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Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn)

 FYN_MOUSE               Reviewed;         537 AA.
P39688; Q3TAT3; Q3U0T5; Q8K2A3;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
03-APR-2013, sequence version 4.
22-NOV-2017, entry version 188.
RecName: Full=Tyrosine-protein kinase Fyn;
EC=2.7.10.2;
AltName: Full=Proto-oncogene c-Fyn;
AltName: Full=p59-Fyn;
Name=Fyn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=2488273;
Cooke M.P., Perlmutter R.M.;
"Expression of a novel form of the fyn proto-oncogene in hematopoietic
cells.";
New Biol. 1:66-74(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=T-cell;
PubMed=9895129;
Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H.;
"Two species of mRNAs for the fyn proto-oncogene are produced by an
alternative polyadenylation.";
Mol. Cells 8:746-749(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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).
[5]
TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=1361685; DOI=10.1126/science.1361685;
Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P.,
Kandel E.R.;
"Impaired long-term potentiation, spatial learning, and hippocampal
development in fyn mutant mice.";
Science 258:1903-1910(1992).
[6]
INTERACTION WITH CSF1R.
PubMed=7681396;
Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D.,
Roussel M.F.;
"Activation of Src family kinases by colony stimulating factor-1, and
their association with its receptor.";
EMBO J. 12:943-950(1993).
[7]
PHOSPHORYLATION AT TYR-420 AND TYR-531, AND ENZYME REGULATION.
PubMed=8441403; DOI=10.1128/MCB.13.3.1651;
Hurley T.R., Hyman R., Sefton B.M.;
"Differential effects of expression of the CD45 tyrosine protein
phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src
tyrosine protein kinases.";
Mol. Cell. Biol. 13:1651-1656(1993).
[8]
PALMITOYLATION AT CYS-3 AND CYS-6, AND MUTAGENESIS OF CYS-3 AND CYS-6.
PubMed=8413237; DOI=10.1128/MCB.13.10.6385;
Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.;
"Palmitylation of an amino-terminal cysteine motif of protein tyrosine
kinases p56lck and p59fyn mediates interaction with glycosyl-
phosphatidylinositol-anchored proteins.";
Mol. Cell. Biol. 13:6385-6392(1993).
[9]
PALMITOYLATION AT CYS-3 AND CYS-6, AND MUTAGENESIS OF GLY-2; CYS-3 AND
CYS-6.
PubMed=7980442; DOI=10.1042/bj3030749;
Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.;
"Palmitoylation of multiple Src-family kinases at a homologous N-
terminal motif.";
Biochem. J. 303:749-753(1994).
[10]
INTERACTION WITH CD79A.
PubMed=8168489;
Clark M.R., Johnson S.A., Cambier J.C.;
"Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels
of binding specificity and tyrosine phosphorylated Ig-alpha
stimulation of Fyn activity.";
EMBO J. 13:1911-1919(1994).
[11]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8007959; DOI=10.1128/MCB.14.7.4554;
Davidson D., Viallet J., Veillette A.;
"Unique catalytic properties dictate the enhanced function of p59fynT,
the hemopoietic cell-specific isoform of the Fyn tyrosine protein
kinase, in T cells.";
Mol. Cell. Biol. 14:4554-4564(1994).
[12]
MYRISTOYLATION AT GLY-2.
PubMed=8655574; DOI=10.1083/jcb.133.5.1007;
Gauen L.K.T., Linder M.E., Shaw A.S.;
"Multiple features of the p59fyn src homology 4 domain define a motif
for immune-receptor tyrosine-based activation motif (ITAM) binding and
for plasma membrane localization.";
J. Cell Biol. 133:1007-1015(1996).
[13]
INTERACTION WITH CSF1R.
PubMed=9312046; DOI=10.1093/emboj/16.19.5880;
Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R.;
"Sequential activation of phoshatidylinositol 3-kinase and
phospholipase C-gamma2 by the M-CSF receptor is necessary for
differentiation signaling.";
EMBO J. 16:5880-5893(1997).
[14]
PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF CYS-3.
PubMed=9201723; DOI=10.1091/mbc.8.6.1159;
Wolven A., Okamura H., Rosenblatt Y., Resh M.D.;
"Palmitoylation of p59fyn is reversible and sufficient for plasma
membrane association.";
Mol. Biol. Cell 8:1159-1173(1997).
[15]
INTERACTION WITH TOM1L1.
PubMed=11711534; DOI=10.1074/jbc.M106813200;
Seykora J.T., Mei L., Dotto G.P., Stein P.L.;
"'Srcasm: a novel Src activating and signaling molecule.";
J. Biol. Chem. 277:2812-2822(2002).
[16]
FUNCTION, AND 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).
[17]
FUNCTION IN PHOSPHORYLATION OF CTNNB1.
PubMed=12640114; DOI=10.1128/MCB.23.7.2287-2297.2003;
Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N.,
Garcia de Herreros A., Dunach M.;
"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-
catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin
Interaction.";
Mol. Cell. Biol. 23:2287-2297(2003).
[18]
SUBCELLULAR LOCATION.
PubMed=14645715; DOI=10.1073/pnas.2432139100;
Shima T., Nada S., Okada M.;
"Transmembrane phosphoprotein Cbp senses cell adhesion signaling
mediated by Src family kinase in lipid rafts.";
Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003).
[19]
FUNCTION IN PHOSPHORYLATION OF MAPT.
PubMed=14999081; DOI=10.1523/JNEUROSCI.4162-03.2004;
Lee G., Thangavel R., Sharma V.M., Litersky J.M., Bhaskar K.,
Fang S.M., Do L.H., Andreadis A., Van Hoesen G., Ksiezak-Reding H.;
"Phosphorylation of tau by fyn: implications for Alzheimer's
disease.";
J. Neurosci. 24:2304-2312(2004).
[20]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=16129412; DOI=10.1016/j.bbrc.2005.08.055;
Roskoski R. Jr.;
"Signaling by Kit protein-tyrosine kinase--the stem cell factor
receptor.";
Biochem. Biophys. Res. Commun. 337:1-13(2005).
[21]
INTERACTION WITH KDR.
PubMed=16966330; DOI=10.1074/jbc.M603928200;
Lamalice L., Houle F., Huot J.;
"Phosphorylation of Tyr1214 within VEGFR-2 triggers the recruitment of
Nck and activation of Fyn leading to SAPK2/p38 activation and
endothelial cell migration in response to VEGF.";
J. Biol. Chem. 281:34009-34020(2006).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[25]
INTERACTION WITH PTPRH; PTPRO AND PTPRB.
PubMed=20398064; DOI=10.1111/j.1365-2443.2010.01398.x;
Murata Y., Mori M., Kotani T., Supriatna Y., Okazawa H., Kusakari S.,
Saito Y., Ohnishi H., Matozaki T.;
"Tyrosine phosphorylation of R3 subtype receptor-type protein tyrosine
phosphatases and their complex formations with Grb2 or Fyn.";
Genes Cells 15:513-524(2010).
[26]
DISRUPTION PHENOTYPE.
PubMed=21872217; DOI=10.1016/j.brainres.2011.07.059;
Babus L.W., Little E.M., Keenoy K.E., Minami S.S., Chen E., Song J.M.,
Caviness J., Koo S.Y., Pak D.T., Rebeck G.W., Turner R.S., Hoe H.S.;
"Decreased dendritic spine density and abnormal spine morphology in
Fyn knockout mice.";
Brain Res. 1415:96-102(2011).
[27]
X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 81-239.
Joint center for structural genomics (JCSG);
"Crystal structure of a SH3 and SH2 domains of fyn protein (proto-
concogene tyrosine-protein kinase fyn) from Mus musculus at 1.98 a
resolution.";
Submitted (DEC-2011) to the PDB data bank.
-!- 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,
KIRREL1 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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12640114,
ECO:0000269|PubMed:14999081, ECO:0000269|PubMed:8007959}.
-!- 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. {ECO:0000269|PubMed:8441403}.
-!- SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8 (By
similarity). Interacts with FYB1, PAG1, and SH2D1A (By
similarity). Interacts with CD79A (tyrosine-phosphorylated form);
the interaction increases FYN activity (PubMed:8168489). Interacts
with TOM1L1 (phosphorylated form) (PubMed:11711534). Interacts
with SH2D1A and SLAMF1 (By similarity). Interacts with and
phosphorylates ITCH, down-regulating its activity (By similarity).
Interacts with FASLG (By similarity). Interacts with RUNX3 (By
similarity). Interacts with KIT (By similarity). Interacts with
EPHA8; possible downstream effector of EPHA8 in regulation of cell
adhesion (By similarity). Interacts with PTK2/FAK1; this
interaction leads to PTK2/FAK1 phosphorylation and activation (By
similarity). Interacts with CAV1; this interaction couples
integrins to the Ras-ERK pathway (By similarity). Interacts (via
SH3 domain) with KLHL2 (via N-terminus) (By similarity). Interacts
with KDR (tyrosine phosphorylated) (PubMed:16966330). Interacts
(via SH2 domain) with CSF1R (tyrosine phosphorylated)
(PubMed:7681396, PubMed:9312046). Interacts with UNC119 (By
similarity). Interacts (via SH2 domain) with PTPRH (phosphorylated
form) (PubMed:20398064). Interacts with PTPRO (phosphorylated
form) (PubMed:20398064). Interacts with PTPRB (phosphorylated
form) (PubMed:20398064). Interacts with FYB2 (By similarity).
{ECO:0000250|UniProtKB:P06241, ECO:0000250|UniProtKB:Q62844,
ECO:0000269|PubMed:11711534, ECO:0000269|PubMed:16966330,
ECO:0000269|PubMed:20398064, ECO:0000269|PubMed:7681396,
ECO:0000269|PubMed:8168489, ECO:0000269|PubMed:9312046}.
-!- INTERACTION:
P22681:CBL (xeno); NbExp=3; IntAct=EBI-524514, EBI-518228;
P22682:Cbl; NbExp=5; IntAct=EBI-524514, EBI-640919;
P51807:Dynlt1; NbExp=3; IntAct=EBI-524514, EBI-642797;
Q14332:FZD2 (xeno); NbExp=4; IntAct=EBI-524514, EBI-6254477;
P35570:Irs1 (xeno); NbExp=4; IntAct=EBI-524514, EBI-520230;
Q60749:Khdrbs1; NbExp=15; IntAct=EBI-524514, EBI-519077;
Q9WU01:Khdrbs2; NbExp=2; IntAct=EBI-524514, EBI-8339046;
P05622:Pdgfrb; NbExp=3; IntAct=EBI-524514, EBI-1554855;
O75051:PLXNA2 (xeno); NbExp=3; IntAct=EBI-524514, EBI-308264;
P18433:PTPRA (xeno); NbExp=2; IntAct=EBI-524514, EBI-2609645;
Q9QUM4:Slamf1; NbExp=4; IntAct=EBI-524514, EBI-7910086;
Q9JIA7:Sphk2; NbExp=2; IntAct=EBI-524514, EBI-985434;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Cell membrane {ECO:0000250}. Note=Present and
active in lipid rafts. Palmitoylation is crucial for proper
trafficking (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=B;
IsoId=P39688-1; Sequence=Displayed;
Name=2; Synonyms=T;
IsoId=P39688-2; Sequence=VSP_024111, VSP_024112;
-!- 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:1361685,
ECO:0000269|PubMed:8007959}.
-!- PTM: Autophosphorylated at Tyr-420. Phosphorylation on the C-
terminal tail at Tyr-531 by CSK maintains the enzyme in an
inactive state. PTPRC/CD45 dephosphorylates Tyr-531 leading to
activation. Ultraviolet B (UVB) strongly increase phosphorylation
at Thr-15 and kinase activity, and promotes translocation from the
cytoplasm to the nucleus. Dephosphorylation at Tyr-420 by PTPN2
negatively regulates T-cell receptor signaling (By similarity).
{ECO:0000250}.
-!- PTM: Palmitoylation at Cys-3 and Cys-6 regulates subcellular
location. {ECO:0000269|PubMed:7980442, ECO:0000269|PubMed:8413237,
ECO:0000269|PubMed:9201723}.
-!- PTM: Myristoylation is required prior to palmitoylation.
{ECO:0000269|PubMed:8655574}.
-!- DISRUPTION PHENOTYPE: Mice have various neural defects, including
defective long term potentiation, impaired spatial memory,
hypomyelination, abnormal dendrite orientation and uncoordinated
hippocampal structure. {ECO:0000269|PubMed:1361685,
ECO:0000269|PubMed:21872217}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; M27266; AAA37644.1; -; mRNA.
EMBL; U70324; AAB09568.1; -; mRNA.
EMBL; AK156584; BAE33766.1; -; mRNA.
EMBL; AK171646; BAE42585.1; -; mRNA.
EMBL; BC032149; AAH32149.1; -; mRNA.
EMBL; BC092217; AAH92217.1; -; mRNA.
CCDS; CCDS23788.1; -. [P39688-2]
CCDS; CCDS48538.1; -. [P39688-1]
PIR; A44991; A44991.
RefSeq; NP_001116364.1; NM_001122892.1. [P39688-2]
RefSeq; NP_001116365.1; NM_001122893.1. [P39688-1]
RefSeq; NP_032080.2; NM_008054.2. [P39688-2]
RefSeq; XP_006512602.1; XM_006512539.3. [P39688-1]
RefSeq; XP_006512603.1; XM_006512540.3. [P39688-1]
RefSeq; XP_011241419.1; XM_011243117.2. [P39688-1]
UniGene; Mm.4848; -.
PDB; 3UF4; X-ray; 1.98 A; A=82-244.
PDBsum; 3UF4; -.
ProteinModelPortal; P39688; -.
SMR; P39688; -.
BioGrid; 199773; 15.
CORUM; P39688; -.
DIP; DIP-198N; -.
ELM; P39688; -.
IntAct; P39688; 41.
MINT; MINT-85422; -.
STRING; 10090.ENSMUSP00000097547; -.
BindingDB; P39688; -.
ChEMBL; CHEMBL4517; -.
iPTMnet; P39688; -.
PhosphoSitePlus; P39688; -.
SwissPalm; P39688; -.
EPD; P39688; -.
MaxQB; P39688; -.
PaxDb; P39688; -.
PeptideAtlas; P39688; -.
PRIDE; P39688; -.
Ensembl; ENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843. [P39688-2]
Ensembl; ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843. [P39688-1]
Ensembl; ENSMUST00000126486; ENSMUSP00000115233; ENSMUSG00000019843. [P39688-2]
Ensembl; ENSMUST00000135242; ENSMUSP00000117111; ENSMUSG00000019843. [P39688-2]
Ensembl; ENSMUST00000146287; ENSMUSP00000114188; ENSMUSG00000019843. [P39688-2]
GeneID; 14360; -.
KEGG; mmu:14360; -.
UCSC; uc007evx.2; mouse. [P39688-1]
UCSC; uc007evy.2; mouse. [P39688-2]
CTD; 2534; -.
MGI; MGI:95602; Fyn.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P39688; -.
KO; K05703; -.
OMA; SHNSGYR; -.
OrthoDB; EOG091G0D46; -.
TreeFam; TF351634; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-373753; Nephrin family interactions.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-389356; CD28 co-stimulation.
Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-MMU-399954; Sema3A PAK dependent Axon repulsion.
Reactome; R-MMU-399955; SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
Reactome; R-MMU-399956; CRMPs in Sema3A signaling.
Reactome; R-MMU-418885; DCC mediated attractive signaling.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-75892; Platelet Adhesion to exposed collagen.
Reactome; R-MMU-8866376; Reelin signalling pathway.
Reactome; R-MMU-912631; Regulation of signaling by CBL.
ChiTaRS; Fyn; mouse.
PRO; PR:P39688; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019843; -.
CleanEx; MM_FYN; -.
ExpressionAtlas; P39688; baseline and differential.
Genevisible; P39688; MM.
GO; GO:0005884; C:actin filament; IDA:MGI.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030425; C:dendrite; IMP:ParkinsonsUK-UCL.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0014069; C:postsynaptic density; IMP: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; ISO:MGI.
GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
GO; GO:0046875; F:ephrin receptor binding; ISO:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0070851; F:growth factor receptor binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
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:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
GO; GO:0004871; F:signal transducer activity; IGI:ARUK-UCL.
GO; GO:0042608; F:T cell receptor binding; IEA:Ensembl.
GO; GO:0015631; F:tubulin binding; IDA:MGI.
GO; GO:0031802; F:type 5 metabotropic glutamate receptor binding; IEA:Ensembl.
GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:MGI.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IGI:MGI.
GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0042552; P:myelination; TAS:MGI.
GO; GO:1902951; P:negative regulation of dendritic spine maintenance; IGI:ARUK-UCL.
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; IMP:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:MGI.
GO; GO:0001764; P:neuron migration; IMP:MGI.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IGI:MGI.
GO; GO:1901216; P:positive regulation of neuron death; IGI:ARUK-UCL.
GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:MGI.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IGI:ARUK-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:CACAO.
GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:1905664; P:regulation of calcium ion import across plasma membrane; IGI:ARUK-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IGI:ARUK-UCL.
GO; GO:1904645; P:response to amyloid-beta; IGI:ARUK-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IGI:MGI.
GO; GO:0050852; P:T cell receptor signaling pathway; ISO:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd12006; SH3_Fyn_Yrk; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035750; Fyn/Yrk_SH3.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
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;
Immunity; Kinase; Lipoprotein; Manganese; Membrane; Metal-binding;
Myristate; Nucleotide-binding; Nucleus; Palmitate; Phosphoprotein;
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_0000088100.
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 21 21 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:P06241}.
MOD_RES 124 124 Phosphoserine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 181 181 Phosphothreonine.
{ECO:0000250|UniProtKB:P06239}.
MOD_RES 185 185 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 214 214 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06240}.
MOD_RES 420 420 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8441403}.
MOD_RES 531 531 Phosphotyrosine.
{ECO:0000244|PubMed:18034455,
ECO:0000269|PubMed:8441403}.
MOD_RES 531 531 Phosphotyrosine; by CSK. {ECO:0000250}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:8655574}.
LIPID 3 3 S-palmitoyl cysteine.
{ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237,
ECO:0000269|PubMed:9201723}.
LIPID 6 6 S-palmitoyl cysteine.
{ECO:0000305|PubMed:7980442,
ECO:0000305|PubMed:8413237}.
VAR_SEQ 234 236 RAA -> KAD (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2488273,
ECO:0000303|PubMed:9895129}.
/FTId=VSP_024111.
VAR_SEQ 240 287 CRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNG
QFGEVWM -> FNLTVVSSSCTPQTSGLAKDAWEVARDSLF
LEKKLGQGCFAEVWL (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2488273,
ECO:0000303|PubMed:9895129}.
/FTId=VSP_024112.
MUTAGEN 2 2 G->A: Abolishes myristoylation and
palmitoylation.
{ECO:0000269|PubMed:7980442}.
MUTAGEN 3 3 C->A: Abolishes palmitoylation and plasma
membrane association; when associated
with A-6. {ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237,
ECO:0000269|PubMed:9201723}.
MUTAGEN 3 3 C->S: Abolishes palmitoylation and plasma
membrane association; when associated
with S-6. Abolishes plasma membrane
association. {ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237,
ECO:0000269|PubMed:9201723}.
MUTAGEN 6 6 C->A: Abolishes palmitoylation and plasma
membrane association; when associated
with A-3. {ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
MUTAGEN 6 6 C->S: Abolishes palmitoylation and plasma
membrane association; when associated
with S-3. {ECO:0000269|PubMed:7980442,
ECO:0000269|PubMed:8413237}.
CONFLICT 179 179 E -> Q (in Ref. 1; AAA37644 and 2;
AAB09568). {ECO:0000305}.
CONFLICT 432 432 W -> R (in Ref. 3; BAE42585).
{ECO:0000305}.
STRAND 87 91 {ECO:0000244|PDB:3UF4}.
STRAND 108 113 {ECO:0000244|PDB:3UF4}.
STRAND 115 124 {ECO:0000244|PDB:3UF4}.
TURN 125 127 {ECO:0000244|PDB:3UF4}.
STRAND 130 134 {ECO:0000244|PDB:3UF4}.
HELIX 135 137 {ECO:0000244|PDB:3UF4}.
STRAND 138 140 {ECO:0000244|PDB:3UF4}.
HELIX 156 163 {ECO:0000244|PDB:3UF4}.
STRAND 173 177 {ECO:0000244|PDB:3UF4}.
STRAND 179 181 {ECO:0000244|PDB:3UF4}.
STRAND 185 192 {ECO:0000244|PDB:3UF4}.
STRAND 194 207 {ECO:0000244|PDB:3UF4}.
STRAND 213 216 {ECO:0000244|PDB:3UF4}.
STRAND 221 223 {ECO:0000244|PDB:3UF4}.
HELIX 224 233 {ECO:0000244|PDB:3UF4}.
STRAND 238 240 {ECO:0000244|PDB:3UF4}.
SEQUENCE 537 AA; 60675 MW; 99558702596DAEE0 CRC64;
MGCVQCKDKE AAKLTEERDG 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 VTEYMSKGSL LDFLKDGEGR
ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY
TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL


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