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P25911 (LYN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase Lyn

EC=2.7.10.2
Alternative name(s):
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene names
Name:Lyn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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'. Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.36 Ref.37 Ref.38 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 Ref.48 Ref.52 Ref.54 Ref.55

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.2 Ref.14 Ref.35 Ref.60

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. Ref.14 Ref.27 Ref.35 Ref.60

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Ref.15 Ref.20 Ref.24 Ref.29 Ref.34 Ref.43 Ref.44 Ref.45 Ref.47 Ref.48 Ref.50 Ref.53

Subcellular location

Cell membrane By similarity. Nucleus By similarity. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. Golgi apparatus By similarity. 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.

Tissue specificity

Detected in bone marrow-derived monocytes (at protein level). Expressed predominantly in B-lymphoid and myeloid cells. Ref.2

Domain

The protein kinase domain plays an important role in its localization in the cell membrane By similarity.

Post-translational modification

Ubiquitinated by CBL, leading to its degradation. Ref.39

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. Ref.2 Ref.5 Ref.14 Ref.18 Ref.27 Ref.35 Ref.43 Ref.60

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. Ref.11 Ref.12 Ref.16 Ref.18 Ref.26 Ref.33 Ref.42

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell homeostasis

Inferred from mutant phenotype Ref.18. Source: UniProtKB

B cell receptor signaling pathway

Inferred from direct assay PubMed 7499277. Source: MGI

Fc receptor mediated inhibitory signaling pathway

Inferred from mutant phenotype Ref.43. Source: UniProtKB

Fc receptor mediated stimulatory signaling pathway

Inferred from mutant phenotype Ref.43. Source: UniProtKB

apoptotic nuclear changes

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to extracellular stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to heat

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cytokine secretion

Inferred from electronic annotation. Source: Ensembl

dendritic cell differentiation

Inferred from mutant phenotype Ref.42. Source: UniProtKB

erythrocyte differentiation

Inferred from mutant phenotype PubMed 10713104. Source: UniProtKB

hemoglobin biosynthetic process

Traceable author statement PubMed 10713104. Source: UniProtKB

hemopoiesis

Inferred from mutant phenotype Ref.33. Source: UniProtKB

histamine secretion by mast cell

Inferred from electronic annotation. Source: Ensembl

immune response-regulating cell surface receptor signaling pathway

Inferred from mutant phenotype Ref.18. Source: UniProtKB

innate immune response

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Inferred from direct assay PubMed 9000133. Source: MGI

lipopolysaccharide-mediated signaling pathway

Inferred from mutant phenotype Ref.55. Source: UniProtKB

negative regulation of B cell proliferation

Inferred from mutant phenotype Ref.18. Source: UniProtKB

negative regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.40Ref.38. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from mutant phenotype Ref.18. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.38Ref.41. Source: UniProtKB

negative regulation of intracellular signal transduction

Inferred from mutant phenotype Ref.40. Source: UniProtKB

negative regulation of mast cell proliferation

Inferred from mutant phenotype Ref.40. Source: UniProtKB

negative regulation of myeloid leukocyte differentiation

Inferred from mutant phenotype Ref.33. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from mutant phenotype Ref.40. Source: UniProtKB

negative regulation of toll-like receptor 2 signaling pathway

Inferred from mutant phenotype Ref.55. Source: UniProtKB

negative regulation of toll-like receptor 4 signaling pathway

Inferred from mutant phenotype Ref.55. Source: UniProtKB

neuron projection development

Inferred from mutant phenotype PubMed 19118221. Source: MGI

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.33. Source: UniProtKB

platelet degranulation

Inferred from mutant phenotype Ref.54. Source: UniProtKB

positive regulation of B cell receptor signaling pathway

Inferred from genetic interaction PubMed 23509253. Source: MGI

positive regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from mutant phenotype Ref.32. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 10713104Ref.32. Source: UniProtKB

positive regulation of dendritic cell apoptotic process

Inferred from mutant phenotype Ref.41. Source: UniProtKB

positive regulation of glial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of oligodendrocyte progenitor proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.44. Source: MGI

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

positive regulation of stress-activated protein kinase signaling cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of tyrosine phosphorylation of STAT protein

Inferred from mutant phenotype PubMed 10713104. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.33. Source: UniProtKB

regulation of B cell apoptotic process

Inferred from mutant phenotype Ref.16. Source: UniProtKB

regulation of B cell receptor signaling pathway

Inferred from mutant phenotype Ref.33. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

regulation of cytokine production

Inferred from mutant phenotype Ref.43. Source: UniProtKB

regulation of cytokine secretion

Inferred from mutant phenotype Ref.55. Source: UniProtKB

regulation of erythrocyte differentiation

Inferred from mutant phenotype Ref.26. Source: UniProtKB

regulation of inflammatory response

Inferred from mutant phenotype Ref.42. Source: UniProtKB

regulation of mast cell activation

Inferred from mutant phenotype Ref.43. Source: UniProtKB

regulation of mast cell degranulation

Inferred from mutant phenotype Ref.43. Source: UniProtKB

regulation of monocyte chemotaxis

Inferred from electronic annotation. Source: Ensembl

regulation of platelet aggregation

Inferred from mutant phenotype Ref.54. Source: UniProtKB

regulation of release of sequestered calcium ion into cytosol

Inferred from genetic interaction PubMed 23509253. Source: MGI

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to carbohydrate

Inferred from electronic annotation. Source: Ensembl

response to hormone

Inferred from direct assay PubMed 10713104. Source: UniProtKB

response to insulin

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to sterol depletion

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 10713104. Source: UniProtKB

tolerance induction to self antigen

Inferred from mutant phenotype Ref.18. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

alpha2-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 10713104. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mast cell granule

Inferred from electronic annotation. Source: GOC

membrane raft

Inferred from electronic annotation. Source: Ensembl

mitochondrial crista

Inferred from electronic annotation. Source: Ensembl

mitochondrial intermembrane space

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 10713104. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.50. Source: MGI

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

SH3 domain binding

Inferred from physical interaction Ref.50. Source: MGI

erythropoietin receptor binding

Traceable author statement PubMed 10713104. Source: UniProtKB

glycosphingolipid binding

Inferred from electronic annotation. Source: Ensembl

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein complex binding

Inferred from physical interaction Ref.50. Source: MGI

protein kinase activity

Inferred from direct assay PubMed 9000133. Source: MGI

protein tyrosine kinase activity

Inferred from direct assay Ref.33. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Hcls1P4971010EBI-643537,EBI-924601
Plcg2Q8CIH52EBI-643537,EBI-617954

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P25911-1)

Also known as: LYN A; p56;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P25911-2)

Also known as: LYN B; p53;

The sequence of this isoform differs from the canonical sequence as follows:
     25-45: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 512511Tyrosine-protein kinase Lyn
PRO_0000088130

Regions

Domain63 – 12361SH3
Domain129 – 22698SH2
Domain247 – 501255Protein kinase
Nucleotide binding253 – 2619ATP Probable

Sites

Active site3671Proton acceptor By similarity
Binding site2751ATP Probable

Amino acid modifications

Modified residue61Phosphoserine By similarity
Modified residue191Phosphoserine Ref.51
Modified residue301Phosphothreonine By similarity
Modified residue321Phosphotyrosine By similarity
Modified residue371Phosphothreonine By similarity
Modified residue1931Phosphotyrosine By similarity
Modified residue1941Phosphotyrosine By similarity
Modified residue2281Phosphoserine By similarity
Modified residue2651Phosphotyrosine By similarity
Modified residue3061Phosphotyrosine By similarity
Modified residue3161Phosphotyrosine By similarity
Modified residue3971Phosphotyrosine; by autocatalysis Ref.27 Ref.43 Ref.51
Modified residue4601Phosphotyrosine By similarity
Modified residue4731Phosphotyrosine By similarity
Modified residue4891Phosphothreonine By similarity
Modified residue5021Phosphothreonine By similarity
Modified residue5081Phosphotyrosine; by autocatalysis, CSK and MATK Ref.27 Ref.49 Ref.51
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence25 – 4521Missing in isoform 2.
VSP_005003

Experimental info

Mutagenesis5081Y → F: Abolishes autoinhibition, leading to increased kinase activity and constitutive phosphorylation of LYN substrates. Ref.33 Ref.35
Sequence conflict771I → F in AAA39471. Ref.2
Sequence conflict771I → F in AAA39472. Ref.2
Sequence conflict1611L → I in AAA39471. Ref.2
Sequence conflict1611L → I in AAA39472. Ref.2
Sequence conflict2791P → L in AAA39471. Ref.2
Sequence conflict2791P → L in AAA39472. Ref.2
Sequence conflict3911V → I in AAA39471. Ref.2
Sequence conflict3911V → I in AAA39472. Ref.2
Sequence conflict4151I → F in AAA40017. Ref.4
Sequence conflict4251D → N in AAA39470. Ref.1
Sequence conflict4321L → P in AAA40017. Ref.4

Secondary structure

.......................................... 512
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LYN A) (p56) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: FDA1D21CC90C50EC

FASTA51258,812
        10         20         30         40         50         60 
MGCIKSKRKD NLNDDEVDSK TQPVRNTDRT IYVRDPTSNK QQRPVPEFHL LPGQRFQTKD 

        70         80         90        100        110        120 
PEEQGDIVVA LYPYDGIHPD DLSFKKGEKM KVLEEHGEWW KAKSLSSKRE GFIPSNYVAK 

       130        140        150        160        170        180 
VNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DYDPMHGDVI 

       190        200        210        220        230        240 
KHYKIRSLDN GGYYISPRIT FPCISDMIKH YQKQSDGLCR RLEKACISPK PQKPWDKDAW 

       250        260        270        280        290        300 
EIPRESIKLV KKLGAGQFGE VWMGYYNNST KVAVKTLKPG TMSVQAFLEE ANLMKTLQHD 

       310        320        330        340        350        360 
KLVRLYAVVT KEEPIYIITE FMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ IAEGMAYIER 

       370        380        390        400        410        420 
KNYIHRDLRA ANVLVSESLM CKIADFGLAR VIEDNEYTAR EGAKFPIKWT APEAINFGCF 

       430        440        450        460        470        480 
TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMSALSQGY RMPRMENCPD ELYDIMKMCW 

       490        500        510 
KEKAEERPTF DYLQSVLDDF YTATEGQYQQ QP 

« Hide

Isoform 2 (LYN B) (p53) [UniParc].

Checksum: 2C82015D510B1F59
Show »

FASTA49156,285

References

« Hide 'large scale' references
[1]"Alternatively spliced murine lyn mRNAs encode distinct proteins."
Stanley E., Ralph S.J., McEwen S., Boulet I., Holtzman D.A., Lock P., Dunn A.R.
Mol. Cell. Biol. 11:3399-3406(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
[2]"Hematopoietic cells express two forms of lyn kinase differing by 21 amino acids in the amino terminus."
Yi T., Bolen J.B., Ihle J.N.
Mol. Cell. Biol. 11:2391-2398(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, TISSUE SPECIFICITY.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Czech II.
Tissue: Mammary gland.
[4]"The application of the polymerase chain reaction to cloning members of the protein tyrosine kinase family."
Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.
Gene 85:67-74(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 364-432.
[5]"Association of B cell antigen receptor with protein tyrosine kinase Lyn."
Yamanashi Y., Kakiuchi T., Mizuguchi J., Yamamoto T., Toyoshima K.
Science 251:192-194(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH B CELL RECEPTOR, AUTOPHOSPHORYLATION.
[6]"Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity."
Clark M.R., Johnson S.A., Cambier J.C.
EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD79A.
[7]"B-cell antigen receptor motifs have redundant signalling capabilities and bind the tyrosine kinases PTK72, Lyn and Fyn."
Law D.A., Chan V.W., Datta S.K., DeFranco A.L.
Curr. Biol. 3:645-657(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD79A AND CD79B, FUNCTION IN PHOSPHORYLATION OF CD79A AND CD79B.
[8]"Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling."
Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T., Yamamoto T., Yamamura H.
J. Exp. Med. 179:1725-1729(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYK PHOSPHORYLATION.
[9]"Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha."
Pleiman C.M., Abrams C., Gauen L.T., Bedzyk W., Jongstra J., Shaw A.S., Cambier J.C.
Proc. Natl. Acad. Sci. U.S.A. 91:4268-4272(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD79A.
[10]"Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit."
Pleiman C.M., Hertz W.M., Cambier J.C.
Science 263:1609-1612(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PIK3R1 ACTIVATION, INTERACTION WITH PIK3R1.
[11]"Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease."
Hibbs M.L., Tarlinton D.M., Armes J., Grail D., Hodgson G., Maglitto R., Stacker S.A., Dunn A.R.
Cell 83:301-311(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[12]"Impaired proliferation of peripheral B cells and indication of autoimmune disease in lyn-deficient mice."
Nishizumi H., Taniuchi I., Yamanashi Y., Kitamura D., Ilic D., Mori S., Watanabe T., Yamamoto T.
Immunity 3:549-560(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN B CELLS AND IN PHOSPHORYLATION OF CBL AND HCLS1.
[13]"Tyrosine phosphorylation and translocation of the c-cbl protein after activation of tyrosine kinase signaling pathways."
Tanaka S., Neff L., Baron R., Levy J.B.
J. Biol. Chem. 270:14347-14351(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL.
[14]"Autophosphorylation induces autoactivation and a decrease in the Src homology 2 domain accessibility of the Lyn protein kinase."
Sotirellis N., Johnson T.M., Hibbs M.L., Stanley I.J., Stanley E., Dunn A.R., Cheng H.C.
J. Biol. Chem. 270:29773-29780(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION.
[15]"Tec protein-tyrosine kinase is an effector molecule of Lyn protein-tyrosine kinase."
Mano H., Yamashita Y., Miyazato A., Miura Y., Ozawa K.
FASEB J. 10:637-642(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TEC PHOSPHORYLATION, INTERACTION WITH TEC.
[16]"Altered antigen receptor signaling and impaired Fas-mediated apoptosis of B cells in Lyn-deficient mice."
Wang J., Koizumi T., Watanabe T.
J. Exp. Med. 184:831-838(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[17]"Activation of BTK by a phosphorylation mechanism initiated by SRC family kinases."
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.
Science 271:822-825(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF BTK.
[18]"Characterization of the B lymphocyte populations in Lyn-deficient mice and the role of Lyn in signal initiation and down-regulation."
Chan V.W., Meng F., Soriano P., DeFranco A.L., Lowell C.A.
Immunity 7:69-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, ALTERNATIVE SPLICING, PHOSPHORYLATION.
[19]"Impaired tyrosine phosphorylation and Ca2+ mobilization, but not degranulation, in lyn-deficient bone marrow-derived mast cells."
Nishizumi H., Yamamoto T.
J. Immunol. 158:2350-2355(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAST CELLS AND IN SIGNALING DOWN-STREAM OF FCER1.
[20]"Lyn physically associates with the erythropoietin receptor and may play a role in activation of the Stat5 pathway."
Chin H., Arai A., Wakao H., Kamiyama R., Miyasaka N., Miura O.
Blood 91:3734-3745(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPOR AND JAK2, FUNCTION.
[21]"Defective negative regulation of antigen receptor signaling in Lyn-deficient B lymphocytes."
Chan V.W., Lowell C.A., DeFranco A.L.
Curr. Biol. 8:545-553(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION AND ACTIVATION OF MAPK1/ERK2; MAPK8/JNK1 AND MAPK9/JNK2.
[22]"Inhibition of the B cell by CD22: a requirement for Lyn."
Smith K.G., Tarlinton D.M., Doody G.M., Hibbs M.L., Fearon D.T.
J. Exp. Med. 187:807-811(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CD22 PHOSPHORYLATION.
[23]"A double-edged kinase Lyn: a positive and negative regulator for antigen receptor-mediated signals."
Nishizumi H., Horikawa K., Mlinaric-Rascan I., Yamamoto T.
J. Exp. Med. 187:1343-1348(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FCGR2 AND CD22 PHOSPHORYLATION.
[24]"Fc epsilon receptor I-associated lyn-dependent phosphorylation of Fc gamma receptor IIB during negative regulation of mast cell activation."
Malbec O., Fong D.C., Turner M., Tybulewicz V.L., Cambier J.C., Fridman W.H., Daeron M.
J. Immunol. 160:1647-1658(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FCGR2 PHOSPHORYLATION, INTERACTION WITH FCGR2.
[25]"The B cell surface protein CD72 recruits the tyrosine phosphatase SHP-1 upon tyrosine phosphorylation."
Adachi T., Flaswinkel H., Yakura H., Reth M., Tsubata T.
J. Immunol. 160:4662-4665(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CD72 PHOSPHORYLATION.
[26]"Regulation of B-1 cell activation and its autoantibody production by Lyn kinase-regulated signallings."
Ochi H., Takeshita H., Suda T., Nisitani S., Honjo T., Watanabe T.
Immunology 98:595-603(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN ERYTHROPOIESIS.
[27]"CD45 negatively regulates lyn activity by dephosphorylating both positive and negative regulatory tyrosine residues in immature B cells."
Katagiri T., Ogimoto M., Hasegawa K., Arimura Y., Mitomo K., Okada M., Clark M.R., Mizuno K., Yakura H.
J. Immunol. 163:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, DEPHOSPHORYLATION BY PTPRC/CD45, ENZYME REGULATION.
[28]"Paired immunoglobulin-like receptor B (PIR-B) inhibits BCR-induced activation of Syk and Btk by SHP-1."
Maeda A., Scharenberg A.M., Tsukada S., Bolen J.B., Kinet J.P., Kurosaki T.
Oncogene 18:2291-2297(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF LILRB3/PIR-B.
[29]"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."
Dahl M.E., Arai K.I., Watanabe S.
Genes Cells 5:143-153(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF CSF2RB, INTERACTION WITH CSF2RB.
[30]"Role of the rasGAP-associated docking protein p62(dok) in negative regulation of B cell receptor-mediated signaling."
Yamanashi Y., Tamura T., Kanamori T., Yamane H., Nariuchi H., Yamamoto T., Baltimore D.
Genes Dev. 14:11-16(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF DOK1.
[31]"Negative regulation of B cell receptor-mediated signaling in B-1 cells through CD5 and Ly49 co-receptors via Lyn kinase activity."
Ochi H., Watanabe T.
Int. Immunol. 12:1417-1423(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CD5 PHOSPHORYLATION.
[32]"Lyn is required for normal stem cell factor-induced proliferation and chemotaxis of primary hematopoietic cells."
O'Laughlin-Bunner B., Radosevic N., Taylor M.L., Shivakrupa R., DeBerry C., Metcalfe D.D., Zhou M., Lowell C., Linnekin D.
Blood 98:343-350(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF CELL PROLIFERATION AND MIGRATION IN RESPONSE TO KITLG.
[33]"Gain- and loss-of-function Lyn mutant mice define a critical inhibitory role for Lyn in the myeloid lineage."
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.
Immunity 15:603-615(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN PHOSPHORYLATION AND ACTIVATION OF SIRPA; PTPN6/SHP-1; PTPN11/SHP-2 AND INPP5D/SHIP-1, MUTAGENESIS OF TYR-508.
[34]"Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis."
Grishin A.V., Azhipa O., Semenov I., Corey S.J.
Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPP1R15A.
[35]"Sustained activation of Lyn tyrosine kinase in vivo leads to autoimmunity."
Hibbs M.L., Harder K.W., Armes J., Kountouri N., Quilici C., Casagranda F., Dunn A.R., Tarlinton D.M.
J. Exp. Med. 196:1593-1604(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IN REGULATION OF IMMUNE RESPONSE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, MUTAGENESIS OF TYR-508.
[36]"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."
Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.
J. Biol. Chem. 277:31703-31714(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATING SYK.
[37]"The Lyn tyrosine kinase negatively regulates neutrophil integrin signaling."
Pereira S., Lowell C.
J. Immunol. 171:1319-1327(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[38]"Lyn tyrosine kinase regulates thrombopoietin-induced proliferation of hematopoietic cell lines and primary megakaryocytic progenitors."
Lannutti B.J., Drachman J.G.
Blood 103:3736-3743(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DOWN-REGULATION OF THPO-MEDIATED CELL PROLIFERATION AND IN DOWN-REGULATION OF MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
[39]"Differential regulation of the B cell receptor-mediated signaling by the E3 ubiquitin ligase Cbl."
Shao Y., Yang C., Elly C., Liu Y.C.
J. Biol. Chem. 279:43646-43653(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[40]"The Src kinase Lyn is a negative regulator of mast cell proliferation."
Hernandez-Hansen V., Mackay G.A., Lowell C.A., Wilson B.S., Oliver J.M.
J. Leukoc. Biol. 75:143-151(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MAST CELL PROLIFERATION AND IN DOWN-REGULATION OF AKT1; MAPK1/ERK2 AND MAPK3/ERK1 ACTIVATION.
[41]"The Lyn tyrosine kinase differentially regulates dendritic cell generation and maturation."
Chu C.L., Lowell C.A.
J. Immunol. 175:2880-2889(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS NEGATIVE REGULATOR OF DENDRITIC CELL DIFFERENTIATION; PROLIFERATION AND SURVIVAL.
[42]"Lyn-deficient mice develop severe, persistent asthma: Lyn is a critical negative regulator of Th2 immunity."
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.
J. Immunol. 175:1867-1875(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION IN MATURATION OF DENDRITIC CELLS AND IN INFLAMMATORY RESPONSE.
[43]"Positive and negative regulation of mast cell activation by Lyn via the FcepsilonRI."
Xiao W., Nishimoto H., Hong H., Kitaura J., Nunomura S., Maeda-Yamamoto M., Kawakami Y., Lowell C.A., Ra C., Kawakami T.
J. Immunol. 175:6885-6892(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, INTERACTION WITH MS4A2/FCER1B.
[44]"LIME acts as a transmembrane adapter mediating BCR-dependent B-cell activation."
Ahn E., Lee H., Yun Y.
Blood 107:1521-1527(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LIME1, FUNCTION IN PHOSPHORYLATION OF LIME1.
[45]"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."
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S., Ronnstrand L.
Blood 108:1542-1550(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FLT3.
[46]"Fer and Fps/Fes participate in a Lyn-dependent pathway from FcepsilonRI to platelet-endothelial cell adhesion molecule 1 to limit mast cell activation."
Udell C.M., Samayawardhena L.A., Kawakami Y., Kawakami T., Craig A.W.
J. Biol. Chem. 281:20949-20957(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[47]"Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets."
Rathore V.B., Okada M., Newman P.J., Newman D.K.
Biochem. J. 403:275-281(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[48]"Leupaxin negatively regulates B cell receptor signaling."
Chew V., Lam K.P.
J. Biol. Chem. 282:27181-27191(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF LPXN, INTERACTION WITH LPXN.
[49]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[50]"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
Samuels A.L., Klinken S.P., Ingley E.
Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ANKRD54.
[51]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; TYR-397 AND TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[52]"Erythropoietin down-regulates stem cell factor receptor (Kit) expression in the leukemic proerythroblast: role of Lyn kinase."
Kosmider O., Buet D., Gallais I., Denis N., Moreau-Gachelin F.
PLoS ONE 4:E5721-E5721(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[53]"Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THEMIS2.
[54]"An important role of the SRC family kinase Lyn in stimulating platelet granule secretion."
Li Z., Zhang G., Liu J., Stojanovic A., Ruan C., Lowell C.A., Du X.
J. Biol. Chem. 285:12559-12570(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PLATELET GRANULE SECRETION AND PLATELET AGGREGATION.
[55]"Activation of murine macrophages via TLR2 and TLR4 is negatively regulated by a Lyn/PI3K module and promoted by SHIP1."
Keck S., Freudenberg M., Huber M.
J. Immunol. 184:5809-5818(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DOWN-REGULATION OF TLR2 AND TLR4 SIGNALING; CYTOKINE RELEASE AND THE INFLAMMATORY RESPONSE TO LIPOPOLYSACCHARIDE.
[56]"Src-family kinases in B-cell development and signaling."
Gauld S.B., Cambier J.C.
Oncogene 23:8001-8006(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN B CELLS.
[57]"Lyn tyrosine kinase: accentuating the positive and the negative."
Xu Y., Harder K.W., Huntington N.D., Hibbs M.L., Tarlinton D.M.
Immunity 22:9-18(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN B CELLS.
[58]"Src-family kinases: rheostats of immune cell signaling."
Lowell C.A.
Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[59]"Multiple roles of Lyn kinase in myeloid cell signaling and function."
Scapini P., Pereira S., Zhang H., Lowell C.A.
Immunol. Rev. 228:23-40(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[60]"Crystal structures of the Lyn protein tyrosine kinase domain in its Apo- and inhibitor-bound state."
Williams N.K., Lucet I.S., Klinken S.P., Ingley E., Rossjohn J.
J. Biol. Chem. 284:284-291(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 239-512 IN COMPLEXES WITH DASATINIB; PP2 AND AMP-PNP, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64608 mRNA. Translation: AAA39470.1.
M57696 mRNA. Translation: AAA39471.1.
M57697 mRNA. Translation: AAA39472.1.
BC031547 mRNA. Translation: AAH31547.1.
M33426 mRNA. Translation: AAA40017.1.
PIRA39719.
RefSeqNP_001104566.1. NM_001111096.1.
UniGeneMm.317331.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZV7X-ray2.50A239-512[»]
2ZV8X-ray2.70A239-512[»]
2ZV9X-ray2.76A239-512[»]
2ZVAX-ray2.60A239-512[»]
ProteinModelPortalP25911.
SMRP25911. Positions 64-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201256. 10 interactions.
DIPDIP-37806N.
IntActP25911. 13 interactions.
MINTMINT-100482.

Chemistry

ChEMBLCHEMBL2258.

PTM databases

PhosphoSiteP25911.

Proteomic databases

PaxDbP25911.
PRIDEP25911.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041377; ENSMUSP00000038838; ENSMUSG00000042228. [P25911-1]
ENSMUST00000103010; ENSMUSP00000100075; ENSMUSG00000042228. [P25911-2]
GeneID17096.
KEGGmmu:17096.
UCSCuc008rwm.2. mouse. [P25911-1]

Organism-specific databases

CTD4067.
MGIMGI:96892. Lyn.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP25911.
KOK05854.
OMAISSMIKH.
OrthoDBEOG7GTT2V.
PhylomeDBP25911.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_188257. Signal Transduction.
REACT_98458. Immune System.

Gene expression databases

ArrayExpressP25911.
BgeeP25911.
GenevestigatorP25911.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25911.
NextBio291240.
PROP25911.
SOURCESearch...

Entry information

Entry nameLYN_MOUSE
AccessionPrimary (citable) accession number: P25911
Secondary accession number(s): Q62127
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot