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Reviewed, UniProtKB/Swiss-Prot P07948 (LYN_HUMAN)

Last modified June 16, 2009. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tyrosine-protein kinase Lyn
    EC=2.7.10.2
Gene names
Name: LYN
OrganismHomo sapiens (Human)
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)

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subunit structure

Interacts with phosphorylated LIME1 and with CD79A upon BCR activation. Interacts with Epstein-Barr virus LMP2A. Interacts with TGFB1I1. 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 PPP1R15A via the SH3 domain. Ref.6 Ref.7 Ref.8 Ref.11

Tissue specificity

Expressed in primary neuroblastoma tumors.

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 processHost-virus interaction
   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
   Technical term3D-structure
Gene Ontology (GO)
   Biological processerythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

interspecies interaction between organisms

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of tyrosine phosphorylation of STAT protein

Inferred from sequence or structural similarity. Source: UniProtKB

protein amino acid phosphorylation Ref.1

Traceable author statement. Source: ProtInc

response to hormone stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement. Source: ProtInc

   Cellular componentGolgi apparatus

Inferred from direct assay. Source: HPA

membrane raft

Inferred from direct assay. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: EC

protein binding

Inferred from physical interaction. Source: UniProtKB

receptor signaling protein tyrosine kinase activity

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

O929722EBI-79452,EBI-710506From a different organism.
P266601EBI-79452,EBI-706322From a different organism.
P279585EBI-79452,EBI-706378From a different organism.
Q9WMX22EBI-79452,EBI-710918From a different organism.
Arap3Q8R5G72EBI-79452,EBI-621463From a different organism.
Asap1Q9QWY8-11EBI-79452,EBI-698517From a different organism.
Asap1Q9QWY8-21EBI-79452,EBI-698524From a different organism.
CD22P202731EBI-79452,EBI-78277
CDK4P118021EBI-79452,EBI-295644
CDKN1BP465272EBI-79452,EBI-519280
CSNK2BP678701EBI-79452,EBI-348169
GP6Q9HCN62EBI-79452,EBI-515278
KHDRBS1Q076661EBI-79452,EBI-1364
Sphk1Q8CI151EBI-79452,EBI-985291From a different organism.
SPHK2Q9NRA01EBI-79452,EBI-985324
Sphk2Q9JIA71EBI-79452,EBI-985434From a different organism.

Alternative products

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

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 LYN B (identifier: P07948-2)

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 By similarity
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 residue111Phosphoserine Ref.10 Ref.15 Ref.16
Modified residue131Phosphoserine Ref.15 Ref.16 Ref.13 Ref.14
Modified residue321Phosphotyrosine Ref.15
Modified residue1931Phosphotyrosine Ref.12
Modified residue1941Phosphotyrosine Ref.15 Ref.12
Modified residue2281Phosphoserine Ref.15
Modified residue3061Phosphotyrosine Ref.12
Modified residue3971Phosphotyrosine; by autocatalysis By similarity
Modified residue4731Phosphotyrosine Ref.15 Ref.12
Modified residue5081Phosphotyrosine Ref.10 Ref.15 Ref.12 Ref.9
Lipidation21N-myristoyl glycine By similarity
Lipidation31S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence23 – 4321Missing in isoform LYN B.
VSP_005002
Natural variant3851D → Y in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.17
VAR_041737

Secondary structure

.............. 512
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform LYN A [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 LYN B.

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: 3561390] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 8125304] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LYN A).
[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: 2247464] [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: 1510669] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
[6]"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: 7895172] [Abstract]
Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
[7]"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: 11517336] [Abstract]
Cited for: INTERACTION WITH PPP1R15A.
[8]"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: 12750561] [Abstract]
Cited for: INTERACTION WITH MUC1.
[9]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, MASS SPECTROMETRY.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND TYR-508, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"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: 17233630] [Abstract]
Cited for: INTERACTION WITH TGFB1I1.
[12]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193; TYR-194; TYR-306; TYR-397; TYR-473 AND TYR-508, MASS SPECTROMETRY.
[13]"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry."
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.
Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, MASS SPECTROMETRY.
[14]"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: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-397, MASS SPECTROMETRY.
Tissue: Platelet.
[15]"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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-13; TYR-32; TYR-194; SER-228; TYR-397; TYR-473 AND TYR-508, MASS SPECTROMETRY.
[16]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, MASS SPECTROMETRY.
[17]"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: 17344846] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TYR-385.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00298625.
IPI00432416.
PIRTVHULY. A26719.
RefSeqNP_002341.1.
UniGeneHs.699154

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1W1FNMR-A61-122[»]
1WA7NMR-A61-123[»]
SMRP07948. Positions 67-512.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:1056N.
IntActP07948. 26 interactions.

PTM databases

PhosphoSiteP07948.

2-D gel databases

REPRODUCTION-2DPAGEP07948.

Proteomic databases

PRIDEP07948.

Genome annotation databases

EnsemblENSG00000147507. Homo sapiens. [Contig view]
GeneID4067.

Organism-specific databases

GeneCardsGC08P056954.
H-InvDBHIX0025560.
HGNCHGNC:6735. LYN.
HPACAB004492.
HPA001231.
MIM165120. gene.
PharmGKBPA30498.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP07948.

Enzyme and pathway databases

BRENDA2.7.10.2. 247.
Pathway_Interaction_DBalphasynuclein_pathway. Alpha-synuclein signaling.
amb2_neutrophils_pathway. amb2 Integrin signaling.
bcr_5pathway. BCR signaling pathway.
pi3kcipathway. Class I PI3K signaling events.
epha_fwdpathway. EPHA forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
epopathway. EPO signaling pathway.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.
glypican_1pathway. Glypican 1 network.
lysophospholipid_pathway. LPA receptor mediated events.
pdgfrbpathway. PDGFR-beta signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
ptp1bpathway. Signaling events mediated by PTP1B.
kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit).
txa2pathway. Thromboxane A2 receptor signaling.
ReactomeREACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP07948.
BgeeP07948.
CleanExHS_LYN.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR001245. Tyr_pkinase.
IPR008266. Tyr_pkinase_AS.
[Graphical view]
Gene3DG3DSA:3.30.505.10. SH2. 1 hit.
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
ProDomPD000001. Prot_kinase. 1 hit.
PD000093. SH2. 1 hit.
PD000066. SH3. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
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 Resources

NextBio15944.
PMAP-CutDBP07948.
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: June 16, 2009
This is version 125 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 8

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents