Fyn is a Src-family non-receptor tyrosine kinase with SH3, SH2, and catalytic kinase domains. It localizes to cytosol and membrane/lipid-raft signaling platforms and phosphorylates tyrosine residues in immune receptor, adhesion, reelin, synaptic, axon guidance, and growth-factor-associated signaling pathways.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Myristoylated and palmitoylated Fyn is targeted to the inner plasma membrane and lipid rafts where it engages receptor-proximal complexes. Reason: Core membrane localization established by lipid modification and experimental evidence (UniProt: Cell membrane, active in lipid rafts). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005102 signaling receptor binding | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Too broad: Fyn docks onto specific receptor complexes (TCR coreceptors, mGluR5, ephrin/RTKs) via its SH2/SH3 domains, but the generic term adds no insight. Reason: Overly broad relative to the specific receptor-binding terms already annotated. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN002521528 SUPPORTS TRANSFER A coherent Src-family kinase node whose seeds are SRC, LCK, LYN and FGR alongside rodent and fly members. The clade is exactly the one Fyn belongs to, so the phylogenetic step is sound and only the term's breadth is at issue. MGI:MGI:95602 Β· mouse Fyn (the review target itself) SUPPORTS TRANSFER The target's own MGI record is among the IBD seeds - the expected marker that Fyn carries its own experimental grounding for receptor engagement, not circular support. UniProtKB:P12931 Β· human SRC (Proto-oncogene tyrosine-protein kinase Src) SUPPORTS TRANSFER The prototypical family member. SFKs genuinely bind signalling receptors, so the biology transfers; "signaling receptor binding" is simply a parent of the specific receptor-binding terms Fyn already carries. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0030154 cell differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Broad differentiation term (IBA); Fyn influences differentiation of T cells and oligodendrocytes via signaling. Reason: Very broad process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0007169 cell surface receptor protein tyrosine kinase signaling pathway | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Fyn acts downstream of receptor tyrosine kinases; as a non-receptor kinase it is an effector, not the receptor itself. Reason: Broad pathway term; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Most precise MF term: Fyn is a cytoplasmic (non-receptor) tyrosine kinase anchored to membranes via myristoylation/palmitoylation rather than a transmembrane receptor kinase. Reason: Most specific and accurate molecular-function term for Fyn; preferred over the generic parent. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0050852 T cell receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Fyn (with Lck) drives proximal TCR signaling, phosphorylating ITAM/downstream substrates and shaping T-cell activation; the hematopoietic isoform's central role. Reason: Core biological process for Fyn's immune isoform, strongly supported. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0004672 protein kinase activity | IEA GO_REF:0000120 | MODIFY | Summary: Fyn is specifically a tyrosine kinase; the generic 'protein kinase activity' term under-specifies and could imply Ser/Thr activity. Reason: Replace with the tyrosine-specific child term to capture the actual substrate chemistry. Proposed replacements: non-membrane spanning protein tyrosine kinase activity Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Most precise MF term: Fyn is a cytoplasmic (non-receptor) tyrosine kinase anchored to membranes via myristoylation/palmitoylation rather than a transmembrane receptor kinase. Reason: Most specific and accurate molecular-function term for Fyn; preferred over the generic parent. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding in the kinase domain is required for Fyn's phosphotransfer reaction (the gamma-phosphate donor). Reason: Obligate cofactor/substrate binding for a protein kinase; core molecular function. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005634 nucleus | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Fyn can translocate to the nucleus (e.g. UVB-induced), but nuclear localization is a minor, context-specific pool. Reason: Secondary/inducible localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Broad cytoplasmic localization; the specific cytosol/membrane-raft terms are more informative. Reason: Generic parent of the specific cytosol annotation; retained as non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Myristoylated and palmitoylated Fyn is targeted to the inner plasma membrane and lipid rafts where it engages receptor-proximal complexes. Reason: Core membrane localization established by lipid modification and experimental evidence (UniProt: Cell membrane, active in lipid rafts). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0043204 perikaryon | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Neuronal soma (perikaryon) localization of the brain-enriched isoform. Reason: Neuronal-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0005515 protein binding | IPI PMID:10077576 Characterization of Sam68-like mammalian proteins SLM-1 and ... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:12372285 Fyn and Cdk5 mediate semaphorin-3A signaling, which is invol... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:15102471 Bioinformatics and cellular signaling. | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:16316995 IgE-dependent activation of sphingosine kinases 1 and 2 and ... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:16847311 Association between SAP and FynT: Inducible SH3 domain-media... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:25417160 A noncanonical Frizzled2 pathway regulates epithelial-mesenc... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:27474268 Co-recruitment analysis of the CBL and CBLB signalosomes in ... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:7730365 Sequence requirements for binding of Src family tyrosine kin... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:8631859 The Fyn tyrosine kinase binds Irs-1 and forms a distinct sig... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:9535845 Physical and functional interactions between receptor-like p... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:9890970 Fyn associates with Cbl and phosphorylates tyrosine 731 in C... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0000304 response to singlet oxygen | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Orthology-inferred response to singlet oxygen; not a Fyn-specific characterized role. Reason: Electronically inferred stress response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0001664 G protein-coupled receptor binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Fyn binds GPCR-class receptors including metabotropic glutamate receptors in neurons. Reason: Specific partner interaction in a context-specific pathway; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0003015 heart process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cardiac phenotypes associated with Fyn in specific genetic backgrounds. Reason: Distal organ-level process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005102 signaling receptor binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Too broad: Fyn docks onto specific receptor complexes (TCR coreceptors, mGluR5, ephrin/RTKs) via its SH2/SH3 domains, but the generic term adds no insight. Reason: Overly broad relative to the specific receptor-binding terms already annotated. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005739 mitochondrion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: A minor mitochondrial pool reported by orthology/IDA in specific contexts. Reason: Secondary localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005768 endosome | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn is found on endosomes in association with receptor trafficking. Reason: Secondary/trafficking localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | IEA GO_REF:0000107 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0007216 G protein-coupled glutamate receptor signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn participates in metabotropic glutamate receptor signaling at synapses. Reason: Synaptic context process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Generic xenobiotic-response term inferred electronically; not a Fyn-specific role. Reason: Broad, electronically inferred response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0010730 negative regulation of hydrogen peroxide biosynthetic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Orthology-inferred role in limiting H2O2 production in particular contexts. Reason: Context-specific, electronically inferred; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0014069 postsynaptic density | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn is recruited to the postsynaptic density via PSD95 to act on NMDA receptors. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0016004 phospholipase activator activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn can promote phospholipase activation downstream of receptor engagement. Reason: Context-specific regulatory activity; non-core relative to kinase function. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0019899 enzyme binding | IEA GO_REF:0000120 | MARK AS OVER ANNOTATED | Summary: Generic enzyme-binding term; the informative interactions (e.g. PI3K, phospholipase) are captured by specific binding annotations. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0030101 natural killer cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn contributes to CD244-mediated NK-cell activation. Reason: Context-specific immune process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0030425 dendrite | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Fyn localizes to dendrites/dendritic spines where it phosphorylates NMDAR subunits. Reason: Synaptic-context localization supporting its neuronal role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0031802 type 5 metabotropic glutamate receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn interacts with mGluR5 in glutamatergic synapses, linking it to NMDAR modulation. Reason: Specific synaptic interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0035556 intracellular signal transduction | IEA GO_REF:0000120 | ACCEPT | Summary: Fyn operates as an intracellular signal-transducing kinase relaying signals from membrane receptors (TCR, integrins, reelin/RTKs) to downstream effectors. Reason: Accurate, appropriately-scoped process term for a cytoplasmic signaling kinase; core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0042220 response to cocaine | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: IEA ortholog projection (GO_REF:0000107); unlike a generic chaperone, Fyn is a neuronal kinase with documented roles in NMDAR phosphorylation and drug-induced synaptic plasticity. Reason: Plausible non-core downstream signaling context for a neuronal kinase (cf. experimental IGI 'response to ethanol'); not a core molecular function. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0042608 T cell receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn is recruited to the TCR complex where it phosphorylates ITAM and downstream substrates. Reason: Interaction underlying its immune signaling role; recruitment partner, non-core MF. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0042609 CD4 receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn associates with the CD4 coreceptor tail in T cells, contributing to TCR-proximal signaling. Reason: Real interaction supporting immune signaling context, but recruitment partner rather than core catalytic function. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0042610 CD8 receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn associates with the CD8 coreceptor in T cells, contributing to TCR-proximal signaling. Reason: Real coreceptor interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Homotypic-binding annotation adds little; Fyn function is defined by its kinase activity and heterotypic docking. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0043274 phospholipase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn binds and can regulate phospholipase activity in receptor-proximal signaling. Reason: Specific interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0043524 negative regulation of neuron apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn signaling can promote neuronal survival in particular contexts. Reason: Context-specific survival outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0043548 phosphatidylinositol 3-kinase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn (via SH3/SH2) binds the PI3K regulatory subunit, coupling to PI3K/AKT signaling. Reason: Specific interaction linking Fyn to PI3K/AKT; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Generic complex-binding term; Fyn's incorporation into receptor-proximal and synaptic complexes is better captured by specific annotations. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0045121 membrane raft | IEA GO_REF:0000107 | ACCEPT | Summary: Fyn is present and active in lipid rafts, the membrane microdomains where TCR and other receptor signaling is nucleated. Reason: Core functional localization (UniProt: present and active in lipid rafts; PubMed:14645715). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0046875 ephrin receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn binds Eph-family receptors during axon guidance/repulsion signaling. Reason: Specific partner interaction in axon-guidance context; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Perinuclear cytoplasmic localization in specific contexts. Reason: Secondary localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0050852 T cell receptor signaling pathway | IEA GO_REF:0000107 | ACCEPT | Summary: Fyn (with Lck) drives proximal TCR signaling, phosphorylating ITAM/downstream substrates and shaping T-cell activation; the hematopoietic isoform's central role. Reason: Core biological process for Fyn's immune isoform, strongly supported. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0050860 negative regulation of T cell receptor signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn phosphorylates PAG1 and PDCD1 to dampen TCR signaling, a feedback arm of its immune function. Reason: Regulatory feedback role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0050868 negative regulation of T cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn also mediates negative feedback on TCR signaling (via PAG1/CSK and PDCD1/SHP-2). Reason: Regulatory feedback role; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0051428 peptide hormone receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn associates with peptide-hormone receptors in particular signaling contexts. Reason: Context-specific partner interaction; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn couples to PI3K/AKT signaling via direct PI3K interaction. Reason: Downstream pathway engagement; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0070301 cellular response to hydrogen peroxide | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn participates in redox/oxidative-stress signaling in specific contexts (mostly orthology-inferred). Reason: Context-specific stress response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0070851 growth factor receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn docks onto activated growth-factor receptors (e.g. via SH2) to relay downstream signals. Reason: Specific interaction in RTK signaling context; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0071363 cellular response to growth factor stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn relays growth-factor receptor signals downstream of RTK engagement. Reason: Context-specific signaling response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0071375 cellular response to peptide hormone stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn transduces specific peptide-hormone receptor signals. Reason: Context-specific signaling response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0097038 perinuclear endoplasmic reticulum | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Perinuclear ER-associated pool reported by orthology. Reason: Secondary localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0097110 scaffold protein binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Fyn associates with scaffolds (e.g. PSD95, PAG1) via SH2/SH3 docking, but 'scaffold protein binding' is generic and non-specific. Reason: Generic binding term superseded by specific complex/partner annotations. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0097718 disordered domain specific binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Non-specific MF descriptor not informative about Fyn's actual signaling role. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn functions at glutamatergic synapses modulating NMDAR signaling and plasticity. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0099092 postsynaptic density, intracellular component | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn associates with the intracellular face of the PSD signaling scaffold. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:1902176 negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn can modulate oxidative-stress-induced apoptosis in specific contexts (orthology-inferred). Reason: Context-specific survival outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:1904646 cellular response to amyloid-beta | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Cellular amyloid-beta response mediated through Fyn-NMDAR/tau signaling in AD models. Reason: Disease-context response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md inhibiting SFK/Fyn activity to disrupt a FynβtauβNMDAR complex implicated in excitotoxicity and seizure progression |
| GO:1905232 cellular response to L-glutamate | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Neuronal response to glutamate involving Fyn-mediated NMDAR phosphorylation. Reason: Context-specific neuronal response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:1905430 cellular response to glycine | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Glycine acts as an NMDAR co-agonist; Fyn participates in the associated receptor signaling. Reason: Context-specific neuronal response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:2001240 negative regulation of extrinsic apoptotic signaling pathway in absence of ligand | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Fyn promotes survival signaling in specific contexts (orthology-inferred). Reason: Context-specific survival outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0003015 heart process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Cardiac phenotypes associated with Fyn in specific genetic backgrounds. Reason: Distal organ-level process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | ISO GO_REF:0000119 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | ISO GO_REF:0000119 | ACCEPT | Summary: Most precise MF term: Fyn is a cytoplasmic (non-receptor) tyrosine kinase anchored to membranes via myristoylation/palmitoylation rather than a transmembrane receptor kinase. Reason: Most specific and accurate molecular-function term for Fyn; preferred over the generic parent. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005768 endosome | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn is found on endosomes in association with receptor trafficking. Reason: Secondary/trafficking localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | ISO GO_REF:0000119 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005886 plasma membrane | ISO GO_REF:0000119 | ACCEPT | Summary: Myristoylated and palmitoylated Fyn is targeted to the inner plasma membrane and lipid rafts where it engages receptor-proximal complexes. Reason: Core membrane localization established by lipid modification and experimental evidence (UniProt: Cell membrane, active in lipid rafts). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0007216 G protein-coupled glutamate receptor signaling pathway | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn participates in metabotropic glutamate receptor signaling at synapses. Reason: Synaptic context process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0016004 phospholipase activator activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn can promote phospholipase activation downstream of receptor engagement. Reason: Context-specific regulatory activity; non-core relative to kinase function. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0019899 enzyme binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Generic enzyme-binding term; the informative interactions (e.g. PI3K, phospholipase) are captured by specific binding annotations. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0030101 natural killer cell activation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn contributes to CD244-mediated NK-cell activation. Reason: Context-specific immune process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0030425 dendrite | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn localizes to dendrites/dendritic spines where it phosphorylates NMDAR subunits. Reason: Synaptic-context localization supporting its neuronal role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0035556 intracellular signal transduction | ISO GO_REF:0000119 | ACCEPT | Summary: Fyn operates as an intracellular signal-transducing kinase relaying signals from membrane receptors (TCR, integrins, reelin/RTKs) to downstream effectors. Reason: Accurate, appropriately-scoped process term for a cytoplasmic signaling kinase; core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0042802 identical protein binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Homotypic-binding annotation adds little; Fyn function is defined by its kinase activity and heterotypic docking. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0043274 phospholipase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn binds and can regulate phospholipase activity in receptor-proximal signaling. Reason: Specific interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0045121 membrane raft | ISO GO_REF:0000119 | ACCEPT | Summary: Fyn is present and active in lipid rafts, the membrane microdomains where TCR and other receptor signaling is nucleated. Reason: Core functional localization (UniProt: present and active in lipid rafts; PubMed:14645715). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0046875 ephrin receptor binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn binds Eph-family receptors during axon guidance/repulsion signaling. Reason: Specific partner interaction in axon-guidance context; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0050852 T cell receptor signaling pathway | ISO GO_REF:0000119 | ACCEPT | Summary: Fyn (with Lck) drives proximal TCR signaling, phosphorylating ITAM/downstream substrates and shaping T-cell activation; the hematopoietic isoform's central role. Reason: Core biological process for Fyn's immune isoform, strongly supported. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0050860 negative regulation of T cell receptor signaling pathway | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn phosphorylates PAG1 and PDCD1 to dampen TCR signaling, a feedback arm of its immune function. Reason: Regulatory feedback role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0050868 negative regulation of T cell activation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn also mediates negative feedback on TCR signaling (via PAG1/CSK and PDCD1/SHP-2). Reason: Regulatory feedback role; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0070851 growth factor receptor binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Fyn docks onto activated growth-factor receptors (e.g. via SH2) to relay downstream signals. Reason: Specific interaction in RTK signaling context; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0097110 scaffold protein binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Fyn associates with scaffolds (e.g. PSD95, PAG1) via SH2/SH3 docking, but 'scaffold protein binding' is generic and non-specific. Reason: Generic binding term superseded by specific complex/partner annotations. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0097718 disordered domain specific binding | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: Non-specific MF descriptor not informative about Fyn's actual signaling role. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:1904646 cellular response to amyloid-beta | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: Cellular amyloid-beta response mediated through Fyn-NMDAR/tau signaling in AD models. Reason: Disease-context response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md inhibiting SFK/Fyn activity to disrupt a FynβtauβNMDAR complex implicated in excitotoxicity and seizure progression |
| GO:0018108 peptidyl-tyrosine phosphorylation | ISO GO_REF:0000096 | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0046777 protein autophosphorylation | ISO GO_REF:0000096 | ACCEPT | Summary: Fyn autophosphorylates its activation-loop Tyr-420, a hallmark of Src-family kinase activation. Reason: Well-established intramolecular activity of Fyn (UniProt PTM, PubMed:8441403); core to its activation cycle. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0000304 response to singlet oxygen | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Orthology-inferred response to singlet oxygen; not a Fyn-specific characterized role. Reason: Electronically inferred stress response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004672 protein kinase activity | ISO GO_REF:0000096 | MODIFY | Summary: Fyn is specifically a tyrosine kinase; the generic 'protein kinase activity' term under-specifies and could imply Ser/Thr activity. Reason: Replace with the tyrosine-specific child term to capture the actual substrate chemistry. Proposed replacements: non-membrane spanning protein tyrosine kinase activity Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005102 signaling receptor binding | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: Too broad: Fyn docks onto specific receptor complexes (TCR coreceptors, mGluR5, ephrin/RTKs) via its SH2/SH3 domains, but the generic term adds no insight. Reason: Overly broad relative to the specific receptor-binding terms already annotated. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005634 nucleus | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn can translocate to the nucleus (e.g. UVB-induced), but nuclear localization is a minor, context-specific pool. Reason: Secondary/inducible localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005739 mitochondrion | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: A minor mitochondrial pool reported by orthology/IDA in specific contexts. Reason: Secondary localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0010730 negative regulation of hydrogen peroxide biosynthetic process | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Orthology-inferred role in limiting H2O2 production in particular contexts. Reason: Context-specific, electronically inferred; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0014069 postsynaptic density | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn is recruited to the postsynaptic density via PSD95 to act on NMDA receptors. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0019899 enzyme binding | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: Generic enzyme-binding term; the informative interactions (e.g. PI3K, phospholipase) are captured by specific binding annotations. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0030425 dendrite | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn localizes to dendrites/dendritic spines where it phosphorylates NMDAR subunits. Reason: Synaptic-context localization supporting its neuronal role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0031802 type 5 metabotropic glutamate receptor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn interacts with mGluR5 in glutamatergic synapses, linking it to NMDAR modulation. Reason: Specific synaptic interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0035556 intracellular signal transduction | ISO GO_REF:0000096 | ACCEPT | Summary: Fyn operates as an intracellular signal-transducing kinase relaying signals from membrane receptors (TCR, integrins, reelin/RTKs) to downstream effectors. Reason: Accurate, appropriately-scoped process term for a cytoplasmic signaling kinase; core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0042608 T cell receptor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn is recruited to the TCR complex where it phosphorylates ITAM and downstream substrates. Reason: Interaction underlying its immune signaling role; recruitment partner, non-core MF. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0042609 CD4 receptor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn associates with the CD4 coreceptor tail in T cells, contributing to TCR-proximal signaling. Reason: Real interaction supporting immune signaling context, but recruitment partner rather than core catalytic function. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0042610 CD8 receptor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn associates with the CD8 coreceptor in T cells, contributing to TCR-proximal signaling. Reason: Real coreceptor interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0043524 negative regulation of neuron apoptotic process | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn signaling can promote neuronal survival in particular contexts. Reason: Context-specific survival outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0043548 phosphatidylinositol 3-kinase binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn (via SH3/SH2) binds the PI3K regulatory subunit, coupling to PI3K/AKT signaling. Reason: Specific interaction linking Fyn to PI3K/AKT; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0044877 protein-containing complex binding | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: Generic complex-binding term; Fyn's incorporation into receptor-proximal and synaptic complexes is better captured by specific annotations. Reason: Uninformative generic binding term. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0048471 perinuclear region of cytoplasm | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Perinuclear cytoplasmic localization in specific contexts. Reason: Secondary localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0051428 peptide hormone receptor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn associates with peptide-hormone receptors in particular signaling contexts. Reason: Context-specific partner interaction; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn couples to PI3K/AKT signaling via direct PI3K interaction. Reason: Downstream pathway engagement; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0070301 cellular response to hydrogen peroxide | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn participates in redox/oxidative-stress signaling in specific contexts (mostly orthology-inferred). Reason: Context-specific stress response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0097038 perinuclear endoplasmic reticulum | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Perinuclear ER-associated pool reported by orthology. Reason: Secondary localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0098978 glutamatergic synapse | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn functions at glutamatergic synapses modulating NMDAR signaling and plasticity. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0099092 postsynaptic density, intracellular component | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn associates with the intracellular face of the PSD signaling scaffold. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:1902176 negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn can modulate oxidative-stress-induced apoptosis in specific contexts (orthology-inferred). Reason: Context-specific survival outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:1905232 cellular response to L-glutamate | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Neuronal response to glutamate involving Fyn-mediated NMDAR phosphorylation. Reason: Context-specific neuronal response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:1905430 cellular response to glycine | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Glycine acts as an NMDAR co-agonist; Fyn participates in the associated receptor signaling. Reason: Context-specific neuronal response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:2001240 negative regulation of extrinsic apoptotic signaling pathway in absence of ligand | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Fyn promotes survival signaling in specific contexts (orthology-inferred). Reason: Context-specific survival outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:9507006 Identification of sirm, a novel insulin-regulated SH3 bindin... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004715 non-membrane spanning protein tyrosine kinase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Most precise MF term: Fyn is a cytoplasmic (non-receptor) tyrosine kinase anchored to membranes via myristoylation/palmitoylation rather than a transmembrane receptor kinase. Reason: Most specific and accurate molecular-function term for Fyn; preferred over the generic parent. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0050860 negative regulation of T cell receptor signaling pathway | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Fyn phosphorylates PAG1 and PDCD1 to dampen TCR signaling, a feedback arm of its immune function. Reason: Regulatory feedback role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0050868 negative regulation of T cell activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Fyn also mediates negative feedback on TCR signaling (via PAG1/CSK and PDCD1/SHP-2). Reason: Regulatory feedback role; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0035556 intracellular signal transduction | IMP PMID:27525436 Tyrosine kinase FYN negatively regulates NOX4 in cardiac rem... | ACCEPT | Summary: Fyn operates as an intracellular signal-transducing kinase relaying signals from membrane receptors (TCR, integrins, reelin/RTKs) to downstream effectors. Reason: Accurate, appropriately-scoped process term for a cytoplasmic signaling kinase; core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0035556 intracellular signal transduction | IGI PMID:22820466 Alzheimer amyloid-Ξ² oligomer bound to postsynaptic prion pro... | ACCEPT | Summary: Fyn operates as an intracellular signal-transducing kinase relaying signals from membrane receptors (TCR, integrins, reelin/RTKs) to downstream effectors. Reason: Accurate, appropriately-scoped process term for a cytoplasmic signaling kinase; core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:1900449 regulation of glutamate receptor signaling pathway | IGI PMID:22820466 Alzheimer amyloid-Ξ² oligomer bound to postsynaptic prion pro... | KEEP AS NON CORE | Summary: Fyn regulates glutamate-receptor (NMDAR/mGluR) signaling at synapses. Reason: Synaptic regulatory role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0004713 protein tyrosine kinase activity | EXP PMID:16709819 Regulation of Ly49D/DAP12 signal transduction by Src-family ... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-MMU-3928613 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-MMU-9763891 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-MMU-983702 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | TAS Reactome:R-NUL-420398 | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0016525 negative regulation of angiogenesis | IMP PMID:10613822 Signals leading to apoptosis-dependent inhibition of neovasc... | KEEP AS NON CORE | Summary: Fyn modulates angiogenic signaling in particular contexts (knockout phenotype). Reason: Distal process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:12526739 Fyn tyrosine kinase is a critical regulator of disabled-1 du... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0038026 reelin-mediated signaling pathway | IDA PMID:12526739 Fyn tyrosine kinase is a critical regulator of disabled-1 du... | ACCEPT | Summary: Fyn phosphorylates DAB1 downstream of reelin binding to its receptors, a defining, well-established neuronal signaling role controlling cortical neuron positioning. Reason: Core, experimentally established neuronal signaling pathway for Fyn (UniProt; PubMed:12526739). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0050804 modulation of chemical synaptic transmission | IMP PMID:1361685 Impaired long-term potentiation, spatial learning, and hippo... | KEEP AS NON CORE | Summary: By phosphorylating NMDAR subunits, Fyn modulates excitatory synaptic transmission and plasticity (LTP). Reason: Synaptic modulatory role downstream of kinase activity; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0050804 modulation of chemical synaptic transmission | IDA PMID:1361685 Impaired long-term potentiation, spatial learning, and hippo... | KEEP AS NON CORE | Summary: By phosphorylating NMDAR subunits, Fyn modulates excitatory synaptic transmission and plasticity (LTP). Reason: Synaptic modulatory role downstream of kinase activity; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0098685 Schaffer collateral - CA1 synapse | IMP PMID:1361685 Impaired long-term potentiation, spatial learning, and hippo... | KEEP AS NON CORE | Summary: Fyn acts at hippocampal Schaffer collateral-CA1 synapses involved in LTP. Reason: Specific synaptic localization underlying plasticity phenotypes; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0098685 Schaffer collateral - CA1 synapse | IDA PMID:1361685 Impaired long-term potentiation, spatial learning, and hippo... | KEEP AS NON CORE | Summary: Fyn acts at hippocampal Schaffer collateral-CA1 synapses involved in LTP. Reason: Specific synaptic localization underlying plasticity phenotypes; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0010467 gene expression | IGI PMID:31461442 A bigenic mouse model of FSGS reveals perturbed pathways in ... | KEEP AS NON CORE | Summary: Very distal: changes in gene expression follow Fyn-dependent signaling. Reason: Highly distal outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md TCR stimulation induces STAT3 phosphorylation at Y705 through a Lck/Fyn-dependent axis |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:23169819 GPRC5B activates obesity-associated inflammatory signaling i... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0090314 positive regulation of protein targeting to membrane | IGI PMID:22820466 Alzheimer amyloid-Ξ² oligomer bound to postsynaptic prion pro... | KEEP AS NON CORE | Summary: Fyn-dependent phosphorylation can promote membrane targeting of partner proteins (e.g. CSK recruitment via PAG1). Reason: Downstream regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:1902951 negative regulation of dendritic spine maintenance | IGI PMID:22820466 Alzheimer amyloid-Ξ² oligomer bound to postsynaptic prion pro... | KEEP AS NON CORE | Summary: Fyn signaling modulates dendritic spine stability in specific contexts. Reason: Context-specific regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:1904645 response to amyloid-beta | IGI PMID:22820466 Alzheimer amyloid-Ξ² oligomer bound to postsynaptic prion pro... | KEEP AS NON CORE | Summary: Fyn transduces amyloid-beta-oligomer signals (via PrPC/mGluR5) to NMDARs/tau in Alzheimer models. Reason: Disease-context response downstream of kinase activity; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md inhibiting SFK/Fyn activity to disrupt a FynβtauβNMDAR complex implicated in excitotoxicity and seizure progression |
| GO:1905664 regulation of calcium ion import across plasma membrane | IGI PMID:22820466 Alzheimer amyloid-Ξ² oligomer bound to postsynaptic prion pro... | KEEP AS NON CORE | Summary: Fyn phosphorylates channels such as TRPC6 affecting calcium entry in specific contexts. Reason: Context-specific regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005886 plasma membrane | IDA PMID:10557075 wt p53 dependent expression of a membrane-associated isoform... | ACCEPT | Summary: Myristoylated and palmitoylated Fyn is targeted to the inner plasma membrane and lipid rafts where it engages receptor-proximal complexes. Reason: Core membrane localization established by lipid modification and experimental evidence (UniProt: Cell membrane, active in lipid rafts). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:28598420 Tespa1 regulates T cell receptor-induced calcium signals by ... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:28598420 Tespa1 regulates T cell receptor-induced calcium signals by ... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0043014 alpha-tubulin binding | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Fyn interacts with the tubulin/microtubule cytoskeleton during neurite and process remodeling. Reason: Cytoskeletal interaction in a context-specific role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0048156 tau protein binding | IPI PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Fyn binds tau (MAPT) and phosphorylates it; the Fyn-tau interaction targets Fyn to dendritic spines and is implicated in excitotoxicity. Reason: Genuine, well-studied interaction (substrate/targeting), but neuronal-context partner binding rather than core MF. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md inhibiting SFK/Fyn activity to disrupt a FynβtauβNMDAR complex implicated in excitotoxicity and seizure progression |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:12681493 Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 ... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:12681493 Targeting of MIST to Src-family kinases via SKAP55-SLAP-130 ... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:26901312 A Central Nervous System-Dependent Intron-Embedded Gene Enco... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:26901312 A Central Nervous System-Dependent Intron-Embedded Gene Enco... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:22685302 Down syndrome cell adhesion molecule (DSCAM) associates with... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0003015 heart process | IGI PMID:27525436 Tyrosine kinase FYN negatively regulates NOX4 in cardiac rem... | KEEP AS NON CORE | Summary: Cardiac phenotypes associated with Fyn in specific genetic backgrounds. Reason: Distal organ-level process; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0044297 cell body | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Neuronal cell-body localization of Fyn. Reason: Neuronal-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0045121 membrane raft | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | ACCEPT | Summary: Fyn is present and active in lipid rafts, the membrane microdomains where TCR and other receptor signaling is nucleated. Reason: Core functional localization (UniProt: present and active in lipid rafts; PubMed:14645715). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0097386 glial cell projection | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Fyn localizes to oligodendrocyte/glial processes during myelination. Reason: Glial-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is active during the myelination period and is required for oligodendrocyte morphological differentiation and myelination programs |
| GO:0005829 cytosol | TAS Reactome:R-MMU-1433273 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-2395436 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-3928613 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-3928635 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9605258 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9680646 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9680706 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9682158 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9682182 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9682572 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9763891 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9763892 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9763903 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9764150 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9817994 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9818009 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-983702 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-NUL-420388 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-NUL-420398 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-NUL-421136 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-NUL-421138 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005886 plasma membrane | TAS Reactome:R-MMU-9032771 | ACCEPT | Summary: Myristoylated and palmitoylated Fyn is targeted to the inner plasma membrane and lipid rafts where it engages receptor-proximal complexes. Reason: Core membrane localization established by lipid modification and experimental evidence (UniProt: Cell membrane, active in lipid rafts). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:20655099 Dendritic function of tau mediates amyloid-beta toxicity in ... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0014069 postsynaptic density | IMP PMID:20655099 Dendritic function of tau mediates amyloid-beta toxicity in ... | KEEP AS NON CORE | Summary: Fyn is recruited to the postsynaptic density via PSD95 to act on NMDA receptors. Reason: Synaptic-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0030425 dendrite | IMP PMID:20655099 Dendritic function of tau mediates amyloid-beta toxicity in ... | KEEP AS NON CORE | Summary: Fyn localizes to dendrites/dendritic spines where it phosphorylates NMDAR subunits. Reason: Synaptic-context localization supporting its neuronal role; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0005515 protein binding | IPI PMID:8551236 Association of tyrosine protein kinase Zap-70 with the proto... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:24627473 Phosphorylation of the antiviral protein interferon-inducibl... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0031397 negative regulation of protein ubiquitination | IDA PMID:24627473 Phosphorylation of the antiviral protein interferon-inducibl... | KEEP AS NON CORE | Summary: Fyn phosphorylation can antagonize ubiquitination of certain substrates. Reason: Context-specific regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0071560 cellular response to transforming growth factor beta stimulus | IGI PMID:21829547 Redox-induced Src kinase and caveolin-1 signaling in TGF-Ξ²1-... | KEEP AS NON CORE | Summary: Fyn intersects TGF-beta/Smad signaling in particular (e.g. fibrotic) contexts. Reason: Context-specific pathway crosstalk; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005768 endosome | IDA PMID:17623777 The membrane targeting and spatial activation of Src, Yes an... | KEEP AS NON CORE | Summary: Fyn is found on endosomes in association with receptor trafficking. Reason: Secondary/trafficking localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005884 actin filament | IDA PMID:17623777 The membrane targeting and spatial activation of Src, Yes an... | KEEP AS NON CORE | Summary: Fyn associates with the actin cytoskeleton during cytoskeletal remodeling. Reason: Cytoskeletal-context localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0036120 cellular response to platelet-derived growth factor stimulus | IDA PMID:17623777 The membrane targeting and spatial activation of Src, Yes an... | KEEP AS NON CORE | Summary: Fyn participates in PDGF-receptor signaling in specific contexts. Reason: Context-specific signaling response; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0071944 cell periphery | IDA PMID:17623777 The membrane targeting and spatial activation of Src, Yes an... | KEEP AS NON CORE | Summary: Generic peripheral localization, subsumed by the specific plasma-membrane/raft terms. Reason: Generic localization; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IGI PMID:23169819 GPRC5B activates obesity-associated inflammatory signaling i... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0001664 G protein-coupled receptor binding | IPI PMID:23169819 GPRC5B activates obesity-associated inflammatory signaling i... | KEEP AS NON CORE | Summary: Fyn binds GPCR-class receptors including metabotropic glutamate receptors in neurons. Reason: Specific partner interaction in a context-specific pathway; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:1900182 positive regulation of protein localization to nucleus | IMP PMID:20142099 Fyn-dependent regulation of energy expenditure and body weig... | KEEP AS NON CORE | Summary: Fyn signaling can promote nuclear translocation of downstream effectors. Reason: Downstream regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md TCR stimulation induces STAT3 phosphorylation at Y705 through a Lck/Fyn-dependent axis |
| GO:0005515 protein binding | IPI PMID:11711534 'Srcasm: a novel Src activating and signaling molecule. | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:10872802 Molecular cloning of the mouse APS as a member of the Lnk fa... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:20142099 Fyn-dependent regulation of energy expenditure and body weig... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:1900182 positive regulation of protein localization to nucleus | IDA PMID:20142099 Fyn-dependent regulation of energy expenditure and body weig... | KEEP AS NON CORE | Summary: Fyn signaling can promote nuclear translocation of downstream effectors. Reason: Downstream regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md TCR stimulation induces STAT3 phosphorylation at Y705 through a Lck/Fyn-dependent axis |
| GO:0042531 positive regulation of tyrosine phosphorylation of STAT protein | IMP PMID:23438599 Fyn regulates adipogenesis by promoting PIKE-A/STAT5a intera... | KEEP AS NON CORE | Summary: Fyn (with Lck) drives STAT3 Y705 phosphorylation downstream of TCR and in neuroinflammation. Reason: Downstream signaling output of Fyn kinase activity; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md TCR stimulation induces STAT3 phosphorylation at Y705 through a Lck/Fyn-dependent axis |
| GO:0005515 protein binding | IPI PMID:9185665 Molecular cloning of Fyn-associated molecules in the mouse c... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0010976 positive regulation of neuron projection development | IGI PMID:18354028 Voltage-gated Na+ channel beta1 subunit-mediated neurite out... | KEEP AS NON CORE | Summary: Fyn promotes neurite/axon outgrowth via cytoskeletal remodeling. Reason: Downstream developmental outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0005515 protein binding | IPI PMID:8196616 Interactions of p59fyn and ZAP-70 with T-cell receptor activ... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:9655502 Diversity revealed by a novel family of cadherins expressed ... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0048813 dendrite morphogenesis | IMP PMID:12372285 Fyn and Cdk5 mediate semaphorin-3A signaling, which is invol... | KEEP AS NON CORE | Summary: Fyn influences dendrite/spine morphology via cytoskeletal and synaptic signaling. Reason: Downstream morphogenetic outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:17923684 Neph1 cooperates with nephrin to transduce a signal that ind... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:17923684 Neph1 cooperates with nephrin to transduce a signal that ind... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:17923684 Neph1 cooperates with nephrin to transduce a signal that ind... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IMP PMID:17923684 Neph1 cooperates with nephrin to transduce a signal that ind... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0007166 cell surface receptor signaling pathway | IDA PMID:9177270 Mouse CD24 as a signaling molecule for integrin-mediated cel... | KEEP AS NON CORE | Summary: Generic receptor-signaling term; Fyn's specific roles are captured by TCR/reelin/synaptic annotations. Reason: Broad pathway term; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0008360 regulation of cell shape | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Fyn regulates cell shape through cytoskeletal-remodeling substrates. Reason: Downstream cytoskeletal outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:10872802 Molecular cloning of the mouse APS as a member of the Lnk fa... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:8196616 Interactions of p59fyn and ZAP-70 with T-cell receptor activ... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0044325 transmembrane transporter binding | IPI PMID:12538589 Regulation of a transient receptor potential (TRP) channel b... | KEEP AS NON CORE | Summary: Fyn binds and phosphorylates membrane transport proteins (e.g. TRPC6) in specific contexts. Reason: Specific partner interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0010629 negative regulation of gene expression | IMP PMID:20978343 CD36 participates in a signaling pathway that regulates ROS ... | KEEP AS NON CORE | Summary: Distal transcriptional consequence of Fyn signaling in specific contexts. Reason: Highly distal outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md TCR stimulation induces STAT3 phosphorylation at Y705 through a Lck/Fyn-dependent axis |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:16841086 Src-family tyrosine kinase fyn phosphorylates phosphatidylin... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0042177 negative regulation of protein catabolic process | IMP PMID:16841086 Src-family tyrosine kinase fyn phosphorylates phosphatidylin... | KEEP AS NON CORE | Summary: Fyn can stabilize substrates against degradation in particular contexts. Reason: Context-specific regulatory outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-420382 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-MMU-420394 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005829 cytosol | TAS Reactome:R-NUL-420386 | ACCEPT | Summary: Fyn is a cytoplasmic kinase; the cytosol/cell membrane interface is a primary site of its action. Reason: Core localization for a non-receptor kinase (UniProt: Cytoplasm). Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:7799925 Association of p62, a multifunctional SH2- and SH3-domain-bi... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IMP PMID:9381182 Fyn-kinase as a determinant of ethanol sensitivity: relation... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0045471 response to ethanol | IGI PMID:9381182 Fyn-kinase as a determinant of ethanol sensitivity: relation... | KEEP AS NON CORE | Summary: Fyn modulates NMDAR responses to ethanol; this annotation has experimental (IGI) support. Reason: Genuine but downstream neuronal drug-response context; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md PSD95 interaction with the SH2 domain of Fyn facilitates Fyn phosphorylation of tyrosines on NMDAR subunits (including NR2A context), increasing NMDAR activity and supporting NMDAR-dependent synaptic potentiation |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:8175795 CD45 regulation of tyrosine phosphorylation and enzyme activ... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0018108 peptidyl-tyrosine phosphorylation | IDA PMID:8175795 CD45 regulation of tyrosine phosphorylation and enzyme activ... | ACCEPT | Summary: Fyn phosphorylates tyrosine residues on numerous substrates (e.g. DAB1, NMDAR subunits, PTK2/FAK, catenins, PAG1); peptidyl-tyrosine phosphorylation is the direct biochemical process it carries out. Reason: Directly reflects Fyn's catalytic output; core process supported by UniProt and primary literature. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0046777 protein autophosphorylation | IDA PMID:8175795 CD45 regulation of tyrosine phosphorylation and enzyme activ... | ACCEPT | Summary: Fyn autophosphorylates its activation-loop Tyr-420, a hallmark of Src-family kinase activation. Reason: Well-established intramolecular activity of Fyn (UniProt PTM, PubMed:8441403); core to its activation cycle. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0050798 activated T cell proliferation | IMP PMID:1516132 Defective T cell receptor signaling in mice lacking the thym... | KEEP AS NON CORE | Summary: Downstream T-cell proliferation outcome of Fyn-dependent TCR signaling. Reason: Downstream cellular outcome; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is positioned in proximal T cell receptor (TCR) signaling networks and can function redundantly/overlapping with Lck in early receptor-triggered phosphorylation cascades |
| GO:0006468 protein phosphorylation | IMP PMID:16190898 Fyn kinase-mediated phosphorylation of NMDA receptor NR2B su... | MODIFY | Summary: Fyn phosphorylates tyrosine, not generic Ser/Thr/Tyr; the precise process is peptidyl-tyrosine phosphorylation. Reason: Replace generic 'protein phosphorylation' with the tyrosine-specific process term. Proposed replacements: peptidyl-tyrosine phosphorylation Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0006468 protein phosphorylation | IMP PMID:9892651 PSD-95 promotes Fyn-mediated tyrosine phosphorylation of the... | MODIFY | Summary: Fyn phosphorylates tyrosine, not generic Ser/Thr/Tyr; the precise process is peptidyl-tyrosine phosphorylation. Reason: Replace generic 'protein phosphorylation' with the tyrosine-specific process term. Proposed replacements: peptidyl-tyrosine phosphorylation Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0050966 detection of mechanical stimulus involved in sensory perception of pain | IMP PMID:16190898 Fyn kinase-mediated phosphorylation of NMDA receptor NR2B su... | KEEP AS NON CORE | Summary: Fyn contributes to nociceptive signaling in specific sensory contexts (knockout phenotype). Reason: Distal organismal/sensory phenotype; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:10872802 Molecular cloning of the mouse APS as a member of the Lnk fa... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0005515 protein binding | IPI PMID:10713104 HS1 interacts with Lyn and is critical for erythropoietin-in... | MARK AS OVER ANNOTATED | Summary: Generic 'protein binding' (24 IPI annotations) conveys no functional specificity for Fyn; its meaningful interactions are SH2/SH3-mediated substrate and adaptor docking already captured by specific terms. Reason: Uninformative generic binding term; per curation guidelines a more specific MF (kinase activity, specific partner binding) should carry the information. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0001764 neuron migration | IMP PMID:15073522 Defective neocortical development in Fyn-tyrosine-kinase-def... | KEEP AS NON CORE | Summary: Neuronal migration defects arise downstream of impaired reelin/DAB1 signaling in Fyn-deficient brains. Reason: Developmental outcome downstream of the core reelin pathway; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0030900 forebrain development | IMP PMID:15073522 Defective neocortical development in Fyn-tyrosine-kinase-def... | KEEP AS NON CORE | Summary: Forebrain cytoarchitecture/myelination phenotypes are downstream consequences of Fyn loss. Reason: Distal developmental phenotype; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0001764 neuron migration | IGI PMID:16162939 Absence of Fyn and Src causes a reeler-like phenotype. | KEEP AS NON CORE | Summary: Neuronal migration defects arise downstream of impaired reelin/DAB1 signaling in Fyn-deficient brains. Reason: Developmental outcome downstream of the core reelin pathway; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0030900 forebrain development | IGI PMID:16162939 Absence of Fyn and Src causes a reeler-like phenotype. | KEEP AS NON CORE | Summary: Forebrain cytoarchitecture/myelination phenotypes are downstream consequences of Fyn loss. Reason: Distal developmental phenotype; non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md In neurons, Fyn regulates neurite outgrowth, microtubule dynamics, dendritic targeting, synaptic transmission, and plasticity |
| GO:0004713 protein tyrosine kinase activity | IDA PMID:8196616 Interactions of p59fyn and ZAP-70 with T-cell receptor activ... | ACCEPT | Summary: Fyn is a Src-family non-receptor tyrosine kinase (EC 2.7.10.2) that transfers phosphate from ATP to tyrosine residues of substrate proteins; this is its defining catalytic activity. Reason: Core catalytic molecular function of Fyn, directly supported by UniProt catalytic activity and extensive experimental assay. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0004672 protein kinase activity | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | MODIFY | Summary: Fyn is specifically a tyrosine kinase; the generic 'protein kinase activity' term under-specifies and could imply Ser/Thr activity. Reason: Replace with the tyrosine-specific child term to capture the actual substrate chemistry. Proposed replacements: non-membrane spanning protein tyrosine kinase activity Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md its SH2/SH3 docking and membrane targeting drive selective incorporation into receptor-proximal and synaptic complexes, while phosphorylation at conserved regulatory tyrosines toggles activity |
| GO:0015631 tubulin binding | IDA PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Fyn associates with tubulin/microtubules in cytoskeletal remodeling. Reason: Cytoskeletal interaction; context-specific, non-core. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is described as linking upstream cues (e.g., integrins/TrkB-associated signaling) to cytoskeletal remodeling pathways, including Rho-family GTPases and p190 RhoGAP phosphorylation, supporting process extension and axon contact |
| GO:0042552 myelination | TAS PMID:11826099 Process outgrowth of oligodendrocytes is promoted by interac... | KEEP AS NON CORE | Summary: Fyn is required for oligodendrocyte differentiation and CNS myelination; Fyn-null mice show forebrain hypomyelination. Reason: Well-supported but downstream developmental/glial process; non-core relative to kinase MF. Supporting Evidence: UniProt:P39688 FUNCTION: Non-receptor tyrosine-protein kinase that plays a role in regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. CATALYTIC ACTIVITY: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H(+). SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane. Present and active in lipid rafts. file:mouse/Fyn/Fyn-deep-research-falcon.md Fyn is active during the myelination period and is required for oligodendrocyte morphological differentiation and myelination programs |
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