ID LYN_RAT Reviewed; 512 AA.
AC Q07014; Q63320;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 214.
DE RecName: Full=Tyrosine-protein kinase Lyn;
DE EC=2.7.10.2;
DE AltName: Full=V-yes-1 Yamaguchi sarcoma viral related oncogene homolog;
DE AltName: Full=p53Lyn;
DE AltName: Full=p56Lyn;
GN Name=Lyn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Minoguchi K., Nishikata H., Siraganian R.P.;
RT "Bacterially expressed rat p56lyn binds several proteins in rat basophilic
RT leukemia cells including pp72, a tyrosine phosphorylated protein prominent
RT in activated cells.";
RL J. Immunol. 150:222-222(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8125304; DOI=10.1016/0378-1119(94)90811-7;
RA Rider L.G., Raben N., Miller L., Jelsema C.;
RT "The cDNAs encoding two forms of the LYN protein tyrosine kinase are
RT expressed in rat mast cells and human myeloid cells.";
RL Gene 138:219-222(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9295361; DOI=10.1074/jbc.272.38.24072;
RA Vonakis B.M., Chen H., Haleem-Smith H., Metzger H.;
RT "The unique domain as the site on Lyn kinase for its constitutive
RT association with the high affinity receptor for IgE.";
RL J. Biol. Chem. 272:24072-24080(1997).
RN [4]
RP PHOSPHORYLATION AT TYR-397 AND TYR-508, CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=9477973; DOI=10.1021/bi971332s;
RA Donella-Deana A., Cesaro L., Ruzzene M., Brunati A.M., Marin O.,
RA Pinna L.A.;
RT "Spontaneous autophosphorylation of Lyn tyrosine kinase at both its
RT activation segment and C-terminal tail confers altered substrate
RT specificity.";
RL Biochemistry 37:1438-1446(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316 AND TYR-508, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Non-receptor tyrosine-protein kinase that transmits signals
CC from cell surface receptors and plays an important role in the
CC regulation of innate and adaptive immune responses, hematopoiesis,
CC responses to growth factors and cytokines, integrin signaling, but also
CC responses to DNA damage and genotoxic agents. Functions primarily as
CC negative regulator, but can also function as activator, depending on
CC the context. Required for the initiation of the B-cell response, but
CC also for its down-regulation and termination. Plays an important role
CC in the regulation of B-cell differentiation, proliferation, survival
CC and apoptosis, and is important for immune self-tolerance. Acts
CC downstream of several immune receptors, including the B-cell receptor,
CC CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4.
CC Plays a role in the inflammatory response to bacterial
CC lipopolysaccharide. Mediates the responses to cytokines and growth
CC factors in hematopoietic progenitors, platelets, erythrocytes, and in
CC mature myeloid cells, such as dendritic cells, neutrophils and
CC eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor
CC CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an
CC important role in integrin signaling. Regulates cell proliferation,
CC survival, differentiation, migration, adhesion, degranulation, and
CC cytokine release. Involved in the regulation of endothelial activation,
CC neutrophil adhesion and transendothelial migration (By similarity).
CC Down-regulates signaling pathways by phosphorylation of immunoreceptor
CC tyrosine-based inhibitory motifs (ITIM), that then serve as binding
CC sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and
CC INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases
CC and their substrates. Phosphorylates LIME1 in response to CD22
CC activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B,
CC CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, SYK and TEC. Promotes
CC phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1.
CC Required for rapid phosphorylation of FER in response to FCER1
CC activation. Mediates KIT phosphorylation. Acts as an effector of EPOR
CC (erythropoietin receptor) in controlling KIT expression and may play a
CC role in erythroid differentiation during the switch between
CC proliferation and maturation. Depending on the context, activates or
CC inhibits several signaling cascades. Regulates phosphatidylinositol 3-
CC kinase activity and AKT1 activation. Regulates activation of the MAP
CC kinase signaling cascade, including activation of MAP2K1/MEK1,
CC MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation
CC of STAT5A and/or STAT5B (By similarity). Phosphorylates LPXN on 'Tyr-
CC 72' (By similarity). Kinase activity facilitates TLR4-TLR6
CC heterodimerization and signal initiation. Phosphorylates SCIMP on 'Tyr-
CC 96'; this enhances binding of SCIMP to TLR4, promoting the
CC phosphorylation of TLR4, and a selective cytokine response to
CC lipopolysaccharide in macrophages (By similarity). Phosphorylates CLNK
CC (By similarity). Phosphorylates BCAR1/CAS and NEDD9/HEF1 (By
CC similarity). {ECO:0000250|UniProtKB:P07948,
CC ECO:0000250|UniProtKB:P25911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:9477973};
CC -!- ACTIVITY REGULATION: Subject to autoinhibition, mediated by
CC intramolecular interactions between the SH2 domain and the C-terminal
CC phosphotyrosine. Phosphorylation at Tyr-397 is required for optimal
CC activity. Phosphorylated by CSK at Tyr-508; phosphorylation at Tyr-508
CC inhibits kinase activity. Kinase activity is modulated by
CC dephosphorylation by PTPRC/CD45. {ECO:0000269|PubMed:9477973}.
CC -!- SUBUNIT: Interacts with TEC. Interacts (via SH2 domain) with FLT3
CC (tyrosine phosphorylated). Interacts with LIME1 and with CD79A upon
CC activation of the B-cell antigen receptor. Interacts with the B-cell
CC receptor complex. Interacts with phosphorylated THEMIS2. Interacts with
CC EPOR. Interacts with MS4A2/FCER1B. Interaction (via the SH2 and SH3
CC domains) with MUC1 is stimulated by IL7 and the subsequent
CC phosphorylation increases the binding between MUC1 and CTNNB1/beta-
CC catenin. Interacts with ADAM15. Interacts with NDFIP2 and more weakly
CC with NDFIP1. Interacts with FASLG. Interacts with KIT. Interacts with
CC HCLS1. Interacts with FCGR2B. Interacts with FCGR1A; the interaction
CC may be indirect. Interacts with CD19, CD22, CD79A and CD79B. Interacts
CC (via SH3 domain) with CBLC, PPP1R15A and PDE4A. Interacts with TGFB1I1.
CC Interacts (via SH3 domain) with PIK3R1, the regulatory subunit of
CC phosphatidylinositol 3-kinase; this interaction enhances
CC phosphatidylinositol 3-kinase activity. Interacts with CSF2RB, the
CC common subunit of the IL3, IL5 and CSF2 receptors. Interacts with PAG1;
CC identified in a complex with PAG1 and STAT3. Interacts with ABL1.
CC Interacts with PTPN6/SHP-1. Interacts (via SH3 domain) with SCIMP (via
CC proline-rich region) (By similarity). This interaction facilitates the
CC phosphorylation of SCIMP 'Tyr-96', which enhances binding of SCIMP to
CC TLR4, and consequently the phosphorylation of TLR4 in response to
CC stimulation by lipopolysaccharide in macrophages (By similarity).
CC Interacts with LPXN (via LD motif 3) and the interaction is induced
CC upon B-cell antigen receptor (BCR) activation. Interacts (via SH3-
CC domain) with ANKRD54 (via ankyrin repeat region) in an activation-
CC independent status of LYN. Forms a multiprotein complex with ANKRD54
CC and HCLS1 (By similarity). Interacts (via SH2 and SH3 domains) with
CC UNC119; leading to LYN activation (By similarity). Interacts with CD36.
CC Interacts with LYN (By similarity). Interacts with SKAP1 and FYB1; this
CC interaction promotes the phosphorylation of CLNK (By similarity).
CC Interacts with BCAR1/CAS and NEDD9/HEF1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P07948, ECO:0000250|UniProtKB:P25911}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Nucleus
CC {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear region
CC {ECO:0000250}. Golgi apparatus {ECO:0000250}. Membrane
CC {ECO:0000250|UniProtKB:P07948}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P07948}. Note=Accumulates in the nucleus by
CC inhibition of Crm1-mediated nuclear export. Nuclear accumulation is
CC increased by inhibition of its kinase activity. The trafficking from
CC the Golgi apparatus to the cell membrane occurs in a kinase domain-
CC dependent but kinase activity independent manner and is mediated by
CC exocytic vesicular transport (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=LYN A;
CC IsoId=Q07014-1; Sequence=Displayed;
CC Name=LYN B;
CC IsoId=Q07014-2; Sequence=VSP_005004;
CC -!- TISSUE SPECIFICITY: Detected in spleen (at protein level). Expressed
CC predominantly in B-lymphoid and myeloid cells.
CC {ECO:0000269|PubMed:9477973}.
CC -!- DOMAIN: The protein kinase domain plays an important role in its
CC localization in the cell membrane. {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Ubiquitination is SH3-dependent (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Autophosphorylated (By similarity). Phosphorylated on tyrosine
CC residues in response to KIT signaling (By similarity). Phosphorylation
CC at Tyr-397 is required for optimal activity (By similarity).
CC Phosphorylation at Tyr-508 inhibits kinase activity (By similarity).
CC Phosphorylated at Tyr-508 by CSK (By similarity). Dephosphorylated by
CC PTPRC/CD45 (By similarity). Becomes rapidly phosphorylated upon
CC activation of the B-cell receptor and the immunoglobulin receptor
CC FCGR1A (By similarity). Phosphorylated in response to integrin ITGB1 in
CC B-cells (By similarity). {ECO:0000250|UniProtKB:P07948,
CC ECO:0000250|UniProtKB:P25911}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; L14951; AAA41549.1; -; mRNA.
DR EMBL; L14782; AAA20944.1; -; mRNA.
DR EMBL; L14823; AAA20945.1; -; mRNA.
DR EMBL; AF000300; AAB71344.1; -; mRNA.
DR EMBL; AF000301; AAB71345.1; -; mRNA.
DR EMBL; AF000302; AAB71346.1; -; mRNA.
DR PIR; I56160; I56160.
DR PIR; PT0198; PT0198.
DR RefSeq; NP_001104568.1; NM_001111098.1. [Q07014-2]
DR RefSeq; NP_110484.1; NM_030857.2. [Q07014-1]
DR RefSeq; XP_006237896.1; XM_006237834.3. [Q07014-1]
DR AlphaFoldDB; Q07014; -.
DR SMR; Q07014; -.
DR BioGRID; 249512; 12.
DR ELM; Q07014; -.
DR IntAct; Q07014; 8.
DR MINT; Q07014; -.
DR STRING; 10116.ENSRNOP00000011130; -.
DR BindingDB; Q07014; -.
DR ChEMBL; CHEMBL4363; -.
DR iPTMnet; Q07014; -.
DR PhosphoSitePlus; Q07014; -.
DR SwissPalm; Q07014; -.
DR jPOST; Q07014; -.
DR PaxDb; 10116-ENSRNOP00000011130; -.
DR Ensembl; ENSRNOT00000011130.6; ENSRNOP00000011130.4; ENSRNOG00000008180.6. [Q07014-1]
DR Ensembl; ENSRNOT00055033678; ENSRNOP00055027327; ENSRNOG00055019728. [Q07014-1]
DR Ensembl; ENSRNOT00060016783; ENSRNOP00060013124; ENSRNOG00060009930. [Q07014-1]
DR Ensembl; ENSRNOT00065025763; ENSRNOP00065020249; ENSRNOG00065015515. [Q07014-1]
DR GeneID; 81515; -.
DR KEGG; rno:81515; -.
DR UCSC; RGD:621017; rat. [Q07014-1]
DR AGR; RGD:621017; -.
DR CTD; 4067; -.
DR RGD; 621017; Lyn.
DR eggNOG; KOG0197; Eukaryota.
DR GeneTree; ENSGT00940000158011; -.
DR HOGENOM; CLU_000288_7_2_1; -.
DR InParanoid; Q07014; -.
DR OMA; TGNMGCI; -.
DR OrthoDB; 1614410at2759; -.
DR PhylomeDB; Q07014; -.
DR TreeFam; TF351634; -.
DR BRENDA; 2.7.10.2; 5301.
DR Reactome; R-RNO-114604; GPVI-mediated activation cascade.
DR Reactome; R-RNO-1433557; Signaling by SCF-KIT.
DR Reactome; R-RNO-1433559; Regulation of KIT signaling.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-2029481; FCGR activation.
DR Reactome; R-RNO-210990; PECAM1 interactions.
DR Reactome; R-RNO-2454202; Fc epsilon receptor (FCERI) signaling.
DR Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
DR Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-RNO-389356; CD28 co-stimulation.
DR Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
DR Reactome; R-RNO-5621480; Dectin-2 family.
DR Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-RNO-5690714; CD22 mediated BCR regulation.
DR Reactome; R-RNO-69231; Cyclin D associated events in G1.
DR Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-RNO-9006335; Signaling by Erythropoietin.
DR Reactome; R-RNO-9027276; Erythropoietin activates Phosphoinositide-3-kinase (PI3K).
DR Reactome; R-RNO-9027284; Erythropoietin activates RAS.
DR Reactome; R-RNO-912631; Regulation of signaling by CBL.
DR Reactome; R-RNO-9674555; Signaling by CSF3 (G-CSF).
DR Reactome; R-RNO-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-RNO-982772; Growth hormone receptor signaling.
DR PRO; PR:Q07014; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000008180; Expressed in spleen and 18 other cell types or tissues.
DR Genevisible; Q07014; RN.
DR GO; GO:0005912; C:adherens junction; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0099091; C:postsynaptic specialization, intracellular component; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:RGD.
DR GO; GO:0043208; F:glycosphingolipid binding; IPI:RGD.
DR GO; GO:0005178; F:integrin binding; IDA:RGD.
DR GO; GO:0016301; F:kinase activity; TAS:RGD.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0141038; F:phosphatidylinositol 3-kinase activator activity; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
DR GO; GO:0140031; F:phosphorylation-dependent protein binding; ISO:RGD.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0001782; P:B cell homeostasis; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0038159; P:C-X-C chemokine receptor CXCR4 signaling pathway; ISO:RGD.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IEP:RGD.
DR GO; GO:0034605; P:cellular response to heat; IEP:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR GO; GO:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
DR GO; GO:0006974; P:DNA damage response; ISO:RGD.
DR GO; GO:0030222; P:eosinophil differentiation; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0002774; P:Fc receptor mediated inhibitory signaling pathway; ISS:UniProtKB.
DR GO; GO:0002431; P:Fc receptor mediated stimulatory signaling pathway; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0002553; P:histamine secretion by mast cell; IMP:RGD.
DR GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0038043; P:interleukin-5-mediated signaling pathway; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:1902532; P:negative regulation of intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:UniProtKB.
DR GO; GO:0070667; P:negative regulation of mast cell proliferation; ISS:UniProtKB.
DR GO; GO:0002762; P:negative regulation of myeloid leukocyte differentiation; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0034136; P:negative regulation of toll-like receptor 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0002576; P:platelet degranulation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0060369; P:positive regulation of Fc receptor mediated stimulatory signaling pathway; IMP:RGD.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IDA:RGD.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IMP:RGD.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; ISO:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
DR GO; GO:0002902; P:regulation of B cell apoptotic process; ISO:RGD.
DR GO; GO:0050855; P:regulation of B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISO:RGD.
DR GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0045646; P:regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0033003; P:regulation of mast cell activation; ISS:UniProtKB.
DR GO; GO:0043304; P:regulation of mast cell degranulation; ISS:UniProtKB.
DR GO; GO:0090025; P:regulation of monocyte chemotaxis; ISO:RGD.
DR GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0006991; P:response to sterol depletion; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0002513; P:tolerance induction to self antigen; ISS:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
DR CDD; cd05072; PTKc_Lyn; 1.
DR CDD; cd10364; SH2_Src_Lyn; 1.
DR CDD; cd12004; SH3_Lyn; 1.
DR Gene3D; 3.30.505.10; SH2 domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR035852; Lyn_SH2.
DR InterPro; IPR035748; Lyn_SH3.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24418:SF42; TYROSINE-PROTEIN KINASE LYN; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; ATP-binding; Cell membrane;
KW Cytoplasm; Golgi apparatus; Immunity; Inflammatory response;
KW Innate immunity; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein; Proto-oncogene;
KW Reference proteome; SH2 domain; SH3 domain; Transferase;
KW Tyrosine-protein kinase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT CHAIN 2..512
FT /note="Tyrosine-protein kinase Lyn"
FT /id="PRO_0000088131"
FT DOMAIN 63..123
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 129..226
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 247..501
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 367
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 253..261
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 193
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT MOD_RES 306
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT MOD_RES 316
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 397
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9477973"
FT MOD_RES 460
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT MOD_RES 508
FT /note="Phosphotyrosine; by autocatalysis, CSK and MATK"
FT /evidence="ECO:0000269|PubMed:9477973,
FT ECO:0007744|PubMed:22673903"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:P07948"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 25..45
FT /note="Missing (in isoform LYN B)"
FT /evidence="ECO:0000305"
FT /id="VSP_005004"
FT CONFLICT 231
FT /note="P -> L (in Ref. 2; AAA20944/AAA20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="V -> A (in Ref. 2; AAA20944/AAA20945)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="C -> Y (in Ref. 2; AAA20944/AAA20945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 58660 MW; E03615E229CD43F1 CRC64;
MGCIKSKRKD NLNDDGVDMK TQPVRNTDRT IYVRDPTSNK QQRPVPESQL LPGQRFQAKD
PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLSSKRE GFIPSNYVAK
VNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DYDPMHGDVI
KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW
EIPRESIKLV KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSAQAFLEE ANLMKTLQHD
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGSKVL LPKLIDFSAQ IAEGMAYIER
KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF
TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMTALSQGY RMPRMENCPD ELYDIMKMCW
KESAEERPTF DYLQSVLDDF YTATEGQYQQ QP
//
