From Wikipedia, the free encyclopedia
Jump to: navigation, search
Fibulin 1
Symbols FBLN1 ; FBLN; FIBL1
External IDs OMIM135820 MGI95487 HomoloGene21295 GeneCards: FBLN1 Gene
RNA expression pattern
PBB GE FBLN1 201787 at tn.png
PBB GE FBLN1 207834 at tn.png
PBB GE FBLN1 202995 s at tn.png
More reference expression data
Species Human Mouse
Entrez 2192 14114
Ensembl ENSG00000077942 ENSMUSG00000006369
UniProt P23142 Q08879
RefSeq (mRNA) NM_001996 NM_010180
RefSeq (protein) NP_001987 NP_034310
Location (UCSC) Chr 22:
45.5 – 45.6 Mb
Chr 15:
85.21 – 85.29 Mb
PubMed search [1] [2]

FBLN1 is the gene encoding fibulin-1, an extracellular matrix and plasma protein.[1][2][3]


Fibulin-1 is a secreted glycoprotein that is found in association with extracellular matrix structures including fibronectin-containing fibers, elastin-containing fibers and basement membranes. Fibulin-1 binds to a number of extracellular matrix constituents including fibronectin,[3] nidogen-1, and the proteoglycan, versican.[3][4] Fibulin-1 is also a blood protein capable of binding to fibrinogen.[5]


Fibulin-1 has modular domain structure and includes a series of nine epidermal growth factor-like modules followed by a fibulin-type module, a module found in all members of the fibulin gene family.[2]

The human fibulin-1 gene, FBLN1, encodes four splice variants designated fibulin-1A, B, C and D, which differ in their carboxy terminal regions. In mouse, chicken and the nematode, C. elegans, only two fibulin-1 variants are produced, fibulin-1C and fibulin-1D.[1]


FBLN1 has been shown to interact with:

See also[edit]


  1. ^ a b "Entrez Gene: FBLN1 fibulin 1". 
  2. ^ a b Argraves WS, Tran H, Burgess WH, Dickerson K (Dec 1990). "Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure". The Journal of Cell Biology 111 (6 Pt 2): 3155–64. doi:10.1083/jcb.111.6.3155. PMC 2116371. PMID 2269669. 
  3. ^ a b c Balbona K, Tran H, Godyna S, Ingham KC, Strickland DK, Argraves WS (Oct 1992). "Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin". The Journal of Biological Chemistry 267 (28): 20120–5. PMID 1400330. 
  4. ^ Timpl R, Sasaki T, Kostka G, Chu ML (Jun 2003). "Fibulins: a versatile family of extracellular matrix proteins". Nature Reviews Molecular Cell Biology 4 (6): 479–89. doi:10.1038/nrm1130. PMID 12778127. 
  5. ^ a b Argraves WS, Tanaka A, Smith EP, Twal WO, Argraves KM, Fan D, Haudenschild CC (Nov 2009). "Fibulin-1 and fibrinogen in human atherosclerotic lesions". Histochemistry and Cell Biology 132 (5): 559–65. doi:10.1007/s00418-009-0628-7. PMID 19693531. 
  6. ^ Perbal B, Martinerie C, Sainson R, Werner M, He B, Roizman B (Feb 1999). "The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling". Proceedings of the National Academy of Sciences of the United States of America 96 (3): 869–74. doi:10.1073/pnas.96.3.869. PMC 15317. PMID 9927660. 
  7. ^ Ohsawa I, Takamura C, Kohsaka S (Mar 2001). "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function". Journal of Neurochemistry 76 (5): 1411–20. doi:10.1046/j.1471-4159.2001.00144.x. PMID 11238726. 
  8. ^ Adam S, Göhring W, Wiedemann H, Chu ML, Timpl R, Kostka G (Sep 1997). "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules". Journal of Molecular Biology 272 (2): 226–36. doi:10.1006/jmbi.1997.1244. PMID 9299350. 
  9. ^ Tran H, VanDusen WJ, Argraves WS (Sep 1997). "The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains". The Journal of Biological Chemistry 272 (36): 22600–6. doi:10.1074/jbc.272.36.22600. PMID 9278415. 
  10. ^ Pan TC, Kluge M, Zhang RZ, Mayer U, Timpl R, Chu ML (Aug 1993). "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands". European Journal of Biochemistry / FEBS 215 (3): 733–40. doi:10.1111/j.1432-1033.1993.tb18086.x. PMID 8354280. 
  11. ^ Deeney JT, Tornheim K, Korchak HM, Prentki M, Corkey BE (Oct 1992). "Acyl-CoA esters modulate intracellular Ca2+ handling by permeabilized clonal pancreatic beta-cells". The Journal of Biological Chemistry 267 (28): 19840–5. PMID 1400300. 

Further reading[edit]