FBLN2

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Fibulin 2
Identifiers
Symbol(s) FBLN2;
External IDs OMIM: 135821 MGI: 95488 HomoloGene: 1514
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 2199 14115
Ensembl ENSG00000163520 ENSMUSG00000064080
Uniprot P98095 P37889
Refseq NM_001004019 (mRNA)
NP_001004019 (protein)		 NM_001081437 (mRNA)
NP_001074906 (protein)
Location Chr 3: 13.57 - 13.65 Mb Chr 6: 91.18 - 91.24 Mb
Pubmed search [1] [2]

Fibulin 2, also known as FBLN2, is a human gene.[1]

This gene encodes an extracellular matrix protein, which belongs to the fibulin family. This protein binds various extracellular ligands and calcium. It may play a role during organ development, in particular, during the differentiation of heart, skeletal and neuronal structures. Alternatively spliced transcript variants encoding different isoforms have been identified.[1]

[edit] References

  1. ^ a b Entrez Gene: FBLN2 fibulin 2.

[edit] Further reading

  • Sasaki T, Göhring W, Pan TC, et al. (1996). "Binding of mouse and human fibulin-2 to extracellular matrix ligands.". J. Mol. Biol. 254 (5): 892–9. doi:10.1006/jmbi.1995.0664. PMID 7500359. 
  • Zhang RZ, Pan TC, Zhang ZY, et al. (1995). "Fibulin-2 (FBLN2): human cDNA sequence, mRNA expression, and mapping of the gene on human and mouse chromosomes.". Genomics 22 (2): 425–30. doi:10.1006/geno.1994.1404. PMID 7806230. 
  • Pan TC, Sasaki T, Zhang RZ, et al. (1994). "Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding.". J. Cell Biol. 123 (5): 1269–77. PMID 8245130. 
  • Reinhardt DP, Sasaki T, Dzamba BJ, et al. (1996). "Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues.". J. Biol. Chem. 271 (32): 19489–96. PMID 8702639. 
  • Miosge N, Götz W, Sasaki T, et al. (1996). "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo.". Histochem. J. 28 (2): 109–16. PMID 8737292. 
  • Collod G, Chu ML, Sasaki T, et al. (1997). "Fibulin-2: genetic mapping and exclusion as a candidate gene in Marfan syndrome type 2.". Eur. J. Hum. Genet. 4 (5): 292–5. PMID 8946175. 
  • Utani A, Nomizu M, Yamada Y (1997). "Fibulin-2 binds to the short arms of laminin-5 and laminin-1 via conserved amino acid sequences.". J. Biol. Chem. 272 (5): 2814–20. PMID 9006922. 
  • Sasaki T, Mann K, Wiedemann H, et al. (1997). "Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge.". EMBO J. 16 (11): 3035–43. doi:10.1093/emboj/16.11.3035. PMID 9214621. 
  • Brown JC, Sasaki T, Göhring W, et al. (1998). "The C-terminal domain V of perlecan promotes beta1 integrin-mediated cell adhesion, binds heparin, nidogen and fibulin-2 and can be modified by glycosaminoglycans.". Eur. J. Biochem. 250 (1): 39–46. PMID 9431988. 
  • Raghunath M, Tschödrich-Rotter M, Sasaki T, et al. (1999). "Confocal laser scanning analysis of the association of fibulin-2 with fibrillin-1 and fibronectin define different stages of skin regeneration.". J. Invest. Dermatol. 112 (1): 97–101. doi:10.1046/j.1523-1747.1999.00483.x. PMID 9886271. 
  • Kuivaniemi H, Marshall A, Ganguly A, et al. (1999). "Fibulin-2 exhibits high degree of variability, but no structural changes concordant with abdominal aortic aneurysms.". Eur. J. Hum. Genet. 6 (6): 642–6. doi:10.1038/sj.ejhg.5200245. PMID 9887386. 
  • Sasaki T, Göhring W, Miosge N, et al. (1999). "Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins.". FEBS Lett. 460 (2): 280–4. PMID 10544250. 
  • Gu YC, Nilsson K, Eng H, Ekblom M (2000). "Association of extracellular matrix proteins fibulin-1 and fibulin-2 with fibronectin in bone marrow stroma.". Br. J. Haematol. 109 (2): 305–13. PMID 10848816. 
  • Talts JF, Sasaki T, Miosge N, et al. (2001). "Structural and functional analysis of the recombinant G domain of the laminin alpha4 chain and its proteolytic processing in tissues.". J. Biol. Chem. 275 (45): 35192–9. doi:10.1074/jbc.M003261200. PMID 10934193. 
  • Olin AI, Mörgelin M, Sasaki T, et al. (2001). "The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding.". J. Biol. Chem. 276 (2): 1253–61. doi:10.1074/jbc.M006783200. PMID 11038354. 
  • Hopf M, Göhring W, Mann K, Timpl R (2001). "Mapping of binding sites for nidogens, fibulin-2, fibronectin and heparin to different IG modules of perlecan.". J. Mol. Biol. 311 (3): 529–41. doi:10.1006/jmbi.2001.4878. PMID 11493006. 
  • Hunzelmann N, Nischt R, Brenneisen P, et al. (2001). "Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibres.". Br. J. Dermatol. 145 (2): 217–22. PMID 11531782. 
  • Sasaki T, Göhring W, Mann K, et al. (2002). "Short arm region of laminin-5 gamma2 chain: structure, mechanism of processing and binding to heparin and proteins.". J. Mol. Biol. 314 (4): 751–63. doi:10.1006/jmbi.2001.5176. PMID 11733994. 
  • Bengtsson E, Mörgelin M, Sasaki T, et al. (2002). "The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor.". J. Biol. Chem. 277 (17): 15061–8. doi:10.1074/jbc.M108285200. PMID 11847210. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
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