P39688 (FYN_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase Fyn
EC=2.7.10.2

Alternative name(s):
Proto-oncogene c-Fyn
p59-Fyn

Gene names

Name:

Fyn

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	537 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motility through phosphorylation of CTNNB1 (beta-catenin) and CTNND1 (delta-catenin). Regulates cytoskeletal remodeling by phosphorylating several proteins including the actin regulator WAS and the microtubule-associated proteins MAP2 and MAPT. Promotes cell survival by phosphorylating AGAP2/PIKE-A and preventing its apoptotic cleavage. Participates in signal transduction pathways that regulate the integrity of the glomerular slit diaphragm (an essential part of the glomerular filter of the kidney) by phosphorylating several slit diaphragm components including NPHS1, KIRREL and TRPC6. Plays a role in neural processes by phosphorylating DPYSL2, a multifunctional adapter protein within the central nervous system, ARHGAP32, a regulator for Rho family GTPases implicated in various neural functions, and SNCA, a small pre-synaptic protein. Participates in the downstream signaling pathways that lead to T-cell differentiation and proliferation following T-cell receptor (TCR) stimulation. Also participates in negative feedback regulation of TCR signaling through phosphorylation of PAG1, thereby promoting interaction between PAG1 and CSK and recruitment of CSK to lipid rafts. CSK maintains LCK and FYN in an inactive form. Promotes CD28-induced phosphorylation of VAV1 By similarity. Ref.11 Ref.16 Ref.17 Ref.19
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
Cofactor	Manganese.
Enzyme regulation	Inhibited by phosphorylation of Tyr-531 by leukocyte common antigen and activated by dephosphorylation of this site. Ref.7
Subunit structure	Interacts (via its SH3 domain) with PIK3R1 and PRMT8. Interacts with FYB, PAG1, and SH2D1A. Interacts with CD79A (tyrosine-phosphorylated form); the interaction increases FYN activity. Interacts with TOM1L1 (phosphorylated form). Interacts with SH2D1A and SLAMF1. Interacts with and phosphorylates ITCH, down-regulating its activity. Interacts with FASLG. Interacts with RUNX3. Interacts with KIT. Interacts with EPHA8; possible downstream effector of EPHA8 in regulation of cell adhesion. Interacts with PTK2/FAK1; this interaction leads to PTK2/FAK1 phosphorylation and activation. Interacts with CAV1; this interaction couples integrins to the Ras-ERK pathway. Interacts (via SH3 domain) with KLHL2 (via N-terminus) By similarity. Interacts with KDR (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Ref.6 Ref.10 Ref.13 Ref.15 Ref.21
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity. Note: Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking By similarity. Ref.16 Ref.18
Tissue specificity	Isoform 1 is highly expressed in the brain, isoform 2 is expressed in cells of hemopoietic lineages, especially T-lymphocytes. Ref.5 Ref.11
Post-translational modification	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 By similarity. Ref.7 Palmitoylation at Cys-3 and Cys-6 regulates subcellular location. Ref.8 Ref.9 Ref.14 Myristoylation is required prior to palmitoylation. Ref.8 Ref.9 Ref.14
Disruption phenotype	Mice have various neural defects, including defective long term potentiation, impaired spatial memory, hypomyelination, abnormal dendrite orientation and uncoordinated hippocampal structure. Ref.5 Ref.25
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily. Contains 1 protein kinase domain. Contains 1 SH2 domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing
Disease	Proto-oncogene
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Manganese Metal-binding Nucleotide-binding
Molecular function	Developmental protein Kinase Transferase Tyrosine-protein kinase
PTM	Lipoprotein Myristate Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell receptor signaling pathway Inferred from electronic annotation. Source: Compara activated T cell proliferation Inferred from mutant phenotype PubMed 1516132. Source: MGI cell surface receptor signaling pathway Inferred from direct assay PubMed 9177270. Source: MGI cellular response to growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara dendrite morphogenesis Inferred from mutant phenotype PubMed 12372285. Source: MGI detection of mechanical stimulus involved in sensory perception of pain Inferred from mutant phenotype PubMed 16190898. Source: MGI forebrain development Inferred from mutant phenotype PubMed 15073522. Source: MGI myelination Traceable author statement PubMed 11826099. Source: MGI negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Inferred from electronic annotation. Source: Compara negative regulation of gene expression Inferred from mutant phenotype PubMed 20978343. Source: BHF-UCL negative regulation of protein catabolic process Inferred from mutant phenotype PubMed 16841086. Source: MGI neuron migration Inferred from mutant phenotype PubMed 15073522. Source: MGI peptidyl-tyrosine phosphorylation Inferred from direct assay PubMed 10872802PubMed 17923684PubMed 8175795PubMed 8196616. Source: MGI positive regulation of neuron projection development Inferred from genetic interaction PubMed 18354028. Source: MGI protein autophosphorylation Inferred from direct assay PubMed 8175795. Source: MGI regulation of cell shape Inferred from direct assay PubMed 11826099. Source: MGI response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from genetic interaction PubMed 9381182. Source: MGI
Cellular_component	cytosol Traceable author statement. Source: Reactome endosome Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic density Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from direct assay PubMed 10872802PubMed 16841086PubMed 17923684PubMed 8175795PubMed 8196616. Source: MGI tubulin binding Inferred from direct assay PubMed 11826099. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Dynlt1	P51807	3	EBI-524514,EBI-642797
Khdrbs1	Q60749	13	EBI-524514,EBI-519077
PLXNA2	O75051	3	EBI-524514,EBI-308264	From a different organism.
Sphk2	Q9JIA7	2	EBI-524514,EBI-985434

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P39688-1)

Also known as: B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P39688-2)

Also known as: T;

The sequence of this isoform differs from the canonical sequence as follows:
     234-236: RAA → KAD
     240-287: CRLVVPCHKG...GNGQFGEVWM → FNLTVVSSSC...GQGCFAEVWL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 537

537

Tyrosine-protein kinase Fyn

PRO_0000088100

Regions

Domain

82 – 143

62

SH3

Domain

149 – 246

98

SH2

Domain

271 – 524

254

Protein kinase

Nucleotide binding

277 – 285

9

ATP By similarity

Sites

Active site

390

1

Proton acceptor By similarity

Binding site

299

1

ATP By similarity

Amino acid modifications

Modified residue

15

1

Phosphothreonine By similarity

Modified residue

21

1

Phosphoserine

Modified residue

25

1

Phosphoserine By similarity

Modified residue

185

1

Phosphotyrosine Ref.22

Modified residue

213

1

Phosphotyrosine By similarity

Modified residue

214

1

Phosphotyrosine By similarity

Modified residue

254

1

Phosphothreonine Ref.24

Modified residue

257

1

Phosphoserine Ref.24

Modified residue

420

1

Phosphotyrosine; by autocatalysis Ref.7 Ref.23

Modified residue

440

1

Phosphotyrosine By similarity

Modified residue

512

1

Phosphothreonine By similarity

Modified residue

531

1

Phosphotyrosine; by CSK By similarity

Lipidation

2

1

N-myristoyl glycine Ref.12

Lipidation

3

1

S-palmitoyl cysteine Ref.8 Ref.9 Ref.14

Lipidation

6

1

S-palmitoyl cysteine Probable

Natural variations

Alternative sequence

234 – 236

3

RAA → KAD in isoform 2.

VSP_024111

Alternative sequence

240 – 287

48

CRLVV…GEVWM → FNLTVVSSSCTPQTSGLAKD AWEVARDSLFLEKKLGQGCF AEVWL in isoform 2.

VSP_024112

Experimental info

Mutagenesis

2

1

G → A: Abolishes myristoylation and palmitoylation. Ref.9

Mutagenesis

3

1

C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-6. Ref.8 Ref.9 Ref.14

Mutagenesis

3

1

C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-6. Abolishes plasma membrane association. Ref.8 Ref.9 Ref.14

Mutagenesis

6

1

C → A: Abolishes palmitoylation and plasma membrane association; when associated with A-3. Ref.8 Ref.9

Mutagenesis

6

1

C → S: Abolishes palmitoylation and plasma membrane association; when associated with S-3. Ref.8 Ref.9

Sequence conflict

179

1

E → Q in AAA37644. Ref.1

Sequence conflict

179

1

E → Q in AAB09568. Ref.2

Sequence conflict

432

1

W → R in BAE42585. Ref.3

Secondary structure

1

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537

Helix Strand Turn

Details...

Beta strand

87 – 91

5

Beta strand

108 – 113

6

Beta strand

115 – 124

10

Turn

125 – 127

3

Beta strand

130 – 134

5

Helix

135 – 137

3

Beta strand

138 – 140

3

Helix

156 – 163

8

Beta strand

173 – 177

5

Beta strand

179 – 181

3

Beta strand

185 – 192

8

Beta strand

194 – 207

14

Beta strand

213 – 216

4

Beta strand

221 – 223

3

Helix

224 – 233

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (B) [UniParc]. Last modified April 3, 2013. Version 4. Checksum: 99558702596DAEE0	FASTA	537	60,675
	10 20 30 40 50 60 MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 70 80 90 100 110 120 LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 130 140 150 160 170 180 EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 190 200 210 220 230 240 TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC 250 260 270 280 290 300 RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWMGTW NGNTKVAIKT 310 320 330 340 350 360 LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR 370 380 390 400 410 420 ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY 430 440 450 460 470 480 TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE 490 500 510 520 530 RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL
	Isoform 2 (T) [UniParc]. Checksum: 782C93B2003B7DCD	FASTA	534	60,059
	10 20 30 40 50 60 MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG 70 80 90 100 110 120 LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW 130 140 150 160 170 180 EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET 190 200 210 220 230 240 TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSEKADGLCF 250 260 270 280 290 300 NLTVVSSSCT PQTSGLAKDA WEVARDSLFL EKKLGQGCFA EVWLGTWNGN TKVAIKTLKP 310 320 330 340 350 360 GTMSPESFLE EAQIMKKLKH DKLVQLYAVV SEEPIYIVTE YMSKGSLLDF LKDGEGRALK 370 380 390 400 410 420 LPNLVDMAAQ VAAGMAYIER MNYIHRDLRS ANILVGNGLI CKIADFGLAR LIEDNEYTAR 430 440 450 460 470 480 QGAKFPIKWT APEAALYGRF TIKSDVWSFG ILLTELVTKG RVPYPGMNNR EVLEQVERGY 490 500 510 520 530 RMPCPQDCPI SLHELMIHCW KKDPEERPTF EYLQGFLEDY FTATEPQYQP GENL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a novel form of the fyn proto-oncogene in hematopoietic cells." Cooke M.P., Perlmutter R.M. New Biol. 1:66-74(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Two species of mRNAs for the fyn proto-oncogene are produced by an alternative polyadenylation." Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H. Mol. Cells 8:746-749(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: T-cell.
[3]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: NOD. Tissue: Spleen.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6 and FVB/N. Tissue: Brain and Mammary tumor.
[5]	"Impaired long-term potentiation, spatial learning, and hippocampal development in fyn mutant mice." Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P., Kandel E.R. Science 258:1903-1910(1992) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[6]	"Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor." Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D., Roussel M.F. EMBO J. 12:943-950(1993) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSF1R.
[7]	"Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases." Hurley T.R., Hyman R., Sefton B.M. Mol. Cell. Biol. 13:1651-1656(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-531, AUTOPHOSPHORYLATION AT TYR-420, ENZYME REGULATION.
[8]	"Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins." Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M. Mol. Cell. Biol. 13:6385-6392(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF CYS-3 AND CYS-6.
[9]	"Palmitoylation of multiple Src-family kinases at a homologous N-terminal motif." Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I. Biochem. J. 303:749-753(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-3 AND CYS-6, MUTAGENESIS OF GLY-2; CYS-3 AND CYS-6.
[10]	"Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity." Clark M.R., Johnson S.A., Cambier J.C. EMBO J. 13:1911-1919(1994) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CD79A.
[11]	"Unique catalytic properties dictate the enhanced function of p59fynT, the hemopoietic cell-specific isoform of the Fyn tyrosine protein kinase, in T cells." Davidson D., Viallet J., Veillette A. Mol. Cell. Biol. 14:4554-4564(1994) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]	"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." Gauen L.K.T., Linder M.E., Shaw A.S. J. Cell Biol. 133:1007-1015(1996) [PubMed] [Europe PMC] [Abstract] Cited for: MYRISTOYLATION AT GLY-2.
[13]	"Sequential activation of phoshatidylinositol 3-kinase and phospholipase C-gamma2 by the M-CSF receptor is necessary for differentiation signaling." Bourette R.P., Myles G.M., Choi J.L., Rohrschneider L.R. EMBO J. 16:5880-5893(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CSF1R.
[14]	"Palmitoylation of p59fyn is reversible and sufficient for plasma membrane association." Wolven A., Okamura H., Rosenblatt Y., Resh M.D. Mol. Biol. Cell 8:1159-1173(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION AT CYS-3, MUTAGENESIS OF CYS-3.
[15]	"'Srcasm: a novel Src activating and signaling molecule." Seykora J.T., Mei L., Dotto G.P., Stein P.L. J. Biol. Chem. 277:2812-2822(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TOM1L1.
[16]	"Fyn is essential for tyrosine phosphorylation of Csk-binding protein/phosphoprotein associated with glycolipid-enriched microdomains in lipid rafts in resting T cells." Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T., Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A. J. Immunol. 169:2813-2817(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[17]	"p120 Catenin-associated Fer and Fyn tyrosine kinases regulate beta-catenin Tyr-142 phosphorylation and beta-catenin-alpha-catenin Interaction." Piedra J., Miravet S., Castano J., Palmer H.G., Heisterkamp N., Garcia de Herreros A., Dunach M. Mol. Cell. Biol. 23:2287-2297(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CTNNB1.
[18]	"Transmembrane phosphoprotein Cbp senses cell adhesion signaling mediated by Src family kinase in lipid rafts." Shima T., Nada S., Okada M. Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[19]	"Phosphorylation of tau by fyn: implications for Alzheimer's disease." 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. J. Neurosci. 24:2304-2312(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT.
[20]	"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor." Roskoski R. Jr. Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[21]	"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." Lamalice L., Houle F., Huot J. J. Biol. Chem. 281:34009-34020(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KDR.
[22]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, MASS SPECTROMETRY. Tissue: Brain.
[23]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-420, MASS SPECTROMETRY. Tissue: Macrophage.
[24]	"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-257, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
[25]	"Decreased dendritic spine density and abnormal spine morphology in Fyn knockout mice." 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. Brain Res. 1415:96-102(2011) [PubMed] [Europe PMC] [Abstract] Cited for: DISRUPTION PHENOTYPE.
[26]	"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." Joint center for structural genomics (JCSG) Submitted (DEC-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 81-239.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M27266 mRNA. Translation: AAA37644.1.
U70324 mRNA. Translation: AAB09568.1.
AK156584 mRNA. Translation: BAE33766.1.
AK171646 mRNA. Translation: BAE42585.1.
BC032149 mRNA. Translation: AAH32149.1.
BC092217 mRNA. Translation: AAH92217.1.

IPI

IPI00322097.
IPI00762435.

PIR

A44991.

RefSeq

NP_001116364.1. NM_001122892.1.
NP_001116365.1. NM_001122893.1.
NP_032080.2. NM_008054.2.

UniGene

Mm.4848.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3UF4	X-ray	1.98	A	81-239	[»]

ProteinModelPortal

P39688.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-198N.

IntAct

P39688. 15 interactions.

MINT

MINT-85422.

PTM databases

PhosphoSite

P39688.

Proteomic databases

PaxDb

P39688.

PRIDE

P39688.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843.
ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843.
ENSMUST00000126486; ENSMUSP00000115233; ENSMUSG00000019843.
ENSMUST00000135242; ENSMUSP00000117111; ENSMUSG00000019843.
ENSMUST00000146287; ENSMUSP00000114188; ENSMUSG00000019843.

GeneID

14360.

KEGG

mmu:14360.

UCSC

uc007evx.2. mouse.
uc007evy.2. mouse.

Organism-specific databases

CTD

2534.

MGI

MGI:95602. Fyn.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00620000087702.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

InParanoid

P39688.

KO

K05703.

OrthoDB

EOG41ZF9H.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.
REACT_115202. Signal Transduction.
REACT_115433. Developmental Biology.
REACT_127416. Developmental Biology.

Gene expression databases

ArrayExpress

P39688.

Bgee

P39688.

CleanEx

MM_FYN.

Genevestigator

P39688.

GermOnline

ENSMUSG00000019843. Mus musculus.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P39688.

ChEMBL

CHEMBL4517.

ChiTaRS

FYN. mouse.

NextBio

285821.

SOURCE

Search...

Entry information

Entry name

FYN_MOUSE

Accession

Primary (citable) accession number: P39688
Secondary accession number(s): Q3TAT3, Q3U0T5, Q8K2A3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	April 3, 2013
Last modified:	May 1, 2013
This is version 137 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program