FGF1 (acidic fibroblast growth factor) is a heparin-binding beta-trefoil member of the paracrine FGF family and the only FGF able to bind and activate all seven principal FGF receptor isoforms (FGFR1-3 IIIb/IIIc and FGFR4). It lacks a signal peptide and is released from cells by a stress-induced, copper- and S100A13/synaptotagmin-1-dependent non-classical export pathway. Extracellular FGF1, stabilized and presented by heparan sulfate proteoglycans, binds the D2-D3 region of FGFRs to drive receptor dimerization and tyrosine kinase activation, engaging FRS2alpha-RAS-ERK, PI3K-AKT and PLCgamma signaling. These pathways make FGF1 a potent mitogen and chemoattractant for fibroblasts, endothelial and epithelial cells and a pro-angiogenic factor. FGF1 has also been reported to bind integrin alphaV-beta3. Internalized FGF1 can translocate into the cytosol and, via an N-terminal NLS, LRRC59 and importins, into the nucleus, and intracellular FGF1 has an FGFR-independent anti-apoptotic activity linked to direct binding of p53. Fgf1-null mice are essentially normal under standard conditions but develop severe insulin resistance and aberrant adipose remodelling on a high-fat diet, where FGF1 is induced by PPARgamma; exogenous FGF1 is a potent insulin sensitizer in rodents.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001658 branching involved in ureteric bud morphogenesis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA electronic annotation of ureteric bud branching. Reason: Consistent with the in vitro UB culture data for FGF1, but no in vivo requirement has been shown; non-core. Supporting Evidence: PMID:11731227 FGF1 and FGF10 appear to be more important for branching and branch elongation |
| GO:0005104 fibroblast growth factor receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT places FGFR binding at the ancestral paracrine FGF node (PTN000160075); FGF1 is a canonical member of that clade and has its own direct experimental evidence. Reason: FGF1 is the prototypic paracrine FGF and the only FGF that activates every principal FGFR splice isoform; receptor binding at the D2-D3 region is its defining molecular activity. The IBA node placement is sound and FGF1 lies squarely inside the inheriting clade. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. PMID:10830168 These structures provide a molecular basis for FGF1 as a universal FGFR ligand file:human/FGF1/FGF1-deep-research-falcon.md FGF1 exhibits remarkable promiscuity as a "universal ligand" capable of binding and activating all four principal FGFRs |
| GO:0005104 fibroblast growth factor receptor binding | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA electronic transfer of FGFR binding; consistent with extensive direct evidence for FGF1. Reason: FGF1 is the prototypic paracrine FGF and the only FGF that activates every principal FGFR splice isoform; receptor binding at the D2-D3 region is its defining molecular activity. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0005104 fibroblast growth factor receptor binding | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | ACCEPT | Summary: Mori et al. showed that FGF1 mutants in the predicted FGFR-binding site lose FGFR1 binding and signaling, while retaining integrin and heparin binding. Reason: FGF1 is the prototypic paracrine FGF and the only FGF that activates every principal FGFR splice isoform; receptor binding at the D2-D3 region is its defining molecular activity. Site-directed mutagenesis separated the FGFR-binding surface from the heparin/integrin surfaces. Supporting Evidence: PMID:18441324 We found that the integrin-binding site of FGF1 overlaps with the heparin-binding site but is distinct from the FGFR-binding site using docking simulation and mutagenesis. |
| GO:0005104 fibroblast growth factor receptor binding | IPI PMID:10830168 Crystal structures of two FGF-FGFR complexes reveal the dete... | ACCEPT | Summary: Crystal structure of FGF1 bound to the D2-D3 ligand-binding domains of FGFR1 (Plotnikov et al. 2000). Reason: FGF1 is the prototypic paracrine FGF and the only FGF that activates every principal FGFR splice isoform; receptor binding at the D2-D3 region is its defining molecular activity. Direct structural evidence of the FGF1-FGFR1 complex. Supporting Evidence: PMID:10830168 These structures provide a molecular basis for FGF1 as a universal FGFR ligand |
| GO:0005104 fibroblast growth factor receptor binding | IPI PMID:12815063 Fibroblast growth factor (FGF) homologous factors share stru... | ACCEPT | Summary: Olsen et al. used FGF1 as the reference ligand that activates FGFRs (including FGFR3 isoforms) in contrast to FGF homologous factors, and mutating FGF1 surface residues reduced receptor activation. Reason: FGF1 is the prototypic paracrine FGF and the only FGF that activates every principal FGFR splice isoform; receptor binding at the D2-D3 region is its defining molecular activity. The GOA rows (FGFR3 isoforms IIIb and IIIc as partners) are consistent with FGF1 activating all seven principal FGFRs; the cached record is abstract-only so the curator's full-text reading is deferred to. Supporting Evidence: PMID:12815063 mutations of the corresponding residues of FGF1 to Arg and Val diminish the capacity of FGF1 to activate FGFRs PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0005104 fibroblast growth factor receptor binding | IPI PMID:12815063 Fibroblast growth factor (FGF) homologous factors share stru... | ACCEPT | Summary: Olsen et al. used FGF1 as the reference ligand that activates FGFRs (including FGFR3 isoforms) in contrast to FGF homologous factors, and mutating FGF1 surface residues reduced receptor activation. Reason: FGF1 is the prototypic paracrine FGF and the only FGF that activates every principal FGFR splice isoform; receptor binding at the D2-D3 region is its defining molecular activity. The GOA rows (FGFR3 isoforms IIIb and IIIc as partners) are consistent with FGF1 activating all seven principal FGFRs; the cached record is abstract-only so the curator's full-text reading is deferred to. Supporting Evidence: PMID:12815063 mutations of the corresponding residues of FGF1 to Arg and Val diminish the capacity of FGF1 to activate FGFRs PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0005178 integrin binding | IDA PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | KEEP AS NON CORE | Summary: FGF1 binds integrin alphaV-beta3 directly (KD ~1 uM); the integrin-binding-defective R50E mutant still binds FGFR and heparin but is defective in mitogenic and migratory signaling. Reason: Direct binding is experimentally supported by solid-phase binding and mutagenesis, but the integrin co-receptor model comes largely from a single laboratory and is an accessory to, not the basis of, FGFR-mediated signaling. Retained as a genuine but non-core activity. Supporting Evidence: PMID:18441324 We discovered that FGF1 directly bound to soluble and cell-surface integrin alphavbeta3 (K(D) about 1 microm). PMID:18441324 R50E was defective in inducing DNA synthesis, cell proliferation, cell migration, and chemotaxis |
| GO:0005515 protein binding | IPI PMID:10618369 Structural interactions of fibroblast growth factor receptor... | MODIFY | Summary: Crystal structure of human FGF1 with the D2-D3 fragment of human FGFR2. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:10618369 We have crystallized a complex between human FGF1 and a two-domain extracellular fragment of human FGFR2. |
| GO:0005515 protein binding | IPI PMID:10830168 Crystal structures of two FGF-FGFR complexes reveal the dete... | MODIFY | Summary: Crystal structure of FGF1 with FGFR1 D2-D3. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:10830168 These structures provide a molecular basis for FGF1 as a universal FGFR ligand |
| GO:0005515 protein binding | IPI PMID:14613973 Proline to arginine mutations in FGF receptors 1 and 3 resul... | MODIFY | Summary: SPR binding of FGF ligands (including FGF1) to wild-type and Pfeiffer-mutant FGFR1c; abstract-only in cache. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. The cached abstract does not name FGF1 explicitly, but the curator had the full text and the FGFR1 partner is fully consistent with FGF1 biology. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:14613973 Both Pro252Arg FGFR1c and Pro250Arg FGFR3c exhibit an enhancement in ligand binding in comparison to their respective wild-type receptors. |
| GO:0005515 protein binding | IPI PMID:14732692 Insights into the molecular basis for fibroblast growth fact... | MODIFY | Summary: Crystal structure and SPR of FGF1 with the three-Ig form of FGFR3c. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:14732692 we report the crystal structure of the three-Ig form of FGFR3c in complex with FGF1, an FGF that binds promiscuously to each of the seven principal FGFRs. |
| GO:0005515 protein binding | IPI PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | MODIFY | Summary: FGF1 binding to FGFR1 assessed alongside integrin-binding mutants. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:18441324 We found that the integrin-binding site of FGF1 overlaps with the heparin-binding site but is distinct from the FGFR-binding site using docking simulation and mutagenesis. |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: In situ proximity ligation screen in HeLa cells detected FGF1 proximity to FGFR1/FGFR2 (abstract-only in cache). Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. The PLA screen on its own reports proximity only, but the partner identity matches the well-established ligand-receptor pairing. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:25241761 we collected ∼ 700 primary antibodies and employed a highly sensitive and specific technique, an in situ proximity ligation assay, to investigate 1204 endogenous PPIs in HeLa cells |
| GO:0005515 protein binding | IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ... | MODIFY | Summary: In situ proximity ligation screen in HeLa cells detected FGF1 proximity to FGFR1/FGFR2 (abstract-only in cache). Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. The PLA screen on its own reports proximity only, but the partner identity matches the well-established ligand-receptor pairing. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:25241761 we collected ∼ 700 primary antibodies and employed a highly sensitive and specific technique, an in situ proximity ligation assay, to investigate 1204 endogenous PPIs in HeLa cells |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: HuRI binary yeast two-hybrid screen reported FGF1 interacting with VBP1 (prefoldin subunit 3). Reason: Generic protein binding is uninformative; the interaction with the cytosolic prefoldin subunit VBP1 comes from a proteome-scale Y2H screen with no functional follow-up and does not support a more specific molecular function. Removal does not assert that the interaction is false. Supporting Evidence: PMID:32296183 A reference map of the human binary protein interactome. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: BioPlex 3.0 affinity-purification mass spectrometry recovered FGF1 with FGFR1/FGFR2. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. High-throughput AP-MS, but the partner identity matches the well-established ligand-receptor pairing. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:33961781 Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: BioPlex 3.0 affinity-purification mass spectrometry recovered FGF1 with FGFR1/FGFR2. Reason: Generic 'protein binding' is uninformative. The partner here is an FGF receptor, and the cited work supports the specific, established activity of FGF1 as an FGFR ligand; replace with fibroblast growth factor receptor binding. High-throughput AP-MS, but the partner identity matches the well-established ligand-receptor pairing. Proposed replacements: fibroblast growth factor receptor binding Supporting Evidence: PMID:33961781 Through affinity-purification mass spectrometry, we have created two proteome-scale, cell-line-specific interaction networks. |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: Extracellular location inherited at the paracrine FGF node. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. PMID:12746488 the signal peptide-less angiogenic polypeptide, FGF1, uses intracellular Cu2+ to facilitate the formation of a multiprotein aggregate that enables the release of FGF1 in response to stress |
| GO:0005576 extracellular region | IDA PMID:12746488 S100A13 mediates the copper-dependent stress-induced release... | ACCEPT | Summary: Stress-induced, Cu2+-dependent release of FGF1 into the extracellular compartment (Maciag laboratory). Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: PMID:12746488 the signal peptide-less angiogenic polypeptide, FGF1, uses intracellular Cu2+ to facilitate the formation of a multiprotein aggregate that enables the release of FGF1 in response to stress |
| GO:0005576 extracellular region | IDA PMID:18400376 The release of fibroblast growth factor-1 from melanoma cell... | ACCEPT | Summary: FGF-1 is secreted from A375 melanoma cells under serum deprivation, dependent on copper and PI3K/Akt. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: PMID:18400376 We demonstrated that FGF-1 is secreted from a human melanoma cell line, A375, under conditions of serum deprivation. |
| GO:0005576 extracellular region | IEA GO_REF:0000120 | ACCEPT | Summary: Combined automated extracellular-region annotation. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-109699 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1839094 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1839098 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1839100 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190245 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190256 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190258 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190260 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190261 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190263 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190265 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190326 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190385 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190388 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190408 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190413 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190427 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-190429 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2012073 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2012074 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2023451 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2023455 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2033472 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2033474 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2033486 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2033488 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2077420 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2077421 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2077424 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2316434 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2400009 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654147 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654148 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654149 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654151 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654157 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654159 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654163 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654165 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654167 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654169 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654222 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654224 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654392 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654397 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654399 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654402 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654404 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654406 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654407 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654408 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654409 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654413 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654416 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654418 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654422 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654423 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654425 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654426 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654428 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654560 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654562 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654565 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654566 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654569 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654571 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654573 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654575 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654578 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654582 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654584 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654586 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654587 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654591 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654592 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654594 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654596 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654597 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654600 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654603 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654605 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654607 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654608 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654612 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654614 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654615 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654618 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654620 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654622 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654623 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654625 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654628 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654631 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654633 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654634 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654637 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654640 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654641 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654643 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654646 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654647 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654651 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654653 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654655 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654658 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654659 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654662 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654663 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654664 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654667 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654669 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654672 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654673 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654677 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654679 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654684 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654690 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654692 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654697 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654701 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654705 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654709 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654714 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654717 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654729 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654730 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654734 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5654748 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655233 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655240 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655241 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655243 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655244 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655245 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655247 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655262 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655263 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655266 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655268 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655269 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655270 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655277 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655278 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655285 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655289 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655290 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655295 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655301 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655315 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655320 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655323 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655326 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655339 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5655343 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5656064 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-5672965 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005576 extracellular region | TAS Reactome:R-NUL-8853328 | ACCEPT | Summary: Reactome places FGF1 in the extracellular region as the ligand in FGF-FGFR binding and activation reactions; one of many source-distinct TAS rows for the same valid location. Reason: FGF1 lacks a signal peptide but is exported by a stress-induced non-classical route and acts on cell-surface FGFR/heparan sulfate complexes; the extracellular region is where its canonical ligand activity is executed. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT nuclear location at node PTN000896537. Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. FGF1 has an N-terminal NLS (KKPK, residues 24-27) and LRRC59/importin-dependent nuclear import. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt Nuclear import from the cytosol requires the classical nuclear import PMID:22321063 Fibroblast growth factor 1 (FGF1) taken up by cells into endocytic vesicles can be translocated across vesicular membranes into the cytosol and the nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular location mapping (Nucleus). Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal sequence. PMID:22321063 Fibroblast growth factor 1 (FGF1) taken up by cells into endocytic vesicles can be translocated across vesicular membranes into the cytosol and the nucleus |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human Protein Atlas immunofluorescence detected FGF1 in the nucleoplasm. Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Supporting Evidence: PMID:22321063 Fibroblast growth factor 1 (FGF1) taken up by cells into endocytic vesicles can be translocated across vesicular membranes into the cytosol and the nucleus |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT cytoplasmic location for the paracrine FGF node. Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. PMID:35159330 FGF1 can act intracellularly, before secretion or after internalization and translocation from the cell exterior. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular location mapping (Cytoplasm). Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. |
| GO:0005829 cytosol | IDA PMID:12746488 S100A13 mediates the copper-dependent stress-induced release... | KEEP AS NON CORE | Summary: Intracellular (cytosolic) FGF1 forms the Cu2+-dependent S100A13 export aggregate prior to release. Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Supporting Evidence: PMID:12746488 the signal peptide-less angiogenic polypeptide, FGF1, uses intracellular Cu2+ to facilitate the formation of a multiprotein aggregate that enables the release of FGF1 in response to stress |
| GO:0005829 cytosol | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular location mapping (Cytoplasm, cytosol). Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt Cytoplasm, cytosol. Nucleus. Note=Lacks a cleavable signal sequence. PMID:22321063 Fibroblast growth factor 1 (FGF1) taken up by cells into endocytic vesicles can be translocated across vesicular membranes into the cytosol and the nucleus |
| GO:0005938 cell cortex | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: UniProt subcellular location mapping (Cytoplasm, cell cortex), reflecting stress-induced sub-membrane accumulation prior to non-classical export. Reason: FGF1 lacks a cleavable signal sequence; an intracellular pool exists before secretion, and exogenous FGF1 can be internalized, translocated to the cytosol and imported into the nucleus. These intracellular locations are well documented but relate to trafficking and a receptor-independent anti-apoptotic role rather than the canonical ligand function. Heat shock relocates FGF1 with AHNAK2 to the cortical F-actin near the plasma membrane before export. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt SUBCELLULAR LOCATION: Secreted. Cytoplasm. Cytoplasm, cell cortex. PMID:25560297 Upon stress, FGF1 is transported to the plasma membrane where it localizes prior to transmembrane translocation. |
| GO:0007165 signal transduction | NAS PMID:3778488 Amino acid sequence of human acidic fibroblast growth factor... | MODIFY | Summary: Generic signal transduction asserted from the amino-acid sequence paper of human acidic FGF. Reason: Not wrong, but far too general and the cited paper is a sequencing study; the informative process is the FGFR signaling pathway, already supported experimentally. Proposed replacements: fibroblast growth factor receptor signaling pathway Supporting Evidence: PMID:3778488 The complete amino acid sequence of human brain acidic fibroblast growth factor (aFGF) has been established. |
| GO:0008083 growth factor activity | IBA GO_REF:0000033 | ACCEPT | Summary: Growth factor activity inherited at the paracrine FGF PAINT node. Reason: FGF1 is a potent extracellular mitogen that acts through FGFR tyrosine kinases; 'growth factor activity' correctly captures the ligand activity and is compatible with the more specific FGFR binding term. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. file:human/FGF1/FGF1-uniprot.txt Functions as a potent mitogen in vitro. |
| GO:0008083 growth factor activity | IDA PMID:20145243 Gentisic acid, a compound associated with plant defense and ... | ACCEPT | Summary: FGF-1-driven mitogenesis of Balb/c 3T3 fibroblasts and FR1c-11 cells, used as the assay for gentisic acid inhibitors. Reason: FGF1 is a potent extracellular mitogen that acts through FGFR tyrosine kinases; 'growth factor activity' correctly captures the ligand activity and is compatible with the more specific FGFR binding term. Supporting Evidence: PMID:20145243 The potential inhibition of FGF mitogenic activity by GA was first assayed in vitro using FGF-1 and Balb/c 3T3 fibroblasts |
| GO:0008083 growth factor activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined automated growth factor activity annotation. Reason: FGF1 is a potent extracellular mitogen that acts through FGFR tyrosine kinases; 'growth factor activity' correctly captures the ligand activity and is compatible with the more specific FGFR binding term. Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt Functions as a potent mitogen in vitro. |
| GO:0008083 growth factor activity | TAS PMID:1693186 Alternative splicing generates two forms of mRNA coding for ... | ACCEPT | Summary: Author statement that HBGF-1 (FGF1) is a mitogen for many cell types and angiogenic in vivo. Reason: FGF1 is a potent extracellular mitogen that acts through FGFR tyrosine kinases; 'growth factor activity' correctly captures the ligand activity and is compatible with the more specific FGFR binding term. Supporting Evidence: PMID:1693186 is a mitogen for a variety of mesoderm- and neutroectoderm-derived cells in vitro as well as an angiogenic factor in vivo. |
| GO:0008201 heparin binding | IDA PMID:20145243 Gentisic acid, a compound associated with plant defense and ... | ACCEPT | Summary: Crystal structures show inhibitors docking in the FGF-1 heparin-binding channel and competing with heparin in heparin-affinity chromatography. Reason: Heparin/heparan sulfate binding through the basic C-terminal region (residues 127-143) is a defining, structurally characterized property of FGF1 that stabilizes the ligand and is required for productive FGFR activation. Supporting Evidence: PMID:20145243 part of the long cationic channel that constitutes the FGF-1 heparin binding site |
| GO:0008201 heparin binding | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | ACCEPT | Summary: Charge-reversal mutations in the heparin-binding region (4xE) abolished FGF1 heparin binding. Reason: Heparin/heparan sulfate binding through the basic C-terminal region (residues 127-143) is a defining, structurally characterized property of FGF1 that stabilizes the ligand and is required for productive FGFR activation. Supporting Evidence: PMID:18441324 the 4xE mutant did not show affinity to heparin |
| GO:0008284 positive regulation of cell population proliferation | IBA GO_REF:0000033 | ACCEPT | Summary: Positive regulation of proliferation inherited at the paracrine FGF node. Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008284 positive regulation of cell population proliferation | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA electronic annotation. Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: file:human/FGF1/FGF1-uniprot.txt Functions as a potent mitogen in vitro. |
| GO:0008284 positive regulation of cell population proliferation | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 plus heparin drove proliferation of BaF3 cells expressing each of the seven FGFR forms (positive control in the betaKlotho study). Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:18187602 All of the BaF3 transfectants could be induced to proliferate with FGF1 plus heparin (Fig. 3), indicating that FGFR signaling was operating in these cells. |
| GO:0008284 positive regulation of cell population proliferation | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 plus heparin drove proliferation of BaF3 cells expressing each of the seven FGFR forms (positive control in the betaKlotho study). Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:18187602 All of the BaF3 transfectants could be induced to proliferate with FGF1 plus heparin (Fig. 3), indicating that FGFR signaling was operating in these cells. |
| GO:0008284 positive regulation of cell population proliferation | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 plus heparin drove proliferation of BaF3 cells expressing each of the seven FGFR forms (positive control in the betaKlotho study). Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:18187602 All of the BaF3 transfectants could be induced to proliferate with FGF1 plus heparin (Fig. 3), indicating that FGFR signaling was operating in these cells. |
| GO:0008284 positive regulation of cell population proliferation | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 plus heparin drove proliferation of BaF3 cells expressing each of the seven FGFR forms (positive control in the betaKlotho study). Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:18187602 All of the BaF3 transfectants could be induced to proliferate with FGF1 plus heparin (Fig. 3), indicating that FGFR signaling was operating in these cells. |
| GO:0008284 positive regulation of cell population proliferation | IGI PMID:8663044 Receptor specificity of the fibroblast growth factor family. | ACCEPT | Summary: Mitogenic assays on BaF3 lines expressing individual FGFR splice variants showed FGF1 activates all of them. Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008284 positive regulation of cell population proliferation | IGI PMID:8663044 Receptor specificity of the fibroblast growth factor family. | ACCEPT | Summary: Mitogenic assays on BaF3 lines expressing individual FGFR splice variants showed FGF1 activates all of them. Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008284 positive regulation of cell population proliferation | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | ACCEPT | Summary: WT FGF1 robustly induced BaF3-FGFR1c proliferation; FGFR-, heparin- or integrin-binding mutants did not. Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:18441324 We found that WT FGF1 robustly induced proliferation of BaF3-FGFR1c cells |
| GO:0008284 positive regulation of cell population proliferation | IMP PMID:23469107 A dominant-negative FGF1 mutant (the R50E mutant) suppresses... | ACCEPT | Summary: WT FGF1 expression enhanced tumor growth in vivo, while the R50E mutant suppressed it. Reason: FGF1 is a prototypic mitogen; stimulation of proliferation via FGFR activation is among its best-established biological outputs (the Ornitz BaF3 receptor-specificity assays are proliferation readouts). Supporting Evidence: PMID:23469107 R50E suppressed tumor growth in vivo while WT FGF1 enhanced it using cancer cells that stably express WT FGF1 or R50E. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: FGFR signaling pathway inherited at the paracrine FGF PAINT node. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IDA PMID:20145243 Gentisic acid, a compound associated with plant defense and ... | ACCEPT | Summary: FGF-1-driven signaling/mitogenesis in cells expressing FGFR1 (FR1c-11) inhibited by 2,5DHPS. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:20145243 A series of experiments were carried out with FR1c-11 cells, a heparin-less lymphoid cell line stably transfected with the full three-Ig domain murine FGF receptor 1 |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA electronic annotation. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 used as the pan-FGFR positive control in BaF3 cells expressing mouse Fgfr1c, Fgfr2c, Fgfr3c and Fgfr4. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:18187602 FGF1 was included as a positive control to stimulate all the FGFR transfectants |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 used as the pan-FGFR positive control in BaF3 cells expressing mouse Fgfr1c, Fgfr2c, Fgfr3c and Fgfr4. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:18187602 FGF1 was included as a positive control to stimulate all the FGFR transfectants |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 used as the pan-FGFR positive control in BaF3 cells expressing mouse Fgfr1c, Fgfr2c, Fgfr3c and Fgfr4. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:18187602 FGF1 was included as a positive control to stimulate all the FGFR transfectants |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:18187602 betaKlotho is required for fibroblast growth factor (FGF) 21... | ACCEPT | Summary: FGF1 used as the pan-FGFR positive control in BaF3 cells expressing mouse Fgfr1c, Fgfr2c, Fgfr3c and Fgfr4. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:18187602 FGF1 was included as a positive control to stimulate all the FGFR transfectants |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:8663044 Receptor specificity of the fibroblast growth factor family. | ACCEPT | Summary: FGF1 activates all FGFR splice variants in engineered BaF3 lines. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:8663044 Receptor specificity of the fibroblast growth factor family. | ACCEPT | Summary: FGF1 activates all FGFR splice variants in engineered BaF3 lines. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IGI PMID:8663044 Receptor specificity of the fibroblast growth factor family. | ACCEPT | Summary: FGF1 activates all FGFR splice variants in engineered BaF3 lines. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:8663044 These studies demonstrate that FGF 1 is the only FGF that can activate all FGF receptor splice variants. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | ACCEPT | Summary: FGF1 mutants in the FGFR-binding site fail to induce FGFR1/FRS2alpha phosphorylation and downstream signaling. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:18441324 We found that the integrin-binding site of FGF1 overlaps with the heparin-binding site but is distinct from the FGFR-binding site using docking simulation and mutagenesis. PMID:18441324 R50E induced phosphorylation of FGFR1 and FRS2alpha and activation of AKT and ERK1/2. |
| GO:0008543 fibroblast growth factor receptor signaling pathway | IPI PMID:10830168 Crystal structures of two FGF-FGFR complexes reveal the dete... | ACCEPT | Summary: Structural basis of FGF1-FGFR1 complex formation. Reason: As the ligand, FGF1 initiates FGFR signaling; this is its central biological process and the one modelled for it in the FGFR signaling pathway. Supporting Evidence: PMID:10830168 These structures provide a molecular basis for FGF1 as a universal FGFR ligand |
| GO:0009653 anatomical structure morphogenesis | TAS PMID:1693186 Alternative splicing generates two forms of mRNA coding for ... | MARK AS OVER ANNOTATED | Summary: Author speculation that HBGF-1 may be involved in embryonic development of the heart. Reason: The cited statement is speculative ('may be involved') and based on fetal heart mRNA expression. Fgf1-null mice have no detectable developmental abnormalities, so a broad morphogenesis annotation overstates FGF1's demonstrated role. Not removed because FGF1 can drive morphogenetic responses when supplied exogenously (e.g. ureteric bud). Supporting Evidence: PMID:1693186 Thus, HBGF-1 may be involved in mediating processes such as embryonic development and vascular growth in the heart. PMID:10688672 Essentially no abnormalities were found in mice lacking only FGF1. |
| GO:0010595 positive regulation of endothelial cell migration | IMP PMID:23469107 A dominant-negative FGF1 mutant (the R50E mutant) suppresses... | KEEP AS NON CORE | Summary: FGF1-induced HUVEC migration was suppressed by the R50E dominant-negative mutant. Reason: FGF1 is a well-established endothelial chemoattractant; this is a downstream cellular output of FGFR signaling. Supporting Evidence: PMID:23469107 We found that excess R50E suppressed FGF1-induced migration and tube formation of endothelial cells, FGF1-induced angiogenesis in matrigel plug assays, and the outgrowth of cells in aorta ring assays. |
| GO:0022008 neurogenesis | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Neurogenesis inherited at the paracrine FGF node. Reason: FGF1 lies inside the inheriting clade and is abundant in brain with neurotrophic/mitogenic effects on neural cells, but it has no demonstrated non-redundant role in neurogenesis in vivo (Fgf1-null mice are essentially normal). Retained as non-core family-level inference. Supporting Evidence: PMID:10688672 Essentially no abnormalities were found in mice lacking only FGF1. |
| GO:0030334 regulation of cell migration | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Regulation of cell migration inherited at the paracrine FGF node. Reason: FGF1 stimulates migration and chemotaxis of fibroblasts and endothelial cells via FGFR signaling; a genuine but downstream cellular output. Supporting Evidence: PMID:18441324 Because FGF1 is a potent inducer of cell migration and chemotaxis |
| GO:0030335 positive regulation of cell migration | IDA PMID:20145243 Gentisic acid, a compound associated with plant defense and ... | KEEP AS NON CORE | Summary: FGF-induced cell migration in denuded endothelial monolayers inhibited by 2,5DHPS. Reason: FGF1 stimulates migration and chemotaxis of fibroblasts and endothelial cells via FGFR signaling; a genuine but downstream cellular output. Supporting Evidence: PMID:20145243 whether 2,5DHPS could inhibit FGF-induced cell migration was evaluated |
| GO:0030335 positive regulation of cell migration | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | KEEP AS NON CORE | Summary: WT FGF1 closed scratch wounds in Balb 3T3 cells; binding-defective mutants did not. Reason: FGF1 stimulates migration and chemotaxis of fibroblasts and endothelial cells via FGFR signaling; a genuine but downstream cellular output. Supporting Evidence: PMID:18441324 Because FGF1 is a potent inducer of cell migration and chemotaxis PMID:18441324 R50E was defective in inducing DNA synthesis, cell proliferation, cell migration, and chemotaxis |
| GO:0031012 extracellular matrix | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara transfer of extracellular matrix location from mouse Fgf1. Reason: Secreted FGF1 is retained by heparan sulfate proteoglycans at the cell surface and in the matrix; plausible and consistent with its heparin binding, but a storage/retention location rather than the site of its receptor-activating function. Supporting Evidence: PMID:20145243 part of the long cationic channel that constitutes the FGF-1 heparin binding site PMID:25043058 binding to heparan sulphate proteoglycans effectively precludes its circulation. |
| GO:0032148 activation of protein kinase B activity | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | KEEP AS NON CORE | Summary: FGF1 induced AKT activation in FGFR1-expressing cells; mutants defective in FGFR binding did not. Reason: AKT activation is a downstream consequence of FGFR/FRS2alpha/GAB1/PI3K signaling rather than a direct activity of FGF1; retained as a valid but non-core signaling output. Supporting Evidence: PMID:18441324 R50E induced phosphorylation of FGFR1 and FRS2alpha and activation of AKT and ERK1/2. |
| GO:0034605 cellular response to heat | IDA PMID:12746488 S100A13 mediates the copper-dependent stress-induced release... | KEEP AS NON CORE | Summary: FGF1 is released in response to heat (temperature) stress via a Cu2+/S100A13-dependent non-classical pathway. Reason: Stress-induced export of FGF1 is well documented by the Maciag/Prudovsky group; the annotation reflects regulated release rather than a role of FGF1 in mounting a heat-shock response. Non-core. Supporting Evidence: PMID:12746488 the signal peptide-less angiogenic polypeptide, FGF1, uses intracellular Cu2+ to facilitate the formation of a multiprotein aggregate that enables the release of FGF1 in response to stress PMID:11432880 tetrathiomolybdate, a Cu2+ chelator, significantly represses in a dose-dependent manner the heat shock-induced release of FGF1 and S100A13. |
| GO:0042060 wound healing | IDA PMID:16756958 Fibroblast growth factor 16 and 18 are expressed in human ca... | KEEP AS NON CORE | Summary: Endothelial migration in response to mechanical damage (scratch assay) in a study focused on FGF16/FGF18; FGF1 presumably used as a comparator in the full text (cache is abstract-only). Reason: The cached abstract does not mention FGF1, but the curator read the full text; FGF1 is a recognized pro-repair factor. Note that a scratch-closure assay is better captured by cell migration terms than by the organismal 'wound healing' process, and Fgf1-null mice show no wound-healing defect beyond that of FGF2-null mice. Kept as non-core rather than removed. Supporting Evidence: PMID:16756958 Both FGFs also enhanced cell migration in response to mechanical damage. |
| GO:0043406 positive regulation of MAP kinase activity | IDA PMID:16756958 Fibroblast growth factor 16 and 18 are expressed in human ca... | KEEP AS NON CORE | Summary: MAPK activation by FGFs in endothelial cells and hepatocytes (FGF16/18 study; abstract-only). Reason: FGF1 robustly activates ERK1/2 via FGFR-FRS2alpha; deferring to the curator's full-text reading. A downstream signaling output rather than a direct activity. Supporting Evidence: PMID:16756958 FGF2, which is mitogenic on endothelial cells and hepatocytes stimulates a sustained MAPK activation in both cell types |
| GO:0043410 positive regulation of MAPK cascade | IBA GO_REF:0000033 | ACCEPT | Summary: Positive regulation of MAPK cascade inherited at the paracrine FGF node. Reason: FGFR-FRS2alpha-GRB2-SOS-RAS-ERK signaling is the principal mitogenic output of FGF1 and is conserved across the paracrine FGF clade. Supporting Evidence: PMID:18441324 R50E induced phosphorylation of FGFR1 and FRS2alpha and activation of AKT and ERK1/2. |
| GO:0044548 S100 protein binding | IPI PMID:11432880 Copper induces the assembly of a multiprotein aggregate impl... | KEEP AS NON CORE | Summary: FGF1 binds S100A13 in a Cu2+-dependent manner, forming the multiprotein aggregate (with p40 Syt1) implicated in its non-classical release. Reason: Specific, reproducible interaction supporting the unconventional export pathway; genuine but it concerns trafficking of FGF1 rather than its signaling activity. Supporting Evidence: PMID:11432880 FGF1, p40 Syt1, and S100A13 are able to bind Cu2+ with similar affinity and to interact in the presence of Cu2+ to form a multiprotein aggregate |
| GO:0045542 positive regulation of cholesterol biosynthetic process | IDA PMID:19229075 FGF-1 induces expression of LXRalpha and production of 25-hy... | KEEP AS NON CORE | Summary: Exogenous FGF-1 increased cholesterol biosynthesis and HMG-CoA reductase expression in rat astrocytes via FGFR1 and MEK/ERK. Reason: Experimentally supported, cell-type-specific downstream effect of FGFR signaling in astrocytes; not a core function of FGF1. Supporting Evidence: PMID:19229075 Cholesterol biosynthesis is increased by FGF-1 ( Fig. 6A ) in association with increase of expression of the HMG-CoA reductase gene ( Fig. 6B ). PMID:19229075 FGF-1 was shown in astrocytes to activate the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase (MEK/ERK) signaling pathway for the increase of cholesterol biosynthesis |
| GO:0045766 positive regulation of angiogenesis | IDA PMID:20145243 Gentisic acid, a compound associated with plant defense and ... | ACCEPT | Summary: FGF-1-soaked sponges induced angiogenesis in rats, suppressed by 2,5DHPS. Reason: FGF1 was one of the first purified angiogenic factors and consistently drives endothelial proliferation, migration and tube formation in vivo and in vitro. Supporting Evidence: PMID:20145243 FGF-1 and FGF-2 were the first two pure polypeptides shown to promote angiogenesis |
| GO:0045944 positive regulation of transcription by RNA polymerase II | IDA PMID:19229075 FGF-1 induces expression of LXRalpha and production of 25-hy... | MARK AS OVER ANNOTATED | Summary: FGF-1 stimulated apoE and LXRalpha transcription in rat astrocytes. Reason: FGF1 is an extracellular ligand; transcriptional induction of apoE/LXRalpha is several steps downstream of FGFR1-MEK/ERK signaling and oxysterol production. Annotating FGF1 to a generic positive regulation of RNA polymerase II transcription over-extends the evidence. Supporting Evidence: PMID:19229075 The effect of FGF-1 on expression of the gene of −450 bp was abolished by inhibition of FGFR1. |
| GO:0051781 positive regulation of cell division | IDA PMID:20145243 Gentisic acid, a compound associated with plant defense and ... | KEEP AS NON CORE | Summary: FGF-1-driven mitogenesis (cell number increase) of Balb/c 3T3 fibroblasts. Reason: Correct in spirit but largely redundant with positive regulation of cell population proliferation, which better describes the mitogenesis readout. Supporting Evidence: PMID:20145243 The potential inhibition of FGF mitogenic activity by GA was first assayed in vitro using FGF-1 and Balb/c 3T3 fibroblasts |
| GO:0060681 branch elongation involved in ureteric bud branching | IDA PMID:11731227 Multiple fibroblast growth factors support growth of the ure... | KEEP AS NON CORE | Summary: Exogenous FGF1 induced elongated ureteric bud branching stalks in isolated rat UB culture. Reason: Clear in vitro gain-of-function effect, but FGF1 loss-of-function mice show no kidney phenotype, so the physiological role is uncertain; kept as non-core. Supporting Evidence: PMID:11731227 FGF1 induced the formation of elongated UB branching stalks with distinct proliferative ampullary tips PMID:11731227 FGF1 and FGF10 appear to be more important for branching and branch elongation PMID:10688672 Essentially no abnormalities were found in mice lacking only FGF1. |
| GO:0070374 positive regulation of ERK1 and ERK2 cascade | IMP PMID:18441324 Direct binding of integrin alphavbeta3 to FGF1 plays a role ... | ACCEPT | Summary: FGF1 induces ERK1/2 activation; FGFR-binding mutants fail to do so. Reason: ERK1/2 activation downstream of FGFR is the principal signaling output of FGF1 and is directly tied to its mitogenic activity. Supporting Evidence: PMID:18441324 R50E induced phosphorylation of FGFR1 and FRS2alpha and activation of AKT and ERK1/2. |
| GO:0072163 mesonephric epithelium development | IDA PMID:11731227 Multiple fibroblast growth factors support growth of the ure... | KEEP AS NON CORE | Summary: FGF1 effects on isolated ureteric bud growth and differentiation (GO classifies ureteric bud development under mesonephric tubule/epithelium development). Reason: Same in vitro evidence as the branch-elongation annotation; valid as an exogenous-factor effect but not a demonstrated physiological role. Supporting Evidence: PMID:11731227 FGF1 induced the formation of elongated UB branching stalks with distinct proliferative ampullary tips |
| GO:1901509 regulation of endothelial tube morphogenesis | IMP PMID:23469107 A dominant-negative FGF1 mutant (the R50E mutant) suppresses... | KEEP AS NON CORE | Summary: FGF1-induced HUVEC tube formation on Matrigel was suppressed by R50E. Reason: Valid angiogenesis-related cellular output; non-core relative to positive regulation of angiogenesis. Supporting Evidence: PMID:23469107 We found that excess R50E suppressed FGF1-induced migration and tube formation of endothelial cells, FGF1-induced angiogenesis in matrigel plug assays, and the outgrowth of cells in aorta ring assays. |
| GO:1902533 positive regulation of intracellular signal transduction | IDA PMID:19229075 FGF-1 induces expression of LXRalpha and production of 25-hy... | KEEP AS NON CORE | Summary: FGF-1 activated MEK/ERK and PI3K/Akt in astrocytes. Reason: Correct but generic; FGFR-mediated activation of intracellular kinase cascades is better represented by FGFR signaling pathway and positive regulation of MAPK/ERK cascade. Supporting Evidence: PMID:19229075 FGF-1 was shown in astrocytes to activate the mitogen-activated protein kinase kinase/extracellular signal-regulated kinase (MEK/ERK) signaling pathway for the increase of cholesterol biosynthesis |
| GO:1903672 positive regulation of sprouting angiogenesis | IEA GO_REF:0000117 | ACCEPT | Summary: ARBA electronic annotation of positive regulation of sprouting angiogenesis. Reason: FGF1 induces endothelial sprouting/outgrowth in aorta ring and CAM assays; consistent with its established angiogenic activity. Supporting Evidence: PMID:23469107 We found that excess R50E suppressed FGF1-induced migration and tube formation of endothelial cells, FGF1-induced angiogenesis in matrigel plug assays, and the outgrowth of cells in aorta ring assays. |
| GO:1903672 positive regulation of sprouting angiogenesis | IMP PMID:23469107 A dominant-negative FGF1 mutant (the R50E mutant) suppresses... | ACCEPT | Summary: FGF1-induced outgrowth in rat aorta ring and CAM angiogenesis assays blocked by the R50E dominant-negative mutant. Reason: Direct experimental support for FGF1-driven sprouting angiogenesis. Supporting Evidence: PMID:23469107 We found that excess R50E suppressed FGF1-induced migration and tube formation of endothelial cells, FGF1-induced angiogenesis in matrigel plug assays, and the outgrowth of cells in aorta ring assays. |
| GO:1905330 regulation of morphogenesis of an epithelium | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA electronic annotation. Reason: FGF1 can modulate epithelial morphogenesis when supplied exogenously (e.g. ureteric bud), but this is a context-dependent downstream effect. Supporting Evidence: PMID:11731227 FGF1 induced the formation of elongated UB branching stalks with distinct proliferative ampullary tips |
| GO:2000544 regulation of endothelial cell chemotaxis to fibroblast growth factor | IDA PMID:16756958 Fibroblast growth factor 16 and 18 are expressed in human ca... | KEEP AS NON CORE | Summary: Endothelial (HUVEC) chemotaxis toward FGFs (FGF16/18 study; abstract-only cache). Reason: FGF1 is a classical endothelial chemoattractant and the curator had the full text. As the ligand, FGF1 is the chemoattractant itself; kept as non-core. Supporting Evidence: PMID:16756958 HUVEC clearly demonstrated chemotaxis towards FGF16 and FGF18. |
| GO:2000544 regulation of endothelial cell chemotaxis to fibroblast growth factor | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA electronic annotation. Reason: Consistent with FGF1 acting as an endothelial chemoattractant; non-core. Supporting Evidence: PMID:18441324 Because FGF1 is a potent inducer of cell migration and chemotaxis |
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Download this section (compressed HTML)Q: Is the FGFR-independent, p53-dependent anti-apoptotic activity of intracellular FGF1 physiologically significant in vivo, and which pool (pre-secretory or internalized) mediates it?
Q: Do the metabolic (insulin-sensitizing, anti-lipolytic) effects of FGF1 reflect a distinct receptor/heparan sulfate configuration from its mitogenic signaling, and are they relevant to human adipose physiology?
Q: Is direct integrin alphaV-beta3 binding required for FGF1 signaling in cells from independent laboratories, or is the R50E phenotype explained by altered heparan sulfate or receptor dimer geometry?
Q: What is the molecular mechanism by which FGF1 crosses the plasma membrane during stress-induced non-classical secretion, and which components (S100A13, SYT1 p40, AHNAK2, Na+/K+-ATPase) are rate-limiting in vivo?
Experiment: Compare Fgf1-null mice rescued with wild-type, NLS-mutant or FGFR-binding-dead FGF1 knock-in alleles under high-fat diet and apoptotic stress to separate extracellular FGFR-dependent from intracellular functions.
Hypothesis: Adipose remodelling and insulin sensitivity require extracellular FGFR activation, whereas the anti-apoptotic function persists with an FGFR-binding-dead intracellular FGF1.
Type: mouse genetics / knock-in
Experiment: Quantify binding kinetics of FGF1 to all seven FGFR isoforms with defined heparan sulfate oligosaccharides by SPR/BLI and correlate with ERK and AKT signaling dynamics in isogenic cell lines.
Hypothesis: Heparan sulfate composition tunes FGF1 receptor selectivity and signaling duration, distinguishing mitogenic and metabolic outputs.
Type: biochemistry / quantitative signaling
Experiment: Test integrin alphaV-beta3 dependence of FGF1 signaling using ITGB3 knockout endothelial cells and orthogonal binding assays of FGF1 R50E versus wild type.
Hypothesis: If integrin binding is required, ITGB3 loss will phenocopy the R50E signaling defect.
Type: genetic manipulation / binding assays
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