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Details on Person UniProt:P02751-9 FN1
| Class:Id | ReferenceIsoform:147335 |
|---|---|
| _chainChangeLog | signal peptide:1-31 added on Fri February 6 2015;chain:32-2386 added on Fri February 6 2015;chain:627-702 added on Fri February 6 2015;chain:723-911 added on Fri February 6 2015;chain:723-903 added on Fri February 6 2015;chain:723- added on Fri February 6 2015;chain:32-2386 for 147335 removed on Fri November 1 2019;chain:32-2477 for 147335 added on Fri November 1 2019 |
| _displayName | UniProt:P02751-9 FN1 |
| _timestamp | 2024-11-03 19:51:12 |
| chain | signal peptide:1-31 chain:32-2477 chain:627-702 chain:723-911 chain:723-903 chain:723- |
| checksum | 6C436A7A5FEE6DEB |
| comment | FUNCTION Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape (PubMed:3024962, PubMed:3593230, PubMed:3900070, PubMed:7989369). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (By similarity). Participates in the regulation of type I collagen deposition by osteoblasts (By similarity). Acts as a ligand for the LILRB4 receptor, inhibiting FCGR1A/CD64-mediated monocyte activation (PubMed:34089617).FUNCTION Binds fibronectin and induces fibril formation. This fibronectin polymer, named superfibronectin, exhibits enhanced adhesive properties. Both anastellin and superfibronectin inhibit tumor growth, angiogenesis and metastasis. Anastellin activates p38 MAPK and inhibits lysophospholipid signaling.FUNCTION Secreted by contracting muscle, induces liver autophagy, a degradative pathway for nutrient mobilization and damage removal, and systemic insulin sensitization via hepatic ITGA5:ITGB1 integrin receptor signaling.SUBUNIT Mostly heterodimers or multimers of alternatively spliced variants, connected by 2 disulfide bonds near the carboxyl ends; to a lesser extent homodimers. Interacts with FBLN1, AMBP, TNR, LGALS3BP and COL13A1. Interacts with FBLN7 (By similarity). Interacts with COMP (PubMed:12225811). Interacts (via type III repeats 9-14) with TNFAIP6 (via CUB domain); this interaction enhances fibronectin fibril assembly. TNFAIP6 may act as a bridging molecule between FN1 and THBS1 (PubMed:18042364). Interacts with TNR; the interaction inhibits cell adhesion and neurite outgrowth (By similarity). Interacts with FST3 and MYOC. Interacts with SVEP1 (By similarity).SUBUNIT (Microbial infection) Interacts with S.aureus FnbA.SUBUNIT (Microbial infection) Interacts with M.bovis FbpB via the collagen-binding region.SUBUNIT (Microbial infection) Interacts with recombinant S.pneumoniae PavA (rqcH).SUBUNIT (Microbial infection) Interacts with recombinant S.suis FbpS (rqcH) via fibronectin's N-terminal 30 kDa region.SUBUNIT (Microbial infection) Interacts with fibronectin-binding proteins from other Mycobacteria.INTERACTION A number of isoforms are produced. The diversity of isoforms depends on the V region and either of the two extra domains which can be either included or excluded (partially or completely for the V region).TISSUE SPECIFICITY Expressed in the inner limiting membrane and around blood vessels in the retina (at protein level) (PubMed:29777959). Plasma FN (soluble dimeric form) is secreted by hepatocytes. Cellular FN (dimeric or cross-linked multimeric forms), made by fibroblasts, epithelial and other cell types, is deposited as fibrils in the extracellular matrix. Ugl-Y1, Ugl-Y2 and Ugl-Y3 are found in urine (PubMed:17614963).DEVELOPMENTAL STAGE Expressed between 12 and 19 weeks post-conception (WPC) in Bruch's membrane, with expression in the choroid evident from 14 WPC onwards (at protein level) (PubMed:29777959). Expressed in the inner limiting membrane at 17 WPC (at protein level) (PubMed:29777959). Ugl-Y1, Ugl-Y2 and Ugl-Y3 are present in the urine from 0 to 17 years of age (PubMed:17614963, PubMed:3584091).PTM Sulfated.PTM It is not known whether both or only one of Thr-2155 and Thr-2156 are/is glycosylated.PTM Forms covalent cross-links mediated by a transglutaminase, such as F13A or TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers (e.g. fibrinogen-fibronectin, collagen-fibronectin heteropolymers).PTM Phosphorylated by FAM20C in the extracellular medium.PTM Proteolytic processing produces the C-terminal NC1 peptide, anastellin.PTM Some lysine residues are oxidized to allysine by LOXL3, promoting fibronectin activation and matrix formation.PTM Serotonylated on Gln residues by TGM2 in response to hypoxia.DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.MISCELLANEOUS Expressed by fetal and tumor-associated cells.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.SEQUENCE CAUTION Extended N-terminus.ONLINE INFORMATION Fibronectin entry |
| description | recommendedName: fullName evidence="61"Fibronectin shortName: FN alternativeName: Cold-insoluble globulin shortName: CIG component recommendedName: Anastellin /component component recommendedName: Ugl-Y1 /component component recommendedName: Ugl-Y2 /component component recommendedName: Ugl-Y3 /component |
| geneName | FN1 FN |
| identifier | P02751 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acute phase Alternative splicing Angiogenesis Cell adhesion Cell shape Direct protein sequencing Disease variant Disulfide bond Dwarfism Extracellular matrix Glycoprotein Heparin-binding Isopeptide bond Oxidation Phosphoprotein Proteomics identification Pyrrolidone carboxylic acid Reference proteome Repeat Secreted Signal Sulfation |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | FN1 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:6789510] ENSEMBL:ENSG00000115414 FN1 [Homo sapiens] |
| secondaryIdentifier | FINC_HUMAN B7ZLF0 E9PE77 E9PG29 O95609 O95610 Q14312 Q14325 Q14326 Q17RV7 Q53S27 Q564H7 Q585T2 Q59EH1 Q60FE4 Q68DP8 Q68DP9 Q68DT4 Q6LDP6 Q6MZS0 Q6MZU5 Q6N025 Q6N0A6 Q7Z391 Q86T27 Q8IVI8 Q96KP7 Q96KP8 Q96KP9 Q9H1B8 Q9HAP3 Q9UMK2 |
| sequenceLength | 2477 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | P02751-9 |
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No pathways have been reviewed or authored by UniProt:P02751-9 FN1 (147335)
