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P07948 (LYN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 183. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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):
Lck/Yes-related novel protein tyrosine kinase
V-yes-1 Yamaguchi sarcoma viral related oncogene homolog
p53Lyn
p56Lyn
Gene names
Name:LYN
Synonyms:JTK8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Mediates phosphorylation of the BCR-ABL fusion protein. 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.6 Ref.14 Ref.16 Ref.17 Ref.19 Ref.20 Ref.21 Ref.23 Ref.26 Ref.28 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.46 Ref.55

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.7 Ref.8 Ref.20 Ref.21

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.9 Ref.30

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. Interacts with Epstein-Barr virus LMP2A. Interacts with Herpes virus saimiri tyrosine kinase interacting protein (Tip). Ref.6 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.43 Ref.44 Ref.47 Ref.49 Ref.58

Subcellular location

Cell membrane. Nucleus. Cytoplasm. Cytoplasmperinuclear region. Golgi apparatus. 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 plasma membrane occurs in a kinase domain-dependent but kinase activity independent manner and is mediated by exocytic vesicular transport. Detected on plasma membrane lipid rafts. Ref.24 Ref.34 Ref.35 Ref.37

Tissue specificity

Detected in monocytes (at protein level). Detected in placenta, and in fetal brain, lung, liver and kidney. Widely expressed in a variety of organs, tissues, and cell types such as epidermoid, hematopoietic, and neuronal cells. Expressed in primary neuroblastoma tumors. Ref.1 Ref.8

Domain

The protein kinase domain plays an important role in its localization in the cell membrane. Ref.24

Post-translational modification

Ubiquitinated by CBL, leading to its degradation. Ubiquitination is SH3-dependent. Ref.30 Ref.47

Autophosphorylated. Phosphorylated on tyrosine residues in response to KIT signaling. 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.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.34 Ref.35 Ref.39

Involvement in disease

Constitutively phosphorylated and activated in cells from a number of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) patients. Mediates phosphorylation of the BCR-ABL fusion protein. Abnormally elevated expression levels or activation of LYN signaling may play a role in survival and proliferation of some types of cancer cells. Ref.34 Ref.36 Ref.39

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
Host-virus interaction
Immunity
Inflammatory response
Innate immunity
   Cellular componentCell membrane
Cytoplasm
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   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 sequence or structural similarity. Source: UniProtKB

B cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

Fc receptor mediated inhibitory signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

Fc receptor mediated stimulatory signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

JAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cellular response to DNA damage stimulus

Inferred from direct assay Ref.19Ref.20. Source: UniProtKB

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 mutant phenotype PubMed 17910947. Source: BHF-UCL

cytokine secretion

Inferred from electronic annotation. Source: Ensembl

dendritic cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

histamine secretion by mast cell

Inferred from electronic annotation. Source: Ensembl

immune response-regulating cell surface receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred by curator Ref.20. Source: UniProtKB

leukocyte migration

Traceable author statement. Source: Reactome

lipopolysaccharide-mediated signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of B cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.23. Source: UniProtKB

negative regulation of immune response

Traceable author statement Ref.51. Source: UniProtKB

negative regulation of intracellular signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mast cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myeloid leukocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of toll-like receptor 2 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of toll-like receptor 4 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cellular component movement

Inferred from direct assay Ref.28. Source: UniProtKB

positive regulation of dendritic cell apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of mast cell proliferation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

positive regulation of neuron projection development

Inferred from mutant phenotype PubMed 17910947. Source: BHF-UCL

positive regulation of oligodendrocyte progenitor proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of stress-activated protein kinase signaling cascade

Inferred from direct assay Ref.19. Source: UniProtKB

positive regulation of tyrosine phosphorylation of STAT protein

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of B cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of B cell receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion mediated by integrin

Inferred from mutant phenotype Ref.38. Source: UniProtKB

regulation of cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cytokine secretion

Inferred from electronic annotation. Source: Ensembl

regulation of erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

regulation of mast cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mast cell degranulation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of monocyte chemotaxis

Inferred from mutant phenotype Ref.38. Source: UniProtKB

regulation of platelet aggregation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of protein phosphorylation

Traceable author statement Ref.51. Source: UniProtKB

regulation of release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

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 drug

Inferred from electronic annotation. Source: Ensembl

response to hormone

Inferred from sequence or structural similarity. 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 7650013. Source: ProtInc

signal transduction by phosphorylation

Traceable author statement Ref.16. Source: GOC

tolerance induction to self antigen

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine kinase signaling pathway

Inferred from mutant phenotype Ref.23. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.24PubMed 20605918. Source: UniProtKB

alpha2-beta1 integrin complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

mast cell granule

Inferred from electronic annotation. Source: GOC

membrane raft

Inferred from direct assay PubMed 11313396. Source: UniProtKB

mitochondrial crista

Inferred from electronic annotation. Source: Ensembl

mitochondrial intermembrane space

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.37. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 20605918. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.24PubMed 20605918. Source: UniProtKB

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction PubMed 20605918PubMed 20605918. Source: UniProtKB

glycosphingolipid binding

Inferred from electronic annotation. Source: Ensembl

ion channel binding

Inferred from physical interaction PubMed 12538589. Source: BHF-UCL

non-membrane spanning protein tyrosine kinase activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction PubMed 23764002. Source: IntAct

protein tyrosine kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Traceable author statement Ref.16. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07948-1)

Also known as: LYN A; p56lyn;

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: P07948-2)

Also known as: LYN B; p53lyn;

The sequence of this isoform differs from the canonical sequence as follows:
     23-43: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Probable
Chain2 – 512511Tyrosine-protein kinase Lyn
PRO_0000088129

Regions

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

Sites

Active site3671Proton acceptor By similarity
Binding site2751ATP By similarity

Amino acid modifications

Modified residue61Phosphoserine
Modified residue111Phosphoserine Ref.41 Ref.45 Ref.56
Modified residue131Phosphoserine Ref.41 Ref.45 Ref.48 Ref.56
Modified residue301Phosphothreonine
Modified residue321Phosphotyrosine
Modified residue371Phosphothreonine
Modified residue1931Phosphotyrosine Ref.39
Modified residue1941Phosphotyrosine
Modified residue2281Phosphoserine Ref.45
Modified residue2651Phosphotyrosine
Modified residue3061Phosphotyrosine Ref.45
Modified residue3161Phosphotyrosine Ref.45
Modified residue3971Phosphotyrosine; by autocatalysis Ref.9 Ref.35
Modified residue4601Phosphotyrosine Ref.39
Modified residue4731Phosphotyrosine Ref.41 Ref.45
Modified residue4891Phosphothreonine
Modified residue5021Phosphothreonine
Modified residue5081Phosphotyrosine; by autocatalysis, CSK and MATK Ref.9 Ref.11 Ref.27 Ref.35 Ref.41 Ref.45
Lipidation21N-myristoyl glycine Probable
Lipidation31S-palmitoyl cysteine Probable

Natural variations

Alternative sequence23 – 4321Missing in isoform 2.
VSP_005002
Natural variant3851D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.60
VAR_041737

Experimental info

Mutagenesis21G → A: Loss of localization to the cell membrane; when associated with A-3. Ref.37
Mutagenesis31C → A: Loss of localization to the cell membrane; when associated with A-2. Ref.37
Mutagenesis2751K → A: Loss of activity and no effect on localization to the cell membrane. Abundant localization in the nucleus; when associated with A-2 and A-3. Ref.17 Ref.20 Ref.24 Ref.37
Mutagenesis2751K → L or R: Loss of kinase activity. Ref.17 Ref.20 Ref.24 Ref.37
Mutagenesis3461D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-353; A-498 and A-499. Ref.24
Mutagenesis3531E → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-498 and A-499. Ref.24
Mutagenesis3971Y → F: Strongly reduced kinase activity. Ref.30
Mutagenesis4981D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-499. Ref.24
Mutagenesis4991D → A: Impedes the trafficking from the Golgi apparatus toward the cell membrane; when associated with A-346; A-353 and A-498. Ref.24
Mutagenesis5081Y → F: Abolishes autoinhibition and thereby increases kinase activity. Ref.30

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LYN A) (p56lyn) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 408D3D461204E378

FASTA51258,574
        10         20         30         40         50         60 
MGCIKSKGKD SLSDDGVDLK TQPVRNTERT IYVRDPTSNK QQRPVPESQL LPGQRFQTKD 

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

       130        140        150        160        170        180 
LNTLETEEWF FKDITRKDAE RQLLAPGNSA GAFLIRESET LKGSFSLSVR DFDPVHGDVI 

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

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

       310        320        330        340        350        360 
KLVRLYAVVT REEPIYIITE YMAKGSLLDF LKSDEGGKVL LPKLIDFSAQ IAEGMAYIER 

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

       430        440        450        460        470        480 
TIKSDVWSFG ILLYEIVTYG KIPYPGRTNA DVMTALSQGY RMPRVENCPD ELYDIMKMCW 

       490        500        510 
KEKAEERPTF DYLQSVLDDF YTATEGQYQQ QP 

« Hide

Isoform 2 (LYN B) (p53lyn) [UniParc].

Checksum: D74E4074D4B0C92A
Show »

FASTA49156,033

References

« Hide 'large scale' references
[1]"The yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p56lck."
Yamanashi Y., Fukushige S., Semba K., Sukegawa J., Miyajima N., Matsubara K., Yamamoto T., Toyoshima K.
Mol. Cell. Biol. 7:237-243(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"The cDNAs encoding two forms of the LYN protein tyrosine kinase are expressed in rat mast cells and human myeloid cells."
Rider L.G., Raben N., Miller L., Jelsema C.
Gene 138:219-222(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
[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).
[4]"Putative tyrosine kinases expressed in K-562 human leukemia cells."
Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K.
Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
[5]"Expression of the B cell-associated tyrosine kinase gene Lyn in primary neuroblastoma tumours and its modulation during the differentiation of neuroblastoma cell lines."
Bielke W., Ziemiecki A., Kappos L., Miescher G.C.
Biochem. Biophys. Res. Commun. 186:1403-1409(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
[6]"CD19 is a substrate of the antigen receptor-associated protein tyrosine kinase in human B cells."
Roifman C.M., Ke S.
Biochem. Biophys. Res. Commun. 194:222-225(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CD19 PHOSPHORYLATION, INTERACTION WITH CD19.
[7]"Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling."
Yamanashi Y., Okada M., Semba T., Yamori T., Umemori H., Tsunasawa S., Toyoshima K., Kitamura D., Watanabe T., Yamamoto T.
Proc. Natl. Acad. Sci. U.S.A. 90:3631-3635(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, INTERACTION WITH HCLS1.
[8]"Physical and functional association of the high affinity immunoglobulin G receptor (Fc gamma RI) with the kinases Hck and Lyn."
Wang A.V., Scholl P.R., Geha R.S.
J. Exp. Med. 180:1165-1170(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, PHOSPHORYLATION.
[9]"Functional analysis of Csk in signal transduction through the B-cell antigen receptor."
Hata A., Sabe H., Kurosaki T., Takata M., Hanafusa H.
Mol. Cell. Biol. 14:7306-7313(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, ENZYME REGULATION.
[10]"Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases."
Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., Kieff E.
Immunity 2:155-166(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
[11]"Translocation of the Csk homologous kinase (Chk/Hyl) controls activity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulated platelets."
Hirao A., Hamaguchi I., Suda T., Yamaguchi N.
EMBO J. 16:2342-2351(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-508 BY MATK.
Tissue: Platelet.
[12]"Fc gamma receptor type IIb induced recruitment of inositol and protein phosphatases to the signal transductory complex of human B-cell."
Sarmay G., Koncz G., Pecht I., Gergely J.
Immunol. Lett. 57:159-164(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCGR2B.
[13]"Lyn associates with the juxtamembrane region of c-Kit and is activated by stem cell factor in hematopoietic cell lines and normal progenitor cells."
Linnekin D., DeBerry C.S., Mou S.
J. Biol. Chem. 272:27450-27455(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIT, PHOSPHORYLATION.
[14]"Functional interaction between SHPTP1 and the Lyn tyrosine kinase in the apoptotic response to DNA damage."
Yoshida K., Kharbanda S., Kufe D.
J. Biol. Chem. 274:34663-34668(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA DAMAGE RESPONSE; APOPTOSIS AND PHOSPHORYLATION OF PTPN6/SHPTP1, INTERACTION WITH PTPN6/SHPTP1.
[15]"cbl-3: a new mammalian cbl family protein."
Keane M.M., Ettenberg S.A., Nau M.M., Banerjee P., Cuello M., Penninger J., Lipkowitz S.
Oncogene 18:3365-3375(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBLC.
[16]"Substrate recognition by the Lyn protein-tyrosine kinase. NMR structure of the immunoreceptor tyrosine-based activation motif signaling region of the B cell antigen receptor."
Gaul B.S., Harrison M.L., Geahlen R.L., Burton R.A., Post C.B.
J. Biol. Chem. 275:16174-16182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CD79A PHOSPHORYLATION, INTERACTION WITH CD79A.
[17]"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 MAST CELL PROLIFERATION, MUTAGENESIS OF LYS-275.
[18]"Molecular cloning, genomic positioning, promoter identification, and characterization of the novel cyclic AMP-specific phosphodiesterase PDE4A10."
Rena G., Begg F., Ross A., MacKenzie C., McPhee I., Campbell L., Huston E., Sullivan M., Houslay M.D.
Mol. Pharmacol. 59:996-1011(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDE4A.
Tissue: Brain.
[19]"Role for Lyn tyrosine kinase as a regulator of stress-activated protein kinase activity in response to DNA damage."
Yoshida K., Weichselbaum R., Kharbanda S., Kufe D.
Mol. Cell. Biol. 20:5370-5380(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"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: FUNCTION IN DNA DAMAGE RESPONSE; APOPTOSIS AND PHOSPHORYLATION OF PPP1R15A, INTERACTION WITH PPP1R15A, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-275.
[21]"Phosphatidylinositol 3-kinase and Src family kinases are required for phosphorylation and membrane recruitment of Dok-1 in c-Kit signaling."
Liang X., Wisniewski D., Strife A., Shivakrupa R., Clarkson B., Resh M.D.
J. Biol. Chem. 277:13732-13738(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF KIT AND DOK1, CATALYTIC ACTIVITY, INTERACTION WITH KIT.
[22]"DF3/MUC1 signaling in multiple myeloma cells is regulated by interleukin-7."
Li Y., Chen W., Ren J., Yu W.H., Li Q., Yoshida K., Kufe D.
Cancer Biol. Ther. 2:187-193(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MUC1.
[23]"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 THPO-MEDIATED CELL PROLIFERATION.
[24]"Trafficking of Lyn through the Golgi caveolin involves the charged residues on alphaE and alphaI helices in the kinase domain."
Kasahara K., Nakayama Y., Ikeda K., Fukushima Y., Matsuda D., Horimoto S., Yamaguchi N.
J. Cell Biol. 165:641-652(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF LYS-275; ASP-346; GLU-353; ASP-498 AND ASP-499.
[25]"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
Roskoski R. Jr.
Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[26]"Thrombin-induced tyrosine phosphorylation of HS1 in human platelets is sequentially catalyzed by Syk and Lyn tyrosine kinases and associated with the cellular migration of the protein."
Brunati A.M., Deana R., Folda A., Massimino M.L., Marin O., Ledro S., Pinna L.A., Donella-Deana A.
J. Biol. Chem. 280:21029-21035(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF HCLS1.
[27]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Integrin inhibition through Lyn-dependent cross talk from CXCR4 chemokine receptors in normal human CD34+ marrow cells."
Nakata Y., Tomkowicz B., Gewirtz A.M., Ptasznik A.
Blood 107:4234-4239(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[29]"Src family kinases phosphorylate the Bcr-Abl SH3-SH2 region and modulate Bcr-Abl transforming activity."
Meyn M.A. III, Wilson M.B., Abdi F.A., Fahey N., Schiavone A.P., Wu J., Hochrein J.M., Engen J.R., Smithgall T.E.
J. Biol. Chem. 281:30907-30916(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ABL1.
[30]"Csk-binding protein mediates sequential enzymatic down-regulation and degradation of Lyn in erythropoietin-stimulated cells."
Ingley E., Schneider J.R., Payne C.J., McCarthy D.J., Harder K.W., Hibbs M.L., Klinken S.P.
J. Biol. Chem. 281:31920-31929(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAG1, MUTAGENESIS OF TYR-397 AND TYR-508, ENZYME REGULATION, UBIQUITINATION.
[31]"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.
[32]"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.
[33]"TOM1L1 is a Lyn substrate involved in FcepsilonRI signaling in mast cells."
Zhang J., Suzuki K., Hitomi T., Siraganian R.P.
J. Biol. Chem. 282:37669-37677(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TOM1L1, FUNCTION IN TOM1L1 PHOSPHORYLATION.
[34]"A critical role for Lyn in acute myeloid leukemia."
Dos Santos C., Demur C., Bardet V., Prade-Houdellier N., Payrastre B., Recher C.
Blood 111:2269-2279(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND SURVIVAL, PHOSPHORYLATION, SUBCELLULAR LOCATION, ROLE IN DISEASE.
[35]"Oncogenic association of the Cbp/PAG adaptor protein with the Lyn tyrosine kinase in human B-NHL rafts."
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D., van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U., Borisch B., Hoessli D.C.
Blood 111:2310-2320(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-397 AND TYR-508, INTERACTION WITH PAG1 AND STAT3, SUBCELLULAR LOCATION.
[36]"Lyn regulates BCR-ABL and Gab2 tyrosine phosphorylation and c-Cbl protein stability in imatinib-resistant chronic myelogenous leukemia cells."
Wu J., Meng F., Lu H., Kong L., Bornmann W., Peng Z., Talpaz M., Donato N.J.
Blood 111:3821-3829(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CBL AND BCR-ABL, FUNCTION IN PHOSPHORYLATION OF BCR-ABL, ROLE IN DISEASE.
[37]"Nuclear localization of Lyn tyrosine kinase mediated by inhibition of its kinase activity."
Ikeda K., Nakayama Y., Togashi Y., Obata Y., Kuga T., Kasahara K., Fukumoto Y., Yamaguchi N.
Exp. Cell Res. 314:3392-3404(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; CYS-3 AND LYS-275.
[38]"Monocyte migration and LFA-1-mediated attachment to brain microvascular endothelia is regulated by SDF-1 alpha through Lyn kinase."
Malik M., Chen Y.-Y., Kienzle M.F., Tomkowicz B.E., Collman R.G., Ptasznik A.
J. Immunol. 181:4632-4637(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ADHESION AND CELL MIGRATION.
[39]"Association between imatinib-resistant BCR-ABL mutation-negative leukemia and persistent activation of LYN kinase."
Wu J., Meng F., Kong L.Y., Peng Z., Ying Y., Bornmann W.G., Darnay B.G., Lamothe B., Sun H., Talpaz M., Donato N.J.
J. Natl. Cancer Inst. 100:926-939(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-193 AND TYR-460, ROLE IN DISEASE.
[40]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[41]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; TYR-473 AND TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[42]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[43]"Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening."
Voss M., Lettau M., Janssen O.
BMC Immunol. 10:53-53(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FASLG.
[44]"Alternative splicing of ADAM15 regulates its interactions with cellular SH3 proteins."
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.
J. Cell. Biochem. 108:877-885(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAM15.
[45]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; SER-228; TYR-306; TYR-316; TYR-473 AND TYR-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[46]"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580 occurs via a distinct mechanism than other receptor systems."
Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B., Houtman J.C.
J. Leukoc. Biol. 87:691-701(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
[47]"Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2."
Mund T., Pelham H.R.
Proc. Natl. Acad. Sci. U.S.A. 107:11429-11434(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDFIP1 AND NDFIP2, UBIQUITINATION.
[48]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[49]"SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling."
Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.
Mol. Cell. Biol. 31:4550-4562(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCIMP.
[50]"Src-family kinases: rheostats of immune cell signaling."
Lowell C.A.
Mol. Immunol. 41:631-643(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[51]"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.
[52]"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.
[53]"The duplicitous nature of the Lyn tyrosine kinase in growth factor signaling."
Hibbs M.L., Harder K.W.
Growth Factors 24:137-149(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN GROWTH FACTOR SIGNALING.
[54]"New insights on mast cell activation via the high affinity receptor for IgE."
Rivera J., Fierro N.A., Olivera A., Suzuki R.
Adv. Immunol. 98:85-120(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN MAST CELLS.
[55]"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: ROLE IN MYELOID CELL FUNCTION, SIGNALING.
[56]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[57]"Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck."
Schweimer K., Hoffmann S., Bauer F., Friedrich U., Kardinal C., Feller S.M., Biesinger B., Sticht H.
Biochemistry 41:5120-5130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 61-123 IN COMPLEX WITH SAIMIRIINE HERPESVIRUS 2 TYROSINE KINASE INTERACTING PROTEIN.
[58]"Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity."
Bauer F., Schweimer K., Meiselbach H., Hoffmann S., Rosch P., Sticht H.
Protein Sci. 14:2487-2498(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 61-122, INTERACTION WITH HERPESVIRUS TYROSINE KINASE INTERACTING PROTEIN.
[59]"Structural basis for the inhibitor recognition of human Lyn kinase domain."
Miyano N., Kinoshita T., Nakai R., Kirii Y., Yokota K., Tada T.
Bioorg. Med. Chem. Lett. 19:6557-6560(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 233-512 IN COMPLEX WITH STAUROSPORINE.
[60]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-385.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M16038 mRNA. Translation: AAA59540.1.
M79321 mRNA. Translation: AAB50019.1.
BC075001 mRNA. Translation: AAH75001.1.
BC075002 mRNA. Translation: AAH75002.1.
BC126456 mRNA. Translation: AAI26457.1.
BC126458 mRNA. Translation: AAI26459.1.
CCDSCCDS47859.1. [P07948-2]
CCDS6162.1. [P07948-1]
PIRTVHULY. A26719.
RefSeqNP_001104567.1. NM_001111097.2. [P07948-2]
NP_002341.1. NM_002350.3. [P07948-1]
XP_005251290.1. XM_005251233.2. [P07948-1]
UniGeneHs.491767.
Hs.545418.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-123[»]
1WA7NMR-A61-123[»]
3A4OX-ray3.00X233-512[»]
ProteinModelPortalP07948.
SMRP07948. Positions 64-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110245. 169 interactions.
DIPDIP-1056N.
IntActP07948. 51 interactions.
MINTMINT-200655.
STRING9606.ENSP00000376688.

Chemistry

BindingDBP07948.
ChEMBLCHEMBL3905.
GuidetoPHARMACOLOGY2060.

PTM databases

PhosphoSiteP07948.

Polymorphism databases

DMDM125480.

2D gel databases

REPRODUCTION-2DPAGEP07948.

Proteomic databases

MaxQBP07948.
PaxDbP07948.
PRIDEP07948.

Protocols and materials databases

DNASU4067.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000519728; ENSP00000428924; ENSG00000254087. [P07948-1]
ENST00000520220; ENSP00000428424; ENSG00000254087. [P07948-2]
GeneID4067.
KEGGhsa:4067.
UCSCuc003xsk.4. human. [P07948-1]
uc003xsl.4. human. [P07948-2]

Organism-specific databases

CTD4067.
GeneCardsGC08P056792.
HGNCHGNC:6735. LYN.
HPACAB004492.
HPA001231.
MIM165120. gene.
neXtProtNX_P07948.
PharmGKBPA30498.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
KOK05854.
OMAWWRAKSL.
PhylomeDBP07948.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP07948.

Gene expression databases

ArrayExpressP07948.
BgeeP07948.
CleanExHS_LYN.
GenevestigatorP07948.

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

ChiTaRSLYN. human.
EvolutionaryTraceP07948.
GeneWikiLYN.
GenomeRNAi4067.
NextBio15944.
PMAP-CutDBP07948.
PROP07948.
SOURCESearch...

Entry information

Entry nameLYN_HUMAN
AccessionPrimary (citable) accession number: P07948
Secondary accession number(s): A0AVQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM