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

 LYN_MOUSE               Reviewed;         512 AA.
P25911; Q62127;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 192.
RecName: Full=Tyrosine-protein kinase Lyn;
EC=2.7.10.2;
AltName: Full=V-yes-1 Yamaguchi sarcoma viral related oncogene homolog;
AltName: Full=p53Lyn;
AltName: Full=p56Lyn;
Name=Lyn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
PubMed=1710766; DOI=10.1128/MCB.11.7.3399;
Stanley E., Ralph S.J., McEwen S., Boulet I., Holtzman D.A., Lock P.,
Dunn A.R.;
"Alternatively spliced murine lyn mRNAs encode distinct proteins.";
Mol. Cell. Biol. 11:3399-3406(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, AND TISSUE SPECIFICITY.
PubMed=2017160; DOI=10.1128/MCB.11.5.2391;
Yi T., Bolen J.B., Ihle J.N.;
"Hematopoietic cells express two forms of lyn kinase differing by 21
amino acids in the amino terminus.";
Mol. Cell. Biol. 11:2391-2398(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary gland;
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 364-432.
PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
"The application of the polymerase chain reaction to cloning members
of the protein tyrosine kinase family.";
Gene 85:67-74(1989).
[5]
INTERACTION WITH B CELL RECEPTOR, AND AUTOPHOSPHORYLATION.
PubMed=1702903; DOI=10.1126/science.1702903;
Yamanashi Y., Kakiuchi T., Mizuguchi J., Yamamoto T., Toyoshima K.;
"Association of B cell antigen receptor with protein tyrosine kinase
Lyn.";
Science 251:192-194(1991).
[6]
INTERACTION WITH CD79A.
PubMed=8168489;
Clark M.R., Johnson S.A., Cambier J.C.;
"Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels
of binding specificity and tyrosine phosphorylated Ig-alpha
stimulation of Fyn activity.";
EMBO J. 13:1911-1919(1994).
[7]
INTERACTION WITH CD79A AND CD79B, AND FUNCTION IN PHOSPHORYLATION OF
CD79A AND CD79B.
PubMed=15335855; DOI=10.1016/0960-9822(93)90062-S;
Law D.A., Chan V.W., Datta S.K., DeFranco A.L.;
"B-cell antigen receptor motifs have redundant signalling capabilities
and bind the tyrosine kinases PTK72, Lyn and Fyn.";
Curr. Biol. 3:645-657(1993).
[8]
FUNCTION IN SYK PHOSPHORYLATION.
PubMed=7513017; DOI=10.1084/jem.179.5.1725;
Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T.,
Yamamoto T., Yamamura H.;
"Syk activation by the Src-family tyrosine kinase in the B cell
receptor signaling.";
J. Exp. Med. 179:1725-1729(1994).
[9]
INTERACTION WITH CD79A.
PubMed=8183901; DOI=10.1073/pnas.91.10.4268;
Pleiman C.M., Abrams C., Gauen L.T., Bedzyk W., Jongstra J.,
Shaw A.S., Cambier J.C.;
"Distinct p53/56lyn and p59fyn domains associate with
nonphosphorylated and phosphorylated Ig-alpha.";
Proc. Natl. Acad. Sci. U.S.A. 91:4268-4272(1994).
[10]
FUNCTION IN PIK3R1 ACTIVATION, AND INTERACTION WITH PIK3R1.
PubMed=8128248; DOI=10.1126/science.8128248;
Pleiman C.M., Hertz W.M., Cambier J.C.;
"Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3
binding to the p85 subunit.";
Science 263:1609-1612(1994).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=7585947; DOI=10.1016/0092-8674(95)90171-X;
Hibbs M.L., Tarlinton D.M., Armes J., Grail D., Hodgson G.,
Maglitto R., Stacker S.A., Dunn A.R.;
"Multiple defects in the immune system of Lyn-deficient mice,
culminating in autoimmune disease.";
Cell 83:301-311(1995).
[12]
DISRUPTION PHENOTYPE, AND FUNCTION IN B CELLS AND IN PHOSPHORYLATION
OF CBL AND HCLS1.
PubMed=7584145; DOI=10.1016/1074-7613(95)90126-4;
Nishizumi H., Taniuchi I., Yamanashi Y., Kitamura D., Ilic D.,
Mori S., Watanabe T., Yamamoto T.;
"Impaired proliferation of peripheral B cells and indication of
autoimmune disease in lyn-deficient mice.";
Immunity 3:549-560(1995).
[13]
INTERACTION WITH CBL.
PubMed=7782294; DOI=10.1074/jbc.270.24.14347;
Tanaka S., Neff L., Baron R., Levy J.B.;
"Tyrosine phosphorylation and translocation of the c-cbl protein after
activation of tyrosine kinase signaling pathways.";
J. Biol. Chem. 270:14347-14351(1995).
[14]
CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND ENZYME REGULATION.
PubMed=8530369; DOI=10.1074/jbc.270.50.29773;
Sotirellis N., Johnson T.M., Hibbs M.L., Stanley I.J., Stanley E.,
Dunn A.R., Cheng H.C.;
"Autophosphorylation induces autoactivation and a decrease in the Src
homology 2 domain accessibility of the Lyn protein kinase.";
J. Biol. Chem. 270:29773-29780(1995).
[15]
FUNCTION IN TEC PHOSPHORYLATION, AND INTERACTION WITH TEC.
PubMed=8621063;
Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.;
"Tec protein-tyrosine kinase is an effector molecule of Lyn protein-
tyrosine kinase.";
FASEB J. 10:637-642(1996).
[16]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=9064343; DOI=10.1084/jem.184.3.831;
Wang J., Koizumi T., Watanabe T.;
"Altered antigen receptor signaling and impaired Fas-mediated
apoptosis of B cells in Lyn-deficient mice.";
J. Exp. Med. 184:831-838(1996).
[17]
FUNCTION IN PHOSPHORYLATION OF BTK.
PubMed=8629002; DOI=10.1126/science.271.5250.822;
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.;
"Activation of BTK by a phosphorylation mechanism initiated by SRC
family kinases.";
Science 271:822-825(1996).
[18]
DISRUPTION PHENOTYPE, FUNCTION, ALTERNATIVE SPLICING, AND
PHOSPHORYLATION.
PubMed=9252121; DOI=10.1016/S1074-7613(00)80511-7;
Chan V.W., Meng F., Soriano P., DeFranco A.L., Lowell C.A.;
"Characterization of the B lymphocyte populations in Lyn-deficient
mice and the role of Lyn in signal initiation and down-regulation.";
Immunity 7:69-81(1997).
[19]
FUNCTION IN MAST CELLS AND IN SIGNALING DOWN-STREAM OF FCER1.
PubMed=9036984;
Nishizumi H., Yamamoto T.;
"Impaired tyrosine phosphorylation and Ca2+ mobilization, but not
degranulation, in lyn-deficient bone marrow-derived mast cells.";
J. Immunol. 158:2350-2355(1997).
[20]
INTERACTION WITH EPOR AND JAK2, AND FUNCTION.
PubMed=9573010;
Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.;
"Lyn physically associates with the erythropoietin receptor and may
play a role in activation of the Stat5 pathway.";
Blood 91:3734-3745(1998).
[21]
FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION AND ACTIVATION OF
MAPK1/ERK2; MAPK8/JNK1 AND MAPK9/JNK2.
PubMed=9601638; DOI=10.1016/S0960-9822(98)70223-4;
Chan V.W., Lowell C.A., DeFranco A.L.;
"Defective negative regulation of antigen receptor signaling in Lyn-
deficient B lymphocytes.";
Curr. Biol. 8:545-553(1998).
[22]
FUNCTION IN CD22 PHOSPHORYLATION.
PubMed=9480991; DOI=10.1084/jem.187.5.807;
Smith K.G., Tarlinton D.M., Doody G.M., Hibbs M.L., Fearon D.T.;
"Inhibition of the B cell by CD22: a requirement for Lyn.";
J. Exp. Med. 187:807-811(1998).
[23]
FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION.
PubMed=9547345; DOI=10.1084/jem.187.8.1343;
Nishizumi H., Horikawa K., Mlinaric-Rascan I., Yamamoto T.;
"A double-edged kinase Lyn: a positive and negative regulator for
antigen receptor-mediated signals.";
J. Exp. Med. 187:1343-1348(1998).
[24]
FUNCTION IN FCGR2 PHOSPHORYLATION, AND INTERACTION WITH FCGR2.
PubMed=9469421;
Malbec O., Fong D.C., Turner M., Tybulewicz V.L., Cambier J.C.,
Fridman W.H., Daeron M.;
"Fc epsilon receptor I-associated lyn-dependent phosphorylation of Fc
gamma receptor IIB during negative regulation of mast cell
activation.";
J. Immunol. 160:1647-1658(1998).
[25]
FUNCTION IN CD72 PHOSPHORYLATION.
PubMed=9590210;
Adachi T., Flaswinkel H., Yakura H., Reth M., Tsubata T.;
"The B cell surface protein CD72 recruits the tyrosine phosphatase
SHP-1 upon tyrosine phosphorylation.";
J. Immunol. 160:4662-4665(1998).
[26]
DISRUPTION PHENOTYPE, AND FUNCTION IN ERYTHROPOIESIS.
PubMed=10594694; DOI=10.1046/j.1365-2567.1999.00899.x;
Ochi H., Takeshita H., Suda T., Nisitani S., Honjo T., Watanabe T.;
"Regulation of B-1 cell activation and its autoantibody production by
Lyn kinase-regulated signallings.";
Immunology 98:595-603(1999).
[27]
PHOSPHORYLATION AT TYR-397 AND TYR-508, DEPHOSPHORYLATION BY
PTPRC/CD45, AND ENZYME REGULATION.
PubMed=10415030;
Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M.,
Clark M.R., Mizuno K., Yakura H.;
"CD45 negatively regulates lyn activity by dephosphorylating both
positive and negative regulatory tyrosine residues in immature B
cells.";
J. Immunol. 163:1321-1326(1999).
[28]
FUNCTION IN PHOSPHORYLATION OF LILRB3/PIR-B.
PubMed=10327049; DOI=10.1038/sj.onc.1202552;
Maeda A., Scharenberg A.M., Tsukada S., Bolen J.B., Kinet J.P.,
Kurosaki T.;
"Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced
activation of Syk and Btk by SHP-1.";
Oncogene 18:2291-2297(1999).
[29]
FUNCTION IN PHOSPHORYLATION OF CSF2RB, AND INTERACTION WITH CSF2RB.
PubMed=10672044; DOI=10.1046/j.1365-2443.2000.00312.x;
Dahl M.E., Arai K.I., Watanabe S.;
"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.";
Genes Cells 5:143-153(2000).
[30]
FUNCTION IN PHOSPHORYLATION OF DOK1.
PubMed=10640270;
Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H.,
Yamamoto T., Baltimore D.;
"Role of the rasGAP-associated docking protein p62(dok) in negative
regulation of B cell receptor-mediated signaling.";
Genes Dev. 14:11-16(2000).
[31]
FUNCTION IN CD5 PHOSPHORYLATION.
PubMed=11007759; DOI=10.1093/intimm/12.10.1417;
Ochi H., Watanabe T.;
"Negative regulation of B cell receptor-mediated signaling in B-1
cells through CD5 and Ly49 co-receptors via Lyn kinase activity.";
Int. Immunol. 12:1417-1423(2000).
[32]
FUNCTION IN REGULATION OF CELL PROLIFERATION AND MIGRATION IN RESPONSE
TO KITLG.
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).
[33]
DISRUPTION PHENOTYPE, FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF
SIRPA; PTPN6/SHP-1; PTPN11/SHP-2 AND INPP5D/SHIP-1, AND MUTAGENESIS OF
TYR-508.
PubMed=11672542; DOI=10.1016/S1074-7613(01)00208-4;
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.;
"Gain- and loss-of-function Lyn mutant mice define a critical
inhibitory role for Lyn in the myeloid lineage.";
Immunity 15:603-615(2001).
[34]
INTERACTION WITH PPP1R15A.
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).
[35]
FUNCTION IN REGULATION OF IMMUNE RESPONSE, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, ENZYME REGULATION, AND MUTAGENESIS OF TYR-508.
PubMed=12486102; DOI=10.1084/jem.20020515;
Hibbs M.L., Harder K.W., Armes J., Kountouri N., Quilici C.,
Casagranda F., Dunn A.R., Tarlinton D.M.;
"Sustained activation of Lyn tyrosine kinase in vivo leads to
autoimmunity.";
J. Exp. Med. 196:1593-1604(2002).
[36]
FUNCTION IN PHOSPHORYLATING SYK.
PubMed=12077122; DOI=10.1074/jbc.M201362200;
Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.;
"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.";
J. Biol. Chem. 277:31703-31714(2002).
[37]
FUNCTION.
PubMed=12874221; DOI=10.4049/jimmunol.171.3.1319;
Pereira S., Lowell C.;
"The Lyn tyrosine kinase negatively regulates neutrophil integrin
signaling.";
J. Immunol. 171:1319-1327(2003).
[38]
FUNCTION IN DOWN-REGULATION OF THPO-MEDIATED CELL PROLIFERATION AND IN
DOWN-REGULATION OF MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
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).
[39]
UBIQUITINATION.
PubMed=15304502; DOI=10.1074/jbc.M404082200;
Shao Y., Yang C., Elly C., Liu Y.C.;
"Differential regulation of the B cell receptor-mediated signaling by
the E3 ubiquitin ligase Cbl.";
J. Biol. Chem. 279:43646-43653(2004).
[40]
FUNCTION IN MAST CELL PROLIFERATION AND IN DOWN-REGULATION OF AKT1;
MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
PubMed=14525964; DOI=10.1189/jlb.0503224;
Hernandez-Hansen V., Mackay G.A., Lowell C.A., Wilson B.S.,
Oliver J.M.;
"The Src kinase Lyn is a negative regulator of mast cell
proliferation.";
J. Leukoc. Biol. 75:143-151(2004).
[41]
FUNCTION AS NEGATIVE REGULATOR OF DENDRITIC CELL DIFFERENTIATION;
PROLIFERATION AND SURVIVAL.
PubMed=16116174; DOI=10.4049/jimmunol.175.5.2880;
Chu C.L., Lowell C.A.;
"The Lyn tyrosine kinase differentially regulates dendritic cell
generation and maturation.";
J. Immunol. 175:2880-2889(2005).
[42]
DISRUPTION PHENOTYPE, AND FUNCTION IN MATURATION OF DENDRITIC CELLS
AND IN INFLAMMATORY RESPONSE.
PubMed=16034130; DOI=10.4049/jimmunol.175.3.1867;
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.;
"Lyn-deficient mice develop severe, persistent asthma: Lyn is a
critical negative regulator of Th2 immunity.";
J. Immunol. 175:1867-1875(2005).
[43]
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, AND INTERACTION WITH
MS4A2/FCER1B.
PubMed=16272347; DOI=10.4049/jimmunol.175.10.6885;
Xiao W., Nishimoto H., Hong H., Kitaura J., Nunomura S.,
Maeda-Yamamoto M., Kawakami Y., Lowell C.A., Ra C., Kawakami T.;
"Positive and negative regulation of mast cell activation by Lyn via
the FcepsilonRI.";
J. Immunol. 175:6885-6892(2005).
[44]
INTERACTION WITH LIME1, AND FUNCTION IN PHOSPHORYLATION OF LIME1.
PubMed=16249387; DOI=10.1182/blood-2005-05-1859;
Ahn E., Lee H., Yun Y.;
"LIME acts as a transmembrane adapter mediating BCR-dependent B-cell
activation.";
Blood 107:1521-1527(2006).
[45]
INTERACTION WITH FLT3.
PubMed=16684964; DOI=10.1182/blood-2005-07-008896;
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S.,
Ronnstrand L.;
"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.";
Blood 108:1542-1550(2006).
[46]
FUNCTION.
PubMed=16731527; DOI=10.1074/jbc.M604252200;
Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.;
"Fer and Fps/Fes participate in a Lyn-dependent pathway from
FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit
mast cell activation.";
J. Biol. Chem. 281:20949-20957(2006).
[47]
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).
[48]
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).
[49]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[50]
INTERACTION WITH ANKRD54.
PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
Samuels A.L., Klinken S.P., Ingley E.;
"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
influences erythropoietin-induced differentiation.";
Blood 113:3845-3856(2009).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; TYR-397 AND TYR-508,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[52]
FUNCTION.
PubMed=19492092; DOI=10.1371/journal.pone.0005721;
Kosmider O., Buet D., Gallais I., Denis N., Moreau-Gachelin F.;
"Erythropoietin down-regulates stem cell factor receptor (Kit)
expression in the leukemic proerythroblast: role of Lyn kinase.";
PLoS ONE 4:E5721-E5721(2009).
[53]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-397, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[54]
INTERACTION WITH THEMIS2.
PubMed=20644716; DOI=10.1371/journal.pone.0011465;
Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S.,
Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.;
"Themis2/ICB1 is a signaling scaffold that selectively regulates
macrophage Toll-like receptor signaling and cytokine production.";
PLoS ONE 5:E11465-E11465(2010).
[55]
FUNCTION IN PLATELET GRANULE SECRETION AND PLATELET AGGREGATION.
PubMed=20189992; DOI=10.1074/jbc.M109.098756;
Li Z., Zhang G., Liu J., Stojanovic A., Ruan C., Lowell C.A., Du X.;
"An important role of the SRC family kinase Lyn in stimulating
platelet granule secretion.";
J. Biol. Chem. 285:12559-12570(2010).
[56]
FUNCTION IN DOWN-REGULATION OF TLR2 AND TLR4 SIGNALING; CYTOKINE
RELEASE AND THE INFLAMMATORY RESPONSE TO LIPOPOLYSACCHARIDE.
PubMed=20385881; DOI=10.4049/jimmunol.0901423;
Keck S., Freudenberg M., Huber M.;
"Activation of murine macrophages via TLR2 and TLR4 is negatively
regulated by a Lyn/PI3K module and promoted by SHIP1.";
J. Immunol. 184:5809-5818(2010).
[57]
INTERACTION WITH CEACAM1.
PubMed=22496641; DOI=10.1371/journal.ppat.1002597;
Lu R., Pan H., Shively J.E.;
"CEACAM1 negatively regulates IL-1beta production in LPS activated
neutrophils by recruiting SHP-1 to a SYK-TLR4-CEACAM1 complex.";
PLoS Pathog. 8:E1002597-E1002597(2012).
[58]
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).
[59]
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).
[60]
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).
[61]
REVIEW.
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).
[62]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 239-512 IN COMPLEXES WITH
DASATINIB; PP2 AND AMP-PNP, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION,
ENZYME REGULATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18984583; DOI=10.1074/jbc.M807850200;
Williams N.K., Lucet I.S., Klinken S.P., Ingley E., Rossjohn J.;
"Crystal structures of the Lyn protein tyrosine kinase domain in its
Apo- and inhibitor-bound state.";
J. Biol. Chem. 284:284-291(2009).
-!- 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. 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:0000250|UniProtKB:P07948,
ECO:0000269|PubMed:10327049, ECO:0000269|PubMed:10594694,
ECO:0000269|PubMed:10640270, ECO:0000269|PubMed:10672044,
ECO:0000269|PubMed:11007759, ECO:0000269|PubMed:11435302,
ECO:0000269|PubMed:11672542, ECO:0000269|PubMed:12077122,
ECO:0000269|PubMed:12874221, ECO:0000269|PubMed:14525964,
ECO:0000269|PubMed:14726379, ECO:0000269|PubMed:15335855,
ECO:0000269|PubMed:16034130, ECO:0000269|PubMed:16116174,
ECO:0000269|PubMed:16249387, ECO:0000269|PubMed:16272347,
ECO:0000269|PubMed:16731527, ECO:0000269|PubMed:17640867,
ECO:0000269|PubMed:19492092, ECO:0000269|PubMed:20189992,
ECO:0000269|PubMed:20385881, ECO:0000269|PubMed:7513017,
ECO:0000269|PubMed:7584145, ECO:0000269|PubMed:7585947,
ECO:0000269|PubMed:8128248, ECO:0000269|PubMed:8621063,
ECO:0000269|PubMed:8629002, ECO:0000269|PubMed:9036984,
ECO:0000269|PubMed:9064343, ECO:0000269|PubMed:9252121,
ECO:0000269|PubMed:9469421, ECO:0000269|PubMed:9480991,
ECO:0000269|PubMed:9547345, ECO:0000269|PubMed:9573010,
ECO:0000269|PubMed:9590210, ECO:0000269|PubMed:9601638}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:12486102,
ECO:0000269|PubMed:18984583, ECO:0000269|PubMed:2017160,
ECO:0000269|PubMed:8530369}.
-!- 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:10415030, ECO:0000269|PubMed:12486102,
ECO:0000269|PubMed:18984583, ECO:0000269|PubMed:8530369}.
-!- 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
(via SH2 and SH3 domains) with UNC119; leading to LYN activation
(By similarity). Interacts with CD36. Interacts with LYN
(PubMed:22496641). {ECO:0000250|UniProtKB:P07948,
ECO:0000269|PubMed:10672044, ECO:0000269|PubMed:11517336,
ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:16249387,
ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:1702903, ECO:0000269|PubMed:17233630,
ECO:0000269|PubMed:17640867, ECO:0000269|PubMed:19064729,
ECO:0000269|PubMed:20644716, ECO:0000269|PubMed:22496641,
ECO:0000269|PubMed:7782294, ECO:0000269|PubMed:8128248,
ECO:0000269|PubMed:8168489, ECO:0000269|PubMed:8621063,
ECO:0000269|PubMed:9469421, ECO:0000269|PubMed:9573010}.
-!- INTERACTION:
Q64355:Efs; NbExp=2; IntAct=EBI-643537, EBI-647907;
P49710:Hcls1; NbExp=11; IntAct=EBI-643537, EBI-924601;
Q8CIH5:Plcg2; NbExp=2; IntAct=EBI-643537, EBI-617954;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Nucleus
{ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
region {ECO:0000250}. Golgi apparatus {ECO:0000250}. Membrane
{ECO:0000250|UniProtKB:P07948}; Lipid-anchor
{ECO:0000250|UniProtKB:P07948}. 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).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LYN A, p56;
IsoId=P25911-1; Sequence=Displayed;
Name=2; Synonyms=LYN B, p53;
IsoId=P25911-2; Sequence=VSP_005003;
-!- TISSUE SPECIFICITY: Detected in bone marrow-derived monocytes (at
protein level). Expressed predominantly in B-lymphoid and myeloid
cells. {ECO:0000269|PubMed:2017160}.
-!- DOMAIN: The protein kinase domain plays an important role in its
localization in the cell membrane. {ECO:0000250}.
-!- PTM: Ubiquitinated by CBL, leading to its degradation.
{ECO:0000269|PubMed:15304502}.
-!- PTM: 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. {ECO:0000250, ECO:0000269|PubMed:10415030,
ECO:0000269|PubMed:16272347, ECO:0000269|PubMed:9252121}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:10594694, ECO:0000269|PubMed:11672542,
ECO:0000269|PubMed:16034130, ECO:0000269|PubMed:7584145,
ECO:0000269|PubMed:7585947, ECO:0000269|PubMed:9064343,
ECO:0000269|PubMed:9252121}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M64608; AAA39470.1; -; mRNA.
EMBL; M57696; AAA39471.1; -; mRNA.
EMBL; M57697; AAA39472.1; -; mRNA.
EMBL; BC031547; AAH31547.1; -; mRNA.
EMBL; M33426; AAA40017.1; -; mRNA.
CCDS; CCDS17939.1; -. [P25911-2]
CCDS; CCDS51109.1; -. [P25911-1]
PIR; A39719; A39719.
RefSeq; NP_001104566.1; NM_001111096.1. [P25911-1]
UniGene; Mm.317331; -.
PDB; 2ZV7; X-ray; 2.50 A; A=239-512.
PDB; 2ZV8; X-ray; 2.70 A; A=239-512.
PDB; 2ZV9; X-ray; 2.76 A; A=239-512.
PDB; 2ZVA; X-ray; 2.60 A; A=239-512.
PDB; 4TZI; X-ray; 2.10 A; A/B=115-229.
PDBsum; 2ZV7; -.
PDBsum; 2ZV8; -.
PDBsum; 2ZV9; -.
PDBsum; 2ZVA; -.
PDBsum; 4TZI; -.
ProteinModelPortal; P25911; -.
SMR; P25911; -.
BioGrid; 201256; 10.
DIP; DIP-37806N; -.
ELM; P25911; -.
IntAct; P25911; 21.
MINT; MINT-100482; -.
STRING; 10090.ENSMUSP00000038838; -.
BindingDB; P25911; -.
ChEMBL; CHEMBL2258; -.
iPTMnet; P25911; -.
PhosphoSitePlus; P25911; -.
SwissPalm; P25911; -.
PaxDb; P25911; -.
PeptideAtlas; P25911; -.
PRIDE; P25911; -.
Ensembl; ENSMUST00000041377; ENSMUSP00000038838; ENSMUSG00000042228. [P25911-1]
Ensembl; ENSMUST00000103010; ENSMUSP00000100075; ENSMUSG00000042228. [P25911-2]
GeneID; 17096; -.
KEGG; mmu:17096; -.
UCSC; uc008rwm.2; mouse. [P25911-1]
CTD; 4067; -.
MGI; MGI:96892; Lyn.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P25911; -.
KO; K05854; -.
OMA; WMAYYNN; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P25911; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-MMU-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-389356; CD28 co-stimulation.
Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
Reactome; R-MMU-982772; Growth hormone receptor signaling.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
EvolutionaryTrace; P25911; -.
PRO; PR:P25911; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000042228; -.
ExpressionAtlas; P25911; baseline and differential.
Genevisible; P25911; MM.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0034666; C:integrin alpha2-beta1 complex; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0045121; C:membrane raft; ISO:MGI.
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; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density of dendrite; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046875; F:ephrin receptor binding; IEA:Ensembl.
GO; GO:0005128; F:erythropoietin receptor binding; TAS: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; ISO:MGI.
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:0032403; F:protein complex binding; IPI:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
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; IMP:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
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; ISO:MGI.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
GO; GO:0050663; P:cytokine secretion; IEA:Ensembl.
GO; GO:0097028; P:dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; IMP:UniProtKB.
GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; IMP:UniProtKB.
GO; GO:0042541; P:hemoglobin biosynthetic process; TAS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
GO; GO:0002553; P:histamine secretion by mast cell; IEA:Ensembl.
GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:1902532; P:negative regulation of intracellular signal transduction; IMP:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB.
GO; GO:0070667; P:negative regulation of mast cell proliferation; IMP:UniProtKB.
GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; IMP:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; IMP:UniProtKB.
GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
GO; GO:0031175; P:neuron projection development; IMP:MGI.
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:0002576; P:platelet degranulation; IMP:UniProtKB.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IEA:Ensembl.
GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IGI:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0051272; P:positive regulation of cellular component movement; ISO:MGI.
GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IMP: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; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; ISO:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0002902; P:regulation of B cell apoptotic process; IMP:UniProtKB.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; IMP:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISO:MGI.
GO; GO:0001817; P:regulation of cytokine production; IMP:UniProtKB.
GO; GO:0050707; P:regulation of cytokine secretion; IMP:UniProtKB.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
GO; GO:0033003; P:regulation of mast cell activation; IMP:UniProtKB.
GO; GO:0043304; P:regulation of mast cell degranulation; IMP:UniProtKB.
GO; GO:0090025; P:regulation of monocyte chemotaxis; ISO:MGI.
GO; GO:0090330; P:regulation of platelet aggregation; IMP:UniProtKB.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IGI:MGI.
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; IDA: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:UniProtKB.
GO; GO:0002513; P:tolerance induction to self antigen; IMP:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
CDD; cd10364; SH2_Src_Lyn; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR035852; Lyn_SH2.
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;
Immunity; Inflammatory response; Innate immunity; Kinase; Lipoprotein;
Membrane; Myristate; Nucleotide-binding; Nucleus; Palmitate;
Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain;
SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P07948}.
CHAIN 2 512 Tyrosine-protein kinase Lyn.
/FTId=PRO_0000088130.
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:0000305}.
ACT_SITE 367 367 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 275 275 ATP. {ECO:0000305}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 193 193 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07948}.
MOD_RES 228 228 Phosphoserine.
{ECO:0000250|UniProtKB:P07948}.
MOD_RES 306 306 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07948}.
MOD_RES 316 316 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07948}.
MOD_RES 397 397 Phosphotyrosine; by autocatalysis.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:10415030,
ECO:0000269|PubMed:16272347}.
MOD_RES 460 460 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07948}.
MOD_RES 473 473 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07948}.
MOD_RES 508 508 Phosphotyrosine; by autocatalysis, CSK
and MATK. {ECO:0000244|PubMed:18034455,
ECO:0000244|PubMed:19144319,
ECO:0000269|PubMed:10415030}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000250|UniProtKB:P07948}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 25 45 Missing (in isoform 2).
{ECO:0000303|PubMed:2017160}.
/FTId=VSP_005003.
MUTAGEN 508 508 Y->F: Abolishes autoinhibition, leading
to increased kinase activity and
constitutive phosphorylation of LYN
substrates. {ECO:0000269|PubMed:11672542,
ECO:0000269|PubMed:12486102}.
CONFLICT 77 77 I -> F (in Ref. 2; AAA39471/AAA39472).
{ECO:0000305}.
CONFLICT 161 161 L -> I (in Ref. 2; AAA39471/AAA39472).
{ECO:0000305}.
CONFLICT 279 279 P -> L (in Ref. 2; AAA39471/AAA39472).
{ECO:0000305}.
CONFLICT 391 391 V -> I (in Ref. 2; AAA39471/AAA39472).
{ECO:0000305}.
CONFLICT 415 415 I -> F (in Ref. 4; AAA40017).
{ECO:0000305}.
CONFLICT 425 425 D -> N (in Ref. 1; AAA39470).
{ECO:0000305}.
CONFLICT 432 432 L -> P (in Ref. 4; AAA40017).
{ECO:0000305}.
HELIX 136 143 {ECO:0000244|PDB:4TZI}.
STRAND 153 157 {ECO:0000244|PDB:4TZI}.
STRAND 159 161 {ECO:0000244|PDB:4TZI}.
STRAND 165 172 {ECO:0000244|PDB:4TZI}.
STRAND 174 187 {ECO:0000244|PDB:4TZI}.
STRAND 193 196 {ECO:0000244|PDB:4TZI}.
STRAND 199 203 {ECO:0000244|PDB:4TZI}.
HELIX 204 213 {ECO:0000244|PDB:4TZI}.
STRAND 218 220 {ECO:0000244|PDB:4TZI}.
HELIX 244 246 {ECO:0000244|PDB:2ZV7}.
STRAND 247 254 {ECO:0000244|PDB:2ZV7}.
STRAND 257 266 {ECO:0000244|PDB:2ZV7}.
TURN 267 269 {ECO:0000244|PDB:2ZV7}.
STRAND 270 277 {ECO:0000244|PDB:2ZV7}.
HELIX 284 294 {ECO:0000244|PDB:2ZV7}.
STRAND 305 309 {ECO:0000244|PDB:2ZV7}.
STRAND 311 314 {ECO:0000244|PDB:2ZV7}.
STRAND 316 320 {ECO:0000244|PDB:2ZV7}.
HELIX 327 332 {ECO:0000244|PDB:2ZV7}.
HELIX 336 338 {ECO:0000244|PDB:2ZV7}.
HELIX 341 360 {ECO:0000244|PDB:2ZV7}.
HELIX 370 372 {ECO:0000244|PDB:2ZV7}.
STRAND 373 375 {ECO:0000244|PDB:2ZV7}.
STRAND 381 383 {ECO:0000244|PDB:2ZV7}.
HELIX 407 409 {ECO:0000244|PDB:2ZV7}.
HELIX 412 417 {ECO:0000244|PDB:2ZV7}.
HELIX 422 438 {ECO:0000244|PDB:2ZV7}.
HELIX 449 455 {ECO:0000244|PDB:2ZV7}.
HELIX 456 458 {ECO:0000244|PDB:2ZV7}.
HELIX 470 479 {ECO:0000244|PDB:2ZV7}.
HELIX 484 486 {ECO:0000244|PDB:2ZV7}.
HELIX 490 498 {ECO:0000244|PDB:2ZV7}.
SEQUENCE 512 AA; 58812 MW; FDA1D21CC90C50EC CRC64;
MGCIKSKRKD NLNDDEVDSK TQPVRNTDRT IYVRDPTSNK QQRPVPEFHL LPGQRFQTKD
PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLSSKRE GFIPSNYVAK
VNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DYDPMHGDVI
KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW
EIPRESIKLV KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ IAEGMAYIER
KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF
TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMSALSQGY RMPRMENCPD ELYDIMKMCW
KEKAEERPTF DYLQSVLDDF YTATEGQYQQ QP


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