTION, AND SIGNALING.
PubMed=19290919; DOI=10.1111/j.1600-065X.2008.00758.x;
Scapini P., Pereira S., Zhang H., Lowell C.A.;
"Multiple roles of Lyn kinase in myeloid cell signaling and
function.";
Immunol. Rev. 228:23-40(2009).
[58]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[59]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[60]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[61]
MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=25255805; DOI=10.1038/ncomms5919;
Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U.,
Wright M.H., Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
"Global profiling of co- and post-translationally N-myristoylated
proteomes in human cells.";
Nat. Commun. 5:4919-4919(2014).
[62]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[63]
STRUCTURE BY NMR OF 61-123 IN COMPLEX WITH SAIMIRIINE HERPESVIRUS 2
TYROSINE KINASE INTERACTING PROTEIN.
PubMed=11955060; DOI=10.1021/bi015986j;
Schweimer K., Hoffmann S., Bauer F., Friedrich U., Kardinal C.,
Feller S.M., Biesinger B., Sticht H.;
"Structural investigation of the binding of a herpesviral protein to
the SH3 domain of tyrosine kinase Lck.";
Biochemistry 41:5120-5130(2002).
[64]
STRUCTURE BY NMR OF 61-122, AND INTERACTION WITH HERPESVIRUS TYROSINE
KINASE INTERACTING PROTEIN.
PubMed=16155203; DOI=10.1110/ps.051563605;
Bauer F., Schweimer K., Meiselbach H., Hoffmann S., Rosch P.,
Sticht H.;
"Structural characterization of Lyn-SH3 domain in complex with a
herpesviral protein reveals an extended recognition motif that
enhances binding affinity.";
Protein Sci. 14:2487-2498(2005).
[65]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-512 IN COMPLEX WITH
STAUROSPORINE.
PubMed=19857964; DOI=10.1016/j.bmcl.2009.10.038;
Miyano N., Kinoshita T., Nakai R., Kirii Y., Yokota K., Tada T.;
"Structural basis for the inhibitor recognition of human Lyn kinase
domain.";
Bioorg. Med. Chem. Lett. 19:6557-6560(2009).
[66]
VARIANT [LARGE SCALE ANALYSIS] TYR-385.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: 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. Mediates
phosphorylation of the BCR-ABL fusion protein. 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'. Kinase activity facilitates TLR4-TLR6 heterodimerization and
signal initiation. {ECO:0000269|PubMed:10574931,
ECO:0000269|PubMed:10748115, ECO:0000269|PubMed:10891478,
ECO:0000269|PubMed:11435302, ECO:0000269|PubMed:11517336,
ECO:0000269|PubMed:11825908, ECO:0000269|PubMed:14726379,
ECO:0000269|PubMed:15795233, ECO:0000269|PubMed:16467205,
ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:17977829,
ECO:0000269|PubMed:18056483, ECO:0000269|PubMed:18070987,
ECO:0000269|PubMed:18235045, ECO:0000269|PubMed:18577747,
ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19290919,
ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20037584,
ECO:0000269|PubMed:7687428}.
-!- 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: 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: 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. Interacts with LYN (By similarity).
{ECO:0000250|UniProtKB:P25911, 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}.
-!- INTERACTION:
O92972:- (xeno); NbExp=2; IntAct=EBI-79452, EBI-710506;
P22575:- (xeno); NbExp=3; IntAct=EBI-79452, EBI-866709;
P27958:- (xeno); NbExp=4; IntAct=EBI-79452, EBI-706378;
Q9WMX2:- (xeno); NbExp=3; IntAct=EBI-79452, EBI-710918;
P10275:AR; NbExp=5; IntAct=EBI-79452, EBI-608057;
Q8R5G7:Arap3 (xeno); NbExp=2; IntAct=EBI-79452, EBI-621463;
P20273:CD22; NbExp=2; IntAct=EBI-79452, EBI-78277;
P25063:CD24; NbExp=6; IntAct=EBI-79452, EBI-6267018;
P16671:CD36; NbExp=3; IntAct=EBI-79452, EBI-2808214;
Q08857:Cd36 (xeno); NbExp=2; IntAct=EBI-79452, EBI-8346984;
P11049:CD37; NbExp=5; IntAct=EBI-79452, EBI-6139068;
P46527:CDKN1B; NbExp=2; IntAct=EBI-79452, EBI-519280;
P00533:EGFR; NbExp=6; IntAct=EBI-79452, EBI-297353;
Q13480:GAB1; NbExp=7; IntAct=EBI-79452, EBI-517684;
Q9HCN6:GP6; NbExp=2; IntAct=EBI-79452, EBI-515278;
P05556:ITGB1; NbExp=4; IntAct=EBI-79452, EBI-703066;
P10721:KIT; NbExp=7; IntAct=EBI-79452, EBI-1379503;
P33993:MCM7; NbExp=5; IntAct=EBI-6895930, EBI-355924;
P08581:MET; NbExp=2; IntAct=EBI-79452, EBI-1039152;
Q9NWQ8:PAG1; NbExp=16; IntAct=EBI-79452, EBI-2828115;
P63244:RACK1; NbExp=2; IntAct=EBI-79452, EBI-296739;
P12931:SRC; NbExp=2; IntAct=EBI-79452, EBI-621482;
-!- SUBCELLULAR LOCATION: Cell membrane. Nucleus. Cytoplasm.
Cytoplasm, perinuclear region. Golgi apparatus. Membrane
{ECO:0000305}; Lipid-anchor {ECO:0000305}. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LYN A, p56lyn;
IsoId=P07948-1; Sequence=Displayed;
Name=2; Synonyms=LYN B, p53lyn;
IsoId=P07948-2; Sequence=VSP_005002;
-!- 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}.
-!- DOMAIN: The protein kinase domain plays an important role in its
localization in the cell membrane. {ECO:0000269|PubMed:15173188}.
-!- PTM: Ubiquitinated by CBL, leading to its degradation.
Ubiquitination is SH3-dependent. {ECO:0000269|PubMed:16920712,
ECO:0000269|PubMed:20534535}.
-!- PTM: 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}.
-!- 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.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M16038; AAA59540.1; -; mRNA.
EMBL; M79321; AAB50019.1; -; mRNA.
EMBL; BC075001; AAH75001.1; -; mRNA.
EMBL; BC075002; AAH75002.1; -; mRNA.
EMBL; BC126456; AAI26457.1; -; mRNA.
EMBL; BC126458; AAI26459.1; -; mRNA.
CCDS; CCDS47859.1; -. [P07948-2]
CCDS; CCDS6162.1; -. [P07948-1]
PIR; A26719; TVHULY.
RefSeq; NP_001104567.1; NM_001111097.2. [P07948-2]
RefSeq; NP_002341.1; NM_002350.3. [P07948-1]
RefSeq; XP_016868905.1; XM_017013416.1. [P07948-2]
UniGene; Hs.491767; -.
UniGene; Hs.545418; -.
PDB; 1W1F; NMR; -; A=61-123.
PDB; 1WA7; NMR; -; A=61-123.
PDB; 3A4O; X-ray; 3.00 A; X=233-512.
PDBsum; 1W1F; -.
PDBsum; 1WA7; -.
PDBsum; 3A4O; -.
ProteinModelPortal; P07948; -.
SMR; P07948; -.
BioGrid; 110245; 193.
DIP; DIP-1056N; -.
ELM; P07948; -.
IntAct; P07948; 72.
MINT; MINT-200655; -.
STRING; 9606.ENSP00000428924; -.
BindingDB; P07948; -.
ChEMBL; CHEMBL3905; -.
DrugBank; DB06616; Bosutinib.
DrugBank; DB09079; Nintedanib.
DrugBank; DB08901; Ponatinib.
GuidetoPHARMACOLOGY; 2060; -.
iPTMnet; P07948; -.
PhosphoSitePlus; P07948; -.
SwissPalm; P07948; -.
BioMuta; LYN; -.
DMDM; 125480; -.
REPRODUCTION-2DPAGE; P07948; -.
EPD; P07948; -.
MaxQB; P07948; -.
PaxDb; P07948; -.
PeptideAtlas; P07948; -.
PRIDE; P07948; -.
DNASU; 4067; -.
Ensembl; ENST00000519728; ENSP00000428924; ENSG00000254087. [P07948-1]
Ensembl; ENST00000520220; ENSP00000428424; ENSG00000254087. [P07948-2]
GeneID; 4067; -.
KEGG; hsa:4067; -.
UCSC; uc003xsk.5; human. [P07948-1]
CTD; 4067; -.
DisGeNET; 4067; -.
GeneCards; LYN; -.
HGNC; HGNC:6735; LYN.
HPA; CAB004492; -.
HPA; HPA001231; -.
MIM; 165120; gene.
neXtProt; NX_P07948; -.
OpenTargets; ENSG00000254087; -.
PharmGKB; PA30498; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P07948; -.
KO; K05854; -.
OMA; WMAYYNN; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P07948; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-5621480; Dectin-2 family.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-982772; Growth hormone receptor signaling.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P07948; -.
SIGNOR; P07948; -.
ChiTaRS; LYN; human.
EvolutionaryTrace; P07948; -.
GeneWiki; LYN; -.
GenomeRNAi; 4067; -.
PMAP-CutDB; P07948; -.
PRO; PR:P07948; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000254087; -.
CleanEx; HS_LYN; -.
ExpressionAtlas; P07948; baseline and differential.
Genevisible; P07948; HS.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0034666; C:integrin alpha2-beta1 complex; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0030061; C:mitochondrial crista; IEA:Ensembl.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IEA:Ensembl.
GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
GO; GO:0004716; F:signal transducer, downstream of receptor, with protein tyrosine kinase activity; TAS:ProtInc.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0031668; P:cellular response to extracellular stimulus; IEA:Ensembl.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IMP:BHF-UCL.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0050663; P:cytokine secretion; IEA:Ensembl.
GO; GO:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; ISS:UniProtKB.
GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; ISS:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0002553; P:histamine secretion by mast cell; IEA:Ensembl.
GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030889; P:negative regulation of B cell proliferation; IBA:GO_Central.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0050777; P:negative regulation of immune response; TAS:UniProtKB.
GO; GO:1902532; P:negative regulation of intracellular signal transduction; ISS:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0070667; P:negative regulation of mast cell proliferation; ISS:UniProtKB.
GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; ISS:UniProtKB.
GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; ISS:UniProtKB.
GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0051272; P:positive regulation of cellular component movement; IDA:UniProtKB.
GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; ISS:UniProtKB.
GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; IEA:Ensembl.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
GO; GO:0070668; P:positive regulation of mast cell proliferation; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:BHF-UCL.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; IDA:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0002902; P:regulation of B cell apoptotic process; IBA:GO_Central.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
GO; GO:0050707; P:regulation of cytokine secretion; IEA:Ensembl.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0045646; P:regulation of erythrocyte differentiation; ISS:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0033003; P:regulation of mast cell activation; ISS:UniProtKB.
GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
GO; GO:0090025; P:regulation of monocyte chemotaxis; IMP:UniProtKB.
GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0001932; P:regulation of protein phosphorylation; TAS:UniProtKB.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0009743; P:response to carbohydrate; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0006991; P:response to sterol depletion; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0002513; P:tolerance induction to self antigen; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IMP:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Golgi apparatus;
Host-virus interaction; Immunity; Inflammatory response;
Innate immunity; Kinase; Lipoprotein; Membrane; Myristate;
Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:25255805}.
CHAIN 2 512 Tyrosine-protein kinase Lyn.
/FTId=PRO_0000088129.
DOMAIN 63 123 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 129 226 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 247 501 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 253 261 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 367 367 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 275 275 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 193 193 Phosphotyrosine.
{ECO:0000269|PubMed:18577747}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 306 306 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 316 316 Phosphotyrosine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 397 397 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:18070987,
ECO:0000269|PubMed:7935444}.
MOD_RES 460 460 Phosphotyrosine.
{ECO:0000269|PubMed:18577747}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 508 508 Phosphotyrosine; by autocatalysis, CSK
and MATK. {ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:18070987,
ECO:0000269|PubMed:7935444,
ECO:0000269|PubMed:9171348}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:25255805,
ECO:0000305|PubMed:18817770}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000305}.
VAR_SEQ 23 43 Missing (in isoform 2).
{ECO:0000303|PubMed:8125304}.
/FTId=VSP_005002.
VARIANT 385 385 D -> Y (in a breast pleomorphic lobular
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041737.
MUTAGEN 2 2 G->A: Loss of localization to the cell
membrane; when associated with A-3.
{ECO:0000269|PubMed:18817770}.
MUTAGEN 3 3 C->A: Loss of localization to the cell
membrane; when associated with A-2.
{ECO:0000269|PubMed:18817770}.
MUTAGEN 275 275 K->A: Loss of activity and no effect on
localization to the cell membrane.
Abundant localization in the nucleus;
when associated with A-2 and A-3.
{ECO:0000269|PubMed:11435302,
ECO:0000269|PubMed:11517336,
ECO:0000269|PubMed:15173188,
ECO:0000269|PubMed:18817770}.
MUTAGEN 275 275 K->L,R: Loss of kinase activity.
{ECO:0000269|PubMed:11435302,
ECO:0000269|PubMed:11517336,
ECO:0000269|PubMed:15173188,
ECO:0000269|PubMed:18817770}.
MUTAGEN 346 346 D->A: Impedes the trafficking from the
Golgi apparatus toward the cell membrane;
when associated with A-353; A-498 and A-
499. {ECO:0000269|PubMed:15173188}.
MUTAGEN 353 353 E->A: Impedes the trafficking from the
Golgi apparatus toward the cell membrane;
when associated with A-346; A-498 and A-
499. {ECO:0000269|PubMed:15173188}.
MUTAGEN 397 397 Y->F: Strongly reduced kinase activity.
{ECO:0000269|PubMed:16920712}.
MUTAGEN 498 498 D->A: Impedes the trafficking from the
Golgi apparatus toward the cell membrane;
when associated with A-346; A-353 and A-
499. {ECO:0000269|PubMed:15173188}.
MUTAGEN 499 499 D->A: Impedes the trafficking from the
Golgi apparatus toward the cell membrane;
when associated with A-346; A-353 and A-
498. {ECO:0000269|PubMed:15173188}.
MUTAGEN 508 508 Y->F: Abolishes autoinhibition and
thereby increases kinase activity.
{ECO:0000269|PubMed:16920712}.
STRAND 66 72 {ECO:0000244|PDB:1W1F}.
STRAND 78 80 {ECO:0000244|PDB:1W1F}.
STRAND 89 95 {ECO:0000244|PDB:1W1F}.
STRAND 97 104 {ECO:0000244|PDB:1W1F}.
TURN 105 107 {ECO:0000244|PDB:1W1F}.
STRAND 110 114 {ECO:0000244|PDB:1W1F}.
TURN 115 117 {ECO:0000244|PDB:1W1F}.
STRAND 118 120 {ECO:0000244|PDB:1W1F}.
STRAND 259 262 {ECO:0000244|PDB:3A4O}.
STRAND 265 269 {ECO:0000244|PDB:3A4O}.
STRAND 273 275 {ECO:0000244|PDB:3A4O}.
STRAND 284 286 {ECO:0000244|PDB:3A4O}.
TURN 287 289 {ECO:0000244|PDB:3A4O}.
HELIX 290 293 {ECO:0000244|PDB:3A4O}.
TURN 294 297 {ECO:0000244|PDB:3A4O}.
STRAND 306 309 {ECO:0000244|PDB:3A4O}.
STRAND 311 314 {ECO:0000244|PDB:3A4O}.
STRAND 316 319 {ECO:0000244|PDB:3A4O}.
HELIX 327 330 {ECO:0000244|PDB:3A4O}.
HELIX 334 338 {ECO:0000244|PDB:3A4O}.
HELIX 341 360 {ECO:0000244|PDB:3A4O}.
STRAND 372 375 {ECO:0000244|PDB:3A4O}.
STRAND 381 383 {ECO:0000244|PDB:3A4O}.
HELIX 407 409 {ECO:0000244|PDB:3A4O}.
HELIX 412 416 {ECO:0000244|PDB:3A4O}.
HELIX 422 437 {ECO:0000244|PDB:3A4O}.
TURN 449 451 {ECO:0000244|PDB:3A4O}.
HELIX 452 457 {ECO:0000244|PDB:3A4O}.
STRAND 466 468 {ECO:0000244|PDB:3A4O}.
HELIX 470 477 {ECO:0000244|PDB:3A4O}.
TURN 478 480 {ECO:0000244|PDB:3A4O}.
TURN 484 486 {ECO:0000244|PDB:3A4O}.
HELIX 490 502 {ECO:0000244|PDB:3A4O}.
SEQUENCE 512 AA; 58574 MW; 408D3D461204E378 CRC64;
MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL LPGQRFQTKD
PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLLTKKE GFIPSNYVAK
LNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DFDPVHGDVI
KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQADGLCR RLEKACISPK PQKPWDKDAW
EIPRESIKLV KRLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
KLVRLYAVVT REEPIYIITE YMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ IAEGMAYIER
KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF
TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMTALSQGY RMPRVENCPD ELYDIMKMCW
KEKAEERPTF DYLQSVLDDF YTATEGQYQQ QP


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