FBLN2

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

FBLN2
Identifiers
Aliases	FBLN2, fibulin 2
External IDs	OMIM: 135821; MGI: 95488; HomoloGene: 1514; GeneCards: FBLN2; OMA:FBLN2 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) Band 3p25.1 Start 13,549,125 bp End 13,638,422 bp
Gene location (Mouse) Chr. Chromosome 6 (mouse) Band 6 D1|6 40.42 cM Start 91,189,437 bp End 91,249,522 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right auricle of heart right coronary artery subcutaneous adipose tissue abdominal fat left coronary artery apex of heart vena cava saphenous vein pericardium tibial nerve Top expressed in stroma of bone marrow umbilical cord external carotid artery internal carotid artery ankle joint decidua efferent ductule plantaris muscle lactiferous gland endothelial cell of lymphatic vessel More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding extracellular matrix structural constituent extracellular matrix binding extracellular matrix constituent conferring elasticity Cellular component extracellular matrix extracellular vesicle extracellular exosome extracellular space extracellular region collagen-containing extracellular matrix Biological process positive regulation of cell-substrate adhesion extracellular matrix organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2199 14115 Ensembl ENSG00000163520 ENSMUSG00000064080 UniProt P98095 P37889 RefSeq (mRNA) NM_001004019 NM_001165035 NM_001998 NM_001081437 NM_007992 RefSeq (protein) NP_001004019 NP_001158507 NP_001989 NP_001074906 NP_032018 Location (UCSC) Chr 3: 13.55 – 13.64 Mb Chr 6: 91.19 – 91.25 Mb PubMed search
Wikidata
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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.

Its role as a biomarker for meningiomas (a common tumour affecting the central nervous system) was recently described where a blood test can predict whether patients have a grade II meningiomas (poor outcome) and not a grade I meningioma (better outcome), without the need for a surgical biopsy.

Interactions

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

Further reading

• Pan TC, Sasaki T, Zhang RZ, Fässler R, Timpl R, Chu ML (December 1993). "Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding". The Journal of Cell Biology. 123 (5): 1269–1277. doi:10.1083/jcb.123.5.1269. PMC 2119879. PMID 8245130.
• Reinhardt DP, Sasaki T, Dzamba BJ, Keene DR, Chu ML, Göhring W, et al. (August 1996). "Fibrillin-1 and fibulin-2 interact and are colocalized in some tissues". The Journal of Biological Chemistry. 271 (32): 19489–19496. doi:10.1074/jbc.271.32.19489. PMID 8702639.
• Miosge N, Götz W, Sasaki T, Chu ML, Timpl R, Herken R (February 1996). "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo". The Histochemical Journal. 28 (2): 109–116. doi:10.1007/BF02331415. PMID 8737292. S2CID 25996538.
• Collod G, Chu ML, Sasaki T, Coulon M, Timpl R, Renkart L, et al. (1996). "Fibulin-2: genetic mapping and exclusion as a candidate gene in Marfan syndrome type 2". European Journal of Human Genetics. 4 (5): 292–295. doi:10.1159/000472216. PMID 8946175. S2CID 9891855.
• Sasaki T, Mann K, Wiedemann H, Göhring W, Lustig A, Engel J, et al. (June 1997). "Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge". The EMBO Journal. 16 (11): 3035–3043. doi:10.1093/emboj/16.11.3035. PMC 1169922. PMID 9214621.
• Brown JC, Sasaki T, Göhring W, Yamada Y, Timpl R (November 1997). "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". European Journal of Biochemistry. 250 (1): 39–46. doi:10.1111/j.1432-1033.1997.t01-1-00039.x. PMID 9431988.
• Raghunath M, Tschödrich-Rotter M, Sasaki T, Meuli M, Chu ML, Timpl R (January 1999). "Confocal laser scanning analysis of the association of fibulin-2 with fibrillin-1 and fibronectin define different stages of skin regeneration". The Journal of Investigative Dermatology. 112 (1): 97–101. doi:10.1046/j.1523-1747.1999.00483.x. PMID 9886271.
• Kuivaniemi H, Marshall A, Ganguly A, Chu ML, Abbott WM, Tromp G (1998). "Fibulin-2 exhibits high degree of variability, but no structural changes concordant with abdominal aortic aneurysms". European Journal of Human Genetics. 6 (6): 642–646. doi:10.1038/sj.ejhg.5200245. PMID 9887386.
• Sasaki T, Göhring W, Miosge N, Abrams WR, Rosenbloom J, Timpl R (October 1999). "Tropoelastin binding to fibulins, nidogen-2 and other extracellular matrix proteins". FEBS Letters. 460 (2): 280–284. doi:10.1016/S0014-5793(99)01362-9. PMID 10544250. S2CID 25139630.
• 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". British Journal of Haematology. 109 (2): 305–313. doi:10.1046/j.1365-2141.2000.02011.x. PMID 10848816. S2CID 37405859.
• Olin AI, Mörgelin M, Sasaki T, Timpl R, Heinegård D, Aspberg A (January 2001). "The proteoglycans aggrecan and Versican form networks with fibulin-2 through their lectin domain binding". The Journal of Biological Chemistry. 276 (2): 1253–1261. doi:10.1074/jbc.M006783200. PMID 11038354.
• Hunzelmann N, Nischt R, Brenneisen P, Eickert A, Krieg T (August 2001). "Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibres". The British Journal of Dermatology. 145 (2): 217–222. doi:10.1046/j.1365-2133.2001.04337.x. PMID 11531782. S2CID 45863539.
• Sasaki T, Göhring W, Mann K, Brakebusch C, Yamada Y, Fässler R, et al. (December 2001). "Short arm region of laminin-5 gamma2 chain: structure, mechanism of processing and binding to heparin and proteins". Journal of Molecular Biology. 314 (4): 751–763. doi:10.1006/jmbi.2001.5176. PMID 11733994.
• Bengtsson E, Mörgelin M, Sasaki T, Timpl R, Heinegård D, Aspberg A (April 2002). "The leucine-rich repeat protein PRELP binds perlecan and collagens and may function as a basement membrane anchor". The Journal of Biological Chemistry. 277 (17): 15061–15068. doi:10.1074/jbc.M108285200. PMID 11847210.