MOUSE:FYN

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Species (Taxon ID)	Mus musculus (Mouse). (taxon:10090)
Gene Name(s)	Fyn
Protein Name(s)	Tyrosine-protein kinase Fyn Proto-oncogene c-Fyn p59-Fyn
External Links
UniProt Identifier	FYN_MOUSE
UniProt Accessions	P39688, Q3TAT3, Q3U0T5, Q8K2A3,
EMBL	M27266, U70324, AK156584, AK171646, BC032149, BC092217,
PIR	A44991,
RefSeq	NP_001116364.1, NP_001116365.1, NP_032080.2,
IntAct	P39688,
Ensembl	ENSMUST00000063091, ENSMUST00000126486, ENSMUST00000135242, ENSMUST00000146287,
Pfam	PF07714, PF00017, PF00018,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005829	cytosol		EXP: Inferred from Experiment		C	Source: Reactome
	GO:0005886	plasma membrane		IEA: Inferred from Electronic Annotation		C	Source: UniProtKB-SubCell
	GO:0005524	ATP binding		IEA: Inferred from Electronic Annotation		F	Source: UniProtKB-KW
	GO:0046872	metal ion binding		IEA: Inferred from Electronic Annotation		F	Source: UniProtKB-KW
	GO:0004715	non-membrane spanning protein tyrosine kinase activity		IEA: Inferred from Electronic Annotation		F	Source: EC
	GO:0015631	tubulin binding		IDA: Inferred from Direct Assay		F	Source: MGI
	GO:0050798	activated T cell proliferation		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0050966	detection of mechanical stimulus involved in sensory perception of pain		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0030900	forebrain development		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0042552	myelination		TAS: Traceable Author Statement		P	Source: MGI
	GO:0042177	negative regulation of protein catabolic process		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0001764	neuron migration		IMP: Inferred from Mutant Phenotype		P	Source: MGI
	GO:0018108	peptidyl-tyrosine phosphorylation		IDA: Inferred from Direct Assay		P	Source: MGI
	GO:0046777	protein autophosphorylation		IDA: Inferred from Direct Assay		P	Source: MGI
	GO:0008360	regulation of cell shape		IDA: Inferred from Direct Assay		P	Source: MGI
	GO:0045471	response to ethanol		IGI: Inferred from Genetic Interaction		P	Source: MGI
	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:20978343^[1]	IDA: Inferred from Direct Assay		P	Treatment of WT VSMCs with 1-(Palmitoyl)- 2-(5-keto-6-octene-dioyl)phosphatidylcholine (KodiA-PC) (24), a specific CD36 ligand, dramatically increased Fyn phosphorylation (Figure 6B)	complete
	GO:0004713	protein tyrosine kinase activity	PMID:20978343^[1]	IDA: Inferred from Direct Assay		F	Treatment of WT VSMCs with 1-(Palmitoyl)- 2-(5-keto-6-octene-dioyl)phosphatidylcholine (KodiA-PC) (24), a specific CD36 ligand, dramatically increased Fyn phosphorylation (Figure 6B)	complete
	GO:0010629	negative regulation of gene expression	PMID:20978343^[1]	IMP: Inferred from Mutant Phenotype		P	Figure 6C. Fyn deletion increases Prdx2 and Nrf2 expression in VSMCs.	complete
	GO:0000166	nucleotide binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0547	F
	GO:0001764	neuron migration	PMID:15073522^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1930480	P
	GO:0001764	neuron migration	PMID:16162939^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:98397	P
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F
	GO:0004672	protein kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	F
	GO:0004672	protein kinase activity	PMID:11826099^[4]	IDA: Inferred from Direct Assay		F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR020635	F
	GO:0004713	protein tyrosine kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0829	F
	GO:0004713	protein tyrosine kinase activity	PMID:10872802^[5]	IDA: Inferred from Direct Assay		F
	GO:0004713	protein tyrosine kinase activity	PMID:16841086^[6]	IDA: Inferred from Direct Assay		F
	GO:0004713	protein tyrosine kinase activity	PMID:8175795^[7]	IDA: Inferred from Direct Assay		F
	GO:0004713	protein tyrosine kinase activity	PMID:8196616^[8]	IDA: Inferred from Direct Assay		F
	GO:0004715	non-membrane spanning protein tyrosine kinase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.7.10.2	F
	GO:0005515	protein binding	PMID:10713104^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P49710	F
	GO:0005515	protein binding	PMID:10713104^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P49710	F
	GO:0005515	protein binding	PMID:15102471^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P51807	F
	GO:0005515	protein binding	PMID:15102471^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q60749	F
	GO:0005515	protein binding	PMID:16316995^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q9JIA7	F
	GO:0005515	protein binding	PMID:16777849^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q80YF9	F
	GO:0005515	protein binding	PMID:16899217^[13]	IPI: Inferred from Physical Interaction	UniProtKB:Q920D3	F
	GO:0005515	protein binding	PMID:16899217^[13]	IPI: Inferred from Physical Interaction	UniProtKB:Q9H204	F
	GO:0005515	protein binding	PMID:7799925^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q60749	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	F
	GO:0005524	ATP binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017441	F
	GO:0005524	ATP binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0067	F
	GO:0005829	cytosol	Reactome:REACT_18301	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_18388	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_18394	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_18408	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_18414	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_19192	TAS: Traceable Author Statement		C
	GO:0005829	cytosol	Reactome:REACT_19300	TAS: Traceable Author Statement		C
	GO:0005886	plasma membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-1003	C
	GO:0005886	plasma membrane	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0039	C
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000719	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001245	P
	GO:0006468	protein phosphorylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR008266	P
	GO:0006468	protein phosphorylation	PMID:16190898^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1930480	P
	GO:0006468	protein phosphorylation	PMID:9892651^[16]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1930480	P
	GO:0007166	cell surface receptor linked signaling pathway	PMID:9177270^[17]	IDA: Inferred from Direct Assay		P
	GO:0007275	multicellular organismal development	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0217	P
	GO:0008360	regulation of cell shape	PMID:11826099^[4]	IDA: Inferred from Direct Assay		P
	GO:0010629	negative regulation of gene expression	PMID:20978343^[1]	IMP: Inferred from Mutant Phenotype		P
	GO:0015631	tubulin binding	PMID:11826099^[4]	IDA: Inferred from Direct Assay		F
	GO:0016020	membrane	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0472	C
	GO:0016301	kinase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	F
	GO:0016310	phosphorylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0418	P
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F
	GO:0016772	transferase activity, transferring phosphorus-containing groups	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR011009	F
	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:10872802^[5]	IDA: Inferred from Direct Assay		P
	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:8175795^[7]	IDA: Inferred from Direct Assay		P
	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:8196616^[8]	IDA: Inferred from Direct Assay		P
	GO:0018108	peptidyl-tyrosine phosphorylation	PMID:9381182^[18]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1930480	P
	GO:0030900	forebrain development	PMID:15073522^[2]	IMP: Inferred from Mutant Phenotype	MGI:MGI:98397	P
	GO:0030900	forebrain development	PMID:16162939^[3]	IGI: Inferred from Genetic Interaction	MGI:MGI:98397	P
	GO:0042177	negative regulation of protein catabolic process	PMID:16841086^[6]	IMP: Inferred from Mutant Phenotype		P
	GO:0042552	myelination	PMID:11826099^[4]	TAS: Traceable Author Statement		P
	GO:0044325	ion channel binding	PMID:12538589^[19]	IPI: Inferred from Physical Interaction	UniProtKB:Q9EPK8	F
	GO:0045471	response to ethanol	PMID:9381182^[18]	IGI: Inferred from Genetic Interaction	MGI:MGI:95819	P
	GO:0046777	protein autophosphorylation	PMID:8175795^[7]	IDA: Inferred from Direct Assay		P
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0050798	activated T cell proliferation	PMID:1516132^[20]	IMP: Inferred from Mutant Phenotype	MGI:MGI:2179145	P
	GO:0050966	detection of mechanical stimulus involved in sensory perception of pain	PMID:16190898^[15]	IMP: Inferred from Mutant Phenotype	MGI:MGI:1930480	P
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Li W et al. (2010) CD36 participates in a signaling pathway that regulates ROS formation in murine VSMCs. J Clin Invest 120: 3996-4006 PubMed GONUTS page
↑ ^2.0 ^2.1 Yuasa S et al. (2004) Defective neocortical development in Fyn-tyrosine-kinase-deficient mice. Neuroreport 15: 819-22 PubMed GONUTS page
↑ ^3.0 ^3.1 Kuo G et al. (2005) Absence of Fyn and Src causes a reeler-like phenotype. J Neurosci 25: 8578-86 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Klein C et al. (2002) Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. J Neurosci 22: 698-707 PubMed GONUTS page
↑ ^5.0 ^5.1 Iseki M et al. (2000) Molecular cloning of the mouse APS as a member of the Lnk family adaptor proteins. Biochem Biophys Res Commun 272: 45-54 PubMed GONUTS page
↑ ^6.0 ^6.1 Tang X et al. (2007) Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-kinase enhancer-activating Akt, preventing its apoptotic cleavage and promoting cell survival. Cell Death Differ 14: 368-77 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Burns CM et al. (1994) CD45 regulation of tyrosine phosphorylation and enzyme activity of src family kinases. J Biol Chem 269: 13594-600 PubMed GONUTS page
↑ ^8.0 ^8.1 Gauen LK et al. (1994) Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif. Mol Cell Biol 14: 3729-41 PubMed GONUTS page
↑ ^9.0 ^9.1 Ingley E et al. (2000) HS1 interacts with Lyn and is critical for erythropoietin-induced differentiation of erythroid cells. J Biol Chem 275: 7887-93 PubMed GONUTS page
↑ ^10.0 ^10.1 Papin J & Subramaniam S (2004) Bioinformatics and cellular signaling. Curr Opin Biotechnol 15: 78-81 PubMed GONUTS page
↑ Olivera A et al. (2006) IgE-dependent activation of sphingosine kinases 1 and 2 and secretion of sphingosine 1-phosphate requires Fyn kinase and contributes to mast cell responses. J Biol Chem 281: 2515-25 PubMed GONUTS page
↑ Liu H et al. (2006) Physical and functional interaction of Fyn tyrosine kinase with a brain-enriched Rho GTPase-activating protein TCGAP. J Biol Chem 281: 23611-9 PubMed GONUTS page
↑ ^13.0 ^13.1 Lee MF et al. (2006) Magicin associates with the Src-family kinases and is phosphorylated upon CD3 stimulation. Biochem Biophys Res Commun 348: 826-31 PubMed GONUTS page
↑ Richard S et al. (1995) Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1. Mol Cell Biol 15: 186-97 PubMed GONUTS page
↑ ^15.0 ^15.1 Abe T et al. (2005) Fyn kinase-mediated phosphorylation of NMDA receptor NR2B subunit at Tyr1472 is essential for maintenance of neuropathic pain. Eur J Neurosci 22: 1445-54 PubMed GONUTS page
↑ Tezuka T et al. (1999) PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A. Proc Natl Acad Sci U S A 96: 435-40 PubMed GONUTS page
↑ Sammar M et al. (1997) Mouse CD24 as a signaling molecule for integrin-mediated cell binding: functional and physical association with src-kinases. Biochem Biophys Res Commun 234: 330-4 PubMed GONUTS page
↑ ^18.0 ^18.1 Miyakawa T et al. (1997) Fyn-kinase as a determinant of ethanol sensitivity: relation to NMDA-receptor function. Science 278: 698-701 PubMed GONUTS page
↑ Xu H et al. (2003) Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress. J Biol Chem 278: 11520-7 PubMed GONUTS page
↑ Appleby MW et al. (1992) Defective T cell receptor signaling in mice lacking the thymic isoform of p59fyn. Cell 70: 751-63 PubMed GONUTS page

[PMID:20978343-0] 1.0 ^1.1 ^1.2 ^1.3 Li W et al. (2010) CD36 participates in a signaling pathway that regulates ROS formation in murine VSMCs. J Clin Invest 120: 3996-4006 PubMed GONUTS page

[PMID:15073522-1] 2.0 ^2.1 Yuasa S et al. (2004) Defective neocortical development in Fyn-tyrosine-kinase-deficient mice. Neuroreport 15: 819-22 PubMed GONUTS page

[PMID:16162939-2] 3.0 ^3.1 Kuo G et al. (2005) Absence of Fyn and Src causes a reeler-like phenotype. J Neurosci 25: 8578-86 PubMed GONUTS page

[PMID:11826099-3] 4.0 ^4.1 ^4.2 ^4.3 Klein C et al. (2002) Process outgrowth of oligodendrocytes is promoted by interaction of fyn kinase with the cytoskeletal protein tau. J Neurosci 22: 698-707 PubMed GONUTS page

[PMID:10872802-4] 5.0 ^5.1 Iseki M et al. (2000) Molecular cloning of the mouse APS as a member of the Lnk family adaptor proteins. Biochem Biophys Res Commun 272: 45-54 PubMed GONUTS page

[PMID:16841086-5] 6.0 ^6.1 Tang X et al. (2007) Src-family tyrosine kinase fyn phosphorylates phosphatidylinositol 3-kinase enhancer-activating Akt, preventing its apoptotic cleavage and promoting cell survival. Cell Death Differ 14: 368-77 PubMed GONUTS page

[PMID:8175795-6] 7.0 ^7.1 ^7.2 Burns CM et al. (1994) CD45 regulation of tyrosine phosphorylation and enzyme activity of src family kinases. J Biol Chem 269: 13594-600 PubMed GONUTS page

[PMID:8196616-7] 8.0 ^8.1 Gauen LK et al. (1994) Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signalling motif. Mol Cell Biol 14: 3729-41 PubMed GONUTS page

[PMID:10713104-8] 9.0 ^9.1 Ingley E et al. (2000) HS1 interacts with Lyn and is critical for erythropoietin-induced differentiation of erythroid cells. J Biol Chem 275: 7887-93 PubMed GONUTS page

[PMID:15102471-9] 10.0 ^10.1 Papin J & Subramaniam S (2004) Bioinformatics and cellular signaling. Curr Opin Biotechnol 15: 78-81 PubMed GONUTS page

[PMID:16316995-10] Olivera A et al. (2006) IgE-dependent activation of sphingosine kinases 1 and 2 and secretion of sphingosine 1-phosphate requires Fyn kinase and contributes to mast cell responses. J Biol Chem 281: 2515-25 PubMed GONUTS page

[PMID:16777849-11] Liu H et al. (2006) Physical and functional interaction of Fyn tyrosine kinase with a brain-enriched Rho GTPase-activating protein TCGAP. J Biol Chem 281: 23611-9 PubMed GONUTS page

[PMID:16899217-12] 13.0 ^13.1 Lee MF et al. (2006) Magicin associates with the Src-family kinases and is phosphorylated upon CD3 stimulation. Biochem Biophys Res Commun 348: 826-31 PubMed GONUTS page

[PMID:7799925-13] Richard S et al. (1995) Association of p62, a multifunctional SH2- and SH3-domain-binding protein, with src family tyrosine kinases, Grb2, and phospholipase C gamma-1. Mol Cell Biol 15: 186-97 PubMed GONUTS page

[PMID:16190898-14] 15.0 ^15.1 Abe T et al. (2005) Fyn kinase-mediated phosphorylation of NMDA receptor NR2B subunit at Tyr1472 is essential for maintenance of neuropathic pain. Eur J Neurosci 22: 1445-54 PubMed GONUTS page

[PMID:9892651-15] Tezuka T et al. (1999) PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the N-methyl-D-aspartate receptor subunit NR2A. Proc Natl Acad Sci U S A 96: 435-40 PubMed GONUTS page

[PMID:9177270-16] Sammar M et al. (1997) Mouse CD24 as a signaling molecule for integrin-mediated cell binding: functional and physical association with src-kinases. Biochem Biophys Res Commun 234: 330-4 PubMed GONUTS page

[PMID:9381182-17] 18.0 ^18.1 Miyakawa T et al. (1997) Fyn-kinase as a determinant of ethanol sensitivity: relation to NMDA-receptor function. Science 278: 698-701 PubMed GONUTS page

[PMID:12538589-18] Xu H et al. (2003) Regulation of a transient receptor potential (TRP) channel by tyrosine phosphorylation. SRC family kinase-dependent tyrosine phosphorylation of TRPV4 on TYR-253 mediates its response to hypotonic stress. J Biol Chem 278: 11520-7 PubMed GONUTS page

[PMID:1516132-19] Appleby MW et al. (1992) Defective T cell receptor signaling in mice lacking the thymic isoform of p59fyn. Cell 70: 751-63 PubMed GONUTS page

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MOUSE:FYN

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