FYN

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. [provided by RefSeq, Jul 2008]

FYN Proto-Oncogene, Src Family Tyrosine Kinase

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. Phosphorylates PTK2B/PYK2 in response to T-cell receptor activation. 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. In mast cells, phosphorylates CLNK after activation of immunoglobulin epsilon receptor signaling (By similarity).

Activated T cell proliferation Source: Ensembl
Adaptive immune response Source: UniProtKB-KW
Axon guidance Source: Reactome
Calcium ion transport Source: UniProtKB
Cell differentiation Source: GO_Central
Cellular response to amyloid-beta Source: ARUK-UCL
Cellular response to glycine Source: ARUK-UCL
Cellular response to L-glutamate Source: ARUK-UCL
Cellular response to peptide hormone stimulus Source: Ensembl
Cellular response to platelet-derived growth factor stimulus Source: Ensembl
Cellular response to transforming growth factor beta stimulus Source: Ensembl
Dendrite morphogenesis Source: Ensembl
Dendritic spine maintenance Source: ARUK-UCL
Detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
Ephrin receptor signaling pathway Source: Reactome
Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
Feeding behavior Source: ProtInc
Forebrain development Source: Ensembl
Heart process Source: ARUK-UCL
Innate immune response Source: GO_Central
Intracellular signal transduction Source: ARUK-UCL
Learning Source: ProtInc
Leukocyte migration Source: Reactome
Modulation of chemical synaptic transmission Source: Ensembl
Negative regulation of dendritic spine maintenance Source: ARUK-UCL
Negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
Negative regulation of gene expression Source: Ensembl
Negative regulation of hydrogen peroxide biosynthetic process Source: ARUK-UCL
Negative regulation of inflammatory response to antigenic stimulus Source: Reactome
Negative regulation of neuron apoptotic process Source: Ensembl
Negative regulation of oxidative stress-induced cell death Source: ARUK-UCL
Negative regulation of protein catabolic process Source: Ensembl
Negative regulation of protein ubiquitination Source: Ensembl
Neuron migration Source: Ensembl
Peptidyl-tyrosine phosphorylation Source: UniProtKB
Positive regulation of cysteine-type endopeptidase activity Source: ARUK-UCL
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
Positive regulation of neuron death Source: ARUK-UCL
Positive regulation of neuron projection development Source: Ensembl
Positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
Positive regulation of protein localization to membrane Source: ARUK-UCL
Positive regulation of protein localization to nucleus Source: Ensembl
Positive regulation of protein targeting to membrane Source: ARUK-UCL
Positive regulation of tyrosine phosphorylation of STAT protein Source: Ensembl
Protein autophosphorylation Source: Ensembl
Protein phosphorylation Source: ARUK-UCL
Regulation of calcium ion import across plasma membrane Source: ARUK-UCL
Regulation of cell shape Source: ARUK-UCL
Regulation of glutamate receptor signaling pathway Source: ARUK-UCL
Regulation of peptidyl-tyrosine phosphorylation Source: ARUK-UCL
Response to amyloid-beta Source: ARUK-UCL
Response to drug Source: Ensembl
Response to ethanol Source: Ensembl
Response to hydrogen peroxide Source: ARUK-UCL
Response to singlet oxygen Source: ARUK-UCL
Stimulatory C-type lectin receptor signaling pathway Source: Reactome
T cell costimulation Source: Reactome
T cell receptor signaling pathway Source: UniProtKB
Transmembrane receptor protein tyrosine kinase signaling pathway Source: GO_Central
Vascular endothelial growth factor receptor signaling pathway Source: Reactome

Cytoplasm; Nucleus; Cell membrane. Present and active in lipid rafts. Palmitoylation is crucial for proper trafficking.

Autophosphorylated at Tyr-420 (By similarity). Phosphorylation on the C-terminal tail at Tyr-531 by CSK maintains the enzyme in an inactive state (PubMed:1699196). PTPRC/CD45 dephosphorylates Tyr-531 leading to activation (PubMed:1533589). Ultraviolet B (UVB) strongly increase phosphorylation at Thr-12 and kinase activity, and promotes translocation from the cytoplasm to the nucleus (PubMed:15537652). Dephosphorylation at Tyr-420 by PTPN2 negatively regulates T-cell receptor signaling (PubMed:22080863). Phosphorylated at tyrosine residues, which can be enhanced by NTN1 (By similarity).
Palmitoylated. Palmitoylation at Cys-3 and Cys-6, probably by ZDHHC21, regulates subcellular location.