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Showing Protein Fibronectin (HMDBP13516)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13516
Secondary Accession Numbers None
Name Fibronectin
Synonyms
  1. FN
Gene Name FN1
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Fibronectins bind cell surfaces and various compounds including collagen, fibrin, heparin, DNA, and actin (By similarity). Fibronectins are involved in cell adhesion, cell motility, opsonization, wound healing, and maintenance of cell shape healing, and maintenance of cell shape (By similarity). Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization (PubMed:21768292). Participates in the regulation of type I collagen deposition by osteoblasts (PubMed:21768292).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.
Pathways
  • AGE-RAGE signaling pathway in diabetic complications
  • Amoebiasis
  • Bacterial invasion of epithelial cells
  • ECM-receptor interaction
  • Focal adhesion
  • Human papillomavirus infection
  • PI3K-Akt signaling pathway
  • Proteoglycans in cancer
  • Regulation of actin cytoskeleton
  • Small cell lung cancer
  • Yersinia infection
Reactions Not Available
GO Classification
Biological Process
wound healing
interaction with symbiont
regulation of cell shape
substrate adhesion-dependent cell spreading
blood coagulation, fibrin clot formation
positive regulation of cell migration
cell-substrate junction assembly
extracellular matrix organization
positive regulation of cell proliferation
negative regulation of apoptotic process
positive regulation of fibroblast proliferation
calcium-independent cell-matrix adhesion
cellular response to mercury ion
integrin activation
negative regulation of collagen biosynthetic process
platelet aggregation
negative regulation of transforming growth factor beta production
neural crest cell migration involved in autonomic nervous system development
positive regulation of substrate-dependent cell migration, cell attachment to substrate
integrin-mediated signaling pathway
cell adhesion
acute-phase response
positive regulation of axon extension
heart development
cellular response to interleukin-1
angiogenesis
endodermal cell differentiation
regulation of ERK1 and ERK2 cascade
nervous system development
glial cell migration
regulation of protein phosphorylation
peptide cross-linking
cell activation
regulation of gene expression
positive regulation of gene expression
positive regulation of phosphatidylinositol 3-kinase cascade
positive regulation of chemotaxis
cell-matrix adhesion
Cellular Component
fibrinogen complex
extracellular vesicular exosome
basement membrane
endoplasmic reticulum-Golgi intermediate compartment
collagen-containing extracellular matrix
extracellular space
extracellular matrix
apical plasma membrane
Molecular Function
protease binding
protein C-terminus binding
mercury ion binding
peptidase activator activity
proteoglycan binding
receptor binding
chaperone binding
integrin binding
disordered domain specific binding
enzyme binding
heparin binding
identical protein binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 2477
Molecular Weight 272536.41
Theoretical pI 5.59
Pfam Domain Function
Signals
  • 1-32;
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P11276
UniProtKB/Swiss-Prot Entry Name FINC_MOUSE
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
  1. Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. doi: 10.1038/nbt.1532. Epub 2009 Apr 6. [PubMed:19349973 ]
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Huttlin EL, Jedrychowski MP, Elias JE, Goswami T, Rad R, Beausoleil SA, Villen J, Haas W, Sowa ME, Gygi SP: A tissue-specific atlas of mouse protein phosphorylation and expression. Cell. 2010 Dec 23;143(7):1174-89. doi: 10.1016/j.cell.2010.12.001. [PubMed:21183079 ]
  4. Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP: Lineage-specific biology revealed by a finished genome assembly of the mouse. PLoS Biol. 2009 May 5;7(5):e1000112. doi: 10.1371/journal.pbio.1000112. Epub 2009 May 26. [PubMed:19468303 ]
  5. Ghesquiere B, Van Damme J, Martens L, Vandekerckhove J, Gevaert K: Proteome-wide characterization of N-glycosylation events by diagonal chromatography. J Proteome Res. 2006 Sep;5(9):2438-47. doi: 10.1021/pr060186m. [PubMed:16944957 ]
  6. Bernhard OK, Kapp EA, Simpson RJ: Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides. J Proteome Res. 2007 Mar;6(3):987-95. doi: 10.1021/pr0604559. [PubMed:17330941 ]
  7. Villen J, Beausoleil SA, Gerber SA, Gygi SP: Large-scale phosphorylation analysis of mouse liver. Proc Natl Acad Sci U S A. 2007 Jan 30;104(5):1488-93. doi: 10.1073/pnas.0609836104. Epub 2007 Jan 22. [PubMed:17242355 ]
  8. Sweet SM, Bailey CM, Cunningham DL, Heath JK, Cooper HJ: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. Mol Cell Proteomics. 2009 May;8(5):904-12. doi: 10.1074/mcp.M800451-MCP200. Epub 2009 Jan 8. [PubMed:19131326 ]
  9. Kraft-Sheleg O, Zaffryar-Eilot S, Genin O, Yaseen W, Soueid-Baumgarten S, Kessler O, Smolkin T, Akiri G, Neufeld G, Cinnamon Y, Hasson P: Localized LoxL3-Dependent Fibronectin Oxidation Regulates Myofiber Stretch and Integrin-Mediated Adhesion. Dev Cell. 2016 Mar 7;36(5):550-61. doi: 10.1016/j.devcel.2016.02.009. [PubMed:26954549 ]
  10. Polly P, Nicholson RC: Sequence of the mouse fibronectin-encoding gene promoter region. Gene. 1993 Dec 31;137(2):353-4. doi: 10.1016/0378-1119(93)90036-3. [PubMed:8299972 ]
  11. Talts JF, Weller A, Timpl R, Ekblom M, Ekblom P: Regulation of mesenchymal extracellular matrix protein synthesis by transforming growth factor-beta and glucocorticoids in tumor stroma. J Cell Sci. 1995 Jun;108 ( Pt 6):2153-62. [PubMed:7673336 ]
  12. Blatti SP, Foster DN, Ranganathan G, Moses HL, Getz MJ: Induction of fibronectin gene transcription and mRNA is a primary response to growth-factor stimulation of AKR-2B cells. Proc Natl Acad Sci U S A. 1988 Feb;85(4):1119-23. doi: 10.1073/pnas.85.4.1119. [PubMed:3124113 ]
  13. Ryseck RP, MacDonald-Bravo H, Zerial M, Bravo R: Coordinate induction of fibronectin, fibronectin receptor, tropomyosin, and actin genes in serum-stimulated fibroblasts. Exp Cell Res. 1989 Feb;180(2):537-45. doi: 10.1016/0014-4827(89)90080-3. [PubMed:2521606 ]
  14. Khandjian EW, Salomon C, Leonard N, Tremblay S, Turler H: Fibronectin gene expression in proliferating, quiescent, and SV40-infected mouse kidney cells. Exp Cell Res. 1992 Oct;202(2):464-70. doi: 10.1016/0014-4827(92)90100-m. [PubMed:1327855 ]
  15. Corbett SA, Lee L, Wilson CL, Schwarzbauer JE: Covalent cross-linking of fibronectin to fibrin is required for maximal cell adhesion to a fibronectin-fibrin matrix. J Biol Chem. 1997 Oct 3;272(40):24999-5005. doi: 10.1074/jbc.272.40.24999. [PubMed:9312106 ]
  16. de Vega S, Iwamoto T, Nakamura T, Hozumi K, McKnight DA, Fisher LW, Fukumoto S, Yamada Y: TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding. J Biol Chem. 2007 Oct 19;282(42):30878-88. doi: 10.1074/jbc.M705847200. Epub 2007 Aug 14. [PubMed:17699513 ]
  17. Zhou H, Ye M, Dong J, Han G, Jiang X, Wu R, Zou H: Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis. J Proteome Res. 2008 Sep;7(9):3957-67. doi: 10.1021/pr800223m. Epub 2008 Jul 17. [PubMed:18630941 ]
  18. Gundry RL, Raginski K, Tarasova Y, Tchernyshyov I, Bausch-Fluck D, Elliott ST, Boheler KR, Van Eyk JE, Wollscheid B: The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation. Mol Cell Proteomics. 2009 Nov;8(11):2555-69. doi: 10.1074/mcp.M900195-MCP200. Epub 2009 Aug 4. [PubMed:19656770 ]
  19. Brunner M, Millon-Fremillon A, Chevalier G, Nakchbandi IA, Mosher D, Block MR, Albiges-Rizo C, Bouvard D: Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition. J Cell Biol. 2011 Jul 25;194(2):307-22. doi: 10.1083/jcb.201007108. Epub 2011 Jul 18. [PubMed:21768292 ]
  20. Felemban M, Dorgau B, Hunt NC, Hallam D, Zerti D, Bauer R, Ding Y, Collin J, Steel D, Krasnogor N, Al-Aama J, Lindsay S, Mellough C, Lako M: Extracellular matrix component expression in human pluripotent stem cell-derived retinal organoids recapitulates retinogenesis in vivo and reveals an important role for IMPG1 and CD44 in the development of photoreceptors and interphotoreceptor matrix. Acta Biomater. 2018 Jul 1;74:207-221. doi: 10.1016/j.actbio.2018.05.023. Epub 2018 May 17. [PubMed:29777959 ]
  21. Copie V, Tomita Y, Akiyama SK, Aota S, Yamada KM, Venable RM, Pastor RW, Krueger S, Torchia DA: Solution structure and dynamics of linked cell attachment modules of mouse fibronectin containing the RGD and synergy regions: comparison with the human fibronectin crystal structure. J Mol Biol. 1998 Apr 3;277(3):663-82. doi: 10.1006/jmbi.1998.1616. [PubMed:9533887 ]