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UniProtKB/Swiss-Prot entry P07948


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LYN_HUMAN
Primary accession number P07948
Secondary accession number A0AVQ5
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 114)
Name and origin of the protein
Protein name Tyrosine-protein kinase Lyn
Synonym EC 2.7.10.2
Gene name
Name: LYN
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3561390 [NCBI, ExPASy, EBI, Israel, Japan]
Yamanashi Y., Fukushige S., Semba K., Sukegawa J., Miyajima N., Matsubara K., Yamamoto T., Toyoshima K.;
"The yes-related cellular gene lyn encodes a possible tyrosine kinase similar to p56lck.";
Mol. Cell. Biol. 7:237-243(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0378-1119(94)90811-7; PubMed=8125304 [NCBI, ExPASy, EBI, Israel, Japan]
Rider L.G., Raben N., Miller L., Jelsema C.;
"The cDNAs encoding two forms of the LYN protein tyrosine kinase are expressed in rat mast cells and human myeloid cells.";
Gene 138:219-222(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LYN A).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
PubMed=2247464 [NCBI, ExPASy, EBI, Israel, Japan]
Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K.;
"Putative tyrosine kinases expressed in K-562 human leukemia cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 369-424.
DOI=10.1016/S0006-291X(05)81562-1; PubMed=1510669 [NCBI, ExPASy, EBI, Israel, Japan]
Bielke W., Ziemiecki A., Kappos L., Miescher G.C.;
"Expression of the B cell-associated tyrosine kinase gene Lyn in primary neuroblastoma tumours and its modulation during the differentiation of neuroblastoma cell lines.";
Biochem. Biophys. Res. Commun. 186:1403-1409(1992).
[6]
INTERACTION WITH EPSTEIN-BARR VIRUS LMP2A.
DOI=10.1016/S1074-7613(95)80040-9; PubMed=7895172 [NCBI, ExPASy, EBI, Israel, Japan]
Miller C.L., Burkhardt A.L., Lee J.H., Stealey B., Longnecker R., Bolen J.B., Kieff E.;
"Integral membrane protein 2 of Epstein-Barr virus regulates reactivation from latency through dominant negative effects on protein-tyrosine kinases.";
Immunity 2:155-166(1995).
[7]
INTERACTION WITH PPP1R15A.
DOI=10.1073/pnas.191130798; PubMed=11517336 [NCBI, ExPASy, EBI, Israel, Japan]
Grishin A.V., Azhipa O., Semenov I., Corey S.J.;
"Interaction between growth arrest-DNA damage protein 34 and Src kinase Lyn negatively regulates genotoxic apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 98:10172-10177(2001).
[8]
INTERACTION WITH MUC1.
PubMed=12750561 [NCBI, ExPASy, EBI, Israel, Japan]
Li Y., Chen W., Ren J., Yu W.H., Li Q., Yoshida K., Kufe D.;
"DF3/MUC1 signaling in multiple myeloma cells is regulated by interleukin-7.";
Cancer Biol. Ther. 2:187-193(2003).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND TYR-508, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
INTERACTION WITH TGFB1I1.
DOI=10.1042/BJ20061618; PubMed=17233630 [NCBI, ExPASy, EBI, Israel, Japan]
Rathore V.B., Okada M., Newman P.J., Newman D.K.;
"Paxillin family members function as Csk-binding proteins that regulate Lyn activity in human and murine platelets.";
Biochem. J. 403:275-281(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193; TYR-194; TYR-306; TYR-397; TYR-473 AND TYR-508, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.T600062-MCP200; PubMed=17192257 [NCBI, ExPASy, EBI, Israel, Japan]
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H.;
"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry.";
Mol. Cell. Proteomics 6:537-547(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND TYR-397, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[15]
VARIANT [LARGE SCALE ANALYSIS] TYR-385.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M16038; AAA59540.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M79321; AAB50019.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC075001; AAH75001.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC075002; AAH75002.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126456; AAI26457.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126458; AAI26459.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A26719; TVHULY.
RefSeq NP_002341.1; -.
UniGene Hs.699154
3D structure databases
PDB
1W1F; NMR; -; A=61-123.[ExPASy / RCSB / EBI]
1WA7; NMR; -; A=61-123.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1W1F; -.
1WA7; -.
SMR P07948; 67-512.
ModBase P07948.
Protein-protein interaction databases
DIP DIP:1056N; -.
IntAct P07948; -.
PTM databases
PhosphoSite P07948; -.
2D gel databases
REPRODUCTION-2DPAGE P07948; -.
Organism-specific databases
H-InvDB HIX0025560; -.
HGNC HGNC:6735; LYN.
GenAtlas LYN.
HPA CAB004492; -.
HPA001231; -.
MIM 165120; gene. [NCBI / EBI]
PharmGKB PA30498; -.
GeneCards P07948.
Gene expression databases
ArrayExpress P07948; -.
CleanEx HS_LYN; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0045121; Cellular component: membrane raft (inferred from direct assay from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from sequence or structural similarity from UniProtKB).
GO:0005886; Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004716; Molecular function: receptor signaling protein tyrosine kinase activity (traceable author statement from ProtInc).
GO:0030218; Biological process: erythrocyte differentiation (inferred from sequence or structural similarity from UniProtKB).
GO:0008284; Biological process: positive regulation of cell proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0042531; Biological process: positive regulation of tyrosine phosphorylation of STAT protein (inferred from sequence or structural similarity from UniProtKB).
GO:0009725; Biological process: response to hormone stimulus (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR000980; SH2.
IPR001452; SH3.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.
Gene3D G3DSA:3.30.505.10; SH2; 1.
Pfam PF07714; Pkinase_Tyr; 1.
PF00017; SH2; 1.
PF00018; SH3_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00401; SH2DOMAIN.
PR00452; SH3DOMAIN.
PR00109; TYRKINASE.
ProDom PD000001; Prot_kinase; 1.
PD000093; SH2; 1.
PD000066; SH3; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00252; SH2; 1.
SM00326; SH3; 1.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.
PROSITE PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PS50001; SH2; 1.
PS50002; SH3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P07948.
Genome annotation databases
Ensembl ENSG00000147507; Homo sapiens. [Contig view]
GeneID 4067; -.
Phylogenomic databases
HOVERGEN P07948; -.
Other
SOURCE LYN; Homo sapiens.
ProtoNet P07948.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Host-virus interaction; Kinase; Lipoprotein; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein; Polymorphism; Proto-oncogene; SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   512  511     Tyrosine-protein kinase Lyn. PRO_0000088129
DOMAIN   63   123  61     SH3. 
DOMAIN   129   226  98     SH2. 
DOMAIN   247   501  255     Protein kinase. 
NP_BIND   253   261  9     ATP (By similarity). 
ACT_SITE   367   367        Proton acceptor (By similarity). 
BINDING   275   275        ATP (By similarity). 
MOD_RES   11    11        Phosphoserine. 
MOD_RES   13    13        Phosphoserine. 
MOD_RES   193   193        Phosphotyrosine. 
MOD_RES   194   194        Phosphotyrosine. 
MOD_RES   306   306        Phosphotyrosine. 
MOD_RES   397   397        Phosphotyrosine; by autocatalysis (By similarity). 
MOD_RES   473   473        Phosphotyrosine. 
MOD_RES   508   508        Phosphotyrosine. 
LIPID   2     2        N-myristoyl glycine (By similarity). 
LIPID   3     3        S-palmitoyl cysteine (By similarity). 
VAR_SEQ   23    43        Missing (in isoform LYN B). VSP_005002
VARIANT   385   385  1     D -> Y (in a breast pleomorphic lobular carcinoma sample; somatic mutation). VAR_041737 [3D]
STRAND   66    72  7      
STRAND   78    80  3      
STRAND   89    95  7      
STRAND   97   104  8      
TURN   105   107  3      
STRAND   110   114  5      
TURN   115   117  3      
STRAND   118   120  3      
Sequence information
Length: 512 AA [This is the length of the unprocessed precursor] Molecular weight: 58574 Da [This is the MW of the unprocessed precursor] CRC64: 408D3D461204E378 [This is a checksum on the sequence]
        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 

P07948 in FASTA format

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