Fibronectin is a secreted, modular glycoprotein that links cells to the extracellular matrix and helps organize fibrillar matrix. Characterized full-length forms assemble as disulfide-linked dimers and can be incorporated into cell-organized fibrils. Its type I, type II and type III modules provide distinct interaction surfaces for integrins, collagen or gelatin, proteoglycans, heparin and fibrin. The RGD-containing type III-10 module and neighboring contacts mediate recognition by integrins such as Ξ±5Ξ²1, coupling matrix attachment to junction assembly, cell spreading and signaling. Fibronectin also supplies a physical scaffold that supports the retention and organization of other extracellular matrix components. These activities contribute to tissue maintenance, wound repair and developmental cell migration. Alternative splicing and extracellular processing generate products with different interaction regions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0007399 nervous system development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Fibronectin contributes to nervous-system development in particular developmental settings. Reason: The exact tree, alignment and original IBD join verify transmission from PTN002709787 to human FN1. Independent enteric neural-crest experiments also support an appropriate developmental setting, while using mouse explants and a fibronectin substrate. Retain nervous-system development contextually without claiming a direct human developmental perturbation or equating every nervous-system process with the matrix protein's core function. Supporting Evidence: PMID:26571399 This appears to be due to the fact that collagen VI is a poor substratum for supporting eNCC migration and can even interfere with the migration-promo... |
| GO:0007044 cell-substrate junction assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Fibronectin supplies the adhesive matrix on which cell-substrate junctions assemble. Reason: The actual positive PTN002709787 IBD lies on the human target path. Fibronectin-integrin adhesion and associated focal-adhesion responses provide target-specific biological support for the conserved assertion. Fibronectin contributes an extracellular ligand and structural substrate to the junction, while the intracellular kinases and adaptors perform their own signaling steps. Supporting Evidence: PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a high-affinity form of fibronectin |
| GO:0007160 cell-matrix adhesion | IBA GO_REF:0000033 | ACCEPT | Summary: Cell-matrix adhesion is a defining activity of fibronectin. Reason: The exact PTN002709787 ancestry and positive original IBD are verified. Human fibronectin integrin-binding structures and functional adhesion assays establish the target protein's contribution as a matrix ligand. This is direct participation in adhesion and does not depend on treating a donor count or a self-containing evidence list as a quality metric. Supporting Evidence: PMID:33962943 The complex of integrin alpha5beta1 with FN7-10 shows three simultaneous interactions critical for the stabilization of integrin opening, namely, (i) at the synergy site of FN9, (ii) at the RGD loop of FN10, and (iii) at the adjacent to MIDAS (ADMIDAS) of the integrin beta1 betaI domain. file:human/FN1/FN1-deep-research-falcon.md Fibronectin's primary role is as a cell-adhesive ECM glycoprotein that forms fibrillar networks and functions as a scaffold to organize other ECM components and associated signaling molecules. |
| GO:0007507 heart development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The conserved heart-development association is retained with developmental scope. Reason: The actual PTHR46708 tree places human FN1 inside the PTN002709787 clade carrying this positive IBD assertion, and the 2,477-residue target sequence exactly matches the family alignment. This supports the inherited developmental role rather than a new human cardiac assay. Heart development is a tissue-specific application of fibronectin matrix and adhesion activity, so retain it as non-core. Neither the short donor list nor the inclusion of target evidence would invalidate the ancestral placement. Supporting Evidence: GO_REF:0000033 |
| GO:0005178 integrin binding | IBA GO_REF:0000033 | ACCEPT | Summary: Integrin recognition is a conserved, directly demonstrated fibronectin function. Reason: The incoming IBA has an exact positive IBD join on the human FN1 path. Human fibronectin fragments directly engage integrins through the RGD region and additional contacts, with structural and functional evidence. The tested domains support the core molecular capacity without establishing identical accessibility or affinity in every natural product. Supporting Evidence: PMID:33962943 Structural insights into integrin Ξ±(5)Ξ²(1) opening by fibronectin ligand PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility PMID:19738201 Quantitative, comparative analyses of the proteomes of two receptor-ligand pairs, alpha(4)beta(1)-vascular cell adhesion molecule-1 and alpha(5)beta(1... |
| GO:0043394 proteoglycan binding | IBA GO_REF:0000033 | ACCEPT | Summary: Fibronectin directly binds proteoglycan partners as part of its matrix interactions. Reason: The positive PTN002709787 IBD and exact target sequence are verified. Direct binding between human plasma fibronectin and recombinant human lubricin/PRG4 regions provides target-specific support for proteoglycan recognition. This establishes a molecular capacity, not binding to every proteoglycan or identical behavior of every FN1 splice product. Supporting Evidence: PMID:29030641 Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface |
| GO:0001525 angiogenesis | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: Fibronectin supports vascular remodeling through matrix-dependent endothelial behavior. Reason: Retain as a contextual matrix contribution to angiogenesis: exogenous fibronectin restores migration and wound closure of LPP3-depleted human microvascular endothelial cells (PMID:20123964). This supports the adhesive matrix contribution to an endothelial behavior used during vascular remodeling; the separate branching rescue is beta-catenin-mediated and should not be described as fibronectin-alone rescue. These experiments support a contextual matrix contribution and do not establish fibronectin-alone vessel formation in vivo or universal pro-angiogenic activity of its products and fragments. Supporting Evidence: |
| GO:0002020 protease binding | IEA GO_REF:0000117 | UNDECIDED | Summary: The protease-binding rule needs evidence that distinguishes binding from substrate cleavage. Reason: The broad ARBA mapping is biologically plausible, but the inspected cathepsin study demonstrates fibronectin degradation rather than an independently resolved fibronectin-protease binding assay. Protease binding does not require inhibitory activity, so being a substrate is not itself a reason for removal. Preserve the rule assertion while its precise supporting interaction evidence remains unresolved. Supporting Evidence: PMID:22952693 Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners. |
| GO:0005576 extracellular region | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Fibronectin has both soluble extracellular and assembled matrix pools. Reason: The combined electronic source supports secretion/extracellular occurrence. FN1 has both soluble and assembled matrix pools; the broad location preserves that combined scope and is not replaced solely from the protein class. Supporting Evidence: GO_REF:0000120 |
| GO:0006953 acute-phase response | IEA GO_REF:0000043 | UNDECIDED | Summary: The historical acute-phase keyword mapping lacks a resolved participation mechanism. Reason: The retained historical source is a UniProt keyword mapping, and the available review evidence does not identify the specific acute-phase experiment or show which step of that response fibronectin performs. Changes in circulating abundance or incorporation into a later wound matrix do not by themselves resolve that question. Preserve the original term and provenance with uncertainty rather than inventing an inflammatory assay or treating its absence from current GOA as refutation. Supporting Evidence: GO_REF:0000043 |
| GO:0007155 cell adhesion | IEA GO_REF:0000043 | TOO GENERAL | Summary: The historical adhesion assertion is covered more specifically by cell-matrix adhesion. Reason: The original keyword mapping describes a real fibronectin function, but official GO ancestry places the retained GO:0007160 cell-matrix adhesion beneath GO:0007155. Preserve the old source context while marking the broader term as too general; no source term ID is rewritten. Supporting Evidence: PMID:1423622 The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions |
| GO:0008201 heparin binding | IEA GO_REF:0000043 | ACCEPT | Summary: Heparin recognition is an established fibronectin molecular capacity. Reason: Preserve the historical keyword-derived assertion. Human FNIII12β14 structural work and its mapped basic surface support heparin binding. The source supports the molecular capacity without requiring an unverified claim about the number or activity of all heparin-binding sites in every natural product. Supporting Evidence: PMID:10075919 Crystal structure of a heparin- and integrin-binding segment of human fibronectin |
| GO:0008360 regulation of cell shape | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: Fibronectin-dependent attachment changes cell morphology in defined adhesion assays. Reason: Human plasma fibronectin promotes beta1-integrin-dependent spreading of mouse fibroblasts in defined surface-coating assays (PMID:19126672). Human wild-type FN10 and native fibronectin also support alphaVbeta3-dependent spreading of engineered human K562 cells, whereas the high-affinity antagonist derivative behaves differently (PMID:24658351). FN1 therefore contributes the extracellular receptor-engaging ligand that regulates these shape changes. Retain this contextual regulation as non-core, with the substrate, receptor and construct limits of the assays; neither universal morphology control nor FN1-specific activation of every downstream PI3K response is established. Supporting Evidence: PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts |
| GO:0005102 signaling receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Checkpoint-receptor recognition is supported in the mouse donor and human receptor assays. Reason: The mouse donor is linked to PMID:34089617, whose inspected abstract explicitly reports fibronectin binding to human ILT3/LILRB4 and mouse gp49B by biolayer interferometry and maps the principal site to the N-terminal 30-kDa module. Preserve the original human IEA and ortholog provenance. This is a receptor-binding capacity in an immune context, without assigning an uninspected human monocyte endpoint from the mouse disease experiment. Supporting Evidence: PMID:34089617 Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin ameliorates autoimmune disease in BXSB/Yaa mice |
| GO:0005604 basement membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Basement-membrane association is a contextual extracellular localization of fibronectin. Reason: The source transfers a mouse FN1 basement-membrane location. FN1 can occur in basement-membrane-associated extracellular structures, while its prominent fibrillar role is in interstitial/provisional matrices. The newly acquired PMID:34572092 review explicitly distinguishes these matrix classes and describes FN1 in both. Retain the contextual basement-membrane assertion without making it a universal constituent of every basement membrane or assigning it to all 17 products; this pass does not replay the original mouse experiment. Supporting Evidence: GO_REF:0000107 |
| GO:0005615 extracellular space | IEA GO_REF:0000120 | MODIFY | Summary: The historical extracellular-space assertion can be reconciled to extracellular region without requiring matrix assembly. Reason: The original GO:0005615 identifier and historical source must remain immutable. Official QuickGO marks extracellular space obsolete because it denotes the same concept as GO:0005576 extracellular region. Propose that current term while retaining the original source-specific extracellular pool; this is ontology reconciliation, not evidence that all secreted FN1 is assembled matrix. The corresponding current source contexts are reviewed separately and inherited quotations must not be copied to new rows. Proposed replacements: extracellular region Supporting Evidence: PMID:15292204 BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding |
| GO:0014850 response to muscle activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Exercise-responsive fibronectin secretion is supported in the mouse donor system. Reason: The exact mouse donor annotation cites PMID:36812915. Selected original Results and Methods show exercise-dependent circulating fibronectin and muscle secretion, including differentiated C2C12 experiments and muscle-directed perturbation. The study separates release from a simple transcriptional increase. Retain the ortholog-derived response context without claiming direct human in-vivo exercise evidence or converting fibronectin into the downstream autophagy machinery. Supporting Evidence: |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor evidence supports fibronectin association with the apical hair-cell surface. Reason: The authentic PMID:10742111 abstract reports fibronectin colocalization with integrin alpha8beta1 and focal adhesion kinase at the apical surface of mouse hair cells. GO:0016324 denotes the apical region of the plasma membrane; its external-side part GO:0098591 explicitly includes peripherally associated proteins, so membrane association does not require an intrinsic transmembrane segment. Retain the source-specific transferred location as non-core, preserving the original human IEA/GO_REF and both mouse donor alternatives. The abstract supports this contextual association, not a universal location for natural FN1 products; full Methods and figure pixels were not read. |
| GO:0016504 peptidase activator activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The donor study supports enhancement of a protease reaction in a defined extracellular assay. Reason: The exact mouse donor annotation cites PMID:16061471. Selected original experiments compare extracellular matrix cofactors in ADAMTS1-mediated aggrecan cleavage and report enhancement by fibronectin, weaker than the fibulin-1 effect. Retain this bounded peptidase-activator capacity through the original human IEA donor mapping. It does not establish activation of all peptidases or a directly measured human FN1 assay. Supporting Evidence: |
| GO:0031012 extracellular matrix | IEA GO_REF:0000107 | ACCEPT | Summary: The transferred extracellular-matrix location agrees with established human fibronectin incorporation. Reason: The electronic mouse-to-human transfer agrees with independently established human FN1 extracellular matrix incorporation. Retain the core structural location without treating the donor list as an assay replay or extending one natural product to all 17 products. Supporting Evidence: PMID:26571399 This appears to be due to the fact that collagen VI is a poor substratum for supporting eNCC migration and can even interfere with the migration-promo... PMID:16157329 Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts |
| GO:0048018 receptor ligand activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The donor study supports a circulating receptor-ligand role in an exercise model. Reason: The exact mouse receptor-ligand annotation cites PMID:36812915. Muscle-derived soluble fibronectin and Ξ±5Ξ²1-integrin dependence link exercise to hepatic autophagy in the tested mouse system, with cell experiments supporting the pathway. Retain the original ortholog inference and its contextual signaling capacity. Human cell hosts do not establish the species of every supplied protein, and downstream IKK/JNK/BECN1 activities are not assigned to fibronectin. Supporting Evidence: |
| GO:0150102 negative regulation of monocyte activation | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise donor evidence for suppression of monocyte activation remains inaccessible. Reason: The mouse donor maps to PMID:34089617, and its abstract establishes fibronectin binding to inhibitory receptors and a mouse autoimmune intervention. The exact monocyte-activation assay and its direction were not recovered from the subscription-limited body. Binding an inhibitory receptor alone is insufficient to reconstruct that specific endpoint. Preserve the electronic assertion and donor context without treating abstract omission as experimental refutation. Supporting Evidence: PMID:34089617 Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin ameliorates autoimmune disease in BXSB/Yaa mice |
| GO:0005515 protein binding | IPI PMID:11377428 Binding of a peptide from a Streptococcus dysgalactiae MSCRA... | KEEP AS NON CORE | Summary: FN fragments bind a streptococcal fibronectin-binding protein. Reason: PMID:11377428 reports solution structural and binding analysis of a bacterial fibronectin-binding segment with fibronectin modules. This supports the recorded Q53971 interaction in the tested fragments. Retain this pathogen-associated interaction as non-core; it does not establish a separate physiological FN1 activity or a function in every natural FN1 product. Supporting Evidence: PMID:11377428 Binding of a peptide from a Streptococcus dysgalactiae MSCRAMM to the N-terminal F1 module pair of human fibronectin involves both modules |
| GO:0005515 protein binding | IPI PMID:12736686 Pathogenic bacteria attach to human fibronectin through a ta... | KEEP AS NON CORE | Summary: FN modules recognize a peptide from staphylococcal FnBPA. Reason: PMID:12736686 reports structural analysis of microbial fibronectin-binding regions and the tandem beta-zipper interaction with FN type-I modules. The original partner context for staphylococcal FnBPA is retained separately. The interaction is biologically credible and source-supported, but the microbial adhesion setting and tested fragments do not define an additional core human FN1 function. Supporting Evidence: PMID:12736686 Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper |
| GO:0005515 protein binding | IPI PMID:16457822 CT domain of CCN2/CTGF directly interacts with fibronectin a... | KEEP AS NON CORE | Summary: Fibronectin binds the C-terminal region of CCN2. Reason: PMID:16457822 identifies a physical interaction between fibronectin and the C-terminal region of CCN2/CTGF and relates it to cell adhesion. Retain the specific extracellular partner association as non-core. Calling CCN2 a connective tissue growth factor does not, by itself, establish a growth-factor-binding mechanism in these assays; no receptor activity or universal product assignment is inferred. Supporting Evidence: PMID:16457822 CT domain of CCN2/CTGF directly interacts with fibronectin and enhances cell adhesion of chondrocytes through integrin alpha5beta1 |
| GO:0005515 protein binding | IPI PMID:1747115 Interaction of the small proteoglycan decorin with fibronect... | MODIFY | Summary: The decorin interaction supports proteoglycan binding. Reason: PMID:1747115 reports binding of decorin core protein to fibronectin in solid-phase assays, with saturable binding and competition by a decorin-derived peptide. Decorin is a proteoglycan, so GO:0043394 is more informative than generic protein binding. The experiment localizes the interaction to the core-protein component; it is not evidence that the carbohydrate chains themselves mediate this particular interaction. Proposed replacements: proteoglycan binding Supporting Evidence: PMID:1747115 Interaction of the small proteoglycan decorin with fibronectin |
| GO:0005515 protein binding | IPI PMID:18042364 TSG-6 binds via its CUB_C domain to the cell-binding domain ... | KEEP AS NON CORE | Summary: TSG-6 can bridge fibronectin and thrombospondin-1. Reason: PMID:18042364 explicitly describes a ternary association in which TSG-6 bridges FN to thrombospondin-1; the exact source-level IntAct record includes a solid-phase assay. Retain this contextual association without claiming that the experiment establishes an isolated direct FNβthrombospondin-1 interface. It does not transfer thrombospondin or TSG-6 functions to FN1. Supporting Evidence: PMID:18042364 TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly |
| GO:0005515 protein binding | IPI PMID:18160478 Novel adhesin from Pasteurella multocida that binds to the i... | KEEP AS NON CORE | Summary: Fibronectin binds the Pasteurella PM1665 protein. Reason: PMID:18160478 reports binding of Pasteurella multocida PM1665 to soluble and immobilized fibronectin, including a recombinant-protein surface-plasmon-resonance assay and localization to FN type-III repeats 9β10. Retain the original bacterial-partner association as non-core. Its adhesin-like behavior does not make the bacterial protein an integrin or establish another human FN1 process. Supporting Evidence: PMID:18160478 Novel adhesin from Pasteurella multocida that binds to the integrin-binding fibronectin FnIII9-10 repeats |
| GO:0005515 protein binding | IPI PMID:18243143 Uteroglobin interacts with the heparin-binding site of fibro... | KEEP AS NON CORE | Summary: Uteroglobin binds a fibronectin heparin-binding region. Reason: PMID:18243143 reports uteroglobin association with fibronectin and interference with an IgAβFN interaction. This supports the specified uteroglobin partner, with the reported binding site and experimental context. Retain as non-core without converting the partner protein into heparin or assigning uteroglobin functions to FN1. Supporting Evidence: PMID:18243143 Uteroglobin interacts with the heparin-binding site of fibronectin and prevents fibronectin-IgA complex formation found in IgA-nephropathy |
| GO:0005515 protein binding | IPI PMID:18323857 NEDD8 acts as a 'molecular switch' defining the functional s... | KEEP AS NON CORE | Summary: The VHLβfibronectin association is supported in its cellular context. Reason: PMID:18323857 reports that NEDD8 modification of VHL changes its association with fibronectin and the ECV ubiquitin-ligase complex. The source supports the recorded VHL interaction, but VHL is a substrate-recognition component rather than evidence that FN binds a catalytically defined ubiquitin-ligase interface. Retain this association as non-core; no FN enzymatic activity is inferred. Supporting Evidence: PMID:18323857 The von Hippel-Lindau (VHL) tumour suppressor protein is important in the E3 ubiquitin ligase ECV (Elongin B/C-CUL2-VHL)-mediated destruction of hypox... |
| GO:0005515 protein binding | IPI PMID:18411296 The surface-exposed carboxyl region of Mycoplasma pneumoniae... | KEEP AS NON CORE | Summary: Fibronectin binds bacterial elongation factor Tu. Reason: PMID:18411296 reports binding of Mycoplasma pneumoniae EF-Tu and recombinant C-terminal portions to human fibronectin, with two interacting regions. Retain this experimentally supported microbial adhesion interaction as non-core for FN1. Although the partner is a GTPase, its catalytic class does not describe the adhesion role demonstrated here; no regulation of translation or GTP hydrolysis is assigned to fibronectin. Supporting Evidence: PMID:18411296 The surface-exposed carboxyl region of Mycoplasma pneumoniae elongation factor Tu interacts with fibronectin |
| GO:0005515 protein binding | IPI PMID:18713862 Crystal structures of fibronectin-binding sites from Staphyl... | KEEP AS NON CORE | Summary: Fibronectin binds staphylococcal FnBPA through the documented moduleβpeptide interface. Reason: PMID:18713862 reports structural analysis of the interaction between staphylococcal FnBPA and fibronectin modules. The positive bacterial adhesin interaction is retained as non-core, with fragment-level scope. It does not establish a new human process or justify treating all naturally spliced FN1 products as equivalently tested. Supporting Evidence: PMID:18713862 Crystal structures of fibronectin-binding sites from Staphylococcus aureus FnBPA in complex with fibronectin domains |
| GO:0005515 protein binding | IPI PMID:19542224 The first draft of the endostatin interaction network. | KEEP AS NON CORE | Summary: The thrombospondin-1 interaction is detected in a surface-binding assay. Reason: PMID:19542224 and the exact source-level IntAct record support a fibronectinβthrombospondin-1 association by surface-plasmon-resonance array. Retain this extracellular interaction as non-core. The assay establishes the measured protein association, without assigning thrombospondin functions to fibronectin or claiming that the study tested all physiological matrix states. Supporting Evidence: PMID:19542224 Epub 2009 Jun 19. The first draft of the endostatin interaction network. |
| GO:0005515 protein binding | IPI PMID:19738201 Proteomic analysis of integrin-associated complexes identifi... | KEEP AS NON CORE | Summary: Fibronectin-associated complexes include transglutaminase 2. Reason: PMID:19738201 captures fibronectin-associated integrin adhesion complexes by chemical cross-linking, and the exact source record identifies TGM2. Retain this supported adhesion-complex association as non-core. The assay does not isolate a catalytic role for the partner in this interaction, so enzyme classification adds little functional specificity to the FN1 assertion; a purified binary affinity is not inferred. Supporting Evidence: PMID:19738201 Quantitative, comparative analyses of the proteomes of two receptor-ligand pairs, alpha(4)beta(1)-vascular cell adhesion molecule-1 and alpha(5)beta(1... |
| GO:0005515 protein binding | IPI PMID:20080707 EGF potentiated oncogenesis requires a tissue transglutamina... | UNDECIDED | Summary: The source-specific FNβTGM2 interaction remains unverified. Reason: PMID:20080707 principally analyzes EGF-dependent TGM2 signaling in human breast-cancer cells. The retained cache contains abstract and Discussion material but does not recover the FN-specific assay or original Results/Methods supporting this curated IPI pair. The source-scoped IntAct extraction did not resolve that pair either. The interaction is plausible and independently known, but that does not verify this particular citation; retain uncertainty rather than rejecting the curator assertion from incomplete access. Supporting Evidence: PMID:20080707 EGF potentiated oncogenesis requires a tissue transglutaminase-dependent signaling pathway leading to Src activation. |
| GO:0005515 protein binding | IPI PMID:20541508 Zinc induces structural reorganization of gelatin binding do... | MODIFY | Summary: The gelatin-binding domain supports collagen binding. Reason: PMID:20541508 explicitly studies the human FN gelatin-binding domain and its binding to high-affinity collagen peptides in solution. This supports collagen binding as the appropriate specific replacement. The authentic abstract describes zinc-dependent structural and binding changes; the full Methods were not recovered, and the results are not generalized to every matrix state or FN1 product. Proposed replacements: collagen binding Supporting Evidence: PMID:20541508 Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding |
| GO:0005515 protein binding | IPI PMID:20875085 Functional analysis of a murine monoclonal antibody against ... | KEEP AS NON CORE | Summary: Fibronectin binding to staphylococcal FnBPA is retained. Reason: PMID:20875085 supports the specified staphylococcal FnBPA association in its microbial adhesin context. Retain the source-specific protein interaction as non-core, rather than deleting a positive interaction solely because the term is generic. The bacterial ligand-binding role is not transferred to a new human FN1 process, and no full-length or all-product structural mechanism is inferred beyond the reported assay scope. Supporting Evidence: PMID:20875085 Functional analysis of a murine monoclonal antibody against the repetitive region of the fibronectin-binding adhesins fibronectin-binding protein A an... |
| GO:0005515 protein binding | IPI PMID:20879998 Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Myco... | KEEP AS NON CORE | Summary: The historical Mycoplasma Mhp271 interaction remains supported. Reason: PMID:20879998 reports that an Mhp271 fragment containing the repeated binding region binds fibronectin, whereas another tested fragment does not. The same paper separately examines porcine cilia. Retain this historical source assertion as non-core even though it is absent from the current source snapshot; current absence alone does not refute the experimental association. The abstract-level species and construct limits are retained. Supporting Evidence: PMID:20879998 Repeat regions R1 and R2 in the P97 paralogue Mhp271 of Mycoplasma hyopneumoniae bind heparin, fibronectin and porcine cilia |
| GO:0005515 protein binding | IPI PMID:21569203 The A domain of fibronectin-binding protein B of Staphylococ... | KEEP AS NON CORE | Summary: Fibronectin binds the A domain of staphylococcal FnBPB. Reason: PMID:21569203 identifies an additional fibronectin-binding site in the A domain of staphylococcal FnBPB. Retain the supported bacterial adhesin interaction as non-core. A positive interaction with this particular domain does not establish a general FN1 receptor function or require a new human biological-process assertion. Supporting Evidence: PMID:21569203 The A domain of fibronectin-binding protein B of Staphylococcus aureus contains a novel fibronectin binding site |
| GO:0005515 protein binding | IPI PMID:22442151 Transglutaminase-2 interaction with heparin: identification ... | KEEP AS NON CORE | Summary: Fibronectin binding to transglutaminase 2 is directly supported. Reason: PMID:22442151 directly measures association of recombinant wild-type and mutant TGM2 with immobilized fibronectin before testing Swiss 3T3 cell adhesion. Fibronectin-associated TGM2 has low transamidating activity under the tested conditions and retains heparin recognition in the adhesive complex. Retain this positive structural/adhesive interaction as non-core, with binding and catalytic measurements kept distinct. The choice not to add enzyme binding reflects the demonstrated FN1 interaction role, not a requirement that binding to an enzyme must regulate its catalysis. Supporting Evidence: PMID:22442151 Transglutaminase-2 interaction with heparin: identification of a heparin binding site that regulates cell adhesion to fibronectin-transglutaminase-2 m... |
| GO:0005515 protein binding | IPI PMID:24136289 Identification and comparative analysis of hepatitis C virus... | KEEP AS NON CORE | Summary: A fibronectin fragment associates with the HCV RNA polymerase chain. Reason: PMID:24136289 has exact source-level records for a partial fibronectin prey and the HCV RNA-directed RNA-polymerase chain Q99IB8-PRO_0000045603 in yeast two-hybrid, pull-down and split-firefly-luciferase assays. Retain the supported interaction as non-core. The assays establish the specified partner association without demonstrating a polymerase-related FN1 operation, a native extracellular encounter or binding by every natural FN1 product; enzyme classification therefore adds no established functional distinction here. Supporting Evidence: PMID:24136289 Identification and comparative analysis of hepatitis C virus-host cell protein interactions. |
| GO:0005515 protein binding | IPI PMID:24388360 SERPINA5 inhibits tumor cell migration by modulating the fib... | KEEP AS NON CORE | Summary: SERPINA5 association with fibronectin is supported in the studied cancer-cell setting. Reason: PMID:24388360 reports SERPINA5 binding to FN and interference with FNβintegrin signaling in hepatocellular carcinoma models. Retain the specific association as non-core. SERPINA5 is a protease inhibitor, so its name does not justify protease-binding or enzyme-binding annotation to FN; cell-migration effects and binding are kept distinct. Supporting Evidence: PMID:24388360 SERPINA5 inhibits tumor cell migration by modulating the fibronectin-integrin Ξ²1 signaling pathway in hepatocellular carcinoma |
| GO:0005515 protein binding | IPI PMID:25034023 Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self... | KEEP AS NON CORE | Summary: Fibronectin directly binds fibrillin-1 fragments. Reason: PMID:25034023 original Methods 2.4β2.6, Results 3.2β3.3 and Table 2 include solid-phase and surface-plasmon-resonance measurements of recombinant fibrillin-1 fragments against immobilized FN. These source-specific data were recovered beyond the abstract, and support retaining the interaction as non-core. Multimerization changes apparent affinity; fragment binding is not an all-product claim or proof of every proposed step in microfibril assembly. Supporting Evidence: PMID:25034023 Epub 2014 Jul 14. Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assembly. |
| GO:0005515 protein binding | IPI PMID:25290767 Structural and functional analysis of the fibronectin-bindin... | MODIFY | Summary: A collagen-I peptide binds the human FN gelatin-binding domain. Reason: PMID:25290767 Results and Figure 3 directly titrate a fluorescent collagen-I alpha-chain peptide, Gly778βGly798, with the human FN gelatin-binding domain. The measured binding and its displacement by FNE support collagen binding. The experiment uses a collagen peptide and a recombinant FN fragment; it is not a whole-fibril affinity measurement or an assertion that all FN1 splice products were tested. Proposed replacements: collagen binding Supporting Evidence: PMID:25290767 Structural and functional analysis of the fibronectin-binding protein FNE from Streptococcus equi spp |
| GO:0005515 protein binding | IPI PMID:25293691 Proteolytic processing of the cilium adhesin MHJ_0194 (P123J... | KEEP AS NON CORE | Summary: The historical Mhp P123 processing-fragment interaction remains supported. Reason: PMID:25293691 reports fibronectin affinity capture and binding-site analysis of processed Mhp P123 fragments in a Mycoplasma hyopneumoniae adhesion study. This supports retaining the historical interaction as non-core despite its absence from the current source snapshot. The porcine infection context and fragment-level assays do not establish an additional core human FN1 function; no source is rejected merely because the abstract foregrounds the pathogen. Supporting Evidence: PMID:25293691 Affinity chromatography using heparin, fibronectin and plasminogen as bait and peptide arrays were used to expand our knowledge of the adhesive capabi... |
| GO:0005515 protein binding | IPI PMID:2531657 Lipoprotein(a) binds to fibronectin and has serine proteinas... | MODIFY | Summary: Fibronectin binds lipoprotein(a) particles in the reported assay. Reason: PMID:2531657 directly reports human lipoprotein(a) binding to immobilized fibronectin and maps an interacting region in FN. The tested ligand is the lipoprotein particle, making lipoprotein particle binding more informative than generic protein binding. This does not adopt the paperβs broader proteolysis interpretation or extend the result to all lipoprotein classes. Proposed replacements: lipoprotein particle binding Supporting Evidence: PMID:2531657 Lipoprotein(a) binds to fibronectin and has serine proteinase activity capable of cleaving it |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | KEEP AS NON CORE | Summary: The FNβUBQLN1 pair is supported by the human interactome assay. Reason: PMID:25416956 has three exact source-level FNβUBQLN1 records covering the yeast two-hybrid screening and validation workflow. Retain this experimentally detected association as non-core. Multiple records from the same study are not independent replication, and the assay does not establish a physiological tissue encounter or transfer ubiquilinβs proteostasis functions to FN1. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network. |
| GO:0005515 protein binding | IPI PMID:26848503 Mapping and Exploring the Collagen-I Proteostasis Network. | MODIFY | Summary: Collagen-I-associated complexes contain fibronectin. Reason: PMID:26848503 original Table 1 explicitly identifies FN1 with nine unique peptides and enrichment of 5.2-fold with ascorbate and 4.5-fold without ascorbate. Results describe cross-linking live human HT-1080 cells followed by immunoprecipitation of tagged collagen-I and quantitative mass spectrometry. Collagen binding is a supported partner-class refinement, with the explicit limitation that this is a cross-linked cellular association, not a purified binary assay or FN-specific proof of collagen folding catalysis. Proposed replacements: collagen binding Supporting Evidence: PMID:26848503 Epub 2016 Mar 9. Mapping and Exploring the Collagen-I Proteostasis Network. |
| GO:0005515 protein binding | IPI PMID:27141819 Mycobacterial antigen 85 complex (Ag85) as a target for fico... | KEEP AS NON CORE | Summary: Fibronectin binds ficolin-3 in solid-phase assays. Reason: PMID:27141819 and three exact source-level interaction records support FN association with ficolin-3 by solid-phase assays. Retain this extracellular association as non-core. Ficolinβs collagen-like and fibrinogen-like domains do not make the partner collagen or fibrinogen, and its immune-recognition roles are not transferred to FN1. Supporting Evidence: PMID:27141819 Furthermore, those PRMs also bound to fibronectin and therefore might influence the Ag85 complex-dependent interaction of Mycobacterium with the extra... |
| GO:0005515 protein binding | IPI PMID:27616280 Interactions of surface-displayed glycolytic enzymes of Myco... | KEEP AS NON CORE | Summary: Fibronectin binds bacterial GAPDH/GapA. Reason: PMID:27616280 explicitly distinguishes fibronectin from fibrinogen and reports fibronectin binding by bacterial GAPDH/GapA. This supports a contextual microbial adhesion interaction with the host extracellular protein. Retain the original binding annotation as non-core; glycolytic enzyme identity does not make this an FN1 metabolic function or establish a more informative adhesion-specific binding subtype. Supporting Evidence: PMID:27616280 interactions of the previously confirmed surface-located glycolytic enzymes...to the human extracellular matrix (ECM) proteins fibrinogen (Fn), fibronectin (Fc), lactoferrin (Lf), laminin (Ln) and vitronectin (Vc) |
| GO:0005515 protein binding | IPI PMID:30082873 Insights into the structure and dynamics of lysyl oxidase pr... | KEEP AS NON CORE | Summary: The LOX propeptide binds an FN anastellin fragment. Reason: PMID:30082873 reports biolayer-interferometry binding between recombinant LOX propeptide and the FN anastellin fragment. Retain this processed-protein interaction as non-core. The source specifically concerns the propeptide, so the catalytic identity of mature lysyl oxidase does not justify replacing this row with enzyme binding. Fragment affinity is not generalized to all full-length FN1 products or matrix states. Supporting Evidence: PMID:30082873 Lysyl oxidase (LOX) catalyzes the oxidative deamination of lysine and hydroxylysine residues in collagens and elastin, which is the first step of the ... |
| GO:0005515 protein binding | IPI PMID:31759052 Scavenger Receptor Cysteine-Rich domains of Lysyl Oxidase-Li... | KEEP AS NON CORE | Summary: Fibronectin associates with lysyl oxidase-like 2. Reason: PMID:31759052 reports an intracellular fibronectinβLOXL2 interaction before extracellular matrix incorporation and proposes a noncatalytic scaffolding role. Retain this supported cellular association as non-core. The recombinant SRCR-domain SPR and catalytic-domain experiments directly concern collagen IV and must not be relabeled as purified fibronectin-binding kinetics or a fibronectin-specific catalytic mechanism. LOXL2 enzyme identity alone is not used to refine this FN1 interaction. Supporting Evidence: PMID:31759052 We here provide evidence that LOXL2 also affects deposition of other ECM components, including fibronectin, thus altering structural and mechanical pr... |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: The BioPlex source supports FN association with transglutaminase 2. Reason: PMID:33961781 has an exact fibronectinβTGM2 record from tagged-bait co-immunoprecipitation in human HEK293T cells. Retain this supported co-complex association as non-core, with its AP-MS and cell-context limits. The source does not establish a catalytic operation in the FN1 interaction, so TGM2βs enzyme classification is not used to manufacture a functionally more specific binding claim. Supporting Evidence: PMID:33961781 2021 May 6. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0005515 protein binding | IPI PMID:34968453 Stabilin-1 mediates beneficial monocyte recruitment and tole... | KEEP AS NON CORE | Summary: Fibronectin associates with the scavenger receptor stabilin-1. Reason: PMID:34968453 reports a stabilin-1βFN interaction by yeast two-hybrid and affinity methods, with source-level records for the exact pair. Retain this receptor-associated binding as non-core. The evidence supports recognition/association, but does not by itself establish that FN acts as an activating ligand for a defined signaling-receptor mechanism; the mouse fibrosis outcomes are distinct from the molecular binding claim. Supporting Evidence: PMID:34968453 Yeast two-hybrid screening, confirmed by affinity chromatography, identified fibronectin as a stabilin-1 interacting partner |
| GO:0005515 protein binding | IPI PMID:9269765 Novel interaction of apolipoprotein(a) with beta-2 glycoprot... | KEEP AS NON CORE | Summary: An apolipoprotein(a) fragment associates with fibronectin. Reason: PMID:9269765 identifies an FN interactor in an apolipoprotein(a) kringle-domain yeast two-hybrid study. Retain the curated association with this fragment as non-core. The independently characterized co-immunoprecipitation in the abstract concerns another partner, and an isolated apolipoprotein domain does not establish binding to an intact lipoprotein particle in this source. Supporting Evidence: PMID:9269765 Among 11 positive clones that emerged from the screen, eight clones were identified as beta-2 glycoprotein I and one as fibronectin |
| GO:0042802 identical protein binding | IPI PMID:17914904 Force-induced unfolding of fibronectin in the extracellular ... | UNDECIDED | Summary: The exact self-interaction assay underlying this citation remains unresolved. Reason: PMID:17914904 describes fibronectin conformational changes and stretching in matrix fibers. Those observations inform assembly, but the inspected abstract and available source record do not resolve the specific identical-protein-binding assay behind this IPI annotation. Preserve the curator's assertion without inferring that a fiber-mechanics study proves a purified binary interaction or that lack of a recovered pair record refutes one. Supporting Evidence: PMID:17914904 Force-induced unfolding of fibronectin in the extracellular matrix of living cells |
| GO:0042802 identical protein binding | IPI PMID:18042364 TSG-6 binds via its CUB_C domain to the cell-binding domain ... | KEEP AS NON CORE | Summary: A source-specific fibronectin self-association experiment is curated for this paper. Reason: The exact retained IntAct record contains human FN1 on both sides, a cross-linking experiment and the same 1420β1813 region for each participant, with a figure locator and direct-interaction curation. That supports retaining a bounded self-association capacity. The fragment and cross-linking context do not establish a physiological stoichiometry or equivalent behavior of all full-length products. Supporting Evidence: PMID:18042364 TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly |
| GO:0042802 identical protein binding | IPI PMID:19826086 Fibronectin forms the most extensible biological fibers disp... | UNDECIDED | Summary: Fiber extension does not by itself resolve the exact curated self-binding experiment. Reason: PMID:19826086 examines stretched fibronectin fibers and exposure of molecular recognition sites. The inspected abstract and retained discussion do not independently identify the experiment supporting this exact identical-protein-binding IPI row. Preserve the source context and uncertainty; fibronectin assembly is well established, but that does not license inventing a specific assay for this citation. Supporting Evidence: PMID:19826086 Fibronectin forms the most extensible biological fibers displaying switchable force-exposed cryptic binding sites |
| GO:0042802 identical protein binding | IPI PMID:19931242 The interaction of angiocidin with tissue transglutaminase. | UNDECIDED | Summary: Covalent matrix cross-linking and noncovalent self-binding need to be distinguished. Reason: The inspected PMID:19931242 discussion reports transglutaminase-dependent fibronectin cross-linking and matrix incorporation experiments. Those are genuine target observations, but a covalent cross-link is not by itself an independent noncovalent identical-protein-binding measurement. The exact curated interaction assay remains unresolved, so retain the IPI assertion as undecided rather than declaring a wrong-gene citation or absence of self-association. Supporting Evidence: PMID:19931242 Cross-linked angiocidin inhibited cell migration in contrast to monomeric angiocidin and inhibited localization of fibronectin (FN), a pro-tumorigenic... |
| GO:0042802 identical protein binding | IPI PMID:20541508 Zinc induces structural reorganization of gelatin binding do... | KEEP AS NON CORE | Summary: The gelatin-binding region can form a zinc-dependent homomeric assembly. Reason: The PMID:20541508 abstract explicitly describes a zinc-mediated compact homodimer of the six-module fibronectin gelatin-binding region and solution changes affecting collagen-peptide binding. Retain this source-specific association capacity with its domain and zinc conditions; it is not evidence that every intact natural FN1 product adopts that assembly in vivo. Supporting Evidence: PMID:20541508 Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-3788061 | MODIFY | Summary: The modeled degradation substrate is assembled fibronectin matrix. Reason: The event explicitly degrades the polymer Fibronectin matrix (2327729), with a cleaved-matrix output. Refinement to extracellular matrix is supported for this modeled pool. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-3788061 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8952289 | KEEP AS NON CORE | Summary: The modeled phosphorylation event places secretory fibronectin in the endoplasmic-reticulum lumen. Reason: The actual FAM20C phosphorylation event 8952289 has a substrate complex 8952321 containing set 8956956 and the human FN1 entity 8956708 in endoplasmic-reticulum lumen; phosphorylated FN1 is8956937. This supports secretory-pathway transit/modification, rather than an ER-resident matrix function. FAM20C is the kinase and FN1 its substrate. Retain as a contextual location rather than a primary site of mature FN1 scaffold activity. Supporting Evidence: Reactome:R-HSA-8952289 |
| GO:0005577 fibrinogen complex | IPI PMID:20541508 Zinc induces structural reorganization of gelatin binding do... | UNDECIDED | Summary: Membership of the assayed fibronectin population in soluble fibrinogen complex remains unresolved. Reason: GO:0005577 denotes the soluble fibrinogen complex that thrombin converts to fibrin, not any FN-containing fibrin clot. PMID:20541508 abstract establishes a human FN gelatin-binding-domain structure, zinc-dependent dimer/conformation changes and collagen-peptide binding. The exact additional assay supporting membership in soluble fibrinogen was not recovered in this bounded read. Preserve the experimental assertion as undecided; do not call the curator wrong or infer absence of an assay from the abstract. Supporting Evidence: PMID:20541508 Zinc induces structural reorganization of gelatin binding domain from human fibronectin and affects collagen binding |
| GO:0005615 extracellular space | IDA PMID:15292204 BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorfe... | MODIFY | Summary: The historical extracellular fibronectin context is retained through the current extracellular-region term. Reason: The original GO:0005615 identifier and historical source must remain immutable. Official QuickGO marks extracellular space obsolete because it denotes the same concept as GO:0005576 extracellular region. Propose that current term while retaining the original source-specific extracellular pool; this is ontology reconciliation, not evidence that all secreted FN1 is assembled matrix. The corresponding current source contexts are reviewed separately and inherited quotations must not be copied to new rows. Proposed replacements: extracellular region Supporting Evidence: PMID:15292204 BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding |
| GO:0072378 blood coagulation, fibrin clot formation | IDA PMID:3997886 Incorporation of thrombospondin into fibrin clots. | KEEP AS NON CORE | Summary: Fibronectin can be incorporated into a fibrin clot under cross-linking conditions. Reason: The PMID:3997886 abstract explicitly distinguishes fibronectin incorporation into fibrin clots from the thrombospondin observations and reports a cross-linking requirement for fibronectin. Retain this established clot-associated context. Do not transfer the paper's thrombospondin-specific polymerization effects to FN1 or infer a fibrinogen-specific binding assay from fibrin incorporation. Supporting Evidence: PMID:3997886 In contrast, incorporation of 125I-fibronectin into clots was dependent upon cross-linking |
| GO:0031012 extracellular matrix | HDA PMID:23658023 Comparative proteomic analysis of supportive and unsupportiv... | ACCEPT | Summary: The feeder-cell study supports fibronectin incorporation into deposited extracellular matrix. Reason: PMID:23658023 selected Results describe alkali/detergent-isolated deposited matrices from mouse and human feeder cells, with FN enriched in immortalized human placental stromal-fibroblast ECM versus primary feeders (paragraphs 62β78; Table 1 description). This directly supports human matrix incorporation. Preserve the distinct original cell-type extension alternatives separately; substrate supplementation and mouse feeder experiments do not establish identical behavior of every human FN1 product. Supporting Evidence: PMID:23658023 We show that identified candidate molecules can support attachment and self-renewal of hESCs alone (fibrillin-1) or in combination with fibronectin (p... |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1566981 | MODIFY | Summary: The modeled protease substrate is fibronectin matrix rather than an unspecified soluble pool. Reason: The modeled MMP/CTSS substrate is Fibronectin matrix (2327729), not just an unspecified secreted monomer. The matrix location is supported; the reaction does not make FN1 the protease. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-1566981 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-202723 | KEEP AS NON CORE | Summary: Integrin binding in this event involves an extracellular fibronectin dimer before matrix assembly. Reason: The modeled substrate is FN1 dimer (266103), binding alpha5beta1 before subsequent matrix assembly. The summary explicitly separates receptor binding from later fibril formation. This source-specific soluble/receptor-bound pool supports extracellular region without requiring assembled matrix. Supporting Evidence: Reactome:R-HSA-202723 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-216050 | MODIFY | Summary: The integrin-binding event explicitly contains the fibronectin matrix pool. Reason: The integrin-binding reaction explicitly consumes Fibronectin matrix (2327729). Its extracellular scaffold remains distinct from the plasma-membrane integrin component, supporting matrix refinement. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-216050 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327733 | KEEP AS NON CORE | Summary: The modeled fibronectinβcollagen association supports extracellular occurrence without requiring fibronectin fibrils. Reason: The input is FN1 monomer (54851) and the product a fibronectinβcollagen complex, with binding and assembly studies summarized. This establishes extracellular association but does not require the particular FN1 pool to have assembled into its own matrix. Preserve the broad location; do not map legacy coordinate labels to a natural product. Supporting Evidence: Reactome:R-HSA-2327733 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327746 | MODIFY | Summary: The assembly event produces integrin-associated fibronectin matrix from extracellular precursors. Reason: This assembly event converts extracellular FN1 molecules/integrin-bound dimer into integrin-associated Fibronectin matrix (2327790 containing polymer 2327729). The output explicitly establishes the matrix pool, while the inputs include soluble precursors. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2327746 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2396337 | MODIFY | Summary: The HSPG2-binding set explicitly includes assembled fibronectin matrix. Reason: The HSPG2-binding ligand set contains the explicit Fibronectin matrix polymer 2327729. Matrix refinement is supported for that FN1 member rather than inferred from all ligands in the set. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2396337 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2533950 | MODIFY | Summary: The MMP14 reaction uses assembled fibronectin matrix as its substrate. Reason: The MMP14 reaction explicitly has Fibronectin matrix 2327729 as substrate and cleaved matrix as product. Matrix refinement concerns the substrate location, not catalytic activity. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2533950 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2537665 | MODIFY | Summary: The fibulin-binding event explicitly uses the fibronectin matrix pool. Reason: The fibulin-binding event explicitly consumes Fibronectin matrix 2327729, supporting extracellular matrix for the modeled FN1 pool. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2537665 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2545196 | KEEP AS NON CORE | Summary: Extracellular fibronectin dimer formation precedes deposition into matrix. Reason: The event joins extracellular FN1 monomers 54851 into the soluble disulfide-linked dimer 266103, a step described before matrix formation. It does not require deposited fibrils; retain extracellular region for this precursor/dimer pool. Supporting Evidence: Reactome:R-HSA-2545196 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2681681 | MODIFY | Summary: The tenascin-binding event explicitly contains fibronectin matrix. Reason: The tenascin-binding event explicitly consumes Fibronectin matrix 2327729, supporting matrix refinement while retaining the extracellular FN1 versus partner distinctions. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2681681 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2731141 | MODIFY | Summary: The syndecan complex contains extracellular fibronectin matrix as its ligand. Reason: The syndecan-binding event explicitly consumes Fibronectin matrix 2327729. The complex is membrane-associated through syndecan; the FN1 component remains extracellular matrix. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-2731141 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-349593 | KEEP AS NON CORE | Summary: The platelet-integrin ligand in this event is extracellular fibronectin without a required fibrillar state. Reason: The alphaIIbbeta3-binding input is extracellular FN1 monomer 54851, not the Fibronectin matrix polymer. Platelet ligand binding can involve soluble plasma fibronectin. Preserve the broader source-specific extracellular location. Supporting Evidence: Reactome:R-HSA-349593 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-354066 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-354066 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-354073 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-354073 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-354087 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-354087 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-354124 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-354124 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-354149 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-354149 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-354165 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-354165 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-372693 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-372693 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-372697 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-372697 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-372705 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-372705 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-377640 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-377640 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-377641 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-377641 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-377643 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-377643 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-377644 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-377644 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-3785684 | KEEP AS NON CORE | Summary: Both the modeled matrix and the described plasma-fibronectin pool support extracellular localization. Reason: The current event graph uses Fibronectin matrix 2327729, but the retained summary specifically describes cathepsin-G degradation of plasma fibronectin. Both support extracellular region; the source/model discrepancy does not justify forcing the plasma pool into assembled matrix. Retain the broad annotation and document this distinction. Supporting Evidence: Reactome:R-HSA-3785684 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-429415 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-429415 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-429441 | KEEP AS NON CORE | Summary: The platelet signaling event contains an extracellular fibronectin ligand without requiring assembled matrix. Reason: The platelet integrin signaling complex traces through ligand set 377603 to FN1 monomer 54851. That set also contains fibrin/VWF and is called ECM ligands, but its label does not establish that this FN1 member is assembled Fibronectin matrix 2327729. Retain extracellular region for the soluble/receptor-associated FN1 pool; intracellular SRC/SYK/FAK signaling components do not relocate FN1. Supporting Evidence: Reactome:R-HSA-429441 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-481007 | KEEP AS NON CORE | Summary: Platelet granule release supplies an extracellular fibronectin pool without establishing matrix deposition. Reason: The alpha-granule exocytosis event contains FN1 in the granule-lumen input 114620 and extracellular monomer 54851 in the released-content set 481033. Secretion establishes an extracellular pool without establishing its subsequent deposition into matrix. Supporting Evidence: Reactome:R-HSA-481007 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-6785895 | KEEP AS NON CORE | Summary: The cytokine-regulated event produces extracellular fibronectin without specifying matrix assembly. Reason: The IL4/IL13 expression event outputs a set containing extracellular FN1 monomer 54851. Regulated expression/secretion does not establish assembled matrix for that measured/modelled pool; retain extracellular region. Supporting Evidence: Reactome:R-HSA-6785895 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9624017 | MODIFY | Summary: The signaling complex retains fibronectin as an extracellular matrix component. Reason: The input integrin alpha5beta1βFibronectin matrix complex 2327790 contains the explicit matrix polymer 2327729. SHC phosphorylation occurs on the intracellular partner, without relocating extracellular FN1; matrix refinement is supported. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9624017 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9638552 | MODIFY | Summary: The bacterial SfaS-binding substrate is explicitly fibronectin matrix. Reason: The bacterial SfaS-binding event explicitly consumes Fibronectin matrix 2327729. Retain the matrix location without transferring bacterial adhesion mechanisms to FN1. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9638552 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9865226 | MODIFY | Summary: The modeled signaling complex contains extracellular fibronectin matrix; other components perform catalysis. Reason: The YAP-dephosphorylation catalyst complex 9865499 explicitly contains Fibronectin matrix 2327729 alongside integrin, PDE4D5, ANXA2 and PP2A. The FN1 location is extracellular matrix; the phosphatase activity and YAP localization belong to other components. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9865226 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9932034 | MODIFY | Summary: The curli-binding event explicitly contains fibronectin matrix. Reason: The bacterial curli/CsgA-binding event explicitly consumes Fibronectin matrix 2327729, supporting matrix refinement for this extracellular structural pool. Proposed replacements: extracellular matrix Supporting Evidence: Reactome:R-HSA-9932034 |
| GO:0031093 platelet alpha granule lumen | TAS Reactome:R-HSA-481007 | KEEP AS NON CORE | Summary: The secretion event supports fibronectin storage in the platelet alpha-granule lumen. Reason: The alpha-granule exocytosis event 481007 contains FN1 entity 114620 in the platelet alpha-granule lumen and releases extracellular FN1 monomer 54851. This supports platelet storage/secretion as a contextual location, distinct from assembled extracellular matrix and from all-product residence in granules. Supporting Evidence: Reactome:R-HSA-481007 |
| GO:0043542 endothelial cell migration | IDA PMID:20123964 Lipid phosphate phosphatase 3 stabilization of beta-catenin ... | KEEP AS NON CORE | Summary: Added fibronectin restores endothelial migration in the tested depletion model. Reason: Selected original PMID:20123964 Results show dose-dependent restoration of migration and wound closure by exogenous fibronectin in LPP3-depleted human dermal microvascular endothelial cells. This is a direct fibronectin intervention, not merely correlation with its expression. Retain the endothelial migration role as a particular biological use of its adhesive matrix function; the separate branching rescue experiments should not all be attributed to fibronectin alone. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700181 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9700181 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700190 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9700190 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700193 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9700193 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712078 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9712078 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712079 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9712079 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712083 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9712083 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712084 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9712084 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9712085 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9712085 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9724099 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9724099 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9850958 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9850958 |
| GO:0005178 integrin binding | IDA PMID:33962943 Structural insights into integrin Ξ±(5)Ξ²(1) opening by fibron... | ACCEPT | Summary: Human fibronectin makes direct, structurally resolved contacts with Ξ±5Ξ²1 integrin. Reason: PMID:33962943 examines human placental Ξ±5Ξ²1 in nanodiscs with FN7β10 and resolves RGD-region, synergy-region and additional contacts, supported by binding experiments. This directly establishes the core integrin-binding capacity. Domain constructs and experimental residue numbering do not establish identical presentation of the site across every FN1 natural product. Supporting Evidence: PMID:33962943 Structural insights into integrin Ξ±(5)Ξ²(1) opening by fibronectin ligand |
| GO:0005515 protein binding | IPI PMID:33962943 Structural insights into integrin Ξ±(5)Ξ²(1) opening by fibron... | MODIFY | Summary: The source directly supports alpha5-beta1 integrin binding. Reason: PMID:33962943 directly studies the complex of fibronectin and human alpha5-beta1 integrin, including the FN type-III 9β10 region and receptor activation-associated structural states. Integrin binding is the appropriate informative replacement. Preserve both original receptor-subunit supporting entities and the tested construct/conformation scope; do not infer that alpha4-beta1 recognition uses the same RGD-centered interface. Proposed replacements: integrin binding Supporting Evidence: PMID:33962943 Structural insights into integrin Ξ±(5)Ξ²(1) opening by fibronectin ligand |
| GO:0005515 protein binding | IPI PMID:12167537 Several regions of the repeat domain of the Staphylococcus c... | KEEP AS NON CORE | Summary: Fibronectin binds a region of the bacterial autolysin AtlC. Reason: PMID:12167537 reports fibronectin binding by the interdomain repeat region of the Staphylococcus caprae autolysin AtlC. Retain the supported microbial adhesion interaction as non-core for FN1. The assayed region provides binding rather than a demonstrated catalytic interface, so the partnerβs hydrolase identity is not used to replace the annotation with enzyme binding. Supporting Evidence: PMID:12167537 Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding |
| GO:0005515 protein binding | IPI PMID:12421310 Elongation factor Tu and E1 beta subunit of pyruvate dehydro... | KEEP AS NON CORE | Summary: Fibronectin binds the bacterial pyruvate-dehydrogenase E1 beta component. Reason: PMID:12421310 reports fibronectin binding by recombinant Mycoplasma pneumoniae PdhB and its N-terminal region using ligand-binding assays. Retain this supported microbial adhesion interaction as non-core, preserving the tested fragment scope. PdhBβs membership in the pyruvate-dehydrogenase E1 enzyme does not describe the adhesion function measured here or imply FN1 participation in pyruvate metabolism. Supporting Evidence: PMID:12421310 Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae |
| GO:0005515 protein binding | IPI PMID:15292204 BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorfe... | KEEP AS NON CORE | Summary: The Borrelia BBK32 interaction with fibronectin is supported. Reason: PMID:15292204 describes the fibronectin-binding protein BBK32 and its interactions with FN in the bacterial adhesion setting. Retain the original partner association as non-core. The pathogen-centered study is not a reason to remove a human FN binding assertion, but the interaction also does not establish a new core human pathway function. Supporting Evidence: PMID:15292204 BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorferi, contains a disordered region that undergoes a conformational change on ligand binding |
| GO:0005515 protein binding | IPI PMID:17849409 Identification of novel bacterial plasminogen-binding protei... | UNDECIDED | Summary: The FNβDnaK pair is not resolved by the retrieved source scope. Reason: PMID:17849409 examines mycobacterial plasminogen-binding proteins. Its authentic abstract explicitly identifies FN binding by GlnA1, whereas it discusses DnaK among plasminogen-binding proteins. The full pair-specific FN experiment for DnaK was not recovered. Preserve the curated assertion as undecided rather than inferring a wrong-gene error or treating the GlnA1 assay as evidence for every protein in the screen. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19429745 Enolase from Paracoccidioides brasiliensis: isolation and id... | KEEP AS NON CORE | Summary: Fibronectin binds the fungal enolase identified in the source. Reason: PMID:19429745 identifies a Paracoccidioides brasiliensis enolase as a fibronectin-binding protein by affinity-based isolation and protein identification, with adhesion-related antibody experiments. This supports a fungal adhesion interaction with FN1, retained as non-core. The enzymeβs glycolytic identity is not used as a substitute for the demonstrated adhesion role, and no human infection process is added. Supporting Evidence: PMID:19429745 Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein |
| GO:0031012 extracellular matrix | IDA PMID:26571399 A collagen VI-dependent pathogenic mechanism for Hirschsprun... | ACCEPT | Summary: The source supports extracellular fibronectin matrix while separating mouse-model and human-material evidence. Reason: PMID:26571399 discusses FN matrix and collagen-VI effects in a mouse Hirschsprung model, with human clinical material separate. The retained HTML body explicitly describes FN in extracellular structures and its migration-supporting substrate role; some mechanistic statements cite earlier studies. Retain the reliable existing FN matrix assertion, while distinguishing mouse model/host assays from human evidence and not claiming a replay of every original figure or product-specific construct. Supporting Evidence: PMID:26571399 This appears to be due to the fact that collagen VI is a poor substratum for supporting eNCC migration and can even interfere with the migration-promo... |
| GO:1901166 neural crest cell migration involved in autonomic nervous system development | IDA PMID:26571399 A collagen VI-dependent pathogenic mechanism for Hirschsprun... | KEEP AS NON CORE | Summary: Fibronectin supports enteric neural-crest-cell migration in the tested developmental system. Reason: Selected original PMID:26571399 experiments culture embryonic mouse midgut explants with GDNF on extracellular matrix coatings. Fibronectin promotes enteric neural-crest outgrowth, while excess collagen VI inhibits that response. Retain the source-specific developmental migration assertion and its original extension branch. The human patient observations concern the disease setting; they are not a direct human fibronectin developmental perturbation, and the commercial coating's species was not independently resolved. Supporting Evidence: PMID:26571399 This appears to be due to the fact that collagen VI is a poor substratum for supporting eNCC migration and can even interfere with the migration-promo... |
| GO:0008284 positive regulation of cell population proliferation | IDA PMID:25834989 Fibulin1C peptide induces cell attachment and extracellular ... | KEEP AS NON CORE | Summary: Fibronectin increases cell number in the tested human cell-culture context. Reason: PMID:25834989 directly tests plasma fibronectin as an extracellular matrix control in addition to fibulin-1 peptides. The study includes cell viability measurements and, in fibroblasts, a separate direct cell-count experiment showing a fibronectin response. Preserve this row's specific cell-type extension and avoid transferring every fibroblast endpoint to airway smooth muscle. It supports a contextual growth response, not a universal proliferative instruction by FN1. Supporting Evidence: |
| GO:0005102 signaling receptor binding | IDA PMID:34089617 Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronec... | KEEP AS NON CORE | Summary: Fibronectin directly binds the immune checkpoint receptor ILT3/LILRB4. Reason: The PMID:34089617 abstract explicitly reports biolayer-interferometry binding to human ILT3/LILRB4 and mouse gp49B, with the principal fibronectin site mapped to its N-terminal 30-kDa module. Retain the receptor-binding capacity without an agonism requirement. The inaccessible full body prevents extending this direct binding result to an uninspected human immune-cell endpoint or claiming that all FN1 products were tested. Supporting Evidence: PMID:34089617 Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin ameliorates autoimmune disease in BXSB/Yaa mice |
| GO:0150102 negative regulation of monocyte activation | IDA PMID:34089617 Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronec... | UNDECIDED | Summary: The human monocyte-activation endpoint cannot be independently verified from the available text. Reason: PMID:34089617 clearly supports checkpoint-receptor binding, but its accessible abstract does not expose the particular human monocyte-activation experiment underlying this IDA row. The full publisher body was not recovered. Preserve the experimental annotation as undecided; do not infer the sign of a cell response solely from receptor class, or treat the mouse-focused title as proof of a human-gene misattribution. Supporting Evidence: PMID:34089617 Blockade of checkpoint ILT3/LILRB4/gp49B binding to fibronectin ameliorates autoimmune disease in BXSB/Yaa mice |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700131 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9700131 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9700179 | MARK AS OVER ANNOTATED | Summary: The cited membrane-localized entity is an FN1βALK disease fusion; the native-FN1 mapping is broader than this source establishes. Reason: The cited Reactome event models the disease-associated FN1(32β1201)βALK(1022β1620) fusion, its phosphorylated form or its dimers at the plasma membrane. The inspected physical-entity paths preserve that fusion context, whereas this GO row names UniProtKB:P02751 without a fusion or fragment qualification. Mark the exported, unqualified native-FN1 assertion as over-annotated: this event-specific evidence does not establish the same localization for a natural FN1 product. This judgment does not dispute the modeled fusion location or exclude independently supported cell-surface association of native fibronectin. A curator check of the subject/context mapping is appropriate; no corrected gene-product identifier is established. Supporting Evidence: Reactome:R-HSA-9700179 |
| GO:0007229 integrin-mediated signaling pathway | IDA PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics dri... | ACCEPT | Summary: Fibronectin-integrin adhesion activates the associated adhesion-signaling machinery. Reason: Selected original PMID:19126672 experiments compare human plasma fibronectin with poly-D-lysine in mouse NIH3T3 fibroblasts. Fibronectin supports Ξ²1-integrin-dependent FAK/paxillin phosphorylation and spreading. Retain integrin-mediated signaling as a core use of the fibronectin matrix ligand, while distinguishing the separate PI3K dynamics that also occur on poly-D-lysine and do not require the same Ξ²1 engagement. Supporting Evidence: PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts |
| GO:0034446 substrate adhesion-dependent cell spreading | IDA PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics dri... | ACCEPT | Summary: A fibronectin substrate supports integrin-dependent cell spreading. Reason: PMID:19126672 directly measures spreading of mouse NIH3T3 cells on human plasma fibronectin and distinguishes this response from poly-D-lysine attachment. Ξ²1-integrin interference affects spreading and focal-adhesion signaling. Fibronectin supplies the extracellular adhesive substrate; the cellular cytoskeletal and kinase activities are not themselves molecular functions of FN1. Supporting Evidence: PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IDA PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics dri... | KEEP AS NON CORE | Summary: Adhesion on fibronectin is associated with PI3K/Akt activation, but the pathway is not fibronectin-integrin exclusive. Reason: In the original PMID:19126672 experiments, PI3K lipid signals and Akt phosphorylation occur in mouse NIH3T3 cells attached to fibronectin and also to poly-D-lysine. Ξ²1-integrin blocking distinguishes FAK/paxillin and spreading responses from the PI3K behavior. Retain the observed adhesion-context association without presenting FN1 as a direct PI3K activator or asserting that this pathway requires a unique fibronectin-integrin signal. Supporting Evidence: PMID:19126672 Spontaneous phosphoinositide 3-kinase signaling dynamics drive spreading and random migration of fibroblasts |
| GO:0005201 extracellular matrix structural constituent | HDA PMID:28344315 Proteomic characterization of human multiple myeloma bone ma... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:28344315 provides the original proteomic context for human myeloma-associated bone-marrow extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:28344315 Proteomic characterization of human multiple myeloma bone marrow extracellular matrix |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:28327460 provides the original proteomic context for human mesenchymal-stromal-cell and fibroblast extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:28327460 In the stem-cell niche, the extracellular matrix (ECM) serves as a structural support that additionally provides stem cells with signals that contribu... |
| GO:0031012 extracellular matrix | HDA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: The stromal-cell study supports the curated fibronectin matrix location in its stated cell contexts. Reason: PMID:28327460 selected primary text describes decellularized ECM produced by human bone-marrow mesenchymal stromal cells, adipose-derived stromal cells and neonatal dermal fibroblasts. Retain the FN matrix localization in each original cell-context alternative. The exact target supplementary spectral row was not independently reprocessed in this pass; the core FN matrix location is independently established and the curated HDA assertion is retained without a false universal-product claim. Supporting Evidence: PMID:28327460 In the stem-cell niche, the extracellular matrix (ECM) serves as a structural support that additionally provides stem cells with signals that contribu... |
| GO:0031012 extracellular matrix | IDA PMID:16157329 Sequential deposition of latent TGF-beta binding proteins (L... | ACCEPT | Summary: The fibroblast-matrix study supports the existing fibronectin matrix assertion within its source limits. Reason: PMID:16157329 authentic abstract concerns isolated insoluble matrices and immunofluorescence/confocal analyses of human lung fibroblast ECM, with LTBP deposition as the main question. Retain the well-established FN matrix location and trusted existing IDA assertion. The abstract does not independently expose the FN-specific panel or all constructs, so do not describe that target experiment as replayed. Supporting Evidence: PMID:16157329 Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts |
| GO:0043394 proteoglycan binding | IDA PMID:29030641 Lubricin binds cartilage proteins, cartilage oligomeric matr... | ACCEPT | Summary: Human fibronectin directly binds the proteoglycan lubricin. Reason: PMID:29030641 tests human blood-derived fibronectin with recombinant human lubricin/PRG4 regions in solid-phase binding assays and localizes an important contribution to the C-terminal lubricin region. Human cartilage proximity observations provide an additional setting but are not the sole evidence for binding. Retain the direct proteoglycan-binding capacity without generalizing to all proteoglycans or all natural FN1 products. Supporting Evidence: PMID:29030641 Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface |
| GO:0031012 extracellular matrix | HDA PMID:28344315 Proteomic characterization of human multiple myeloma bone ma... | ACCEPT | Summary: The human bone-marrow proteomics context supports the curated fibronectin matrix location. Reason: PMID:28344315 authentic abstract describes proteomic profiling of human bone-marrow ECM in MGUS, multiple myeloma and healthy donors. Retain the source-context FN matrix annotation as a core location; this bounded pass did not recover/replay the FN-specific supplementary identification, nor does it transfer the ANXA2/LGALS1 findings to FN1. Supporting Evidence: PMID:28344315 Proteomic characterization of human multiple myeloma bone marrow extracellular matrix |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:28675934 provides the original proteomic context for human breast and omental extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:28675934 Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: The tissue-proteomics study supports fibronectin in extracellular-matrix preparations. Reason: PMID:28675934 selected primary text explains ECM enrichment/decellularization and proteomic analysis of paired human breast-cancer/adjacent mammary and ovarian-cancer omental/normal omental tissues. Preserve each original tissue alternative and the reliable FN matrix location. The target supplementary peptide table was not independently replayed; no tumor-cell-autonomous or all-product mechanism follows from tissue proteomics. Supporting Evidence: PMID:28675934 Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:23979707 SILAC-based proteomics of human primary endothelial cell mor... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:23979707 provides the original proteomic context for primary human endothelial extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:23979707 By comparing proteomic changes in primary human endothelial cells morphogenesis on matrigel to general adhesion mechanisms in cells spreading on cultu... |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:27559042 provides the original proteomic context for human atrial extracellular glycoproteins. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:27559042 We used proteomics to profile glycoproteins in the human cardiac extracellular matrix (ECM) |
| GO:0005201 extracellular matrix structural constituent | ISS GO_REF:0000024 | ACCEPT | Summary: The ortholog inference agrees with the established structural matrix role of human fibronectin. Reason: Preserve the bovine F1SS24 similarity source and original ISS context. Human fibronectin polymerization and matrix-maintenance experiments independently demonstrate the relevant structural scaffold work. The conserved function is well supported without assuming an uninspected bovine assay or transferring all tissue-specific splice-product behavior. Supporting Evidence: |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:20551380 provides the original proteomic context for human aortic extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:20551380 For instance, we were able to detect matrix metalloproteinase-9 by mass spectrometry and relate its presence to degradation of fibronectin in a clinic... |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:25037231 provides the original proteomic context for human primary colorectal-tumor and metastatic extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. Supporting Evidence: PMID:25037231 Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver |
| GO:0031012 extracellular matrix | HDA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: The colorectal and liver-tissue study supports fibronectin as an extracellular-matrix constituent. Reason: PMID:25037231 describes enriched ECM proteomes from human colorectal cancers, corresponding liver metastases and normal tissue comparisons. Retain FN as a matrix constituent while preserving the separate colon/liver source contexts. Selected primary narrative and methods context were read, not a fresh FN peptide-level analysis; statements about targeted FN splice variants in the discussion cite other work and are not natural-product assignments from these samples. Supporting Evidence: PMID:25037231 Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver |
| GO:0005576 extracellular region | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | KEEP AS NON CORE | Summary: The assayed vascular fibronectin fraction supports extracellular occurrence without requiring insoluble matrix. Reason: PMID:27068509 uses sequential extraction of human saphenous veins. FN1 is identified in the NaCl fraction (Table 1) and separately confirmed by immunohistochemistry/immunoblotting; the authors describe NaCl-soluble/newly synthesized extracellular proteins separately from guanidine-solubilized insoluble ECM. This supports extracellular occurrence in vessel tissue but does not establish that the assayed FN1 fraction is assembled insoluble matrix. Preserve extracellular region with the extraction boundary. Supporting Evidence: PMID:27068509 Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins |
| GO:0031012 extracellular matrix | HDA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: The human atrial-matrix study supports the curated fibronectin matrix identification. Reason: PMID:27559042 retained text describes mass spectrometry after ECM extraction and glycoprotein/glycopeptide enrichment from paired human left/right atrial appendages. The main mechanistic results concern decorin; they must not be transferred to FN1. Retain the curator-supported FN matrix identification, preserving both conjunctive tissue-extension components, and state that the exact FN supplementary target row was not replayed. Supporting Evidence: PMID:27559042 We used proteomics to profile glycoproteins in the human cardiac extracellular matrix (ECM) |
| GO:0005615 extracellular space | HDA PMID:20551380 Proteomics characterization of extracellular space component... | MODIFY | Summary: The historical extracellular source pool is preserved through the current extracellular-region term. Reason: The original GO:0005615 identifier and historical source must remain immutable. Official QuickGO marks extracellular space obsolete because it denotes the same concept as GO:0005576 extracellular region. Propose that current term while retaining the original source-specific extracellular pool; this is ontology reconciliation, not evidence that all secreted FN1 is assembled matrix. The corresponding current source contexts are reviewed separately and inherited quotations must not be copied to new rows. Proposed replacements: extracellular region Supporting Evidence: PMID:20551380 For instance, we were able to detect matrix metalloproteinase-9 by mass spectrometry and relate its presence to degradation of fibronectin in a clinic... |
| GO:0031012 extracellular matrix | HDA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: The aortic study supports matrix-associated fibronectin alongside a separate soluble or loosely bound pool. Reason: PMID:20551380 selected primary Methods/Results examine human ascending-aorta extracellular extracts after plasma-contaminant washes and decellularization. FN products occur in both NaCl and guanidine extracts and are independently probed by immunoblotting (Figure 3 caption/paragraph86). Retain the matrix pool as well as the separate broader extracellular annotation, distinguishing loosely bound/degraded protein from matrix-associated material. This does not assign all FN products or all extraction pools to insoluble fibrils. Supporting Evidence: PMID:20551380 For instance, we were able to detect matrix metalloproteinase-9 by mass spectrometry and relate its presence to degradation of fibronectin in a clinic... |
| GO:0031012 extracellular matrix | ISS PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeli... | ACCEPT | Summary: The porcine myocardial donor supports a conserved fibronectin matrix location with explicit transfer limits. Reason: PMID:22261194 authentic abstract describes sequential ECM extraction in a porcine myocardial ischemia/reperfusion model, followed by human validation for selected ECM proteins. Preserve the original pig donor/ISS source and heart context. The FN-specific transferred location is consistent with established human FN matrix function, but this abstract alone does not identify which human validation assay tested FN1; do not claim an independently replayed human target assay. Supporting Evidence: PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury |
| GO:0031012 extracellular matrix | HDA PMID:23979707 SILAC-based proteomics of human primary endothelial cell mor... | ACCEPT | Summary: The source supports fibronectin-containing matrix in the human endothelial context. Reason: PMID:23979707 retained primary discussion explicitly reports FN1-containing ECM during HUVEC morphogenesis and CLEC14A binding/colocalization with FN1 (Figure 4 cited); mouse tumor-model experiments are separate. Retain the human endothelial-context matrix location while noting that this cached HTML extraction is selective and the exact figure pixels/SI were not independently inspected. Supporting Evidence: PMID:23979707 By comparing proteomic changes in primary human endothelial cells morphogenesis on matrigel to general adhesion mechanisms in cells spreading on cultu... |
| GO:1904237 positive regulation of substrate-dependent cell migration, cell attachment to substrate | IDA PMID:25834989 Fibulin1C peptide induces cell attachment and extracellular ... | ACCEPT | Summary: Fibronectin directly promotes the attachment component of cell migration. Reason: PMID:25834989 directly tests human plasma fibronectin and reports increased attachment of human lung fibroblasts from the studied groups. GO:1904237 concerns the cell-attachment step of migration, so a separate whole-cell migration trajectory is not required to support that step. Preserve each original cell-type extension branch, and distinguish the fibronectin control results from effects reported specifically for the fibulin-1C peptide. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10788510 The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aure... | KEEP AS NON CORE | Summary: The source supports the fibronectin-binding staphylococcal FnBPA protein. Reason: PMID:10788510 establishes FnBPA as a bifunctional adhesin with distinguishable FN- and fibrinogen-binding properties. Retain the sourceβs FnBPAβFN association as non-core. The fibrinogen experiments and competition by clumping factor A cannot be copied into a separate FNβClfA binding claim without its own evidence. Supporting Evidence: PMID:10788510 The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aureus is a bifunctional protein that also binds to fibrinogen |
| GO:0051702 biological process involved in interaction with symbiont | IDA PMID:12167537 Several regions of the repeat domain of the Staphylococcus c... | KEEP AS NON CORE | Summary: Microbial adhesins can exploit fibronectin as a host binding substrate. Reason: The PMID:12167537 abstract directly identifies fibronectin binding by recombinant repeat-containing regions of the Staphylococcus caprae AtlC adhesin using ELISA and surface-plasmon-resonance experiments. Retain the original host-symbiont context and both projected source objects. This is an organism-specific exploitation of a matrix-binding capacity, not a microbial catalytic or virulence activity of human FN1. Supporting Evidence: PMID:12167537 Several regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding |
| GO:0005515 protein binding | IPI PMID:16677310 Mycobacterium tuberculosis malate synthase is a laminin-bind... | KEEP AS NON CORE | Summary: Fibronectin binds the mycobacterial malate-synthase protein. Reason: PMID:16677310 reports fibronectin and laminin association with Mycobacterium tuberculosis malate synthase and maps adhesion to its C-terminal region. Retain the supported fibronectin interaction as non-core. This noncatalytic adhesion interface is the relevant experimental context; the enzymeβs metabolic class does not establish a distinct FN1 catalytic or regulatory role. Supporting Evidence: PMID:16677310 tb malate synthase (MS) has adapted to function as an adhesin which binds to laminin and fibronectin |
| GO:0051702 biological process involved in interaction with symbiont | IDA PMID:19429745 Enolase from Paracoccidioides brasiliensis: isolation and id... | KEEP AS NON CORE | Summary: A fungal surface protein binds fibronectin in an adhesion context. Reason: The PMID:19429745 abstract reports fibronectin recognition by a Paracoccidioides brasiliensis surface enolase and adhesion-related blocking observations. Retain the host interaction as a non-core context. The fungal protein's enolase activity and organism-level pathogenic functions are not assigned to FN1, and the precise host interaction extension remains the original curator assertion. Supporting Evidence: PMID:19429745 Enolase from Paracoccidioides brasiliensis: isolation and identification as a fibronectin-binding protein |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | UNDECIDED | Summary: The individual FN interaction with OppD remains unresolved. Reason: PMID:19220903 identifies OppD among five proteins co-migrating in a roughly 40-kDa Lactobacillus plantarum band detected by an FN overlay. Mass spectrometry identifies the proteins present in that band but does not isolate which one binds FN. The retrieved Results and Table 1 do not provide a separate binding measurement for OppD. Preserve the original pair as undecided rather than treating the band-level result as five validated binary interactions or as proof of nonbinding. Supporting Evidence: PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is a fibronectin binding protein |
| GO:0051702 biological process involved in interaction with symbiont | IDA PMID:12421310 Elongation factor Tu and E1 beta subunit of pyruvate dehydro... | KEEP AS NON CORE | Summary: Mycoplasma surface proteins can bind fibronectin during host attachment. Reason: The PMID:12421310 abstract reports fibronectin-affinity isolation and recombinant binding tests for Mycoplasma pneumoniae EF-Tu and pyruvate-dehydrogenase E1Ξ², with adhesion inhibition by antibodies. Retain the host-symbiont context without transferring the microbial enzymes' catalytic functions to FN1 or treating this organism-specific interaction as its defining matrix function. Supporting Evidence: PMID:12421310 Elongation factor Tu and E1 beta subunit of pyruvate dehydrogenase complex act as fibronectin binding proteins in Mycoplasma pneumoniae |
| GO:0001755 neural crest cell migration | IDA PMID:26571399 A collagen VI-dependent pathogenic mechanism for Hirschsprun... | KEEP AS NON CORE | Summary: Fibronectin supports neural-crest-cell movement in the tested enteric explant model. Reason: The selected original PMID:26571399 Results directly compare extracellular matrix substrates for embryonic mouse enteric neural-crest outgrowth. Fibronectin promotes migration in the GDNF-supported culture, and collagen VI alters that response. Retain this developmental context rather than dismissing FN1 because collagen VI is prominent in the title; no direct human developmental assay or autonomous cell-fate instruction is inferred. Supporting Evidence: PMID:26571399 This appears to be due to the fact that collagen VI is a poor substratum for supporting eNCC migration and can even interfere with the migration-promo... |
| GO:0048484 enteric nervous system development | IDA PMID:26571399 A collagen VI-dependent pathogenic mechanism for Hirschsprun... | KEEP AS NON CORE | Summary: The enteric nervous-system annotation is supported by a bounded developmental matrix experiment. Reason: PMID:26571399 tests fibronectin-supported migration of enteric neural-crest cells from embryonic mouse gut explants, a cellular component of enteric nervous-system development. Fibronectin supplies the migratory substrate, while the study does not demonstrate that it alone specifies the lineage or reproduces the full human developmental process. Retain the original experimental annotation with that scope. Supporting Evidence: PMID:26571399 This appears to be due to the fact that collagen VI is a poor substratum for supporting eNCC migration and can even interfere with the migration-promo... |
| GO:0005515 protein binding | IPI PMID:26627825 Extracellular Fibrinogen-binding Protein (Efb) from Staphylo... | KEEP AS NON CORE | Summary: The source supports a fibrinogen-mediated EfbβFN association. Reason: PMID:26627825 Table 1 and Figure 5 identify FN in Efb pull-downs from human platelet lysates. The FN immunoblot association is detected with added fibrinogen, and the authors describe it as fibrinogen-mediated. Retain this co-complex association as non-core; it is not evidence of a direct isolated FNβEfb interface. The paperβs direct surface-plasmon-resonance assay for P-selectin must not be reassigned to FN. Supporting Evidence: PMID:26627825 2015 Dec 1. Extracellular Fibrinogen-binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet-Leukocyte Complexes. |
| GO:0001932 regulation of protein phosphorylation | IDA PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion... | KEEP AS NON CORE | Summary: Fibronectin-dependent adhesion is coupled to cellular phosphorylation responses. Reason: The PMID:11792823 abstract describes fibulin-1 modulation of fibronectin-mediated adhesion and associated phosphorylation responses. Preserve this broad regulatory context while distinguishing the extracellular fibronectin ligand from the intracellular enzymes that catalyze phosphorylation. It is not an FN1 kinase annotation or evidence for a universal phosphorylation response in every cell type. Supporting Evidence: PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility |
| GO:0010628 positive regulation of gene expression | IDA PMID:25834989 Fibulin1C peptide induces cell attachment and extracellular ... | KEEP AS NON CORE | Summary: Fibronectin changes the accumulation of selected extracellular gene products in cultured fibroblasts. Reason: The original PMID:25834989 experiments report increased EDA-fibronectin and perlecan matrix deposition after plasma-fibronectin treatment of human lung fibroblasts. Those are measured protein-product endpoints, not a direct transcription assay or proof that every change reflects altered synthesis rather than deposition and turnover. Retain the broad contextual gene-expression annotation with that mechanistic limit, without attributing the separate fibulin-1C-specific effects to fibronectin. Supporting Evidence: |
| GO:0048146 positive regulation of fibroblast proliferation | IDA PMID:25834989 Fibulin1C peptide induces cell attachment and extracellular ... | KEEP AS NON CORE | Summary: Fibronectin increases fibroblast number in the tested culture conditions. Reason: PMID:25834989 directly compares plasma fibronectin and fibulin-1 peptides in human lung fibroblasts. In addition to an MTT-type viability assay, a separate cell-count measurement reports a fibronectin-dependent increase. Retain this contextual proliferation role rather than deriving it only from metabolic viability; it does not establish a universal mitogenic effect or autonomous differentiation signal. Supporting Evidence: |
| GO:0071635 negative regulation of transforming growth factor beta production | IDA PMID:25834989 Fibulin1C peptide induces cell attachment and extracellular ... | KEEP AS NON CORE | Summary: Fibronectin lowers the measured TGF-Ξ²1 output in the tested fibroblast cultures. Reason: The original PMID:25834989 experiments measure total secreted TGF-Ξ²1 by ELISA after several days and report a reduction with plasma fibronectin. Retain the source-specific negative-regulation context. The endpoint does not by itself separate transcription, secretion, activation, sequestration and turnover, and it should not be replaced by the different effects observed with the fibulin-1C peptide. Supporting Evidence: |
| GO:0005178 integrin binding | IPI PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion... | ACCEPT | Summary: Fibronectin-integrin recognition is the relevant adhesive interaction in this study. Reason: PMID:11792823 examines modulation of fibronectin-mediated adhesion and explicitly distinguishes integrin engagement from the effects of fibulin-1. Direct human FN1-integrin binding is independently established by structural and functional work. Retain the core interaction without treating fibulin-1's inhibitory effects as intrinsic FN1 activity or claiming a purified binary assay absent from the inspected abstract. Supporting Evidence: PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility |
| GO:0070372 regulation of ERK1 and ERK2 cascade | IDA PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion... | KEEP AS NON CORE | Summary: Fibronectin adhesion is associated with ERK-pathway responses in a defined cell context. Reason: The PMID:11792823 abstract reports ERK phosphorylation in the fibronectin-dependent adhesion setting and its modulation by fibulin-1. Retain this downstream signaling context without assigning ERK catalytic activity to FN1 or assuming that the response is constitutive across tissues. The molecular work by FN1 remains extracellular ligand and matrix engagement. Supporting Evidence: PMID:11792823 Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility |
| GO:0005515 protein binding | IPI PMID:9278415 The self-association and fibronectin-binding sites of fibuli... | KEEP AS NON CORE | Summary: Fibronectin binds fibulin-1 through defined extracellular regions. Reason: PMID:9278415 reports an FNβfibulin-1 interaction and maps it to tested FN type-III and fibulin regions. Retain this matrix-partner association as non-core. It does not establish a separate catalytic activity or require an invented fibrillin/fibulin-binding GO term, and the construct evidence is not generalized to all FN1 splice products. Supporting Evidence: PMID:9278415 The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains |
| GO:0005515 protein binding | IPI PMID:1400330 Fibulin binds to itself and to the carboxyl-terminal heparin... | KEEP AS NON CORE | Summary: The earlier fibulin-1βfibronectin interaction remains supported. Reason: PMID:1400330 directly reports fibulin-1 binding to FN in solid-phase assays, with localization to the heparin-binding region of FN. Retain this distinct source context as non-core. A protein binding to that FN region is not itself heparin, and no carbohydrate-binding specificity is inferred for this particular interaction. Supporting Evidence: PMID:1400330 Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin |
| GO:0005515 protein binding | IPI PMID:10627046 The PE-PGRS glycine-rich proteins of Mycobacterium tuberculo... | KEEP AS NON CORE | Summary: Fibronectin binds the mycobacterial WAG22 antigen region. Reason: PMID:10627046 reports FN binding by a region of the Mycobacterium tuberculosis Rv1759c/WAG22 protein. Retain this pathogen-associated molecular interaction as non-core, with the tested-fragment limitation. The study does not establish another core physiological human FN1 function or equivalent binding by all FN1 natural products. Supporting Evidence: PMID:10627046 The PE-PGRS glycine-rich proteins of Mycobacterium tuberculosis: a new family of fibronectin-binding proteins |
| GO:0005515 protein binding | IPI PMID:3141278 Characterization of fibronectin-binding antigens released by... | KEEP AS NON CORE | Summary: Fibronectin binds the mycobacterial antigen-85 enzyme Ag85B. Reason: PMID:3141278 reports fibronectin recognition of purified mycobacterial antigen-85 components, including the original Ag85B context. Retain this experimentally supported microbial adhesion interaction as non-core, within the historical protein-preparation and strain scope. Its mycolyltransferase identity does not describe the binding role measured here or establish FN1 regulation of mycolyl transfer. Supporting Evidence: PMID:3141278 Characterization of fibronectin-binding antigens released by Mycobacterium tuberculosis and Mycobacterium bovis BCG |
| GO:0031012 extracellular matrix | IDA PMID:1632457 Plasminogen activator inhibitor-1 deposition in the extracel... | ACCEPT | Summary: The mesangial-cell source supports the curated fibronectin matrix localization. Reason: PMID:1632457 authentic abstract concerns human mesangial-cell matrix and PAI-1 deposition. Retain FN matrix localization, independently well established, and defer to the existing target IDA curation without claiming that the abstract itself exposes the FN-specific immunostaining. PAI-1 synthesis/deposition and t-PA activity belong to those proteins, not FN1. Supporting Evidence: PMID:1632457 Plasminogen activator inhibitor-1 deposition in the extracellular matrix of cultured human mesangial cells |
| GO:0005178 integrin binding | IMP PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a h... | ACCEPT | Summary: The wild-type fibronectin cell-binding domain engages Ξ±VΞ²3 integrin. Reason: PMID:24658351 compares wild-type human FN10 with an engineered high-affinity FN10 antagonist. The wild-type ligand supports receptor engagement, activation-associated changes and spreading, whereas the altered RGD-loop construct separates binding from agonism. Retain native integrin binding; do not generalize the engineered antagonist's behavior to all natural FN1 products. Supporting Evidence: PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a high-affinity form of fibronectin |
| GO:0033622 integrin activation | IMP PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a h... | ACCEPT | Summary: Wild-type fibronectin ligand engagement can activate integrin. Reason: The original PMID:24658351 experiments distinguish activation induced by wild-type FN10 from an engineered higher-affinity antagonist that binds without the same activation response. This is direct support for the native ligand's integrin-activation capacity. The artificial construct is a mechanistic comparator, not an unrecognized natural splice product or evidence that all fibronectin ligands antagonize integrins. Supporting Evidence: PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a high-affinity form of fibronectin |
| GO:0034446 substrate adhesion-dependent cell spreading | IMP PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a h... | ACCEPT | Summary: Wild-type fibronectin supports integrin-dependent spreading. Reason: PMID:24658351 measures spreading on native fibronectin and wild-type FN10 and contrasts it with the engineered high-affinity antagonist. Retain spreading as a core consequence of the adhesive matrix ligand. The construct-specific differences should remain explicit rather than being assigned uniformly to the natural products. Supporting Evidence: PMID:24658351 Structural basis for pure antagonism of integrin Ξ±VΞ²3 by a high-affinity form of fibronectin |
| GO:0035987 endodermal cell differentiation | IDA PMID:23154389 Regulation of endodermal differentiation of human embryonic ... | KEEP AS NON CORE | Summary: Fibronectin contributes to a matrix environment supporting definitive-endoderm differentiation. Reason: PMID:23154389 tests human fibronectin and vitronectin coatings in human embryonic stem-cell cultures with Activin A and Wnt3a. Matrix combination and integrin perturbation experiments support participation of fibronectin-mediated adhesion in the differentiation setting. Retain the original developmental annotation without claiming that FN1 alone determines cell fate or that necessity for the outcome establishes a separate catalytic function. Supporting Evidence: PMID:23154389 From this screen we identified fibronectin (FN) and vitronectin (VTN) as ECMP components that promoted DE differentiation |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: Fibronectin association with urinary exosome-enriched preparations is retained as contextual. Reason: PMID:23533145 selected full cached text describes exosome-enriched expressed-prostatic-secretion urine samples from controls and prostate-cancer patients. Retain the curated FN association with the vesicle preparation as contextual; no target-specific supplementary row, topology, lumen-versus-surface partition or vesicle-biogenesis mechanism was independently replayed. Supporting Evidence: PMID:23533145 2013 Apr 23. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. |
| GO:0070062 extracellular exosome | IDA PMID:21276792 Morphologic and proteomic characterization of exosomes relea... | KEEP AS NON CORE | Summary: The trophoblast-cell source supports the curated fibronectin association with exosome preparations. Reason: PMID:21276792 authentic abstract describes exosomes isolated from conditioned medium of human Swan71 trophoblast cells by ultrafiltration/ultracentrifugation, with density, morphology, size and proteomic characterization. Retain the experimental FN exosome association with its original trophoblast context; the abstract does not expose the FN-specific assay or vesicle topology, which remains a source-access limit. Supporting Evidence: PMID:21276792 Epub 2011 Jan 26. Morphologic and proteomic characterization of exosomes released by cultured extravillous trophoblast cells. |
| GO:0005515 protein binding | IPI PMID:11773026 In vitro localization of TIGR/MYOC in trabecular meshwork ex... | KEEP AS NON CORE | Summary: Fibronectin binds recombinant myocilin. Reason: PMID:11773026 reports recombinant myocilin interaction with FN in a solid-phase binding assay, including an FN heparin-binding region. Retain the association as non-core. The experiment does not turn myocilin into a glycosaminoglycan ligand or establish a universal FN1 role in intraocular-pressure control. Supporting Evidence: PMID:11773026 In vitro localization of TIGR/MYOC in trabecular meshwork extracellular matrix and binding to fibronectin |
| GO:0002020 protease binding | IPI PMID:22952693 Cleavage of nidogen-1 by cathepsin S impairs its binding to ... | UNDECIDED | Summary: The exact fibronectinβcathepsin L binding assertion remains unresolved. Reason: PMID:22952693 directly exposes human plasma fibronectin to cysteine cathepsins and measures degradation, including the cathepsin L context. The inspected binding experiments chiefly concern nidogen and its matrix partners; they do not independently resolve this particular fibronectin-protease IPI edge. Protease binding need not be inhibitory, and substrate status is not a refutation. Preserve the original partner and curator assertion with uncertainty rather than declaring a wrong-gene paper or converting proteolysis into an invented affinity measurement. Supporting Evidence: PMID:22952693 Cleavage of nidogen-1 by cathepsin S impairs its binding to basement membrane partners. |
| GO:0072562 blood microparticle | HDA PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy d... | KEEP AS NON CORE | Summary: Fibronectin association with human blood microparticles is retained without assigning vesicle topology. Reason: PMID:22516433 authentic abstract profiles sub-220-nm microvesicles purified from healthy human plasma and emphasizes substantial donor variability. Retain the curated blood-microparticle association; do not infer that FN1 is an integral membrane protein, a universal vesicle cargo, or itself performs vesicle production. Supporting Evidence: PMID:22516433 Epub 2012 Apr 10. Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: The urinary-exosome source supports the curated fibronectin association within its assay-access limits. Reason: PMID:19056867 authentic abstract describes human urinary-exosome proteomics. Retain the curator-supported FN association and the original urine context, with explicit limits: this pass did not replay the FN target supplemental record or establish whether it is external adsorption, membrane-associated or luminal cargo. The established extracellular protein identity does not by itself refute vesicle association. Supporting Evidence: PMID:19056867 2008 Dec 3. Large-scale proteomics and phosphoproteomics of urinary exosomes. |
| GO:0005178 integrin binding | IDA PMID:19738201 Proteomic analysis of integrin-associated complexes identifi... | ACCEPT | Summary: Fibronectin specifically associates with the Ξ±5Ξ²1 integrin complex in the isolation assay. Reason: PMID:19738201 uses fibronectin-coated beads and cross-link stabilization to isolate human integrin-associated complexes, with comparison to another ligand and enrichment of Ξ±5 integrin. Retain the core fibronectin-integrin interaction. The experiment does not make every captured intracellular partner a direct FN1-binding protein or transfer RCC2 signaling activities to fibronectin. Supporting Evidence: PMID:19738201 Quantitative, comparative analyses of the proteomes of two receptor-ligand pairs, alpha(4)beta(1)-vascular cell adhesion molecule-1 and alpha(5)beta(1... |
| GO:0005515 protein binding | IPI PMID:16336961 A novel role for fibronectin type I domain in the regulation... | KEEP AS NON CORE | Summary: Fibronectin interacts with follistatin-related protein 3. Reason: PMID:16336961 reports FN recognition by FSTL3 and links it to adhesion in the studied human hematopoietic setting. Retain the specified protein interaction as non-core. FSTL3βs activin-binding function is a property of the partner and is not transferred to FN1, and the yeast/region-level evidence is not treated as an all-product physiological mechanism. Supporting Evidence: PMID:16336961 A novel role for fibronectin type I domain in the regulation of human hematopoietic cell adhesiveness through binding to follistatin domains of FLRG a... |
| GO:0005515 protein binding | IPI PMID:12225811 Matrix-matrix interaction of cartilage oligomeric matrix pro... | KEEP AS NON CORE | Summary: Fibronectin binds cartilage oligomeric matrix protein. Reason: PMID:12225811 reports a high-affinity FNβCOMP association using solid-phase and structural-localization approaches. Retain this extracellular matrix partner interaction as non-core. COMP is not collagen despite its name and matrix context; the result does not justify collagen-binding replacement for this particular pair or a new process annotation. Supporting Evidence: PMID:12225811 Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin |
| GO:0034446 substrate adhesion-dependent cell spreading | IDA PMID:16236823 Laminin-10 and Lutheran blood group glycoproteins in adhesio... | ACCEPT | Summary: Fibronectin supports the matrix-adhesion setting required for cell spreading. Reason: The PMID:16236823 abstract describes human endothelial cells depositing fibronectin and organizing fibrillar adhesions during spreading on laminin-10, with protein-synthesis dependence. This source places FN1 within an assembled matrix system rather than establishing it as the sole initiating substrate. Independently demonstrated fibronectin spreading assays support retaining the core process with that source-specific distinction. Supporting Evidence: PMID:16236823 Field emission scanning electron microscopy and immunohistochemistry showed that the endothelial cells spread on laminin-10 and formed fibronectin-pos... |
| GO:0005577 fibrinogen complex | IDA PMID:3997886 Incorporation of thrombospondin into fibrin clots. | UNDECIDED | Summary: The reported fibrin-clot association does not resolve membership in soluble fibrinogen complex. Reason: GO:0005577 names soluble fibrinogen before thrombin conversion. PMID:3997886 authentic abstract explicitly reports cross-link-dependent incorporation of labeled fibronectin into fibrin clots, contrasting it with thrombospondin behavior. This supports a fibrin-clot association, but the exact assay for FN membership of soluble fibrinogen was not verified. Retain the original experimental assertion as undecided rather than equating fibrin with fibrinogen or removing it from incomplete full-text access. Supporting Evidence: PMID:3997886 In contrast, incorporation of 125I-fibronectin into clots was dependent upon cross-linking |
| GO:0005515 protein binding | IPI PMID:11956183 The type XIII collagen ectodomain is a 150-nm rod and capabl... | MODIFY | Summary: The collagen-XIII interaction supports collagen binding. Reason: PMID:11956183 reports binding of the recombinant human collagen-XIII ectodomain to FN, including surface-plasmon-resonance measurements. Collagen binding is an informative replacement for generic protein binding. Preserve the soluble ectodomain and heterologous-expression limits rather than assuming all membrane-bound collagen-XIII or FN1 product configurations were tested. Proposed replacements: collagen binding Supporting Evidence: PMID:11956183 The type XIII collagen ectodomain is a 150-nm rod and capable of binding to fibronectin, nidogen-2, perlecan, and heparin |
| GO:0005515 protein binding | IPI PMID:15165854 Molecular structure and interaction of recombinant human typ... | MODIFY | Summary: The collagen-XVI interaction supports collagen binding. Reason: PMID:15165854 reports FN interaction with recombinant human collagen XVI expressed in HEK293 cells. Collagen binding specifies the assayed partner class. The recombinant secreted protein/assembly setting is retained, without inferring binding by all FN1 products or assigning collagen-XVI functions to FN1. Proposed replacements: collagen binding Supporting Evidence: PMID:15165854 Recombinant collagen XVI interacts with fibrillin-1 and with fibronectin indicating multiple molecular interactions in which this ubiquitously express... |
| GO:0005793 endoplasmic reticulum-Golgi intermediate compartment | IDA PMID:15308636 Proteomics of endoplasmic reticulum-Golgi intermediate compa... | KEEP AS NON CORE | Summary: The perturbed ERGIC preparation supports a contextual secretory-transit pool of fibronectin. Reason: PMID:15308636 authentic abstract describes an ERGIC-membrane proteome from brefeldin-A-treated human HepG2 cells. FN1 is secretory cargo, so a transit-pool ERGIC location is plausible and the existing target IDA curation is retained. The assay enriches an experimentally perturbed compartment; the abstract does not expose the FN-specific target record, and the cycling/receptor claims about ERGIC32/Erv46 must not be transferred to FN1. Supporting Evidence: PMID:15308636 2004 Aug 11. Proteomics of endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membranes from brefeldin A-treated HepG2 cells identifies ERGIC-32, a new cycling protein that interacts with human Erv46. |
| GO:0005576 extracellular region | NAS PMID:14718574 The human plasma proteome: a nonredundant list developed by ... | KEEP AS NON CORE | Summary: The plasma and serum survey supports a soluble extracellular fibronectin pool. Reason: PMID:14718574 explicitly surveys human plasma/serum proteins. The authentic abstract supports a soluble extracellular FN1 pool, not matrix deposition. Retain extracellular region without replacing it solely from FN1 structural function. Supporting Evidence: PMID:14718574 Epub 2004 Jan 12. The human plasma proteome: a nonredundant list developed by combination of four separate sources. |
| GO:0005518 collagen binding | NAS PMID:3024962 Mapping the collagen-binding site of human fibronectin by ex... | ACCEPT | Summary: The fibronectin collagen-binding region binds gelatin in the reported assay. Reason: PMID:3024962 describes recombinant human fibronectin collagen-binding fragments retained on gelatin-Sepharose. Retain the established collagen/gelatin-recognition capacity while noting that the accessible assay uses denatured collagen and does not resolve affinity for every native collagen type or every FN1 natural product. Supporting Evidence: PMID:3024962 Mapping the collagen-binding site of human fibronectin by expression in Escherichia coli |
| GO:0007155 cell adhesion | NAS PMID:1423622 The three-dimensional structure of the tenth type III module... | TOO GENERAL | Summary: Cell adhesion is broader than the established cell-matrix adhesion role. Reason: The PMID:1423622 abstract describes the fibronectin type-III-10 RGD-containing structure, which supports its matrix-ligand function. Official ontology ancestry places the retained GO:0007160 cell-matrix adhesion beneath GO:0007155. Mark the broad NAS term as too general without disputing the underlying adhesive activity. Supporting Evidence: PMID:1423622 The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions |
| GO:0008201 heparin binding | NAS PMID:10075919 Crystal structure of a heparin- and integrin-binding segment... | ACCEPT | Summary: Human fibronectin contains a directly characterized heparin-binding region. Reason: The PMID:10075919 abstract describes the human FNIII12β14 structure and a basic heparin-binding surface centered in FNIII13 with an additional contribution from FNIII14. Retain the core heparin-binding capacity without turning the limited accessible structural description into a complete audit of all heparin-binding sites or all splice products. Supporting Evidence: PMID:10075919 Crystal structure of a heparin- and integrin-binding segment of human fibronectin |
| GO:0009611 response to wounding | NAS PMID:7989369 Further characterization of the NH2-terminal fibrin-binding ... | KEEP AS NON CORE | Summary: Fibronectin has a defined molecular role in the provisional wound matrix. Reason: PMID:7989369 examines fibronectin fibrin-binding regions relevant to localization in a fibrin-rich provisional matrix. Retain the contextual wound-response annotation. Fibrin recognition must not be relabeled as a fibrinogen-specific assay, and the measured fragment behavior does not establish every cellular event of wound repair. Supporting Evidence: PMID:7989369 Further characterization of the NH2-terminal fibrin-binding site on fibronectin |
| GO:0030198 extracellular matrix organization | IMP PMID:12388756 Fibronectin polymerization regulates the composition and sta... | NEW | Summary: Polymerized fibronectin provides an extracellular scaffold that organizes and stabilizes matrix fibrils. Reason: Fibronectin itself performs the structural step through polymerization and matrix-binding sites. In PMID:12388756, blocking polymerization disrupts fibronectin fibrils in human fibroblasts and aortic smooth-muscle cells; purified human fibronectin and fragment experiments distinguish scaffold assembly from integrin ligation alone. Retain this independently supported structural participation, replacing the earlier alignment-only rationale and unsupported quotation. Supporting Evidence: |
| GO:0031589 cell-substrate adhesion | IEA GO_REF:0000117 | TOO GENERAL | Summary: Cell-substrate adhesion is broader than the supported cell-matrix adhesion function. Reason: Official ontology ancestry places the retained cell-matrix adhesion term GO:0007160 beneath cell-substrate adhesion. Fibronectin supplies extracellular matrix ligands for integrin-mediated attachment, so the existing more-specific assertion captures this rule-derived biological role. The broader term is not biologically false. |
| GO:0140151 solid phase of interstitial matrix | IEA GO_REF:0000117 | ACCEPT | Summary: Assembled fibronectin belongs to the solid phase of interstitial matrix. Reason: The official GO:0140151 definition explicitly includes fibronectin among non-collagenous glycoproteins of the solid interstitial matrix. This matches assembled FN matrix described in PMID:34572092. Retain the existing electronic core location while distinguishing this deposited pool from soluble plasma FN and not assigning the matrix-forming capacity to every truncated natural product. Supporting Evidence: GO_REF:0000117 |
| GO:0005515 protein binding | IPI PMID:12736686 Pathogenic bacteria attach to human fibronectin through a ta... | KEEP AS NON CORE | Summary: FN modules recognize a peptide from streptococcal Sfb. Reason: PMID:12736686 reports structural analysis of microbial fibronectin-binding regions and the tandem beta-zipper interaction with FN type-I modules. The original partner context for streptococcal Sfb is retained separately. The interaction is biologically credible and source-supported, but the microbial adhesion setting and tested fragments do not define an additional core human FN1 function. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12736686 Pathogenic bacteria attach to human fibronectin through a ta... | KEEP AS NON CORE | Summary: FN modules recognize a peptide from the Q53971 streptococcal fibronectin-binding protein. Reason: PMID:12736686 reports structural analysis of microbial fibronectin-binding regions and the tandem beta-zipper interaction with FN type-I modules. The original partner context for the Q53971 streptococcal fibronectin-binding protein is retained separately. The interaction is biologically credible and source-supported, but the microbial adhesion setting and tested fragments do not define an additional core human FN1 function. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18042364 TSG-6 binds via its CUB_C domain to the cell-binding domain ... | KEEP AS NON CORE | Summary: Fibronectin binds the TSG-6 protein through its CUB_C region. Reason: PMID:18042364 directly reports human plasma and cellular fibronectin binding to full-length TSG-6 and its CUB_C region rather than the isolated Link module. The reported FN1 role is an extracellular association with bridging and matrix-assembly consequences. Retain the interaction as non-core; the separate heavy-chain-transfer chemistry discussed for TSG-6 is not demonstrated to be the functional basis of this fibronectin-binding assay. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20875085 Functional analysis of a murine monoclonal antibody against ... | KEEP AS NON CORE | Summary: Fibronectin binding to staphylococcal FnBPB is retained. Reason: PMID:20875085 supports the specified staphylococcal FnBPB association in its microbial adhesin context. Retain the source-specific protein interaction as non-core, rather than deleting a positive interaction solely because the term is generic. The bacterial ligand-binding role is not transferred to a new human FN1 process, and no full-length or all-product structural mechanism is inferred beyond the reported assay scope. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25034023 Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self... | KEEP AS NON CORE | Summary: Fibronectin directly binds fibrillin-2 fragments. Reason: PMID:25034023 original Methods 2.4β2.6, Results 3.2β3.3 and Table 2 include solid-phase and surface-plasmon-resonance measurements of recombinant fibrillin-2 fragments against immobilized FN. These source-specific data were recovered beyond the abstract, and support retaining the interaction as non-core. Multimerization changes apparent affinity; fragment binding is not an all-product claim or proof of every proposed step in microfibril assembly. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25290767 Structural and functional analysis of the fibronectin-bindin... | KEEP AS NON CORE | Summary: The bacterial FNE protein binds the human FN gelatin-binding domain. Reason: PMID:25290767 directly characterizes FNE association with recombinant human FN gelatin-binding fragments by calorimetry, size-exclusion/light scattering and other assays. The FNE C-terminal region contributes the interaction, and FNE competes with a collagen peptide for overlapping FN binding sites. Retain this bacterial-partner interaction as non-core, separately from the same paperβs collagen-binding context. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:27616280 Interactions of surface-displayed glycolytic enzymes of Myco... | KEEP AS NON CORE | Summary: Fibronectin binds bacterial PdhC, the E2 dihydrolipoyl acetyltransferase. Reason: PMID:27616280 explicitly distinguishes fibronectin from fibrinogen and reports fibronectin binding by bacterial PdhC. Retain this supported microbial adhesion interaction as non-core. PdhC is the E2 dihydrolipoyl acetyltransferase, but that catalytic identity does not characterize the adhesion function demonstrated in the binding assays or assign pyruvate metabolism to FN1. Supporting Evidence: |
| GO:0140144 non-collagenous component of basement membrane | TAS PMID:36399478 MatrisomeDB 2.0: 2023 updates to the ECM-protein knowledge d... | KEEP AS NON CORE | Summary: Fibronectin can occur in the non-collagenous component of basement-membrane-associated matrix. Reason: The original MatrisomeDB TAS assertion places FN1 in a non-collagenous basement-membrane component. PMID:36399478 documents curated human/mouse ECM proteomics and retains both soluble and insoluble datasets; it is not by itself a universal basement-membrane imaging experiment. Independent review PMID:34572092 explicitly describes FN in both basement-membrane and interstitial ECM. Retain the contextual basement-membrane assertion without claiming ubiquitous basement-membrane incorporation or treating FN1 as a collagen/laminin. Supporting Evidence: |
| GO:0140149 non-collagenous component of interstitial matrix | TAS PMID:36399478 MatrisomeDB 2.0: 2023 updates to the ECM-protein knowledge d... | ACCEPT | Summary: Assembled fibronectin is a non-collagenous component of interstitial matrix. Reason: GO:0140149 explicitly describes non-collagenous interstitial ECM including fibronectin. PMID:36399478 supplies curated ECM proteomics context, with mixed extraction pools, and independent review PMID:34572092 describes assembled FN interstitial matrices. Retain the core location of the assembled pool; do not conflate the database paper with an isoform-resolved localization experiment. Supporting Evidence: |
| GO:0061800 fibronectin fibril | TAS PMID:34572092 Fibronectin: Molecular Structure, Fibrillar Structure and Me... | ACCEPT | Summary: Fibronectin molecules form the fibrils represented by this matrix location. Reason: The genuine newly acquired PMID:34572092 is a review specifically addressing FN fibrils, their assembly, composition and mechanics. Its abstract and selected sections explicitly distinguish soluble dimers, cell-assembled fibrils and artificial anastellin-derived fibers. GO:0061800 is a fiber made from FN molecules. Retain this core fibril location for the matrix-forming protein population; the review is synthesis rather than a new primary assay, and truncated/alternative products are not universally assigned fibrillogenesis. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:23658023 Comparative proteomic analysis of supportive and unsupportiv... | ACCEPT | Summary: The feeder-cell study supports fibronectin incorporation into deposited extracellular matrix. Reason: PMID:23658023 selected Results describe alkali/detergent-isolated deposited matrices from mouse and human feeder cells, with FN enriched in immortalized human placental stromal-fibroblast ECM versus primary feeders (paragraphs 62β78; Table 1 description). This directly supports human matrix incorporation. Preserve the distinct original cell-type extension alternatives separately; substrate supplementation and mouse feeder experiments do not establish identical behavior of every human FN1 product. Supporting Evidence: |
| GO:0005576 extracellular region | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The transferred extracellular location preserves soluble as well as matrix-associated fibronectin. Reason: The existing mouse-supported ISS extracellular-region assertion is consistent with the distinct soluble, secreted and matrix-associated FN1 pools. Retain the broad context; no donor-count or circularity argument is used, and this pass does not claim replay of the original donor assay. Supporting Evidence: GO_REF:0000024 |
| GO:0005515 protein binding | IPI PMID:17849409 Identification of novel bacterial plasminogen-binding protei... | KEEP AS NON CORE | Summary: Fibronectin binds mycobacterial glutamine synthetase GlnA1. Reason: PMID:17849409 explicitly reports recombinant mycobacterial GlnA1 binding to fibronectin in addition to plasminogen. Retain this specified microbial interaction as non-core, supported by the authentic abstract. The result is not transferred to the separate DnaK or antigen-85B assertions, and the partnerβs glutamine-synthetase identity is not used to infer an FN1 metabolic function. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17849409 Identification of novel bacterial plasminogen-binding protei... | UNDECIDED | Summary: The source-specific FNβantigen 85B pair remains unresolved. Reason: PMID:17849409 foregrounds plasminogen-binding proteins and its authentic abstract explicitly assigns FN binding to GlnA1. The FN-specific assay for antigen 85B was not recovered. Antigen 85βFN association is independently plausible, but that does not establish the exact evidence from this citation; retain uncertainty without asserting that the curator confused partners or that binding is biologically absent. Supporting Evidence: |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:28327460 provides the original proteomic context for human mesenchymal-stromal-cell and fibroblast extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:28327460 provides the original proteomic context for human mesenchymal-stromal-cell and fibroblast extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. |
| GO:0031012 extracellular matrix | HDA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: The stromal-cell study supports the curated fibronectin matrix location in its stated cell contexts. Reason: PMID:28327460 selected primary text describes decellularized ECM produced by human bone-marrow mesenchymal stromal cells, adipose-derived stromal cells and neonatal dermal fibroblasts. Retain the FN matrix localization in each original cell-context alternative. The exact target supplementary spectral row was not independently reprocessed in this pass; the core FN matrix location is independently established and the curated HDA assertion is retained without a false universal-product claim. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: The stromal-cell study supports the curated fibronectin matrix location in its stated cell contexts. Reason: PMID:28327460 selected primary text describes decellularized ECM produced by human bone-marrow mesenchymal stromal cells, adipose-derived stromal cells and neonatal dermal fibroblasts. Retain the FN matrix localization in each original cell-context alternative. The exact target supplementary spectral row was not independently reprocessed in this pass; the core FN matrix location is independently established and the curated HDA assertion is retained without a false universal-product claim. Supporting Evidence: |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:28675934 provides the original proteomic context for human breast and omental extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: The tissue-proteomics study supports fibronectin in extracellular-matrix preparations. Reason: PMID:28675934 selected primary text explains ECM enrichment/decellularization and proteomic analysis of paired human breast-cancer/adjacent mammary and ovarian-cancer omental/normal omental tissues. Preserve each original tissue alternative and the reliable FN matrix location. The target supplementary peptide table was not independently replayed; no tumor-cell-autonomous or all-product mechanism follows from tissue proteomics. Supporting Evidence: |
| GO:0005201 extracellular matrix structural constituent | RCA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Fibronectin is a structural constituent of extracellular matrix. Reason: PMID:25037231 provides the original proteomic context for human primary colorectal-tumor and metastatic extracellular matrix. The exact target peptide or supplementary tissue table was not independently replayed, so the original evidence code and each extension branch remain intact. The molecular function itself is independently established by fibronectin matrix-assembly and maintenance experiments: fibronectin supplies a physical scaffold supporting other matrix components. This does not convert detection in a tissue into an assay of every natural product. |
| GO:0031012 extracellular matrix | HDA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: The colorectal and liver-tissue study supports fibronectin as an extracellular-matrix constituent. Reason: PMID:25037231 describes enriched ECM proteomes from human colorectal cancers, corresponding liver metastases and normal tissue comparisons. Retain FN as a matrix constituent while preserving the separate colon/liver source contexts. Selected primary narrative and methods context were read, not a fresh FN peptide-level analysis; statements about targeted FN splice variants in the discussion cite other work and are not natural-product assignments from these samples. Supporting Evidence: |
| GO:1901166 neural crest cell migration involved in autonomic nervous system development | IDA PMID:26571399 A collagen VI-dependent pathogenic mechanism for Hirschsprun... | KEEP AS NON CORE | Summary: Fibronectin supports enteric neural-crest-cell migration in the tested developmental system. Reason: Selected original PMID:26571399 experiments culture embryonic mouse midgut explants with GDNF on extracellular matrix coatings. Fibronectin promotes enteric neural-crest outgrowth, while excess collagen VI inhibits that response. Retain the source-specific developmental migration assertion and its original extension branch. The human patient observations concern the disease setting; they are not a direct human fibronectin developmental perturbation, and the commercial coating's species was not independently resolved. Supporting Evidence: |
| GO:0031012 extracellular matrix | IDA PMID:26571399 A collagen VI-dependent pathogenic mechanism for Hirschsprun... | ACCEPT | Summary: The source supports extracellular fibronectin matrix while separating mouse-model and human-material evidence. Reason: PMID:26571399 discusses FN matrix and collagen-VI effects in a mouse Hirschsprung model, with human clinical material separate. The retained HTML body explicitly describes FN in extracellular structures and its migration-supporting substrate role; some mechanistic statements cite earlier studies. Retain the reliable existing FN matrix assertion, while distinguishing mouse model/host assays from human evidence and not claiming a replay of every original figure or product-specific construct. Supporting Evidence: |
| GO:0005576 extracellular region | HDA PMID:20551380 Proteomics characterization of extracellular space component... | KEEP AS NON CORE | Summary: The aortic source also supports extracellular fibronectin outside a strictly insoluble-matrix pool. Reason: PMID:20551380 includes both loosely bound/newly synthesized or degraded extracellular proteins in NaCl and matrix-associated material recovered by guanidine. The separate extracellular-region row can preserve that broader human aortic pool rather than being mechanically collapsed into the matrix row. Figure 3 text independently identifies FN products in both fractions; no all-fractions-insoluble inference is made. Supporting Evidence: |
| GO:1904237 positive regulation of substrate-dependent cell migration, cell attachment to substrate | IDA PMID:25834989 Fibulin1C peptide induces cell attachment and extracellular ... | ACCEPT | Summary: Fibronectin directly promotes the attachment component of cell migration. Reason: PMID:25834989 directly tests human plasma fibronectin and reports increased attachment of human lung fibroblasts from the studied groups. GO:1904237 concerns the cell-attachment step of migration, so a separate whole-cell migration trajectory is not required to support that step. Preserve each original cell-type extension branch, and distinguish the fibronectin control results from effects reported specifically for the fibulin-1C peptide. Supporting Evidence: |
| GO:0005576 extracellular region | IDA PMID:15292204 BBK32, a fibronectin binding MSCRAMM from Borrelia burgdorfe... | KEEP AS NON CORE | Summary: The existing extracellular fibronectin context is retained without inferring matrix assembly from bacterial binding. Reason: PMID:15292204 authentic abstract demonstrates recombinant bacterial BBK32 domain binding to fibronectin and its N-terminal region. Retain the existing extracellular FN context, independently established, without treating the abstract as an in-vivo FN localization experiment or inferring that the assayed FN fragment has assembled into matrix. Bacterial binding does not assign bacterial functions to FN1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10788510 The fibronectin-binding MSCRAMM FnbpA of Staphylococcus aure... | UNDECIDED | Summary: The distinct FNβClfA pairing is not verified by the available source. Reason: PMID:10788510 describes FnBPA binding to FN and fibrinogen, and ClfA competition in the fibrinogen setting. The full FN-specific ClfA experiment was not recovered. Preserve this original partner context as undecided; neither the proteinβs fibrinogen-binding name nor a title focused on FnBPA is sufficient to declare a curation error, and the FnBPA result is not evidence for the distinct ClfA pair. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | UNDECIDED | Summary: The individual FN interaction with RibA remains unresolved. Reason: PMID:19220903 identifies RibA among five proteins co-migrating in a roughly 40-kDa Lactobacillus plantarum band detected by an FN overlay. Mass spectrometry identifies the proteins present in that band but does not isolate which one binds FN. The retrieved Results and Table 1 do not provide a separate binding measurement for RibA. Preserve the original pair as undecided rather than treating the band-level result as five validated binary interactions or as proof of nonbinding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | UNDECIDED | Summary: The individual FN interaction with OpuA remains unresolved. Reason: PMID:19220903 identifies OpuA among five proteins co-migrating in a roughly 40-kDa Lactobacillus plantarum band detected by an FN overlay. Mass spectrometry identifies the proteins present in that band but does not isolate which one binds FN. The retrieved Results and Table 1 do not provide a separate binding measurement for OpuA. Preserve the original pair as undecided rather than treating the band-level result as five validated binary interactions or as proof of nonbinding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | UNDECIDED | Summary: The individual FN interaction with DltD remains unresolved. Reason: PMID:19220903 identifies DltD among five proteins co-migrating in a roughly 40-kDa Lactobacillus plantarum band detected by an FN overlay. Mass spectrometry identifies the proteins present in that band but does not isolate which one binds FN. The retrieved Results and Table 1 do not provide a separate binding measurement for DltD. Preserve the original pair as undecided rather than treating the band-level result as five validated binary interactions or as proof of nonbinding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | UNDECIDED | Summary: The individual FN interaction with PdhA remains unresolved. Reason: PMID:19220903 identifies PdhA among five proteins co-migrating in a roughly 40-kDa Lactobacillus plantarum band detected by an FN overlay. Mass spectrometry identifies the proteins present in that band but does not isolate which one binds FN. The retrieved Results and Table 1 do not provide a separate binding measurement for PdhA. Preserve the original pair as undecided rather than treating the band-level result as five validated binary interactions or as proof of nonbinding. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | UNDECIDED | Summary: The FN interaction assigned to EnoA2 is not separated from the sourceβs EnoA1 result. Reason: PMID:19220903 distinguishes EnoA1 from a second enolase form. The FN-positive 48-kDa band and the gene-deletion adhesion experiments support EnoA1, while an additional enolase-reactive band persists after enoA1 disruption. That observation alone does not establish FN binding by EnoA2. Preserve the EnoA2 source context as undecided without declaring biological nonbinding or copying the EnoA1 result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19220903 Surface displaced alfa-enolase of Lactobacillus plantarum is... | KEEP AS NON CORE | Summary: Fibronectin binds the bacterial enolase EnoA1 in adhesion assays. Reason: PMID:19220903 identifies EnoA1 in the fibronectin-positive 48-kDa band and reports reduced fibronectin adherence after enoA1 disruption. Retain the supported EnoA1 adhesion interaction as non-core, separately from unresolved proteins in the 40-kDa band and the second enolase form. Ligand overlay and cellular adhesion support this context without establishing purified binary kinetics; the partnerβs glycolytic identity does not provide the functional distinction measured here. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12421310 Elongation factor Tu and E1 beta subunit of pyruvate dehydro... | KEEP AS NON CORE | Summary: Fibronectin binds bacterial elongation factor Tu in the sourceβs recombinant-protein assays. Reason: PMID:12421310 reports recombinant Mycoplasma pneumoniae EF-Tu association with fibronectin in ligand immunoblotting and ELISA-type assays. Retain this supported microbial adhesion interaction as non-core. The partnerβs GTPase identity does not further specify the adhesion role measured here, and the assays do not assign translation or catalytic regulation to FN1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:3141278 Characterization of fibronectin-binding antigens released by... | KEEP AS NON CORE | Summary: Fibronectin binds the mycobacterial antigen-85 enzyme Ag85A. Reason: PMID:3141278 reports fibronectin recognition of purified mycobacterial antigen-85 components, including the original Ag85A context. Retain this experimentally supported microbial adhesion interaction as non-core, within the historical protein-preparation and strain scope. Its mycolyltransferase identity does not describe the binding role measured here or establish FN1 regulation of mycolyl transfer. Supporting Evidence: |
| GO:0002020 protease binding | IPI PMID:22952693 Cleavage of nidogen-1 by cathepsin S impairs its binding to ... | UNDECIDED | Summary: The exact fibronectinβcathepsin S binding assertion remains unresolved. Reason: PMID:22952693 directly exposes human plasma fibronectin to cysteine cathepsins and measures degradation, including the cathepsin S context. The inspected binding experiments chiefly concern nidogen and its matrix partners; they do not independently resolve this particular fibronectin-protease IPI edge. Protease binding need not be inhibitory, and substrate status is not a refutation. Preserve the original partner and curator assertion with uncertainty rather than declaring a wrong-gene paper or converting proteolysis into an invented affinity measurement. Supporting Evidence: |
| GO:0002020 protease binding | IPI PMID:22952693 Cleavage of nidogen-1 by cathepsin S impairs its binding to ... | UNDECIDED | Summary: The exact fibronectinβcathepsin K binding assertion remains unresolved. Reason: PMID:22952693 directly exposes human plasma fibronectin to cysteine cathepsins and measures degradation, including the cathepsin K context. The inspected binding experiments chiefly concern nidogen and its matrix partners; they do not independently resolve this particular fibronectin-protease IPI edge. Protease binding need not be inhibitory, and substrate status is not a refutation. Preserve the original partner and curator assertion with uncertainty rather than declaring a wrong-gene paper or converting proteolysis into an invented affinity measurement. Supporting Evidence: |
| GO:0007507 heart development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The historical heart-development assertion is retained as a distinct developmental source context. Reason: The unchanged historical GOA snapshot records this positive IBA with its complete four-entity WITH/FROM list. The actual PTHR46708 tree places human FN1 within the PTN002709787 clade carrying the positive heart-development IBD, and the target sequence matches the family alignment. This supports an inherited developmental role, a tissue-specific application of fibronectin matrix and adhesion activity, rather than a new direct human cardiac assay. Retain the historical source context as non-core alongside the current three-entity context; the changed donor list does not by itself establish loss or invalidate the ancestral placement. Supporting Evidence: GO_REF:0000033 |
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