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Database: UniProt
Entry: P06241
LinkDB: P06241
Original site: P06241 
ID   FYN_HUMAN               Reviewed;         537 AA.
AC   P06241; B5BU57; E1P557; H0UI48; Q16248; Q5R3A6; Q5R3A7; Q8N5D7;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   12-AUG-2020, entry version 254.
DE   RecName: Full=Tyrosine-protein kinase Fyn;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene Syn;
DE   AltName: Full=Proto-oncogene c-Fyn;
DE   AltName: Full=Src-like kinase;
DE            Short=SLK;
DE   AltName: Full=p59-Fyn;
GN   Name=FYN;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3099169; DOI=10.1128/mcb.6.12.4195;
RA   Kawakami T., Pennington C.Y., Robbins K.C.;
RT   "Isolation and oncogenic potential of a novel human src-like gene.";
RL   Mol. Cell. Biol. 6:4195-4201(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=3526330; DOI=10.1073/pnas.83.15.5459;
RA   Semba K., Nishizawa M., Miyajima N., Yoshida M.C., Sukegawa J.,
RA   Yamanashi Y., Sasaki M., Yamamoto T., Toyoshima K.;
RT   "Yes-related protooncogene, syn, belongs to the protein-tyrosine kinase
RT   family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:5459-5463(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC   TISSUE=T-cell;
RX   PubMed=7822789;
RA   Rigley K., Slocombe P., Proudfoot K., Wahid S., Mandair K., Bebbington C.;
RT   "Human p59fyn(T) regulates OKT3-induced calcium influx by a mechanism
RT   distinct from PIP2 hydrolysis in Jurkat T cells.";
RL   J. Immunol. 154:1136-1145(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=19054851; DOI=10.1038/nmeth.1273;
RA   Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA   Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA   Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA   Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA   Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA   Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA   Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA   Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA   Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA   Nomura N.;
RT   "Human protein factory for converting the transcriptome into an in vitro-
RT   expressed proteome.";
RL   Nat. Methods 5:1011-1017(2008).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Blood;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT TYR-531.
RX   PubMed=1699196;
RA   Peters D.J., McGrew B.R., Perron D.C., Liptak L.M., Laudano A.P.;
RT   "In vivo phosphorylation and membrane association of the fyn proto-oncogene
RT   product in IM-9 human lymphoblasts.";
RL   Oncogene 5:1313-1319(1990).
RN   [9]
RP   DEPHOSPHORYLATION AT TYR-531 BY PTPRC.
RX   PubMed=1533589; DOI=10.1002/eji.1830220510;
RA   Mustelin T., Pessa-Morikawa T., Autero M., Gassmann M., Andersson L.C.,
RA   Gahmberg C.G., Burn P.;
RT   "Regulation of the p59fyn protein tyrosine kinase by the CD45
RT   phosphotyrosine phosphatase.";
RL   Eur. J. Immunol. 22:1173-1178(1992).
RN   [10]
RP   INTERACTION WITH PIK3R1.
RX   PubMed=8394019; DOI=10.1073/pnas.90.15.7366;
RA   Prasad K.V., Janssen O., Kapeller R., Raab M., Cantley L.C., Rudd C.E.;
RT   "Src-homology 3 domain of protein kinase p59fyn mediates binding to
RT   phosphatidylinositol 3-kinase in T cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:7366-7370(1993).
RN   [11]
RP   PALMITOYLATION.
RX   PubMed=8206991;
RA   Alland L., Peseckis S.M., Atherton R.E., Berthiaume L., Resh M.D.;
RT   "Dual myristylation and palmitylation of Src family member p59fyn affects
RT   subcellular localization.";
RL   J. Biol. Chem. 269:16701-16705(1994).
RN   [12]
RP   FUNCTION IN PHOSPHORYLATION OF CD28.
RX   PubMed=7568038; DOI=10.1073/pnas.92.19.8891;
RA   Raab M., Cai Y.C., Bunnell S.C., Heyeck S.D., Berg L.J., Rudd C.E.;
RT   "p56Lck and p59Fyn regulate CD28 binding to phosphatidylinositol 3-kinase,
RT   growth factor receptor-bound protein GRB-2, and T cell-specific protein-
RT   tyrosine kinase ITK: implications for T-cell costimulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8891-8895(1995).
RN   [13]
RP   INTERACTION WITH KIT.
RX   PubMed=9038210; DOI=10.1074/jbc.272.9.5915;
RA   Price D.J., Rivnay B., Fu Y., Jiang S., Avraham S., Avraham H.;
RT   "Direct association of Csk homologous kinase (CHK) with the
RT   diphosphorylated site Tyr568/570 of the activated c-KIT in
RT   megakaryocytes.";
RL   J. Biol. Chem. 272:5915-5920(1997).
RN   [14]
RP   INTERACTION WITH FYB1.
RC   TISSUE=Tonsil;
RX   PubMed=9207119; DOI=10.1073/pnas.94.14.7493;
RA   da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.;
RT   "Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-
RT   containing leukocyte protein 76 and modulates interleukin 2 production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997).
RN   [15]
RP   INTERACTION WITH CAV1.
RX   PubMed=9741627; DOI=10.1016/s0092-8674(00)81604-9;
RA   Wary K.K., Mariotti A., Zurzolo C., Giancotti F.G.;
RT   "A requirement for caveolin-1 and associated kinase Fyn in integrin
RT   signaling and anchorage-dependent cell growth.";
RL   Cell 94:625-634(1998).
RN   [16]
RP   TISSUE SPECIFICITY, PHOSPHORYLATION, AND ALTERNATIVE SPLICING.
RX   PubMed=10196263;
RA   Weil R., Levraud J.P., Dodon M.D., Bessia C., Hazan U., Kourilsky P.,
RA   Israel A.;
RT   "Altered expression of tyrosine kinases of the Src and Syk families in
RT   human T-cell leukemia virus type 1-infected T-cell lines.";
RL   J. Virol. 73:3709-3717(1999).
RN   [17]
RP   INTERACTION WITH EPHA8.
RX   PubMed=10498895; DOI=10.1038/sj.onc.1202917;
RA   Choi S., Park S.;
RT   "Phosphorylation at Tyr-838 in the kinase domain of EphA8 modulates Fyn
RT   binding to the Tyr-615 site by enhancing tyrosine kinase activity.";
RL   Oncogene 18:5413-5422(1999).
RN   [18]
RP   INTERACTION WITH PAG1.
RX   PubMed=10790433; DOI=10.1084/jem.191.9.1591;
RA   Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P.,
RA   Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K.,
RA   Kuramitsu Y., Horejsi V., Schraven B.;
RT   "Phosphoprotein associated with glycosphingolipid-enriched microdomains
RT   (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds
RT   the protein tyrosine kinase csk and is involved in regulation of T cell
RT   activation.";
RL   J. Exp. Med. 191:1591-1604(2000).
RN   [19]
RP   FUNCTION IN PHOSPHORYLATION OF VAV1.
RX   PubMed=11005864; DOI=10.1073/pnas.97.20.10923;
RA   Huang J., Tilly D., Altman A., Sugie K., Grey H.M.;
RT   "T-cell receptor antagonists induce Vav phosphorylation by selective
RT   activation of Fyn kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000).
RN   [20]
RP   FUNCTION IN PHOSPHORYLATION OF SNCA.
RX   PubMed=11162638; DOI=10.1006/bbrc.2000.4253;
RA   Nakamura T., Yamashita H., Takahashi T., Nakamura S.;
RT   "Activated Fyn phosphorylates alpha-synuclein at tyrosine residue 125.";
RL   Biochem. Biophys. Res. Commun. 280:1085-1092(2001).
RN   [21]
RP   INTERACTION WITH HEV ORF3 PROTEIN (MICROBIAL INFECTION).
RX   PubMed=11518702; DOI=10.1074/jbc.m101546200;
RA   Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M.,
RA   Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.;
RT   "The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and
RT   activates MAPK.";
RL   J. Biol. Chem. 276:42389-42400(2001).
RN   [22]
RP   FUNCTION.
RX   PubMed=11536198; DOI=10.1002/neu.1066;
RA   Wolf R.M., Wilkes J.J., Chao M.V., Resh M.D.;
RT   "Tyrosine phosphorylation of p190 RhoGAP by Fyn regulates oligodendrocyte
RT   differentiation.";
RL   J. Neurobiol. 49:62-78(2001).
RN   [23]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12218089; DOI=10.4049/jimmunol.169.6.2813;
RA   Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y.,
RA   Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
RT   "Fyn is essential for tyrosine phosphorylation of Csk-binding
RT   protein/phosphoprotein associated with glycolipid-enriched microdomains in
RT   lipid rafts in resting T cells.";
RL   J. Immunol. 169:2813-2817(2002).
RN   [24]
RP   FUNCTION IN PHOSPHORYLATION OF ARHGAP32.
RX   PubMed=12788081; DOI=10.1016/s0006-291x(03)00923-9;
RA   Taniguchi S., Liu H., Nakazawa T., Yokoyama K., Tezuka T., Yamamoto T.;
RT   "p250GAP, a neural RhoGAP protein, is associated with and phosphorylated by
RT   Fyn.";
RL   Biochem. Biophys. Res. Commun. 306:151-155(2003).
RN   [25]
RP   FUNCTION IN PHOSPHORYLATION OF TRPC6.
RX   PubMed=14761972; DOI=10.1074/jbc.m311274200;
RA   Hisatsune C., Kuroda Y., Nakamura K., Inoue T., Nakamura T., Michikawa T.,
RA   Mizutani A., Mikoshiba K.;
RT   "Regulation of TRPC6 channel activity by tyrosine phosphorylation.";
RL   J. Biol. Chem. 279:18887-18894(2004).
RN   [26]
RP   FUNCTION.
RX   PubMed=15557120; DOI=10.1083/jcb.200405053;
RA   Meriane M., Tcherkezian J., Webber C.A., Danek E.I., Triki I.,
RA   McFarlane S., Bloch-Gallego E., Lamarche-Vane N.;
RT   "Phosphorylation of DCC by Fyn mediates Netrin-1 signaling in growth cone
RT   guidance.";
RL   J. Cell Biol. 167:687-698(2004).
RN   [27]
RP   FUNCTION IN PHOSPHORYLATION OF WAS.
RX   PubMed=14707117; DOI=10.1084/jem.20030976;
RA   Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.;
RT   "Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein
RT   (WASp) tyrosine phosphorylation is required for coupling T cell antigen
RT   receptor engagement to WASp effector function and T cell activation.";
RL   J. Exp. Med. 199:99-112(2004).
RN   [28]
RP   INTERACTION WITH UNC119.
RX   PubMed=14757743; DOI=10.1084/jem.20030589;
RA   Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.;
RT   "Unc119, a novel activator of Lck/Fyn, is essential for T cell
RT   activation.";
RL   J. Exp. Med. 199:369-379(2004).
RN   [29]
RP   REVIEW ON FUNCTION.
RX   PubMed=15489916; DOI=10.1038/sj.onc.1208074;
RA   Palacios E.H., Weiss A.;
RT   "Function of the Src-family kinases, Lck and Fyn, in T-cell development and
RT   activation.";
RL   Oncogene 23:7990-8000(2004).
RN   [30]
RP   FUNCTION IN PHOSPHORYLATION OF MAP2.
RX   PubMed=15536091; DOI=10.1074/jbc.m411380200;
RA   Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B.;
RT   "Fyn phosphorylates human MAP-2c on tyrosine 67.";
RL   J. Biol. Chem. 280:1962-1970(2005).
RN   [31]
RP   PHOSPHORYLATION AT THR-12, AND SUBCELLULAR LOCATION.
RX   PubMed=15537652; DOI=10.1074/jbc.m402053200;
RA   He Z., Cho Y.Y., Ma W.Y., Choi H.S., Bode A.M., Dong Z.;
RT   "Regulation of ultraviolet B-induced phosphorylation of histone H3 at
RT   serine 10 by Fyn kinase.";
RL   J. Biol. Chem. 280:2446-2454(2005).
RN   [32]
RP   INTERACTION WITH ITCH, AND FUNCTION.
RX   PubMed=16387660; DOI=10.1016/j.molcel.2005.11.014;
RA   Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H., Liu Y.C.;
RT   "Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated
RT   tyrosine phosphorylation.";
RL   Mol. Cell 21:135-141(2006).
RN   [33]
RP   FUNCTION IN PHOSPHORYLATION OF AGAP2.
RX   PubMed=16841086; DOI=10.1038/sj.cdd.4402011;
RA   Tang X., Feng Y., Ye K.;
RT   "Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-
RT   kinase enhancer-activating Akt, preventing its apoptotic cleavage and
RT   promoting cell survival.";
RL   Cell Death Differ. 14:368-377(2007).
RN   [34]
RP   INTERACTION WITH PRMT8.
RX   PubMed=17925405; DOI=10.1074/jbc.m704650200;
RA   Sayegh J., Webb K., Cheng D., Bedford M.T., Clarke S.G.;
RT   "Regulation of protein arginine methyltransferase 8 (PRMT8) activity by its
RT   N-terminal domain.";
RL   J. Biol. Chem. 282:36444-36453(2007).
RN   [35]
RP   FUNCTION IN PHOSPHORYLATION OF CTNND1.
RX   PubMed=17194753; DOI=10.1128/mcb.01974-06;
RA   Castano J., Solanas G., Casagolda D., Raurell I., Villagrasa P.,
RA   Bustelo X.R., Garcia de Herreros A., Dunach M.;
RT   "Specific phosphorylation of p120-catenin regulatory domain differently
RT   modulates its binding to RhoA.";
RL   Mol. Cell. Biol. 27:1745-1757(2007).
RN   [36]
RP   FUNCTION IN PHOSPHORYLATION OF PAG1.
RX   PubMed=18056706; DOI=10.1074/jbc.m705215200;
RA   Solheim S.A., Torgersen K.M., Tasken K., Berge T.;
RT   "Regulation of FynT function by dual domain docking on PAG/Cbp.";
RL   J. Biol. Chem. 283:2773-2783(2008).
RN   [37]
RP   FUNCTION IN PHOSPHORYLATION OF KIRREL1.
RX   PubMed=18258597; DOI=10.1074/jbc.m707247200;
RA   Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T.,
RA   Hattori S.;
RT   "Neph1, a component of the kidney slit diaphragm, is tyrosine-
RT   phosphorylated by the Src family tyrosine kinase and modulates
RT   intracellular signaling by binding to Grb2.";
RL   J. Biol. Chem. 283:9177-9186(2008).
RN   [38]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [39]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND TYR-531, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [40]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [41]
RP   INTERACTION WITH FASLG.
RX   PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA   Voss M., Lettau M., Janssen O.;
RT   "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT   phage display screening.";
RL   BMC Immunol. 10:53-53(2009).
RN   [42]
RP   FUNCTION IN PHOSPHORYLATION OF NPHS1.
RX   PubMed=19179337; DOI=10.1074/jbc.m806851200;
RA   Harita Y., Kurihara H., Kosako H., Tezuka T., Sekine T., Igarashi T.,
RA   Ohsawa I., Ohta S., Hattori S.;
RT   "Phosphorylation of nephrin triggers Ca2+ signaling by recruitment and
RT   activation of phospholipase C-{gamma}1.";
RL   J. Biol. Chem. 284:8951-8962(2009).
RN   [43]
RP   FUNCTION IN PHOSPHORYLATION OF DPYSL2.
RX   PubMed=19652227; DOI=10.1074/jbc.m109.000240;
RA   Uchida Y., Ohshima T., Yamashita N., Ogawara M., Sasaki Y., Nakamura F.,
RA   Goshima Y.;
RT   "Semaphorin3A signaling mediated by Fyn-dependent tyrosine phosphorylation
RT   of collapsin response mediator protein 2 at tyrosine 32.";
RL   J. Biol. Chem. 284:27393-27401(2009).
RN   [44]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [45]
RP   FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
RX   PubMed=20028775; DOI=10.1189/jlb.0409227;
RA   Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B.,
RA   Houtman J.C.;
RT   "The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402 and 580
RT   occurs via a distinct mechanism than other receptor systems.";
RL   J. Leukoc. Biol. 87:691-701(2010).
RN   [46]
RP   FUNCTION, AND INTERACTION WITH RUNX3.
RX   PubMed=20100835; DOI=10.1074/jbc.m109.071381;
RA   Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W., Li Y.H.,
RA   Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.;
RT   "Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the
RT   protein in the cytoplasm.";
RL   J. Biol. Chem. 285:10122-10129(2010).
RN   [47]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [48]
RP   FUNCTION IN TCR SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION AT
RP   TYR-420 BY PTPN2.
RX   PubMed=22080863; DOI=10.1172/jci59492;
RA   Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C.,
RA   Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.;
RT   "T cell protein tyrosine phosphatase attenuates T cell signaling to
RT   maintain tolerance in mice.";
RL   J. Clin. Invest. 121:4758-4774(2011).
RN   [49]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-26, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [50]
RP   INTERACTION WITH FYB2 AND FYB1.
RX   PubMed=27335501; DOI=10.4049/jimmunol.1501913;
RA   Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y., Lee J.R.;
RT   "ARAP, a novel adaptor protein, is required for TCR signaling and integrin-
RT   mediated adhesion.";
RL   J. Immunol. 197:942-952(2016).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF SH3 DOMAIN.
RX   PubMed=7687536; DOI=10.2210/pdb1shf/pdb;
RA   Noble M.E.M., Musacchio A., Saraste M., Courtneidge S.A., Wierenga R.K.;
RT   "Crystal structure of the SH3 domain in human Fyn; comparison of the three-
RT   dimensional structures of SH3 domains in tyrosine kinases and spectrin.";
RL   EMBO J. 12:2617-2624(1993).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 81-142.
RX   PubMed=7664083; DOI=10.1038/nsb0894-546;
RA   Musacchio A., Saraste M., Wilmanns M.;
RT   "High-resolution crystal structures of tyrosine kinase SH3 domains
RT   complexed with proline-rich peptides.";
RL   Nat. Struct. Biol. 1:546-551(1994).
RN   [53]
RP   STRUCTURE BY NMR.
RX   PubMed=8961927; DOI=10.1021/bi9620969;
RA   Renzoni D.A., Pugh D.J., Siligardi G., Das P., Morton C.J., Rossi C.,
RA   Waterfield M.D., Campbell I.D., Ladbury J.E.;
RT   "Structural and thermodynamic characterization of the interaction of the
RT   SH3 domain from Fyn with the proline-rich binding site on the p85 subunit
RT   of PI3-kinase.";
RL   Biochemistry 35:15646-15653(1996).
RN   [54]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 85-141 IN COMPLEX WITH NEF.
RX   PubMed=8681387; DOI=10.1016/s0092-8674(00)81276-3;
RA   Lee C.H., Saksela K., Mirza U.A., Chait B.T., Kuriyan J.;
RT   "Crystal structure of the conserved core of HIV-1 Nef complexed with a Src
RT   family SH3 domain.";
RL   Cell 85:931-942(1996).
RN   [55]
RP   STRUCTURE BY NMR OF SH3 DOMAIN.
RX   PubMed=8805554; DOI=10.1016/s0969-2126(96)00076-7;
RA   Morton C.J., Pugh D.J.R., Brown E.L.J., Kahmann J.D., Renzoni D.A.C.,
RA   Campbell I.D.;
RT   "Solution structure and peptide binding of the SH3 domain from human Fyn.";
RL   Structure 4:705-714(1996).
RN   [56]
RP   STRUCTURE BY NMR OF SH2 DOMAIN.
RX   PubMed=9351806; DOI=10.1016/s0969-2126(97)00283-9;
RA   Mulhern T.D., Shaw G.L., Morton C.J., Day A.J., Campbell I.D.;
RT   "The SH2 domain from the tyrosine kinase Fyn in complex with a
RT   phosphotyrosyl peptide reveals insights into domain stability and binding
RT   specificity.";
RL   Structure 5:1313-1323(1997).
RN   [57]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 84-144 IN COMPLEX WITH SLAMF1 AND
RP   SH2D1A.
RX   PubMed=12545174; DOI=10.1038/ncb920;
RA   Chan B., Lanyi A., Song H.K., Griesbach J., Simarro-Grande M., Poy F.,
RA   Howie D., Sumegi J., Terhorst C., Eck M.J.;
RT   "SAP couples Fyn to SLAM immune receptors.";
RL   Nat. Cell Biol. 5:155-160(2003).
RN   [58]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-243; ARG-410 AND GLU-506.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in
CC       many biological processes including regulation of cell growth and
CC       survival, cell adhesion, integrin-mediated signaling, cytoskeletal
CC       remodeling, cell motility, immune response and axon guidance. Inactive
CC       FYN is phosphorylated on its C-terminal tail within the catalytic
CC       domain. Following activation by PKA, the protein subsequently
CC       associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation,
CC       activation and targeting to focal adhesions. Involved in the regulation
CC       of cell adhesion and motility through phosphorylation of CTNNB1 (beta-
CC       catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling
CC       by phosphorylating several proteins including the actin regulator WAS
CC       and the microtubule-associated proteins MAP2 and MAPT. Promotes cell
CC       survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic
CC       cleavage. Participates in signal transduction pathways that regulate
CC       the integrity of the glomerular slit diaphragm (an essential part of
CC       the glomerular filter of the kidney) by phosphorylating several slit
CC       diaphragm components including NPHS1, KIRREL1 and TRPC6. Plays a role
CC       in neural processes by phosphorylating DPYSL2, a multifunctional
CC       adapter protein within the central nervous system, ARHGAP32, a
CC       regulator for Rho family GTPases implicated in various neural
CC       functions, and SNCA, a small pre-synaptic protein. Participates in the
CC       downstream signaling pathways that lead to T-cell differentiation and
CC       proliferation following T-cell receptor (TCR) stimulation.
CC       Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation.
CC       Also participates in negative feedback regulation of TCR signaling
CC       through phosphorylation of PAG1, thereby promoting interaction between
CC       PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK
CC       and FYN in an inactive form. Promotes CD28-induced phosphorylation of
CC       VAV1. In mast cells, phosphorylates CLNK after activation of
CC       immunoglobulin epsilon receptor signaling (By similarity).
CC       {ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:11005864,
CC       ECO:0000269|PubMed:11162638, ECO:0000269|PubMed:11536198,
CC       ECO:0000269|PubMed:12788081, ECO:0000269|PubMed:14707117,
CC       ECO:0000269|PubMed:14761972, ECO:0000269|PubMed:15536091,
CC       ECO:0000269|PubMed:15557120, ECO:0000269|PubMed:16387660,
CC       ECO:0000269|PubMed:16841086, ECO:0000269|PubMed:17194753,
CC       ECO:0000269|PubMed:18056706, ECO:0000269|PubMed:18258597,
CC       ECO:0000269|PubMed:19179337, ECO:0000269|PubMed:19652227,
CC       ECO:0000269|PubMed:20028775, ECO:0000269|PubMed:20100835,
CC       ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:7568038,
CC       ECO:0000269|PubMed:7822789}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- ACTIVITY REGULATION: Inhibited by phosphorylation of Tyr-531 by
CC       leukocyte common antigen and activated by dephosphorylation of this
CC       site.
CC   -!- SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8.
CC       Interacts with FYB1, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-
CC       phosphorylated form); the interaction increases FYN activity. Interacts
CC       (via SH2 domain) with CSF1R (tyrosine phosphorylated) (By similarity).
CC       Interacts with TOM1L1 (phosphorylated form). Interacts with KDR
CC       (tyrosine phosphorylated). Interacts (via SH3 domain) with KLHL2 (via
CC       N-terminus) (By similarity). Interacts with SH2D1A and SLAMF1.
CC       Interacts with ITCH; the interaction phosphorylates ITCH and negatively
CC       regulates its activity. Interacts with FASLG. Interacts with RUNX3.
CC       Interacts with KIT. Interacts with EPHA8; possible downstream effector
CC       of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this
CC       interaction leads to PTK2/FAK1 phosphorylation and activation.
CC       Interacts with CAV1; this interaction couples integrins to the Ras-ERK
CC       pathway. Interacts with UNC119. Interacts (via SH2 domain) with PTPRH
CC       (phosphorylated form) (By similarity). Interacts with PTPRO
CC       (phosphorylated form) (By similarity). Interacts with PTPRB
CC       (phosphorylated form) (By similarity). Interacts with FYB2
CC       (PubMed:27335501). Interacts with DSCAM (By similarity). Interacts with
CC       SKAP1 and FYB1; this interaction promotes the phosphorylation of CLNK
CC       (By similarity). {ECO:0000250|UniProtKB:P39688,
CC       ECO:0000250|UniProtKB:Q62844, ECO:0000269|PubMed:10498895,
CC       ECO:0000269|PubMed:10790433, ECO:0000269|PubMed:12545174,
CC       ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:16387660,
CC       ECO:0000269|PubMed:17925405, ECO:0000269|PubMed:19807924,
CC       ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:27335501,
CC       ECO:0000269|PubMed:8394019, ECO:0000269|PubMed:8681387,
CC       ECO:0000269|PubMed:9038210, ECO:0000269|PubMed:9207119,
CC       ECO:0000269|PubMed:9741627}.
CC   -!- SUBUNIT: (Microbial infection) Interacts (via its SH3 domain) with
CC       hepatitis E virus/HEV protein ORF3. {ECO:0000269|PubMed:11518702}.
CC   -!- INTERACTION:
CC       P06241; P42684: ABL2; NbExp=2; IntAct=EBI-515315, EBI-1102694;
CC       P06241; O14672: ADAM10; NbExp=2; IntAct=EBI-515315, EBI-1536151;
CC       P06241; Q13444: ADAM15; NbExp=2; IntAct=EBI-515315, EBI-77818;
CC       P06241; A7KAX9: ARHGAP32; NbExp=4; IntAct=EBI-515315, EBI-308663;
CC       P06241; O14559: ARHGAP33; NbExp=2; IntAct=EBI-515315, EBI-1210010;
CC       P06241; Q9ULH1: ASAP1; NbExp=3; IntAct=EBI-515315, EBI-346622;
CC       P06241; P56945: BCAR1; NbExp=4; IntAct=EBI-515315, EBI-702093;
CC       P06241; Q9Y5K6: CD2AP; NbExp=2; IntAct=EBI-515315, EBI-298152;
CC       P06241; Q16543: CDC37; NbExp=3; IntAct=EBI-515315, EBI-295634;
CC       P06241; O43281: EFS; NbExp=4; IntAct=EBI-515315, EBI-718488;
CC       P06241; P04626: ERBB2; NbExp=2; IntAct=EBI-515315, EBI-641062;
CC       P06241; P48023: FASLG; NbExp=2; IntAct=EBI-515315, EBI-495538;
CC       P06241; P36888: FLT3; NbExp=2; IntAct=EBI-515315, EBI-3946257;
CC       P06241; P02751-7: FN1; NbExp=2; IntAct=EBI-515315, EBI-7133890;
CC       P06241; O15117: FYB1; NbExp=4; IntAct=EBI-515315, EBI-1753267;
CC       P06241; P06241: FYN; NbExp=3; IntAct=EBI-515315, EBI-515315;
CC       P06241; Q9HCN6: GP6; NbExp=2; IntAct=EBI-515315, EBI-515278;
CC       P06241; Q9HCN6-1: GP6; NbExp=2; IntAct=EBI-515315, EBI-15816577;
CC       P06241; P08238: HSP90AB1; NbExp=4; IntAct=EBI-515315, EBI-352572;
CC       P06241; P50406: HTR6; NbExp=7; IntAct=EBI-515315, EBI-1182222;
CC       P06241; Q07666: KHDRBS1; NbExp=7; IntAct=EBI-515315, EBI-1364;
CC       P06241; Q92918: MAP4K1; NbExp=2; IntAct=EBI-515315, EBI-881;
CC       P06241; P10636: MAPT; NbExp=3; IntAct=EBI-515315, EBI-366182;
CC       P06241; P10636-2: MAPT; NbExp=2; IntAct=EBI-515315, EBI-7796412;
CC       P06241; P10636-5: MAPT; NbExp=2; IntAct=EBI-515315, EBI-21313635;
CC       P06241; P10636-6: MAPT; NbExp=3; IntAct=EBI-515315, EBI-7796455;
CC       P06241; P10636-8: MAPT; NbExp=9; IntAct=EBI-515315, EBI-366233;
CC       P06241; Q9H204: MED28; NbExp=6; IntAct=EBI-515315, EBI-514199;
CC       P06241; Q9NZQ3: NCKIPSD; NbExp=2; IntAct=EBI-515315, EBI-745080;
CC       P06241; Q8WX92: NELFB; NbExp=2; IntAct=EBI-515315, EBI-347721;
CC       P06241; Q9NWQ8: PAG1; NbExp=5; IntAct=EBI-515315, EBI-2828115;
CC       P06241; Q8WUM4: PDCD6IP; NbExp=6; IntAct=EBI-515315, EBI-310624;
CC       P06241; P09619: PDGFRB; NbExp=3; IntAct=EBI-515315, EBI-641237;
CC       P06241; O43900: PRICKLE3; NbExp=2; IntAct=EBI-515315, EBI-1751761;
CC       P06241; Q05655: PRKCD; NbExp=5; IntAct=EBI-515315, EBI-704279;
CC       P06241; Q04759: PRKCQ; NbExp=7; IntAct=EBI-515315, EBI-374762;
CC       P06241; Q14289: PTK2B; NbExp=4; IntAct=EBI-515315, EBI-298640;
CC       P06241; Q13905: RAPGEF1; NbExp=2; IntAct=EBI-515315, EBI-976876;
CC       P06241; P12931: SRC; NbExp=3; IntAct=EBI-515315, EBI-621482;
CC       P06241; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-515315, EBI-714455;
CC       P06241; P31424-2: Grm5; Xeno; NbExp=2; IntAct=EBI-515315, EBI-8830305;
CC       P06241; Q8BHK6: Slamf7; Xeno; NbExp=2; IntAct=EBI-515315, EBI-11463802;
CC       P06241; O92972; Xeno; NbExp=2; IntAct=EBI-515315, EBI-710506;
CC       P06241; P27958; Xeno; NbExp=4; IntAct=EBI-515315, EBI-706378;
CC       P06241; Q9WMX2; Xeno; NbExp=2; IntAct=EBI-515315, EBI-710918;
CC       P06241-3; O95429: BAG4; NbExp=3; IntAct=EBI-10691738, EBI-2949658;
CC       P06241-3; P56945: BCAR1; NbExp=3; IntAct=EBI-10691738, EBI-702093;
CC       P06241-3; Q13191: CBLB; NbExp=4; IntAct=EBI-10691738, EBI-744027;
CC       P06241-3; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-10691738, EBI-12000556;
CC       P06241-3; Q8N9I9: DTX3; NbExp=4; IntAct=EBI-10691738, EBI-2340258;
CC       P06241-3; O43281-2: EFS; NbExp=5; IntAct=EBI-10691738, EBI-11525448;
CC       P06241-3; Q9UJM3: ERRFI1; NbExp=3; IntAct=EBI-10691738, EBI-2941912;
CC       P06241-3; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-10691738, EBI-6658203;
CC       P06241-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10691738, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Note=Present
CC       and active in lipid rafts. Palmitoylation is crucial for proper
CC       trafficking.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=B;
CC         IsoId=P06241-1; Sequence=Displayed;
CC       Name=2; Synonyms=T;
CC         IsoId=P06241-2; Sequence=VSP_024110;
CC       Name=3;
CC         IsoId=P06241-3; Sequence=VSP_024108;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the brain. Isoform
CC       2 is expressed in cells of hemopoietic lineages, especially T-
CC       lymphocytes. {ECO:0000269|PubMed:10196263}.
CC   -!- PTM: Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on
CC       the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an
CC       inactive state (PubMed:1699196). PTPRC/CD45 dephosphorylates Tyr-531
CC       leading to activation (PubMed:1533589). Ultraviolet B (UVB) strongly
CC       increase phosphorylation at Thr-12 and kinase activity, and promotes
CC       translocation from the cytoplasm to the nucleus (PubMed:15537652).
CC       Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell
CC       receptor signaling (PubMed:22080863). Phosphorylated at tyrosine
CC       residues, which can be enhanced by NTN1 (By similarity).
CC       {ECO:0000250|UniProtKB:P39688, ECO:0000269|PubMed:10196263,
CC       ECO:0000269|PubMed:1533589, ECO:0000269|PubMed:15537652,
CC       ECO:0000269|PubMed:1699196, ECO:0000269|PubMed:22080863}.
CC   -!- PTM: Palmitoylation at Cys-3 and Cys-6 regulates subcellular location.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
DR   EMBL; M14676; AAA36615.1; -; mRNA.
DR   EMBL; M14333; AAC08285.1; -; mRNA.
DR   EMBL; S74774; AAB33113.2; -; mRNA.
DR   EMBL; AB451293; BAG70107.1; -; mRNA.
DR   EMBL; AB451426; BAG70240.1; -; mRNA.
DR   EMBL; Z97989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48278.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48279.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48281.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48282.1; -; Genomic_DNA.
DR   EMBL; CH471051; EAW48283.1; -; Genomic_DNA.
DR   EMBL; BC032496; AAH32496.1; -; mRNA.
DR   CCDS; CCDS5094.1; -. [P06241-1]
DR   CCDS; CCDS5095.1; -. [P06241-2]
DR   CCDS; CCDS5096.1; -. [P06241-3]
DR   PIR; A24314; TVHUSY.
DR   RefSeq; NP_002028.1; NM_002037.5. [P06241-1]
DR   RefSeq; NP_694592.1; NM_153047.3. [P06241-2]
DR   RefSeq; NP_694593.1; NM_153048.3. [P06241-3]
DR   RefSeq; XP_005266947.1; XM_005266890.3.
DR   RefSeq; XP_005266949.1; XM_005266892.3. [P06241-3]
DR   RefSeq; XP_016866139.1; XM_017010650.1. [P06241-1]
DR   RefSeq; XP_016866140.1; XM_017010651.1. [P06241-1]
DR   RefSeq; XP_016866141.1; XM_017010652.1. [P06241-1]
DR   RefSeq; XP_016866142.1; XM_017010653.1. [P06241-1]
DR   RefSeq; XP_016866143.1; XM_017010654.1.
DR   PDB; 1A0N; NMR; -; B=80-148.
DR   PDB; 1AOT; NMR; -; F=143-248.
DR   PDB; 1AOU; NMR; -; F=143-248.
DR   PDB; 1AVZ; X-ray; 3.00 A; C=85-141.
DR   PDB; 1AZG; NMR; -; B=82-148.
DR   PDB; 1EFN; X-ray; 2.50 A; A/C=86-143.
DR   PDB; 1FYN; X-ray; 2.30 A; A=81-142.
DR   PDB; 1G83; X-ray; 2.60 A; A/B=82-246.
DR   PDB; 1M27; X-ray; 2.50 A; C=84-144.
DR   PDB; 1NYF; NMR; -; A=82-148.
DR   PDB; 1NYG; NMR; -; A=82-148.
DR   PDB; 1SHF; X-ray; 1.90 A; A/B=84-142.
DR   PDB; 1ZBJ; NMR; -; A=84-142.
DR   PDB; 2DQ7; X-ray; 2.80 A; X=261-537.
DR   PDB; 2MQI; NMR; -; A=148-248.
DR   PDB; 2MRJ; NMR; -; A=148-248.
DR   PDB; 2MRK; NMR; -; A=149-248, B=528-537.
DR   PDB; 3H0F; X-ray; 2.61 A; A=73-142.
DR   PDB; 3H0H; X-ray; 1.76 A; A=73-142.
DR   PDB; 3H0I; X-ray; 2.20 A; A/B=73-142.
DR   PDB; 3UA6; X-ray; 1.85 A; A/B=81-143.
DR   PDB; 3UA7; X-ray; 1.50 A; A/B/C/D=81-143.
DR   PDB; 4D8D; X-ray; 2.52 A; A/C=84-141.
DR   PDB; 4EIK; X-ray; 1.60 A; A=81-143.
DR   PDB; 4U17; X-ray; 1.99 A; A/B/C=148-248.
DR   PDB; 4U1P; X-ray; 1.40 A; A=148-248.
DR   PDB; 4ZNX; X-ray; 2.10 A; A/B/C/D=84-141.
DR   PDB; 5ZAU; NMR; -; A=85-141.
DR   PDB; 6EDF; X-ray; 1.40 A; A=83-146.
DR   PDB; 6IPY; X-ray; 1.34 A; A=82-144.
DR   PDB; 6IPZ; X-ray; 1.58 A; Z=82-144.
DR   PDBsum; 1A0N; -.
DR   PDBsum; 1AOT; -.
DR   PDBsum; 1AOU; -.
DR   PDBsum; 1AVZ; -.
DR   PDBsum; 1AZG; -.
DR   PDBsum; 1EFN; -.
DR   PDBsum; 1FYN; -.
DR   PDBsum; 1G83; -.
DR   PDBsum; 1M27; -.
DR   PDBsum; 1NYF; -.
DR   PDBsum; 1NYG; -.
DR   PDBsum; 1SHF; -.
DR   PDBsum; 1ZBJ; -.
DR   PDBsum; 2DQ7; -.
DR   PDBsum; 2MQI; -.
DR   PDBsum; 2MRJ; -.
DR   PDBsum; 2MRK; -.
DR   PDBsum; 3H0F; -.
DR   PDBsum; 3H0H; -.
DR   PDBsum; 3H0I; -.
DR   PDBsum; 3UA6; -.
DR   PDBsum; 3UA7; -.
DR   PDBsum; 4D8D; -.
DR   PDBsum; 4EIK; -.
DR   PDBsum; 4U17; -.
DR   PDBsum; 4U1P; -.
DR   PDBsum; 4ZNX; -.
DR   PDBsum; 5ZAU; -.
DR   PDBsum; 6EDF; -.
DR   PDBsum; 6IPY; -.
DR   PDBsum; 6IPZ; -.
DR   SMR; P06241; -.
DR   BioGRID; 108810; 211.
DR   CORUM; P06241; -.
DR   DIP; DIP-33876N; -.
DR   ELM; P06241; -.
DR   IntAct; P06241; 392.
DR   MINT; P06241; -.
DR   STRING; 9606.ENSP00000346671; -.
DR   BindingDB; P06241; -.
DR   ChEMBL; CHEMBL1841; -.
DR   DrugBank; DB01254; Dasatinib.
DR   DrugBank; DB12010; Fostamatinib.
DR   DrugBank; DB02078; Triglyme.
DR   DrugCentral; P06241; -.
DR   GuidetoPHARMACOLOGY; 2026; -.
DR   MoonDB; P06241; Predicted.
DR   iPTMnet; P06241; -.
DR   PhosphoSitePlus; P06241; -.
DR   SwissPalm; P06241; -.
DR   BioMuta; FYN; -.
DR   DMDM; 125370; -.
DR   CPTAC; CPTAC-1792; -.
DR   EPD; P06241; -.
DR   jPOST; P06241; -.
DR   MassIVE; P06241; -.
DR   MaxQB; P06241; -.
DR   PaxDb; P06241; -.
DR   PeptideAtlas; P06241; -.
DR   PRIDE; P06241; -.
DR   ProteomicsDB; 51877; -. [P06241-1]
DR   ProteomicsDB; 51878; -. [P06241-2]
DR   ProteomicsDB; 51879; -. [P06241-3]
DR   ABCD; P06241; 2 sequenced antibodies.
DR   Antibodypedia; 3559; 985 antibodies.
DR   DNASU; 2534; -.
DR   Ensembl; ENST00000229471; ENSP00000229471; ENSG00000010810. [P06241-3]
DR   Ensembl; ENST00000354650; ENSP00000346671; ENSG00000010810. [P06241-1]
DR   Ensembl; ENST00000368667; ENSP00000357656; ENSG00000010810. [P06241-1]
DR   Ensembl; ENST00000368678; ENSP00000357667; ENSG00000010810. [P06241-2]
DR   Ensembl; ENST00000368682; ENSP00000357671; ENSG00000010810. [P06241-2]
DR   Ensembl; ENST00000538466; ENSP00000440646; ENSG00000010810. [P06241-2]
DR   GeneID; 2534; -.
DR   KEGG; hsa:2534; -.
DR   UCSC; uc003pvh.3; human. [P06241-1]
DR   CTD; 2534; -.
DR   DisGeNET; 2534; -.
DR   EuPathDB; HostDB:ENSG00000010810.17; -.
DR   GeneCards; FYN; -.
DR   HGNC; HGNC:4037; FYN.
DR   HPA; ENSG00000010810; Low tissue specificity.
DR   MIM; 137025; gene.
DR   neXtProt; NX_P06241; -.
DR   OpenTargets; ENSG00000010810; -.
DR   PharmGKB; PA28454; -.
DR   eggNOG; KOG0197; Eukaryota.
DR   GeneTree; ENSGT00940000155462; -.
DR   HOGENOM; CLU_000288_7_2_1; -.
DR   InParanoid; P06241; -.
DR   KO; K05703; -.
DR   OMA; XWYFGKL; -.
DR   OrthoDB; 539311at2759; -.
DR   PhylomeDB; P06241; -.
DR   TreeFam; TF351634; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   PathwayCommons; P06241; -.
DR   Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR   Reactome; R-HSA-1227986; Signaling by ERBB2.
DR   Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR   Reactome; R-HSA-1433557; Signaling by SCF-KIT.
DR   Reactome; R-HSA-1433559; Regulation of KIT signaling.
DR   Reactome; R-HSA-164944; Nef and signal transduction.
DR   Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-HSA-2029481; FCGR activation.
DR   Reactome; R-HSA-210990; PECAM1 interactions.
DR   Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR   Reactome; R-HSA-2424491; DAP12 signaling.
DR   Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR   Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
DR   Reactome; R-HSA-373753; Nephrin family interactions.
DR   Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
DR   Reactome; R-HSA-389356; CD28 co-stimulation.
DR   Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR   Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
DR   Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
DR   Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR   Reactome; R-HSA-3928664; Ephrin signaling.
DR   Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR   Reactome; R-HSA-399954; Sema3A PAK dependent Axon repulsion.
DR   Reactome; R-HSA-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
DR   Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR   Reactome; R-HSA-418885; DCC mediated attractive signaling. [P06241-1]
DR   Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-HSA-5621480; Dectin-2 family.
DR   Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
DR   Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR   Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR   Reactome; R-HSA-8866376; Reelin signalling pathway.
DR   Reactome; R-HSA-9032500; Activated NTRK2 signals through FYN. [P06241-1]
DR   Reactome; R-HSA-9032759; NTRK2 activates RAC1. [P06241-1]
DR   Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR   Reactome; R-HSA-9607240; FLT3 Signaling.
DR   Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR   Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR   Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR   SignaLink; P06241; -.
DR   SIGNOR; P06241; -.
DR   BioGRID-ORCS; 2534; 4 hits in 901 CRISPR screens.
DR   ChiTaRS; FYN; human.
DR   EvolutionaryTrace; P06241; -.
DR   GeneWiki; FYN; -.
DR   GenomeRNAi; 2534; -.
DR   Pharos; P06241; Tclin.
DR   PRO; PR:P06241; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; P06241; protein.
DR   Bgee; ENSG00000010810; Expressed in corpus callosum and 243 other tissues.
DR   ExpressionAtlas; P06241; baseline and differential.
DR   Genevisible; P06241; HS.
DR   GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR   GO; GO:0044297; C:cell body; ISS:ARUK-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030425; C:dendrite; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005768; C:endosome; IDA:HGNC-UCL.
DR   GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0045121; C:membrane raft; IMP:ARUK-UCL.
DR   GO; GO:0005739; C:mitochondrion; ISS:ARUK-UCL.
DR   GO; GO:0005634; C:nucleus; ISS:ARUK-UCL.
DR   GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISS:ARUK-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:ARUK-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0014069; C:postsynaptic density; ISS:ARUK-UCL.
DR   GO; GO:0099092; C:postsynaptic density, intracellular component; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISS:ARUK-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042609; F:CD4 receptor binding; IEA:Ensembl.
DR   GO; GO:0042610; F:CD8 receptor binding; IEA:Ensembl.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0019899; F:enzyme binding; IPI:ARUK-UCL.
DR   GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR   GO; GO:0070851; F:growth factor receptor binding; IPI:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
DR   GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IMP:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR   GO; GO:0042608; F:T cell receptor binding; IEA:Ensembl.
DR   GO; GO:0048156; F:tau protein binding; ISS:ARUK-UCL.
DR   GO; GO:0050321; F:tau-protein kinase activity; NAS:ARUK-UCL.
DR   GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; ISS:ARUK-UCL.
DR   GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; TAS:Reactome.
DR   GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR   GO; GO:0006816; P:calcium ion transport; NAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IMP:ARUK-UCL.
DR   GO; GO:1905430; P:cellular response to glycine; ISS:ARUK-UCL.
DR   GO; GO:1905232; P:cellular response to L-glutamate; ISS:ARUK-UCL.
DR   GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR   GO; GO:0097062; P:dendritic spine maintenance; TAS:ARUK-UCL.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
DR   GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
DR   GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR   GO; GO:0003015; P:heart process; IGI:ARUK-UCL.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR   GO; GO:0007612; P:learning; TAS:ProtInc.
DR   GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR   GO; GO:1902951; P:negative regulation of dendritic spine maintenance; ISS:ARUK-UCL.
DR   GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0010730; P:negative regulation of hydrogen peroxide biosynthetic process; ISS:ARUK-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; ISS:ARUK-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR   GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
DR   GO; GO:0030168; P:platelet activation; TAS:Reactome.
DR   GO; GO:2001056; P:positive regulation of cysteine-type endopeptidase activity; ISS:ARUK-UCL.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR   GO; GO:1901216; P:positive regulation of neuron death; ISS:ARUK-UCL.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:1903997; P:positive regulation of non-membrane spanning protein tyrosine kinase activity; TAS:Reactome.
DR   GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; TAS:Reactome.
DR   GO; GO:1905477; P:positive regulation of protein localization to membrane; TAS:ARUK-UCL.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
DR   GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:ARUK-UCL.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:ARUK-UCL.
DR   GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; ISS:ARUK-UCL.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:ARUK-UCL.
DR   GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR   GO; GO:1900449; P:regulation of glutamate receptor signaling pathway; ISS:ARUK-UCL.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:ARUK-UCL.
DR   GO; GO:1904645; P:response to amyloid-beta; ISS:ARUK-UCL.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0042542; P:response to hydrogen peroxide; ISS:ARUK-UCL.
DR   GO; GO:0000304; P:response to singlet oxygen; ISS:ARUK-UCL.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
DR   CDD; cd12006; SH3_Fyn_Yrk; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR035750; Fyn/Yrk_SH3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Adaptive immunity; Alternative splicing; ATP-binding;
KW   Cell membrane; Cytoplasm; Developmental protein; Host-virus interaction;
KW   Immunity; Kinase; Lipoprotein; Manganese; Membrane; Metal-binding;
KW   Myristate; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
KW   Polymorphism; Proto-oncogene; Reference proteome; SH2 domain; SH3 domain;
KW   Transferase; Tyrosine-protein kinase.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..537
FT                   /note="Tyrosine-protein kinase Fyn"
FT                   /id="PRO_0000088099"
FT   DOMAIN          82..143
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          149..246
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          271..524
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         277..285
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        390
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         299
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         12
FT                   /note="Phosphothreonine; by PKC"
FT                   /evidence="ECO:0000269|PubMed:15537652"
FT   MOD_RES         21
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18088087,
FT                   ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976,
FT                   ECO:0000244|PubMed:19369195, ECO:0000244|PubMed:20068231,
FT                   ECO:0000244|PubMed:23186163"
FT   MOD_RES         26
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         185
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P39688"
FT   MOD_RES         420
FT                   /note="Phosphotyrosine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P39688"
FT   MOD_RES         531
FT                   /note="Phosphotyrosine; by CSK"
FT                   /evidence="ECO:0000244|PubMed:18691976,
FT                   ECO:0000269|PubMed:1699196"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000269|PubMed:1699196"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           6
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         233..287
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_024108"
FT   VAR_SEQ         234..287
FT                   /note="RAAGLCCRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNGQFGEV
FT                   WM -> KADGLCFNLTVIASSCTPQTSGLAKDAWEVARRSLCLEKKLGQGCFAEVWL
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:7822789"
FT                   /id="VSP_024110"
FT   VARIANT         243
FT                   /note="V -> L (in a lung squamous cell carcinoma sample;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041704"
FT   VARIANT         410
FT                   /note="G -> R (in a metastatic melanoma sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041705"
FT   VARIANT         445
FT                   /note="I -> F (in dbSNP:rs1801121)"
FT                   /id="VAR_014661"
FT   VARIANT         506
FT                   /note="D -> E (in dbSNP:rs28763975)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041706"
FT   CONFLICT        184
FT                   /note="A -> S (in Ref. 1; AAA36615)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        437
FT                   /note="A -> R (in Ref. 1; AAA36615 and 3; AAB33113)"
FT                   /evidence="ECO:0000305"
FT   STRAND          87..91
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   STRAND          97..100
FT                   /evidence="ECO:0000244|PDB:6EDF"
FT   STRAND          108..113
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   STRAND          116..124
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   TURN            125..127
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   STRAND          130..134
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   HELIX           135..137
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   STRAND          138..140
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   HELIX           141..143
FT                   /evidence="ECO:0000244|PDB:6IPY"
FT   HELIX           144..146
FT                   /evidence="ECO:0000244|PDB:1G83"
FT   STRAND          147..150
FT                   /evidence="ECO:0000244|PDB:1G83"
FT   HELIX           156..163
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   TURN            165..167
FT                   /evidence="ECO:0000244|PDB:1AOT"
FT   STRAND          172..177
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   STRAND          179..181
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   STRAND          185..193
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   TURN            194..196
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   STRAND          197..207
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   TURN            209..211
FT                   /evidence="ECO:0000244|PDB:1AOT"
FT   STRAND          213..216
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   STRAND          219..223
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   HELIX           224..233
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   STRAND          238..240
FT                   /evidence="ECO:0000244|PDB:4U1P"
FT   STRAND          263..265
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           268..270
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          271..278
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          285..290
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   TURN            291..293
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          294..299
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   TURN            303..305
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           308..318
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          329..333
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          335..337
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          339..343
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           350..354
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          355..357
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   TURN            358..360
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           364..383
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           393..395
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          396..399
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   TURN            400..402
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          403..406
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   STRAND          416..418
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   TURN            430..432
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           435..438
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           445..460
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           472..481
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           496..502
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           507..509
FT                   /evidence="ECO:0000244|PDB:2DQ7"
FT   HELIX           513..521
FT                   /evidence="ECO:0000244|PDB:2DQ7"
SQ   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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