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Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene Syn) (Proto-oncogene c-Fyn) (Src-like kinase) (SLK) (p59-Fyn)

 FYN_HUMAN               Reviewed;         537 AA.
P06241; B5BU57; E1P557; H0UI48; Q16248; Q5R3A6; Q5R3A7; Q8N5D7;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 225.
RecName: Full=Tyrosine-protein kinase Fyn;
EC=2.7.10.2;
AltName: Full=Proto-oncogene Syn;
AltName: Full=Proto-oncogene c-Fyn;
AltName: Full=Src-like kinase;
Short=SLK;
AltName: Full=p59-Fyn;
Name=FYN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3099169; DOI=10.1128/MCB.6.12.4195;
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; DOI=10.1073/pnas.83.15.5459;
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;
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 MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT TYR-531.
PubMed=1699196;
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).
[9]
DEPHOSPHORYLATION AT TYR-531 BY PTPRC.
PubMed=1533589; DOI=10.1002/eji.1830220510;
Mustelin T., Pessa-Morikawa T., Autero M., Gassmann M.,
Andersson L.C., Gahmberg C.G., Burn P.;
"Regulation of the p59fyn protein tyrosine kinase by the CD45
phosphotyrosine phosphatase.";
Eur. J. Immunol. 22:1173-1178(1992).
[10]
INTERACTION WITH PIK3R1.
PubMed=8394019; DOI=10.1073/pnas.90.15.7366;
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).
[11]
PALMITOYLATION.
PubMed=8206991;
Alland L., Peseckis S.M., Atherton R.E., Berthiaume L., Resh M.D.;
"Dual myristylation and palmitylation of Src family member p59fyn
affects subcellular localization.";
J. Biol. Chem. 269:16701-16705(1994).
[12]
FUNCTION IN PHOSPHORYLATION OF CD28.
PubMed=7568038; DOI=10.1073/pnas.92.19.8891;
Raab M., Cai Y.C., Bunnell S.C., Heyeck S.D., Berg L.J., Rudd C.E.;
"p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-
kinase, growth factor receptor-bound protein GRB-2, and T cell-
specific protein-tyrosine kinase ITK: implications for T-cell
costimulation.";
Proc. Natl. Acad. Sci. U.S.A. 92:8891-8895(1995).
[13]
INTERACTION WITH KIT.
PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
"Direct association of Csk homologous kinase (CHK) with the
diphosphorylated site Tyr568/570 of the activated c-KIT in
megakaryocytes.";
J. Biol. Chem. 272:5915-5920(1997).
[14]
INTERACTION WITH FYB.
TISSUE=Tonsil;
PubMed=9207119; DOI=10.1073/pnas.94.14.7493;
da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.;
"Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-
containing leukocyte protein 76 and modulates interleukin 2
production.";
Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997).
[15]
INTERACTION WITH CAV1.
PubMed=9741627; DOI=10.1016/S0092-8674(00)81604-9;
Wary K.K., Mariotti A., Zurzolo C., Giancotti F.G.;
"A requirement for caveolin-1 and associated kinase Fyn in integrin
signaling and anchorage-dependent cell growth.";
Cell 94:625-634(1998).
[16]
TISSUE SPECIFICITY, PHOSPHORYLATION, AND ALTERNATIVE SPLICING.
PubMed=10196263;
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).
[17]
INTERACTION WITH EPHA8.
PubMed=10498895; DOI=10.1038/sj.onc.1202917;
Choi S., Park S.;
"Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates
Fyn binding to the Tyr-615 site by enhancing tyrosine kinase
activity.";
Oncogene 18:5413-5422(1999).
[18]
INTERACTION WITH PAG1.
PubMed=10790433; DOI=10.1084/jem.191.9.1591;
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).
[19]
FUNCTION IN PHOSPHORYLATION OF VAV1.
PubMed=11005864; DOI=10.1073/pnas.97.20.10923;
Huang J., Tilly D., Altman A., Sugie K., Grey H.M.;
"T-cell receptor antagonists induce Vav phosphorylation by selective
activation of Fyn kinase.";
Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000).
[20]
FUNCTION IN PHOSPHORYLATION OF SNCA.
PubMed=11162638; DOI=10.1006/bbrc.2000.4253;
Nakamura T., Yamashita H., Takahashi T., Nakamura S.;
"Activated Fyn phosphorylates alpha-synuclein at tyrosine residue
125.";
Biochem. Biophys. Res. Commun. 280:1085-1092(2001).
[21]
INTERACTION WITH HEV ORF3 PROTEIN.
PubMed=11518702; DOI=10.1074/jbc.M101546200;
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).
[22]
FUNCTION.
PubMed=11536198; DOI=10.1002/neu.1066;
Wolf R.M., Wilkes J.J., Chao M.V., Resh M.D.;
"Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates
oligodendrocyte differentiation.";
J. Neurobiol. 49:62-78(2001).
[23]
SUBCELLULAR LOCATION.
PubMed=12218089; DOI=10.4049/jimmunol.169.6.2813;
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).
[24]
FUNCTION IN PHOSPHORYLATION OF ARHGAP32.
PubMed=12788081; DOI=10.1016/S0006-291X(03)00923-9;
Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T.,
Yamamoto T.;
"p250GAP, a neural RhoGAP protein, is associated with and
phosphorylated by Fyn.";
Biochem. Biophys. Res. Commun. 306:151-155(2003).
[25]
FUNCTION IN PHOSPHORYLATION OF TRPC6.
PubMed=14761972; DOI=10.1074/jbc.M311274200;
Hisatsune C., Kuroda Y., Nakamura K., Inoue T., Nakamura T.,
Michikawa T., Mizutani A., Mikoshiba K.;
"Regulation of TRPC6 channel activity by tyrosine phosphorylation.";
J. Biol. Chem. 279:18887-18894(2004).
[26]
FUNCTION.
PubMed=15557120; DOI=10.1083/jcb.200405053;
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).
[27]
FUNCTION IN PHOSPHORYLATION OF WAS.
PubMed=14707117; DOI=10.1084/jem.20030976;
Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.;
"Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome
protein (WASp) tyrosine phosphorylation is required for coupling T
cell antigen receptor engagement to WASp effector function and T cell
activation.";
J. Exp. Med. 199:99-112(2004).
[28]
INTERACTION WITH UNC119.
PubMed=14757743; DOI=10.1084/jem.20030589;
Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.;
"Unc119, a novel activator of Lck/Fyn, is essential for T cell
activation.";
J. Exp. Med. 199:369-379(2004).
[29]
REVIEW ON FUNCTION.
PubMed=15489916; DOI=10.1038/sj.onc.1208074;
Palacios E.H., Weiss A.;
"Function of the Src-family kinases, Lck and Fyn, in T-cell
development and activation.";
Oncogene 23:7990-8000(2004).
[30]
FUNCTION IN PHOSPHORYLATION OF MAP2.
PubMed=15536091; DOI=10.1074/jbc.M411380200;
Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B.;
"Fyn phosphorylates human MAP-2c on tyrosine 67.";
J. Biol. Chem. 280:1962-1970(2005).
[31]
PHOSPHORYLATION AT THR-12, AND SUBCELLULAR LOCATION.
PubMed=15537652; DOI=10.1074/jbc.M402053200;
He Z., Cho Y.Y., Ma W.Y., Choi H.S., Bode A.M., Dong Z.;
"Regulation of ultraviolet B-induced phosphorylation of histone H3 at
serine 10 by Fyn kinase.";
J. Biol. Chem. 280:2446-2454(2005).
[32]
INTERACTION WITH ITCH, AND FUNCTION.
PubMed=16387660; DOI=10.1016/j.molcel.2005.11.014;
Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H.,
Liu Y.C.;
"Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated
tyrosine phosphorylation.";
Mol. Cell 21:135-141(2006).
[33]
FUNCTION IN PHOSPHORYLATION OF AGAP2.
PubMed=16841086; DOI=10.1038/sj.cdd.4402011;
Tang X., Feng Y., Ye K.;
"Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-
kinase enhancer-activating Akt, preventing its apoptotic cleavage and
promoting cell survival.";
Cell Death Differ. 14:368-377(2007).
[34]
INTERACTION WITH PRMT8.
PubMed=17925405; DOI=10.1074/jbc.M704650200;
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).
[35]
FUNCTION IN PHOSPHORYLATION OF CTNND1.
PubMed=17194753; DOI=10.1128/MCB.01974-06;
Castano J., Solanas G., Casagolda D., Raurell I., Villagrasa P.,
Bustelo X.R., Garcia de Herreros A., Dunach M.;
"Specific phosphorylation of p120-catenin regulatory domain
differently modulates its binding to RhoA.";
Mol. Cell. Biol. 27:1745-1757(2007).
[36]
FUNCTION IN PHOSPHORYLATION OF PAG1.
PubMed=18056706; DOI=10.1074/jbc.M705215200;
Solheim S.A., Torgersen K.M., Tasken K., Berge T.;
"Regulation of FynT function by dual domain docking on PAG/Cbp.";
J. Biol. Chem. 283:2773-2783(2008).
[37]
FUNCTION IN PHOSPHORYLATION OF KIRREL.
PubMed=18258597; DOI=10.1074/jbc.M707247200;
Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T.,
Hattori S.;
"Neph1, a component of the kidney slit diaphragm, is tyrosine-
phosphorylated by the Src family tyrosine kinase and modulates
intracellular signaling by binding to Grb2.";
J. Biol. Chem. 283:9177-9186(2008).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
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).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-531, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
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).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
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).
[41]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL
(CD178) by phage display screening.";
BMC Immunol. 10:53-53(2009).
[42]
FUNCTION IN PHOSPHORYLATION OF NPHS1.
PubMed=19179337; DOI=10.1074/jbc.M806851200;
Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T.,
Ohsawa I., Ohta S., Hattori S.;
"Phosphorylation of nephrin triggers Ca2+ signaling by recruitment and
activation of phospholipase C-{gamma}1.";
J. Biol. Chem. 284:8951-8962(2009).
[43]
FUNCTION IN PHOSPHORYLATION OF DPYSL2.
PubMed=19652227; DOI=10.1074/jbc.M109.000240;
Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y.,
Nakamura F., Goshima Y.;
"Semaphorin3A signaling mediated by Fyn-dependent tyrosine
phosphorylation of collapsin response mediator protein 2 at tyrosine
32.";
J. Biol. Chem. 284:27393-27401(2009).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[45]
FUNCTION, AND INTERACTION WITH RUNX3.
PubMed=20100835; DOI=10.1074/jbc.M109.071381;
Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W.,
Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.;
"Src kinase phosphorylates RUNX3 at tyrosine residues and localizes
the protein in the cytoplasm.";
J. Biol. Chem. 285:10122-10129(2010).
[46]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[47]
FUNCTION IN TCR SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION AT
TYR-420 BY PTPN2.
PubMed=22080863; DOI=10.1172/JCI59492;
Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C.,
Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.;
"T cell protein tyrosine phosphatase attenuates T cell signaling to
maintain tolerance in mice.";
J. Clin. Invest. 121:4758-4774(2011).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-26, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[49]
INTERACTION WITH ARAP AND FYB.
PubMed=27335501; DOI=10.4049/jimmunol.1501913;
Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y.,
Lee J.R.;
"ARAP, a novel adaptor protein, is required for TCR signaling and
integrin-mediated adhesion.";
J. Immunol. 197:942-952(2016).
[50]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
PubMed=7687536;
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).
[51]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-142.
PubMed=7664083; DOI=10.1038/nsb0894-546;
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).
[52]
STRUCTURE BY NMR.
PubMed=8961927; DOI=10.1021/bi9620969;
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).
[53]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 85-141 IN COMPLEX WITH NEF.
PubMed=8681387; DOI=10.1016/S0092-8674(00)81276-3;
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).
[54]
STRUCTURE BY NMR OF SH3 DOMAIN.
PubMed=8805554; DOI=10.1016/S0969-2126(96)00076-7;
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).
[55]
STRUCTURE BY NMR OF SH2 DOMAIN.
PubMed=9351806; DOI=10.1016/S0969-2126(97)00283-9;
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).
[56]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-144 IN COMPLEX WITH SLAMF1
AND SH2D1A.
PubMed=12545174; DOI=10.1038/ncb920;
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).
[57]
VARIANTS [LARGE SCALE ANALYSIS] LEU-243; ARG-410 AND GLU-506.
PubMed=17344846; DOI=10.1038/nature05610;
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).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role
in many biological processes including regulation of cell growth
and survival, cell adhesion, integrin-mediated signaling,
cytoskeletal remodeling, cell motility, immune response and axon
guidance. Inactive FYN is phosphorylated on its C-terminal tail
within the catalytic domain. Following activation by PKA, the
protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1
phosphorylation, activation and targeting to focal adhesions.
Involved in the regulation of cell adhesion and motility through
phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-
catenin). Regulates cytoskeletal remodeling by phosphorylating
several proteins including the actin regulator WAS and the
microtubule-associated proteins MAP2 and MAPT. Promotes cell
survival by phosphorylating AGAP2/PIKE-A and preventing its
apoptotic cleavage. Participates in signal transduction pathways
that regulate the integrity of the glomerular slit diaphragm (an
essential part of the glomerular filter of the kidney) by
phosphorylating several slit diaphragm components including NPHS1,
KIRREL and TRPC6. Plays a role in neural processes by
phosphorylating DPYSL2, a multifunctional adapter protein within
the central nervous system, ARHGAP32, a regulator for Rho family
GTPases implicated in various neural functions, and SNCA, a small
pre-synaptic protein. Participates in the downstream signaling
pathways that lead to T-cell differentiation and proliferation
following T-cell receptor (TCR) stimulation. Also participates in
negative feedback regulation of TCR signaling through
phosphorylation of PAG1, thereby promoting interaction between
PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains
LCK and FYN in an inactive form. Promotes CD28-induced
phosphorylation of VAV1. {ECO:0000269|PubMed:11005864,
ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11536198,
ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:14707117,
ECO:0000269|PubMed:14761972, ECO:0000269|PubMed:15536091,
ECO:0000269|PubMed:15557120, ECO:0000269|PubMed:16387660,
ECO:0000269|PubMed:16841086, ECO:0000269|PubMed:17194753,
ECO:0000269|PubMed:18056706, ECO:0000269|PubMed:18258597,
ECO:0000269|PubMed:19179337, ECO:0000269|PubMed:19652227,
ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:22080863,
ECO:0000269|PubMed:7568038, ECO:0000269|PubMed:7822789}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- ENZYME REGULATION: Inhibited by phosphorylation of Tyr-531 by
leukocyte common antigen and activated by dephosphorylation of
this site.
-!- SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8.
Interacts with FYB, PAG1, and SH2D1A. Interacts with CD79A
(tyrosine-phosphorylated form); the interaction increases FYN
activity. Interacts (via SH2 domain) with CSF1R (tyrosine
phosphorylated) (By similarity). Interacts with TOM1L1
(phosphorylated form). Interacts with KDR (tyrosine
phosphorylated). Interacts (via SH3 domain) with KLHL2 (via N-
terminus) (By similarity). Interacts with SH2D1A and SLAMF1.
Interacts (via its SH3 domain) with HEV ORF3 protein. Interacts
with ITCH; the interaction phosphorylates ITCH and negatively
regulates its activity. Interacts with FASLG. Interacts with
RUNX3. Interacts with KIT. Interacts with EPHA8; possible
downstream effector of EPHA8 in regulation of cell adhesion.
Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1
phosphorylation and activation. Interacts with CAV1; this
interaction couples integrins to the Ras-ERK pathway. Interacts
with UNC119. Interacts (via SH2 domain) with PTPRH (phosphorylated
form) (By similarity). Interacts with PTPRO (phosphorylated form)
(By similarity). Interacts with PTPRB (phosphorylated form) (By
similarity). Interacts with ARAP (PubMed:27335501).
{ECO:0000250|UniProtKB:P39688, ECO:0000250|UniProtKB:Q62844,
ECO:0000269|PubMed:10498895, ECO:0000269|PubMed:10790433,
ECO:0000269|PubMed:11518702, ECO:0000269|PubMed:12545174,
ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:16387660,
ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:27335501,
ECO:0000269|PubMed:8394019, ECO:0000269|PubMed:8681387,
ECO:0000269|PubMed:9038210, ECO:0000269|PubMed:9207119,
ECO:0000269|PubMed:9741627}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-515315, EBI-515315;
O92972:- (xeno); NbExp=2; IntAct=EBI-515315, EBI-710506;
P27958:- (xeno); NbExp=4; IntAct=EBI-515315, EBI-706378;
Q9WMX2:- (xeno); NbExp=2; IntAct=EBI-515315, EBI-710918;
P42684:ABL2; NbExp=2; IntAct=EBI-515315, EBI-1102694;
Q13444:ADAM15; NbExp=2; IntAct=EBI-515315, EBI-77818;
A7KAX9:ARHGAP32; NbExp=4; IntAct=EBI-515315, EBI-308663;
O14559:ARHGAP33; NbExp=2; IntAct=EBI-515315, EBI-1210010;
Q9ULH1:ASAP1; NbExp=3; IntAct=EBI-515315, EBI-346622;
P56945:BCAR1; NbExp=3; IntAct=EBI-515315, EBI-702093;
Q13191:CBLB; NbExp=3; IntAct=EBI-10691738, EBI-744027;
O43281:EFS; NbExp=3; IntAct=EBI-515315, EBI-718488;
P04626:ERBB2; NbExp=2; IntAct=EBI-515315, EBI-641062;
P48023:FASLG; NbExp=2; IntAct=EBI-515315, EBI-495538;
P02751-7:FN1; NbExp=2; IntAct=EBI-515315, EBI-7133890;
O15117:FYB; NbExp=4; IntAct=EBI-515315, EBI-1753267;
P31424-2:Grm5 (xeno); NbExp=2; IntAct=EBI-515315, EBI-8830305;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-515315, EBI-352572;
P50406:HTR6; NbExp=7; IntAct=EBI-515315, EBI-1182222;
Q07666:KHDRBS1; NbExp=4; IntAct=EBI-515315, EBI-1364;
Q92918:MAP4K1; NbExp=2; IntAct=EBI-515315, EBI-881;
Q9H204:MED28; NbExp=6; IntAct=EBI-515315, EBI-514199;
Q9NZQ3:NCKIPSD; NbExp=2; IntAct=EBI-515315, EBI-745080;
Q8WX92:NELFB; NbExp=2; IntAct=EBI-515315, EBI-347721;
Q9NWQ8:PAG1; NbExp=5; IntAct=EBI-515315, EBI-2828115;
Q8WUM4:PDCD6IP; NbExp=6; IntAct=EBI-515315, EBI-310624;
P09619:PDGFRB; NbExp=3; IntAct=EBI-515315, EBI-641237;
O43900:PRICKLE3; NbExp=2; IntAct=EBI-515315, EBI-1751761;
Q05655:PRKCD; NbExp=5; IntAct=EBI-515315, EBI-704279;
Q04759:PRKCQ; NbExp=7; IntAct=EBI-515315, EBI-374762;
Q13905:RAPGEF1; NbExp=2; IntAct=EBI-515315, EBI-976876;
O60880:SH2D1A; NbExp=3; IntAct=EBI-515315, EBI-6983382;
Q8BHK6:Slamf7 (xeno); NbExp=2; IntAct=EBI-515315, EBI-11463802;
Q9Y2W2:WBP11; NbExp=3; IntAct=EBI-515315, EBI-714455;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane.
Note=Present and active in lipid rafts. Palmitoylation is crucial
for proper trafficking.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=B;
IsoId=P06241-1; Sequence=Displayed;
Name=2; Synonyms=T;
IsoId=P06241-2; Sequence=VSP_024110;
Name=3;
IsoId=P06241-3; Sequence=VSP_024108;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the brain.
Isoform 2 is expressed in cells of hemopoietic lineages,
especially T-lymphocytes. {ECO:0000269|PubMed:10196263}.
-!- PTM: Autophosphorylated at Tyr-420. Phosphorylation on the C-
terminal tail at Tyr-531 by CSK maintains the enzyme in an
inactive state (By similarity). PTPRC/CD45 dephosphorylates Tyr-
531 leading to activation. Ultraviolet B (UVB) strongly increase
phosphorylation at Thr-12 and kinase activity, and promotes
translocation from the cytoplasm to the nucleus. Dephosphorylation
at Tyr-420 by PTPN2 negatively regulates T-cell receptor
signaling. {ECO:0000250, ECO:0000269|PubMed:10196263,
ECO:0000269|PubMed:15537652, ECO:0000269|PubMed:1699196,
ECO:0000269|PubMed:22080863}.
-!- PTM: Palmitoylation at Cys-3 and Cys-6 regulates subcellular
location. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-----------------------------------------------------------------------
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EMBL; M14676; AAA36615.1; -; mRNA.
EMBL; M14333; AAC08285.1; -; mRNA.
EMBL; S74774; AAB33113.2; -; mRNA.
EMBL; AB451293; BAG70107.1; -; mRNA.
EMBL; AB451426; BAG70240.1; -; mRNA.
EMBL; Z97989; CAI22300.1; -; Genomic_DNA.
EMBL; Z97989; CAI22301.1; -; Genomic_DNA.
EMBL; CH471051; EAW48278.1; -; Genomic_DNA.
EMBL; CH471051; EAW48279.1; -; Genomic_DNA.
EMBL; CH471051; EAW48281.1; -; Genomic_DNA.
EMBL; CH471051; EAW48282.1; -; Genomic_DNA.
EMBL; CH471051; EAW48283.1; -; Genomic_DNA.
EMBL; BC032496; AAH32496.1; -; mRNA.
CCDS; CCDS5094.1; -. [P06241-1]
CCDS; CCDS5095.1; -. [P06241-2]
CCDS; CCDS5096.1; -. [P06241-3]
PIR; A24314; TVHUSY.
RefSeq; NP_002028.1; NM_002037.5. [P06241-1]
RefSeq; NP_694592.1; NM_153047.3. [P06241-2]
RefSeq; NP_694593.1; NM_153048.3. [P06241-3]
RefSeq; XP_005266947.1; XM_005266890.3. [P06241-2]
RefSeq; XP_005266949.1; XM_005266892.3. [P06241-3]
RefSeq; XP_016866139.1; XM_017010650.1. [P06241-1]
RefSeq; XP_016866140.1; XM_017010651.1. [P06241-1]
RefSeq; XP_016866141.1; XM_017010652.1. [P06241-1]
RefSeq; XP_016866142.1; XM_017010653.1. [P06241-1]
RefSeq; XP_016866143.1; XM_017010654.1. [P06241-1]
UniGene; Hs.390567; -.
UniGene; Hs.664520; -.
PDB; 1A0N; NMR; -; B=80-148.
PDB; 1AOT; NMR; -; F=143-248.
PDB; 1AOU; NMR; -; F=143-248.
PDB; 1AVZ; X-ray; 3.00 A; C=85-141.
PDB; 1AZG; NMR; -; B=82-148.
PDB; 1EFN; X-ray; 2.50 A; A/C=86-143.
PDB; 1FYN; X-ray; 2.30 A; A=81-142.
PDB; 1G83; X-ray; 2.60 A; A/B=82-246.
PDB; 1M27; X-ray; 2.50 A; C=84-144.
PDB; 1NYF; NMR; -; A=82-148.
PDB; 1NYG; NMR; -; A=82-148.
PDB; 1SHF; X-ray; 1.90 A; A/B=84-142.
PDB; 1ZBJ; NMR; -; A=84-142.
PDB; 2DQ7; X-ray; 2.80 A; X=261-537.
PDB; 2MQI; NMR; -; A=148-248.
PDB; 2MRJ; NMR; -; A=148-248.
PDB; 2MRK; NMR; -; A=149-248, B=528-537.
PDB; 3H0F; X-ray; 2.61 A; A=73-142.
PDB; 3H0H; X-ray; 1.76 A; A=73-142.
PDB; 3H0I; X-ray; 2.20 A; A/B=73-142.
PDB; 3UA6; X-ray; 1.85 A; A/B=81-143.
PDB; 3UA7; X-ray; 1.50 A; A/B/C/D=81-143.
PDB; 4D8D; X-ray; 2.52 A; A/C=84-141.
PDB; 4EIK; X-ray; 1.60 A; A=81-143.
PDB; 4U17; X-ray; 1.99 A; A/B/C=148-248.
PDB; 4U1P; X-ray; 1.40 A; A=148-248.
PDB; 4ZNX; X-ray; 2.10 A; A/B/C/D=84-141.
PDBsum; 1A0N; -.
PDBsum; 1AOT; -.
PDBsum; 1AOU; -.
PDBsum; 1AVZ; -.
PDBsum; 1AZG; -.
PDBsum; 1EFN; -.
PDBsum; 1FYN; -.
PDBsum; 1G83; -.
PDBsum; 1M27; -.
PDBsum; 1NYF; -.
PDBsum; 1NYG; -.
PDBsum; 1SHF; -.
PDBsum; 1ZBJ; -.
PDBsum; 2DQ7; -.
PDBsum; 2MQI; -.
PDBsum; 2MRJ; -.
PDBsum; 2MRK; -.
PDBsum; 3H0F; -.
PDBsum; 3H0H; -.
PDBsum; 3H0I; -.
PDBsum; 3UA6; -.
PDBsum; 3UA7; -.
PDBsum; 4D8D; -.
PDBsum; 4EIK; -.
PDBsum; 4U17; -.
PDBsum; 4U1P; -.
PDBsum; 4ZNX; -.
ProteinModelPortal; P06241; -.
SMR; P06241; -.
BioGrid; 108810; 187.
DIP; DIP-33876N; -.
ELM; P06241; -.
IntAct; P06241; 240.
MINT; MINT-93594; -.
STRING; 9606.ENSP00000346671; -.
BindingDB; P06241; -.
ChEMBL; CHEMBL1841; -.
DrugBank; DB02078; 1-Methoxy-2-[2-(2-Methoxy-Ethoxy]-Ethane.
DrugBank; DB01254; Dasatinib.
GuidetoPHARMACOLOGY; 2026; -.
iPTMnet; P06241; -.
PhosphoSitePlus; P06241; -.
SwissPalm; P06241; -.
BioMuta; FYN; -.
DMDM; 125370; -.
EPD; P06241; -.
MaxQB; P06241; -.
PaxDb; P06241; -.
PeptideAtlas; P06241; -.
PRIDE; P06241; -.
DNASU; 2534; -.
Ensembl; ENST00000229471; ENSP00000229471; ENSG00000010810. [P06241-3]
Ensembl; ENST00000354650; ENSP00000346671; ENSG00000010810. [P06241-1]
Ensembl; ENST00000368667; ENSP00000357656; ENSG00000010810. [P06241-1]
Ensembl; ENST00000368678; ENSP00000357667; ENSG00000010810. [P06241-2]
Ensembl; ENST00000368682; ENSP00000357671; ENSG00000010810. [P06241-2]
Ensembl; ENST00000538466; ENSP00000440646; ENSG00000010810. [P06241-2]
GeneID; 2534; -.
KEGG; hsa:2534; -.
UCSC; uc003pvh.3; human. [P06241-1]
CTD; 2534; -.
DisGeNET; 2534; -.
GeneCards; FYN; -.
HGNC; HGNC:4037; FYN.
HPA; CAB005034; -.
HPA; CAB018387; -.
HPA; HPA023887; -.
HPA; HPA063770; -.
MIM; 137025; gene.
neXtProt; NX_P06241; -.
OpenTargets; ENSG00000010810; -.
PharmGKB; PA28454; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOVERGEN; HBG008761; -.
InParanoid; P06241; -.
KO; K05703; -.
OMA; SHNSGYR; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P06241; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1227986; Signaling by ERBB2.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-164944; Nef and signal transduction.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-373753; Nephrin interactions.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
Reactome; R-HSA-418885; DCC mediated attractive signaling.
Reactome; R-HSA-418886; Netrin mediated repulsion signals.
Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5621480; Dectin-2 family.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-8866376; Reelin signalling pathway.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLink; P06241; -.
SIGNOR; P06241; -.
ChiTaRS; FYN; human.
EvolutionaryTrace; P06241; -.
GeneWiki; FYN; -.
GenomeRNAi; 2534; -.
PMAP-CutDB; P06241; -.
PRO; PR:P06241; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000010810; -.
CleanEx; HS_FYN; -.
ExpressionAtlas; P06241; baseline and differential.
Genevisible; P06241; HS.
GO; GO:0005884; C:actin filament; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
GO; GO:0005768; C:endosome; IDA:HGNC.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IMP:ARUK-UCL.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0014069; C:postsynaptic density; ISS:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042609; F:CD4 receptor binding; IEA:Ensembl.
GO; GO:0042610; F:CD8 receptor binding; IEA:Ensembl.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0001948; F:glycoprotein binding; IPI:BHF-UCL.
GO; GO:0070851; F:growth factor receptor binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0004871; F:signal transducer activity; IEA:Ensembl.
GO; GO:0042608; F:T cell receptor binding; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; ISS:ARUK-UCL.
GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0007612; P:learning; TAS:ProtInc.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IEA:Ensembl.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IEA:Ensembl.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:1904645; P:response to amyloid-beta; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0042110; P:T cell activation; IBA:GO_Central.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm; Developmental protein;
Host-virus interaction; Immunity; Kinase; Lipoprotein; Manganese;
Membrane; Metal-binding; Myristate; Nucleotide-binding; Nucleus;
Palmitate; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase.
INIT_MET 1 1 Removed.
CHAIN 2 537 Tyrosine-protein kinase Fyn.
/FTId=PRO_0000088099.
DOMAIN 82 143 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 149 246 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 271 524 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 277 285 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 390 390 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 299 299 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 12 12 Phosphothreonine; by PKC.
{ECO:0000269|PubMed:15537652}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000250|UniProtKB:P39688}.
MOD_RES 214 214 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06240}.
MOD_RES 420 420 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P39688}.
MOD_RES 531 531 Phosphotyrosine; by CSK.
{ECO:0000244|PubMed:18691976,
ECO:0000269|PubMed:1699196}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:1699196}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 6 6 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 233 287 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024108.
VAR_SEQ 234 287 RAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLI
KRLGNGQFGEVWM -> KADGLCFNLTVIASSCTPQTSGLA
KDAWEVARRSLCLEKKLGQGCFAEVWL (in isoform
2). {ECO:0000303|PubMed:7822789}.
/FTId=VSP_024110.
VARIANT 243 243 V -> L (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041704.
VARIANT 410 410 G -> R (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041705.
VARIANT 445 445 I -> F (in dbSNP:rs1801121).
/FTId=VAR_014661.
VARIANT 506 506 D -> E (in dbSNP:rs28763975).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041706.
CONFLICT 184 184 A -> S (in Ref. 1; AAA36615).
{ECO:0000305}.
CONFLICT 437 437 A -> R (in Ref. 1; AAA36615 and 3;
AAB33113). {ECO:0000305}.
STRAND 87 91 {ECO:0000244|PDB:3UA7}.
STRAND 96 100 {ECO:0000244|PDB:3UA6}.
STRAND 108 113 {ECO:0000244|PDB:3UA7}.
STRAND 115 124 {ECO:0000244|PDB:3UA7}.
TURN 125 127 {ECO:0000244|PDB:3UA7}.
STRAND 130 134 {ECO:0000244|PDB:3UA7}.
HELIX 135 137 {ECO:0000244|PDB:3UA7}.
STRAND 138 141 {ECO:0000244|PDB:3UA7}.
HELIX 144 146 {ECO:0000244|PDB:1G83}.
STRAND 147 150 {ECO:0000244|PDB:1G83}.
HELIX 156 163 {ECO:0000244|PDB:4U1P}.
TURN 165 167 {ECO:0000244|PDB:1AOT}.
STRAND 172 177 {ECO:0000244|PDB:4U1P}.
STRAND 179 181 {ECO:0000244|PDB:4U1P}.
STRAND 185 193 {ECO:0000244|PDB:4U1P}.
TURN 194 196 {ECO:0000244|PDB:4U1P}.
STRAND 197 207 {ECO:0000244|PDB:4U1P}.
TURN 209 211 {ECO:0000244|PDB:1AOT}.
STRAND 213 216 {ECO:0000244|PDB:4U1P}.
STRAND 219 223 {ECO:0000244|PDB:4U1P}.
HELIX 224 233 {ECO:0000244|PDB:4U1P}.
STRAND 238 240 {ECO:0000244|PDB:4U1P}.
STRAND 263 265 {ECO:0000244|PDB:2DQ7}.
HELIX 268 270 {ECO:0000244|PDB:2DQ7}.
STRAND 271 278 {ECO:0000244|PDB:2DQ7}.
STRAND 285 290 {ECO:0000244|PDB:2DQ7}.
TURN 291 293 {ECO:0000244|PDB:2DQ7}.
STRAND 294 299 {ECO:0000244|PDB:2DQ7}.
TURN 303 305 {ECO:0000244|PDB:2DQ7}.
HELIX 308 318 {ECO:0000244|PDB:2DQ7}.
STRAND 329 333 {ECO:0000244|PDB:2DQ7}.
STRAND 335 337 {ECO:0000244|PDB:2DQ7}.
STRAND 339 343 {ECO:0000244|PDB:2DQ7}.
HELIX 350 354 {ECO:0000244|PDB:2DQ7}.
STRAND 355 357 {ECO:0000244|PDB:2DQ7}.
TURN 358 360 {ECO:0000244|PDB:2DQ7}.
HELIX 364 383 {ECO:0000244|PDB:2DQ7}.
HELIX 393 395 {ECO:0000244|PDB:2DQ7}.
STRAND 396 399 {ECO:0000244|PDB:2DQ7}.
TURN 400 402 {ECO:0000244|PDB:2DQ7}.
STRAND 403 406 {ECO:0000244|PDB:2DQ7}.
STRAND 416 418 {ECO:0000244|PDB:2DQ7}.
TURN 430 432 {ECO:0000244|PDB:2DQ7}.
HELIX 435 438 {ECO:0000244|PDB:2DQ7}.
HELIX 445 460 {ECO:0000244|PDB:2DQ7}.
HELIX 472 481 {ECO:0000244|PDB:2DQ7}.
HELIX 496 502 {ECO:0000244|PDB:2DQ7}.
HELIX 507 509 {ECO:0000244|PDB:2DQ7}.
HELIX 513 521 {ECO:0000244|PDB:2DQ7}.
SEQUENCE 537 AA; 60762 MW; 4A1E443A4B5A0977 CRC64;
MGCVQCKDKE ATKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG
LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET
TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC
RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT
LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMNKGSL LDFLKDGEGR
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQSFL EDYFTATEPQ YQPGENL


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