FBLN2

Fibulin 2
Identifiers
Symbols	FBLN2;
External IDs	OMIM: 135821 MGI: 95488 HomoloGene: 1514 GeneCards: FBLN2 Gene
Gene Ontology Molecular function • extracellular matrix structural constituent • calcium ion binding Cellular component • extracellular region • proteinaceous extracellular matrix Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2199	14115
Ensembl	ENSG00000163520	ENSMUSG00000064080
UniProt	P98095	P37889
RefSeq (mRNA)	NM_001004019.1	NM_001081437
RefSeq (protein)	NP_001004019.1	NP_001074906
Location (UCSC)	Chr 3: 13.57 – 13.68 Mb	Chr 6: 91.16 – 91.22 Mb
PubMed search	[1]	[2]

Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.

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.

Interactions

FBLN2 has been shown to interact with Laminin, alpha 1, Laminin, alpha 5 and Perlecan.

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. 
• 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. doi:10.1083/jcb.123.5.1269. PMC 2119879. PMID 8245130. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2119879. 
• 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. doi:10.1074/jbc.271.32.19489. 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. doi:10.1007/BF02331415. 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. doi:10.1074/jbc.272.5.2814. 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. PMC 1169922. PMID 9214621. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1169922. 
• 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. doi:10.1111/j.1432-1033.1997.t01-1-00039.x. 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. doi:10.1016/S0014-5793(99)01362-9. 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. doi:10.1046/j.1365-2141.2000.02011.x. 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. doi:10.1046/j.1365-2133.2001.04337.x. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.