ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P06241

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

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name FYN_HUMAN
Primary accession number P06241
Secondary accession numbers Q16248 Q5R3A6 Q5R3A7 Q8N5D7
Integrated into Swiss-Prot on January 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 131)
Name and origin of the protein
Protein name Proto-oncogene tyrosine-protein kinase Fyn
Synonyms EC 2.7.10.2
p59-Fyn
Protooncogene Syn
SLK
Gene name
Name: FYN
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] (ISOFORM 1).
PubMed=3099169 [NCBI, ExPASy, EBI, Israel, Japan]
Kawakami T., Pennington C.Y., Robbins K.C.;
"Isolation and oncogenic potential of a novel human src-like gene.";
Mol. Cell. Biol. 6:4195-4201(1986).
[2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
DOI=10.1073/pnas.83.15.5459; PubMed=3526330 [NCBI, ExPASy, EBI, Israel, Japan]
Semba K., Nishizawa M., Miyajima N., Yoshida M.C., Sukegawa J., Yamanashi Y., Sasaki M., Yamamoto T., Toyoshima K.;
"Yes-related protooncogene, syn, belongs to the protein-tyrosine kinase family.";
Proc. Natl. Acad. Sci. U.S.A. 83:5459-5463(1986).
[3]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
TISSUE=T-cell;
PubMed=7822789 [NCBI, ExPASy, EBI, Israel, Japan]
Rigley K., Slocombe P., Proudfoot K., Wahid S., Mandair K., Bebbington C.;
"Human p59fyn(T) regulates OKT3-induced calcium influx by a mechanism distinct from PIP2 hydrolysis in Jurkat T cells.";
J. Immunol. 154:1136-1145(1995).
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Blood;
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).
[6]
 MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT TYR-531.
PubMed=1699196 [NCBI, ExPASy, EBI, Israel, Japan]
Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P.;
"In vivo phosphorylation and membrane association of the fyn proto-oncogene product in IM-9 human lymphoblasts.";
Oncogene 5:1313-1319(1990).
[7]
 BINDING OF SH3 DOMAIN TO PI 3-KINASE.
DOI=10.1073/pnas.90.15.7366; PubMed=8394019 [NCBI, ExPASy, EBI, Israel, Japan]
Prasad K.V., Janssen O., Kapeller R., Raab M., Cantley L.C., Rudd C.E.;
"Src-homology 3 domain of protein kinase p59fyn mediates binding to phosphatidylinositol 3-kinase in T cells.";
Proc. Natl. Acad. Sci. U.S.A. 90:7366-7370(1993).
[8]
 TISSUE SPECIFICITY, PHOSPHORYLATION, AND ALTERNATIVE SPLICING.
PubMed=10196263 [NCBI, ExPASy, EBI, Israel, Japan]
Weil R., Levraud J.P., Dodon M.D., Bessia C., Hazan U., Kourilsky P., Israel A.;
"Altered expression of tyrosine kinases of the Src and Syk families in human T-cell leukemia virus type 1-infected T-cell lines.";
J. Virol. 73:3709-3717(1999).
[9]
 INTERACTION WITH PAG1.
DOI=10.1084/jem.191.9.1591; PubMed=10790433 [NCBI, ExPASy, EBI, Israel, Japan]
Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.;
"Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation.";
J. Exp. Med. 191:1591-1604(2000).
[10]
 INTERACTION WITH HEV ORF3 PROTEIN.
DOI=10.1074/jbc.M101546200; PubMed=11518702 [NCBI, ExPASy, EBI, Israel, Japan]
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M., Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.;
"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK.";
J. Biol. Chem. 276:42389-42400(2001).
[11]
 SUBCELLULAR LOCATION.
PubMed=12218089 [NCBI, ExPASy, EBI, Israel, Japan]
Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
"Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells.";
J. Immunol. 169:2813-2817(2002).
[12]
 FUNCTION.
DOI=10.1083/jcb.200405053; PubMed=15557120 [NCBI, ExPASy, EBI, Israel, Japan]
Meriane M., Tcherkezian J., Webber C.A., Danek E.I., Triki I., McFarlane S., Bloch-Gallego E., Lamarche-Vane N.;
"Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone guidance.";
J. Cell Biol. 167:687-698(2004).
[13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213; TYR-214; TYR-420 AND TYR-440, AND MASS SPECTROMETRY.
TISSUE=Lung;
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).
[14]
 INTERACTION WITH PRMT8.
DOI=10.1074/jbc.M704650200; PubMed=17925405 [NCBI, ExPASy, EBI, Israel, Japan]
Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.;
"Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its N-terminal domain.";
J. Biol. Chem. 282:36444-36453(2007).
[15]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-420, 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).
[16]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-420, 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).
[17]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-25; SER-257 AND TYR-531, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
PubMed=7687536 [NCBI, ExPASy, EBI, Israel, Japan]
Noble M.E.M., Musacchio A., Saraste M., Courtneidge S.A., Wierenga R.K.;
"Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.";
EMBO J. 12:2617-2624(1993).
[20]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-142.
DOI=10.1038/nsb0894-546; PubMed=7664083 [NCBI, ExPASy, EBI, Israel, Japan]
Musacchio A., Saraste M., Wilmanns M.;
"High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.";
Nat. Struct. Biol. 1:546-551(1994).
[21]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 85-141 IN COMPLEX WITH NEF.
DOI=10.1016/S0092-8674(00)81276-3; PubMed=8681387 [NCBI, ExPASy, EBI, Israel, Japan]
Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J.;
"Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain.";
Cell 85:931-942(1996).
[22]
 STRUCTURE BY NMR OF SH3 DOMAIN.
DOI=10.1016/S0969-2126(96)00076-7; PubMed=8805554 [NCBI, ExPASy, EBI, Israel, Japan]
Morton C.J., Pugh D.J.R., Brown E.L.J., Kahmann J.D., Renzoni D.A.C., Campbell I.D.;
"Solution structure and peptide binding of the SH3 domain from human Fyn.";
Structure 4:705-714(1996).
[23]
 STRUCTURE BY NMR.
DOI=10.1021/bi9620969; PubMed=8961927 [NCBI, ExPASy, EBI, Israel, Japan]
Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C., Waterfield M.D., Campbell I.D., Ladbury J.E.;
"Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.";
Biochemistry 35:15646-15653(1996).
[24]
 STRUCTURE BY NMR OF SH2 DOMAIN.
DOI=10.1016/S0969-2126(97)00283-9; PubMed=9351806 [NCBI, ExPASy, EBI, Israel, Japan]
Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.;
"The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.";
Structure 5:1313-1323(1997).
[25]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-144 IN COMPLEX WITH SLAMF1 AND SH2D1A.
DOI=10.1038/ncb920; PubMed=12545174 [NCBI, ExPASy, EBI, Israel, Japan]
Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F., Howie D., Sumegi J., Terhorst C., Eck M.J.;
"SAP couples Fyn to SLAM immune receptors.";
Nat. Cell Biol. 5:155-160(2003).
[26]
 VARIANTS [LARGE SCALE ANALYSIS] LEU-243; ARG-410 AND GLU-506.
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
M14676; AAA36615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M14333; AAC08285.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S74774; AAB33113.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97989; CAI22300.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z97989; CAI22301.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC032496; AAH32496.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00166845; -.
IPI00219012; -.
IPI00640091; -.
PIR A24314; TVHUSY.
RefSeq NP_002028.1; -.
NP_694592.1; -.
NP_694593.1; -.
UniGene Hs.390567
3D structure databases
PDB
1A0N; NMR; -; B=82-148.[ExPASy / RCSB / EBI]
1AOT; NMR; -; F=143-248.[ExPASy / RCSB / EBI]
1AOU; NMR; -; F=143-248.[ExPASy / RCSB / EBI]
1AVZ; X-ray; 3.00 A; C=85-140.[ExPASy / RCSB / EBI]
1AZG; NMR; -; B=82-148.[ExPASy / RCSB / EBI]
1EFN; X-ray; 2.50 A; A/C=86-143.[ExPASy / RCSB / EBI]
1FYN; X-ray; 2.30 A; A=81-142.[ExPASy / RCSB / EBI]
1G83; X-ray; 2.60 A; A/B=82-245.[ExPASy / RCSB / EBI]
1M27; X-ray; 2.50 A; C=84-144.[ExPASy / RCSB / EBI]
1NYF; NMR; -; A=82-148.[ExPASy / RCSB / EBI]
1NYG; NMR; -; A=82-148.[ExPASy / RCSB / EBI]
1SHF; X-ray; 1.90 A; A/B=84-142.[ExPASy / RCSB / EBI]
1ZBJ; NMR; -; A=84-141.[ExPASy / RCSB / EBI]
2DQ7; X-ray; 2.80 A; X=261-536.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A0N; -.
1AOT; -.
1AOU; -.
1AVZ; -.
1AZG; -.
1EFN; -.
1FYN; -.
1G83; -.
1M27; -.
1NYF; -.
1NYG; -.
1SHF; -.
1ZBJ; -.
2DQ7; -.
ModBase P06241.
Protein-protein interaction databases
IntAct P06241; 164.
PTM databases
PhosphoSite P06241; -.
Enzyme and pathway databases
BRENDA 2.7.10.2; 247.
Pathway_Interaction_DB alphasynuclein_pathway; Alpha-synuclein signaling.
amb2_neutrophils_pathway; amb2 Integrin signaling.
angiopoietinreceptor_pathway; Angiopoietin receptor Tie2-mediated signaling.
pi3kcipathway; Class I PI3K signaling events.
epha_fwdpathway; EPHA forward signaling.
ephrinarevpathway; Ephrin A reverse signaling.
ephrinbrevpathway; Ephrin B reverse signaling.
fcer1pathway; Fc-epsilon receptor I signaling in mast cells.
glypican_1pathway; Glypican 1 network.
il2_1pathway; IL2-mediated signaling events.
pdgfrbpathway; PDGFR-beta signaling pathway.
reelinpathway; Reelin signaling pathway.
p38alphabetapathway; Regulation of p38-alpha and p38-beta.
ptp1bpathway; Signaling events mediated by PTP1B.
vegfr1_2_pathway; Signaling events mediated by VEGFR1 and VEGFR2.
syndecan_3_pathway; Syndecan-3-mediated signaling events.
tcrpathway; TCR signaling in naive CD4+ T cells.
cd8tcrpathway; TCR signaling in naive CD8+ T cells.
txa2pathway; Thromboxane A2 receptor signaling.
Reactome REACT_604; Hemostasis.
REACT_6185; HIV Infection.
REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC06M112089; -.
H-InvDB HIX0006144; -.
HIX0076254; -.
HGNC HGNC:4037; FYN.
GenAtlas FYN.
HPA CAB005034; -.
CAB018387; -.
MIM 137025; gene. [NCBI / EBI]
PharmGKB PA28454; -.
Gene expression databases
ArrayExpress P06241; -.
Bgee P06241; -.
CleanEx HS_FYN; -.
GermOnline ENSG00000010810; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005768; Cellular component: endosome (inferred from direct assay from HGNC).
GO:0005886; Cellular component: plasma membrane (inferred from direct assay from HGNC).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0001948; Molecular function: glycoprotein binding (inferred from physical interaction from UniProtKB).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0030145; Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004715; Molecular function: non-membrane spanning protein tyrosine kinase activity (non-traceable author statement from UniProtKB).
GO:0006816; Biological process: calcium ion transport (non-traceable author statement from UniProtKB).
GO:0007631; Biological process: feeding behavior (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007612; Biological process: learning (traceable author statement from ProtInc).
GO:0007275; Biological process: multicellular organismal development (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (non-traceable author statement from UniProtKB).
GO:0007243; Biological process: protein kinase cascade (traceable author statement from ProtInc).
GO:0050852; Biological process: T cell receptor signaling pathway (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR000980; SH2.
IPR001452; SH3_domain.
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.
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).
Other
SWISS-3DIMAGE P06241.
Proteomic databases
PRIDE P06241; -.
Genome annotation databases
Ensembl ENSG00000010810; Homo sapiens. [Contig view]
GeneID 2534; -.
KEGG hsa:2534; -.
Phylogenomic databases
HOGENOM P06241; -.
HOVERGEN P06241; -.
OMA P06241; XWYFGKL.
Other
DrugBank DB01254; Dasatinib.
NextBio 9997; -.
PMAP-CutDB P06241; -.
SOURCE FYN; Homo sapiens.
ProtoNet P06241.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Cell membrane; Developmental protein; Host-virus interaction; Kinase; Lipoprotein; Manganese; Membrane; Metal-binding; 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. 
CHAIN   2   537  536     Proto-oncogene tyrosine-protein kinase Fyn. PRO_0000088099
DOMAIN   82   143  62     SH3. 
DOMAIN   149   246  98     SH2. 
DOMAIN   271   524  254     Protein kinase. 
NP_BIND   277   285  9     ATP (By similarity). 
ACT_SITE   390   390        Proton acceptor (By similarity). 
BINDING   299   299        ATP (By similarity). 
MOD_RES   12    12        Phosphothreonine; by PKC (By similarity). 
MOD_RES   21    21        Phosphoserine. 
MOD_RES   25    25        Phosphoserine. 
MOD_RES   185   185        Phosphotyrosine (By similarity). 
MOD_RES   213   213        Phosphotyrosine. 
MOD_RES   214   214        Phosphotyrosine. 
MOD_RES   254   254        Phosphothreonine (By similarity). 
MOD_RES   257   257        Phosphoserine. 
MOD_RES   420   420        Phosphotyrosine; by autocatalysis. 
MOD_RES   440   440        Phosphotyrosine. 
MOD_RES   531   531        Phosphotyrosine. 
LIPID   2     2        N-myristoyl glycine. 
LIPID   3     3        S-palmitoyl cysteine (By similarity). 
LIPID   6     6        S-palmitoyl cysteine (By similarity). 
VAR_SEQ   233   287        Missing (in isoform 3). VSP_024108
VAR_SEQ   234   236        RAA -> KAD (in isoform 2). VSP_024109
VAR_SEQ   240   283        CRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLG NGQFG -> FNLTVIASSCTPQTSGLAKDAWEVARRSLCLEKKLG QGCFA (in isoform 2). VSP_024110
VARIANT   243   243  1     V -> L (in a lung squamous cell carcinoma sample; somatic mutation). VAR_041704 
VARIANT   410   410  1     G -> R (in a metastatic melanoma sample; somatic mutation). VAR_041705 [3D]
VARIANT   445   445  1     I -> F (in dbSNP:rs1801121 [NCBI]). VAR_014661 [3D]
VARIANT   506   506  1     D -> E. VAR_041706 [3D]
CONFLICT   184   184        A -> S (in Ref. 1; AAA36615). 
CONFLICT   287   287        M -> L (in Ref. 3; AAB33113 and 4; CAI22301). 
CONFLICT   437   437        A -> R (in Ref. 1; AAA36615 and 3; AAB33113). 
STRAND   86    91  6      
STRAND   97   100  4      
STRAND   108   113  6      
STRAND   117   124  8      
TURN   125   127  3      
STRAND   130   134  5      
HELIX   135   137  3      
STRAND   138   140  3      
HELIX   144   146  3      
STRAND   147   150  4      
HELIX   156   164  9      
STRAND   173   177  5      
STRAND   179   181  3      
STRAND   185   192  8      
STRAND   194   196  3      
STRAND   198   207  10      
STRAND   220   223  4      
HELIX   224   233  10      
STRAND   238   240  3      
STRAND   263   265  3      
HELIX   268   270  3      
STRAND   271   278  8      
STRAND   285   290  6      
TURN   291   293  3      
STRAND   294   299  6      
TURN   303   305  3      
HELIX   308   318  11      
STRAND   329   333  5      
STRAND   335   337  3      
STRAND   339   343  5      
HELIX   350   354  5      
STRAND   355   357  3      
TURN   358   360  3      
HELIX   364   383  20      
HELIX   393   395  3      
STRAND   396   399  4      
TURN   400   402  3      
STRAND   403   406  4      
STRAND   416   418  3      
TURN   430   432  3      
HELIX   435   438  4      
HELIX   445   460  16      
HELIX   472   481  10      
HELIX   496   502  7      
HELIX   507   509  3      
HELIX   513   521  9      
Sequence information
Length: 537 AA [This is the length of the unprocessed precursor] Molecular weight: 60762 Da [This is the MW of the unprocessed precursor] CRC64: 4A1E443A4B5A0977 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 

        70         80         90        100        110        120 
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 

       130        140        150        160        170        180 
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 

       190        200        210        220        230        240 
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC 

       250        260        270        280        290        300 
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 

       310        320        330        340        350        360 
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR 

       370        380        390        400        410        420 
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY 

       430        440        450        460        470        480 
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE 

       490        500        510        520        530 
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL
P06241 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ch flag SIB Switzerland Mirror sites: Australia Brazil Canada China Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!