LYN information

LYN
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1W1F, 1WA7, 3A4O
Identifiers
Aliases	LYN, LYN proto-oncogene, Src family tyrosine kinase, JTK8, p53Lyn, p56Lyn
External IDs	OMIM: 165120 MGI: 96892 HomoloGene: 55649 GeneCards: LYN
Gene location (Human)
Chr.	Chromosome 8 (human)
End	56,014,169 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	3,813,122 bp
RNA expression pattern
	Top expressed in
	monocyte; ; blood; ; palpebral conjunctiva; ; bone marrow; ; bone marrow cells; ; appendix; ; periodontal fiber; ; trabecular bone; ; pancreatic ductal cell; ; spleen;
	Top expressed in
	blood; ; spleen; ; right lung lobe; ; left lung; ; left lung lobe; ; submandibular gland; ; conjunctival fornix; ; lacrimal gland; ; jejunum; ; epithelium of stomach;
	More reference expression data
	n/a
Gene ontology
Molecular function	transmembrane transporter binding; SH3 domain binding; protein-containing complex binding; kinase activity; gamma-tubulin binding; signaling receptor binding; ATP binding; protein kinase activity; non-membrane spanning protein tyrosine kinase activity; enzyme binding; transferase activity; platelet-derived growth factor receptor binding; integrin binding; protein binding; glycosphingolipid binding; protein tyrosine kinase activity; nucleotide binding; phosphoprotein binding; ubiquitin protein ligase binding; ephrin receptor binding; phosphorylation-dependent protein binding;
Cellular component	cytoplasm; cytosol; membrane; extrinsic component of cytoplasmic side of plasma membrane; mitochondrial intermembrane space; perinuclear region of cytoplasm; nucleus; mitochondrial membranes; membrane raft; extracellular exosome; Golgi apparatus; plasma membrane; postsynaptic density; mast cell granule; integrin alpha2-beta1 complex; mitochondrial crista; intracellular membrane-bounded organelle; glutamatergic synapse; postsynaptic specialization, intracellular component;
Biological process	regulation of protein phosphorylation; cellular response to extracellular stimulus; cellular response to retinoic acid; positive regulation of B cell receptor signaling pathway; tolerance induction to self antigen; regulation of mast cell activation; regulation of cell adhesion mediated by integrin; cellular response to heat; response to amino acid; hemopoiesis; adaptive immune response; regulation of erythrocyte differentiation; cellular response to DNA damage stimulus; positive regulation of Fc receptor mediated stimulatory signaling pathway; platelet activation; Fc-epsilon receptor signaling pathway; protein phosphorylation; regulation of B cell apoptotic process; positive regulation of dendritic cell apoptotic process; positive regulation of glial cell proliferation; response to carbohydrate; regulation of platelet aggregation; negative regulation of cell population proliferation; B cell receptor signaling pathway; negative regulation of myeloid leukocyte differentiation; dendritic cell differentiation; Fc receptor mediated inhibitory signaling pathway; Fc-gamma receptor signaling pathway involved in phagocytosis; transmembrane receptor protein tyrosine kinase signaling pathway; regulation of B cell receptor signaling pathway; stimulatory C-type lectin receptor signaling pathway; response to sterol depletion; positive regulation of stress-activated protein kinase signaling cascade; regulation of cytokine production; response to insulin; positive regulation of mast cell proliferation; negative regulation of MAP kinase activity; regulation of ERK1 and ERK2 cascade; positive regulation of peptidyl-tyrosine phosphorylation; erythrocyte differentiation; protein autophosphorylation; oligodendrocyte development; regulation of mast cell degranulation; positive regulation of phosphorylation; viral process; response to toxic substance; negative regulation of protein phosphorylation; Fc receptor mediated stimulatory signaling pathway; growth hormone receptor signaling pathway via JAK-STAT; phosphorylation; immune system process; regulation of release of sequestered calcium ion into cytosol; positive regulation of tyrosine phosphorylation of STAT protein; B cell homeostasis; immune response-regulating cell surface receptor signaling pathway; response to axon injury; negative regulation of mast cell proliferation; regulation of inflammatory response; peptidyl-tyrosine autophosphorylation; response to hormone; regulation of monocyte chemotaxis; leukocyte migration; lipopolysaccharide-mediated signaling pathway; histamine secretion by mast cell; intracellular signal transduction; response to organic cyclic compound; negative regulation of intracellular signal transduction; positive regulation of cell migration; ephrin receptor signaling pathway; negative regulation of toll-like receptor 2 signaling pathway; T cell costimulation; response to peptide hormone; platelet degranulation; blood coagulation; positive regulation of phosphatidylinositol 3-kinase activity; positive regulation of oligodendrocyte progenitor proliferation; negative regulation of immune response; positive regulation of cell population proliferation; positive regulation of neuron projection development; negative regulation of ERK1 and ERK2 cascade; peptidyl-tyrosine phosphorylation; negative regulation of B cell proliferation; negative regulation of toll-like receptor 4 signaling pathway; signal transduction; innate immune response; neuron projection development; central nervous system development; inflammatory response; positive regulation of protein phosphorylation; positive regulation of phosphatidylinositol 3-kinase signaling; cell differentiation; positive regulation of Ras protein signal transduction; positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process;
	Sources:Amigo / QuickGO
Orthologs
	4067
	17096
	ENSG00000254087
	ENSMUSG00000042228
	P07948
	P25911
	NM_001111097; NM_002350
	NM_001111096; NM_010747
	NP_001104567; NP_002341
	NP_001104566; NP_034877
	Wikidata
View/Edit Human	View/Edit Mouse

Tyrosine-protein kinase Lyn is a protein that in humans is encoded by the LYN gene.^[5]

Lyn is a member of the Src family of protein tyrosine kinases, which is mainly expressed in hematopoietic cells,^[6] in neural tissues^[7] liver, and adipose tissue.^[8] In various hematopoietic cells, Lyn has emerged as a key enzyme involved in the regulation of cell activation. In these cells, a small amount of LYN is associated with cell surface receptor proteins, including the B cell antigen receptor (BCR),^[9]^[10] CD40,^[11] or CD19.^[12] The abbreviation Lyn is derived from Lck/Yes novel tyrosine kinase, Lck and Yes also being members of the Src kinase family.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000254087 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000042228 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Yamanashi Y, Fukushige S, Semba K, Sukegawa J, Miyajima N, Matsubara K, Yamamoto T, Toyoshima K (Jan 1987). "The yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p56lck". Molecular and Cellular Biology. 7 (1): 237–43. doi:10.1128/MCB.7.1.237. PMC 365062. PMID 3561390.
^ Yamanashi Y, Mori S, Yoshida M, Kishimoto T, Inoue K, Yamamoto T, Toyoshima K (Sep 1989). "Selective expression of a protein-tyrosine kinase, p56lyn, in hematopoietic cells and association with production of human T-cell lymphotropic virus type I". Proceedings of the National Academy of Sciences of the United States of America. 86 (17): 6538–42. Bibcode:1989PNAS...86.6538Y. doi:10.1073/pnas.86.17.6538. PMC 297879. PMID 2505253.
^ Umemori H, Wanaka A, Kato H, Takeuchi M, Tohyama M, Yamamoto T (Dec 1992). "Specific expressions of Fyn and Lyn, lymphocyte antigen receptor-associated tyrosine kinases, in the central nervous system". Brain Research. Molecular Brain Research. 16 (3–4): 303–10. doi:10.1016/0169-328X(92)90239-8. PMID 1337939.
^ Yamada E, Pessin JE, Kurland IJ, Schwartz GJ, Bastie CC (Feb 2010). "Fyn-dependent regulation of energy expenditure and body weight is mediated by tyrosine phosphorylation of LKB1". Cell Metabolism. 11 (2): 113–124. doi:10.1016/j.cmet.2009.12.010. PMC 2830006. PMID 20142099.
^ Yamamoto T, Yamanashi Y, Toyoshima K (Apr 1993). "Association of Src-family kinase Lyn with B-cell antigen receptor". Immunological Reviews. 132: 187–206. doi:10.1111/j.1600-065X.1993.tb00843.x. PMID 8349296. S2CID 10782326.
^ Campbell MA, Sefton BM (May 1992). "Association between B-lymphocyte membrane immunoglobulin and multiple members of the Src family of protein tyrosine kinases". Molecular and Cellular Biology. 12 (5): 2315–21. doi:10.1128/MCB.12.5.2315. PMC 364403. PMID 1569953.
^ Ren CL, Morio T, Fu SM, Geha RS (Feb 1994). "Signal transduction via CD40 involves activation of lyn kinase and phosphatidylinositol-3-kinase, and phosphorylation of phospholipase C gamma 2". The Journal of Experimental Medicine. 179 (2): 673–80. doi:10.1084/jem.179.2.673. PMC 2191357. PMID 7507510.
^ Campbell 1999

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000254087 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000042228 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid3561390-5] Yamanashi Y, Fukushige S, Semba K, Sukegawa J, Miyajima N, Matsubara K, Yamamoto T, Toyoshima K (Jan 1987). "The yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p56lck". Molecular and Cellular Biology. 7 (1): 237–43. doi:10.1128/MCB.7.1.237. PMC 365062. PMID 3561390.

[6] Yamanashi Y, Mori S, Yoshida M, Kishimoto T, Inoue K, Yamamoto T, Toyoshima K (Sep 1989). "Selective expression of a protein-tyrosine kinase, p56lyn, in hematopoietic cells and association with production of human T-cell lymphotropic virus type I". Proceedings of the National Academy of Sciences of the United States of America. 86 (17): 6538–42. Bibcode:1989PNAS...86.6538Y. doi:10.1073/pnas.86.17.6538. PMC 297879. PMID 2505253.

[7] Umemori H, Wanaka A, Kato H, Takeuchi M, Tohyama M, Yamamoto T (Dec 1992). "Specific expressions of Fyn and Lyn, lymphocyte antigen receptor-associated tyrosine kinases, in the central nervous system". Brain Research. Molecular Brain Research. 16 (3–4): 303–10. doi:10.1016/0169-328X(92)90239-8. PMID 1337939.

[8] Yamada E, Pessin JE, Kurland IJ, Schwartz GJ, Bastie CC (Feb 2010). "Fyn-dependent regulation of energy expenditure and body weight is mediated by tyrosine phosphorylation of LKB1". Cell Metabolism. 11 (2): 113–124. doi:10.1016/j.cmet.2009.12.010. PMC 2830006. PMID 20142099.

[9] Yamamoto T, Yamanashi Y, Toyoshima K (Apr 1993). "Association of Src-family kinase Lyn with B-cell antigen receptor". Immunological Reviews. 132: 187–206. doi:10.1111/j.1600-065X.1993.tb00843.x. PMID 8349296. S2CID 10782326.

[10] Campbell MA, Sefton BM (May 1992). "Association between B-lymphocyte membrane immunoglobulin and multiple members of the Src family of protein tyrosine kinases". Molecular and Cellular Biology. 12 (5): 2315–21. doi:10.1128/MCB.12.5.2315. PMC 364403. PMID 1569953.

[11] Ren CL, Morio T, Fu SM, Geha RS (Feb 1994). "Signal transduction via CD40 involves activation of lyn kinase and phosphatidylinositol-3-kinase, and phosphorylation of phospholipase C gamma 2". The Journal of Experimental Medicine. 179 (2): 673–80. doi:10.1084/jem.179.2.673. PMC 2191357. PMID 7507510.

[Campbell-12] Campbell 1999

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