Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 LYN_RAT                 Reviewed;         512 AA.
Q07014; Q63320;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-FEB-2018, entry version 177.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Minoguchi K., Nishikata H., Siraganian R.P.;
"Bacterially expressed rat p56lyn binds several proteins in rat
basophilic leukemia cells including pp72, a tyrosine phosphorylated
protein prominent in activated cells.";
J. Immunol. 150:222-222(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
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 [MRNA].
PubMed=9295361; DOI=10.1074/jbc.272.38.24072;
Vonakis B.M., Chen H., Haleem-Smith H., Metzger H.;
"The unique domain as the site on Lyn kinase for its constitutive
association with the high affinity receptor for IgE.";
J. Biol. Chem. 272:24072-24080(1997).
[4]
PHOSPHORYLATION AT TYR-397 AND TYR-508, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, ENZYME REGULATION, AND TISSUE SPECIFICITY.
PubMed=9477973; DOI=10.1021/bi971332s;
Donella-Deana A., Cesaro L., Ruzzene M., Brunati A.M., Marin O.,
Pinna L.A.;
"Spontaneous autophosphorylation of Lyn tyrosine kinase at both its
activation segment and C-terminal tail confers altered substrate
specificity.";
Biochemistry 37:1438-1446(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316 AND TYR-508, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (By similarity). Phosphorylates
LPXN on 'Tyr-72' (By similarity). Kinase activity facilitates
TLR4-TLR6 heterodimerization and signal initiation. {ECO:0000250,
ECO:0000250|UniProtKB:P07948}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:9477973}.
-!- 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.
{ECO:0000269|PubMed:9477973}.
-!- 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 (By
similarity). Interacts (via SH2 and SH3 domains) with UNC119;
leading to LYN activation (By similarity). Interacts with CD36.
Interacts with LYN (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P07948, ECO:0000250|UniProtKB:P25911}.
-!- 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=LYN A;
IsoId=Q07014-1; Sequence=Displayed;
Name=LYN B;
IsoId=Q07014-2; Sequence=VSP_005004;
-!- TISSUE SPECIFICITY: Detected in spleen (at protein level).
Expressed predominantly in B-lymphoid and myeloid cells.
{ECO:0000269|PubMed:9477973}.
-!- DOMAIN: The protein kinase domain plays an important role in its
localization in the cell membrane. {ECO:0000250}.
-!- PTM: Ubiquitinated. Ubiquitination is SH3-dependent (By
similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L14951; AAA41549.1; -; mRNA.
EMBL; L14782; AAA20944.1; -; mRNA.
EMBL; L14823; AAA20945.1; -; mRNA.
EMBL; AF000300; AAB71344.1; -; mRNA.
EMBL; AF000301; AAB71345.1; -; mRNA.
EMBL; AF000302; AAB71346.1; -; mRNA.
PIR; I56160; I56160.
PIR; PT0198; PT0198.
RefSeq; NP_001104568.1; NM_001111098.1. [Q07014-2]
RefSeq; NP_110484.1; NM_030857.2. [Q07014-1]
RefSeq; XP_006237896.1; XM_006237834.3. [Q07014-1]
UniGene; Rn.4338; -.
ProteinModelPortal; Q07014; -.
SMR; Q07014; -.
BioGrid; 249512; 7.
ELM; Q07014; -.
IntAct; Q07014; 3.
MINT; Q07014; -.
STRING; 10116.ENSRNOP00000011130; -.
BindingDB; Q07014; -.
ChEMBL; CHEMBL4363; -.
iPTMnet; Q07014; -.
PhosphoSitePlus; Q07014; -.
PaxDb; Q07014; -.
PRIDE; Q07014; -.
Ensembl; ENSRNOT00000011130; ENSRNOP00000011130; ENSRNOG00000008180. [Q07014-1]
GeneID; 81515; -.
KEGG; rno:81515; -.
UCSC; RGD:621017; rat. [Q07014-1]
CTD; 4067; -.
RGD; 621017; Lyn.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; Q07014; -.
KO; K05854; -.
OMA; WMAYYNN; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; Q07014; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-114604; GPVI-mediated activation cascade.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-1433559; Regulation of KIT signaling.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-2029481; FCGR activation.
Reactome; R-RNO-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-RNO-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-RNO-2871796; FCERI mediated MAPK activation.
Reactome; R-RNO-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-RNO-2871837; FCERI mediated NF-kB activation.
Reactome; R-RNO-389356; CD28 co-stimulation.
Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-RNO-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-RNO-5690714; CD22 mediated BCR regulation.
Reactome; R-RNO-69231; Cyclin D associated events in G1.
Reactome; R-RNO-75892; Platelet Adhesion to exposed collagen.
Reactome; R-RNO-912631; Regulation of signaling by CBL.
Reactome; R-RNO-982772; Growth hormone receptor signaling.
PRO; PR:Q07014; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000008180; -.
Genevisible; Q07014; RN.
GO; GO:0005913; C:cell-cell adherens junction; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
GO; GO:0034666; C:integrin alpha2-beta1 complex; IDA:RGD.
GO; GO:0042629; C:mast cell granule; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0030061; C:mitochondrial crista; IDA:RGD.
GO; GO:0005758; C:mitochondrial intermembrane space; IDA:RGD.
GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
GO; GO:0043015; F:gamma-tubulin binding; IDA:RGD.
GO; GO:0043208; F:glycosphingolipid binding; IPI:RGD.
GO; GO:0005178; F:integrin binding; IDA:RGD.
GO; GO:0044325; F:ion channel binding; ISO:RGD.
GO; GO:0016301; F:kinase activity; TAS:RGD.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0051219; F:phosphoprotein binding; IPI:RGD.
GO; GO:0140031; F:phosphorylation-dependent protein binding; ISO:RGD.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IDA:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0017124; F:SH3 domain binding; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
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; ISO:RGD.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:RGD.
GO; GO:0031668; P:cellular response to extracellular stimulus; IEP:RGD.
GO; GO:0034605; P:cellular response to heat; IEP:RGD.
GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
GO; GO:0050663; P:cytokine secretion; IMP:RGD.
GO; GO:0097028; P:dendritic cell differentiation; ISS:UniProtKB.
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:0030097; P:hemopoiesis; ISO:RGD.
GO; GO:0002553; P:histamine secretion by mast cell; IMP:RGD.
GO; GO:0002768; P:immune response-regulating cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030889; P:negative regulation of B cell proliferation; ISO:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS: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; ISO:RGD.
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; ISO:RGD.
GO; GO:0014003; P:oligodendrocyte development; IEP:RGD.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0002576; P:platelet degranulation; ISS:UniProtKB.
GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; ISO:RGD.
GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISO:RGD.
GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0051272; P:positive regulation of cellular component movement; ISO:RGD.
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; IMP:RGD.
GO; GO:0060252; P:positive regulation of glial cell proliferation; IDA:RGD.
GO; GO:0070668; P:positive regulation of mast cell proliferation; ISO:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
GO; GO:0070447; P:positive regulation of oligodendrocyte progenitor proliferation; IMP:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISO:RGD.
GO; GO:0042327; P:positive regulation of phosphorylation; IMP:RGD.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
GO; GO:0070304; P:positive regulation of stress-activated protein kinase signaling cascade; ISO:RGD.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISS:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
GO; GO:0002902; P:regulation of B cell apoptotic process; ISO:RGD.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; ISO:RGD.
GO; GO:0001817; P:regulation of cytokine production; ISS:UniProtKB.
GO; GO:0050707; P:regulation of cytokine secretion; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
GO; GO:0090330; P:regulation of platelet aggregation; ISS:UniProtKB.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:RGD.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0048678; P:response to axon injury; IEP:RGD.
GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0009725; P:response to hormone; ISS:UniProtKB.
GO; GO:0032868; P:response to insulin; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
GO; GO:0006991; P:response to sterol depletion; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
GO; GO:0002513; P:tolerance induction to self antigen; ISS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:RGD.
CDD; cd10364; SH2_Src_Lyn; 1.
CDD; cd12004; SH3_Lyn; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR035852; Lyn_SH2.
InterPro; IPR035748; Lyn_SH3.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
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;
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_0000088131.
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 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:0000244|PubMed:22673903}.
MOD_RES 397 397 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:9477973}.
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:22673903,
ECO:0000269|PubMed:9477973}.
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 LYN B).
{ECO:0000305}.
/FTId=VSP_005004.
CONFLICT 231 231 P -> L (in Ref. 2; AAA20944/AAA20945).
{ECO:0000305}.
CONFLICT 308 308 V -> A (in Ref. 2; AAA20944/AAA20945).
{ECO:0000305}.
CONFLICT 419 419 C -> Y (in Ref. 2; AAA20944/AAA20945).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
FP-0045 v-yes-1 Yamaguchi sarcoma viral related oncogene homolog 10ug
201-20-6672 LYN{v-yes-1 Yamaguchi sarcoma viral related oncogene homolog}mouse.mAb 0.2ml
E96523Hu ELISA Kit for V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN) 96T/Kit
FP-0045 v_yes_1 Yamaguchi sarcoma viral related oncogene homolog 10 ug
FP-0045 v-yes-1 Yamaguchi sarcoma viral related oncogene homolog; SH2-Domain: LYN 10ug
LYPD1 LYN Gene v-yes-1 Yamaguchi sarcoma viral related oncogene homolog
DL-LYN-Hu Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN) ELISA Kit 96T
201-12-2622 Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN)ELISA Kit 48T
FP-0045 Fusion proteins: v-yes-1 Yamaguchi sarcoma viral related oncogene homolog, LYN 10ug
E2621Hu Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN)ELISA Kit 48T
UT-E04483 Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN) ELISA Kit 96T
I1796 V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN), Human, ELISA Kit 96T
E2621Hu Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN)ELISA Kit 96T
201-12-2622 Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN)ELISA Kit 96T
UB-E04483 Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog(LYN)ELISA Kit 96T
YHB3225Hu Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN)ELISA Kit 96T
QY-E04483 Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog(LYN)ELISA Kit 96T
YHB3225Hu Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN)ELISA Kit 48T
201-12-2622 Human V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog(LYN)ELISA Kit 96T
SEG523Hu ELISA Kit for V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN) Homo sapiens (Human) 96T
MA-20123 Mouse Monoclonal Anti-Human v-yes-1 Yamaguchi sarcoma viral related oncogene homolog (LYN) 100 ul
GS-1239a v-yes-1 Yamaguchi sarcoma viral related oncogene homolog primary antibody, Host: Rabbit 200ul
E96523Hu ELISA Kit for V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog (LYN) Organism: Homo sapiens (Human) 96T
CSB-EL013259RA Rat v-yes-1 Yamaguchi sarcoma viral related oncogene homolog (LYN) ELISA kit, Species Rat, Sample Type serum, plasma 96T
MA-20123 Mouse Monoclonal Anti-Human v-yes-1 Yamaguchi sarcoma viral related oncogene homolog (LYN) Species Reactivity: Human 100 ul Product tipe: Antibodies


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur