FYN oncogene related to SRC, FGR, YES
PDB rendering based on 1a0n.
Available structures
1a0n, 1aot, 1aou, 1avz, 1azg, 1efn, 1fyn, 1g83, 1m27, 1nyf, 1nyg, 1shf, 1zbj, 2dq7
Identifiers
Symbols	FYN; MGC45350; SLK; SYN
External IDs	OMIM: 137025 MGI: 95602 HomoloGene: 48068
Gene ontology Molecular function • nucleotide binding • protein-tyrosine kinase activity • non-membrane spanning protein tyrosine kinase activity • protein binding • ATP binding • tubulin binding • transferase activity • identical protein binding Cellular component • cellular_component Biological process • neuron migration • protein amino acid phosphorylation • calcium ion transport • intracellular signaling cascade • protein kinase cascade • learning • feeding behavior • regulation of cell shape • peptidyl-tyrosine phosphorylation • forebrain development • T cell receptor signaling pathway
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2534	14360
Ensembl	ENSG00000010810	ENSMUSG00000019843
UniProt	P06241	Q3TAT3
RefSeq	NM_002037 (mRNA)	NM_008054 (mRNA)
	NP_002028 (protein)	NP_032080 (protein)
Location	Chr 6: 112.09 - 112.3 Mb	Chr 10: 39.06 - 39.25 Mb
PubMed search	[1]	[2]

Proto-oncogene tyrosine-protein kinase Fyn is an enzyme that in humans is encoded by the FYN gene.^[1][1]

This gene is a member of the protein-tyrosine kinase oncogene family. It encodes a membrane-associated tyrosine kinase that has been implicated in the control of cell growth. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist.^[2]

[edit] Function

Fyn is a protein, present in the signaling pathway of [integrin]s, which activates ras. Fyn is a tyrosine specific phospho-transferase that is a member of the Src family of tyrosine protein kinases.^[3] Fyn is primarily localized to the cytoplasmic leaflet of the plasma membrane, where it phosphorylates tyrosine residues on key targets involved in a variety of different signaling pathways. Tyrosine phosphorylation of target proteins by Fyn serves to either regulate target protein activity, and/or to generate a binding site on the target protein that recruits other signaling molecules.

[edit] Role in signaling pathways

At least three tools have been useful in discerning a requirement for Fyn function in a particular signaling system:

• cells derived from Fyn-/- mice (as well as cells derived from Fyn, Src, Yes, Fyn triple knockout mice (SYF));
• a kinase-inactive, dominant negative mutant form of Fyn (K299M);
• pharmacologic inhibitors of Src family kinases, such as PP2 (4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine; note that PP2 also inhibits other tyrosine protein kinases such as Abl, PDGFR and c-Kit).

Using these tools, a requirement for Fyn has been shown for the following signaling pathways: T and B cell receptor signaling,^[4][5] integrin-mediated signaling, growth factor and cytokine receptor signaling, platelet activation, ion channel function, cell adhesion, axon guidance, fertilization, entry into mitosis, and differentiation of natural killer cells, oligodendrocytes and keratinocytes.

[edit] Interactions

FYN has been shown to interact with:

• CD36^[6][7]
• KHDRBS1^[8][9]
• Janus kinase 2,^[10]
• ZAP-70^[11]
• CDH1^[12]
• PTK2B^[13][14][15]
• GRIN2A^{[16][17][18][19]}
• Fas ligand^[20][21]
• Nephrin^[22][23]
• PAG1^[24]
• TRPC6^[25]
• BCAR1^[26][27]
• C-Raf^[28]
• CD44^[29]
• PIK3R2^[30]
• ITK^[31][32]
• Alpha-tubulin 3C,^[33]
• Tau protein^[33]
• SH2D1A^[34][35]
• Tyrosine kinase 2^[36]
• EPHA8^[37]
• CBLC^[38]
• PRKCQ^[39]
• CTNND1^[40][12]
• SKAP1^[41][42][43]
• Syk^[44]
• DLG4^[17][18]
• Wiskott-Aldrich syndrome protein^[45][46][47]
• PTK2^[48][49]
• RICS^[50]
• TrkB^[51]
• Cbl gene^[52][44]
• Dystroglycan^[53]
• CHRNA7^[54]
• Protein unc-119 homolog^[55]
• TNK2,^[56]
• FYB^[57][43]
• Colony stimulating factor 1 receptor^[58]
• ADD2^[59]
• GNB2L1^[60][61]

[edit] References

[edit] Further reading

v • d • e PDB Gallery 1a0n: NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, FAMILY OF 25 STRUCTURES   1aot: NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, MINIMIZED AVERAGE STRUCTURE   1aou: NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, 22 STRUCTURES   1avz: V-1 NEF PROTEIN IN COMPLEX WITH WILD TYPE FYN SH3 DOMAIN   1azg: NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, MINIMIZED AVERAGE (PROBMAP) STRUCTURE   1efn: HIV-1 NEF PROTEIN IN COMPLEX WITH R96I MUTANT FYN SH3 DOMAIN   1fyn: PHOSPHOTRANSFERASE   1g83: CRYSTAL STRUCTURE OF FYN SH3-SH2   1m27: Crystal structure of SAP/FynSH3/SLAM ternary complex   1nyf: NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, MINIMIZED AVERAGE (PROBMAP) STRUCTURE   1nyg: NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE, FAMILY OF 20 STRUCTURES   1shf: CRYSTAL STRUCTURE OF THE SH3 DOMAIN IN HUMAN FYN; COMPARISON OF THE THREE-DIMENSIONAL STRUCTURES OF SH3 DOMAINS IN TYROSINE KINASES AND SPECTRIN   1zbj: Inferential Structure Determination of the Fyn SH3 domain using NOESY data from a 15N,H2 enriched protein   2dq7: Crystal Structure of Fyn kinase domain complexed with staurosporine

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