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UniProtKB/Swiss-Prot entry P06241

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

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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    November 4, 2008 (Entry version 121)
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;
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.
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 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).
[14]
 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).
[15]
 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).
[16]
 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).
[17]
 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).
[18]
 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).
[19]
 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).
[20]
 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).
[21]
 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]
PIR A24314; TVHUSY.
RefSeq NP_002028.1; -.
NP_694592.1; -.
NP_694593.1; -.
UniGene Hs.390567
3D structure databases
PDB
1A0N; NMR; -; B=80-148.[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=85-141.[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=84-142.[ExPASy / RCSB / EBI]
2DQ7; X-ray; 2.80 A; X=261-537.[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; -.
PTM databases
PhosphoSite P06241; -.
Enzyme and pathway databases
Reactome REACT_6185; HIV Infection.
Organism-specific databases
H-InvDB HIX0006144; -.
HIX0076254; -.
HGNC HGNC:4037; FYN.
GenAtlas FYN.
HPA CAB005034; -.
CAB018387; -.
MIM 137025; gene. [NCBI / EBI]
PharmGKB PA28454; -.
GeneCards P06241.
Gene expression databases
ArrayExpress 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:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
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:0007612; Biological process: learning (traceable author statement from ProtInc).
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_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 P06241.
ProtoNet P06241.
Other
SWISS-3DIMAGE P06241.
Genome annotation databases
Ensembl ENSG00000010810; Homo sapiens. [Contig view]
GeneID 2534; -.
KEGG hsa:2534; -.
Phylogenomic databases
HOGENOM P06241; -.
HOVERGEN P06241; -.
Other
DrugBank DB01254; Dasatinib.
LinkHub P06241; -.
NextBio 9997; -.
SOURCE FYN; Homo sapiens.
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.