Protein-coding gene in the species Homo sapiens
| FBLN2 |
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| Identifiers |
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| Aliases | FBLN2, fibulin 2 |
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| External IDs | OMIM: 135821; MGI: 95488; HomoloGene: 1514; GeneCards: FBLN2; OMA:FBLN2 - orthologs |
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| Gene location (Human) |
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 | | Chr. | Chromosome 3 (human)[1] |
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| | Band | 3p25.1 | Start | 13,549,125 bp[1] |
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| End | 13,638,422 bp[1] |
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| Gene location (Mouse) |
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 | | Chr. | Chromosome 6 (mouse)[2] |
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| | Band | 6 D1|6 40.42 cM | Start | 91,189,437 bp[2] |
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| End | 91,249,522 bp[2] |
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| RNA expression pattern |
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| Bgee | | Human | Mouse (ortholog) |
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| Top expressed in | - right auricle
- right coronary artery
- subcutaneous adipose tissue
- abdominal fat
- left coronary artery
- apex of heart
- vena cava
- saphenous vein
- pericardium
- tibial nerve
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| | Top expressed in | - stroma of bone marrow
- belly cord
- external carotid artery
- internal carotid artery
- ankle joint
- decidua
- efferent ductule
- plantaris muscle
- lactiferous gland
- endothelial cell of lymphatic vessel
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| | More reference expression data |
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| BioGPS |  | | More reference expression data |
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| Gene ontology |
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| 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 |
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| Orthologs |
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| Species | Human | Mouse |
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| Entrez | | |
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| Ensembl | | |
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| UniProt | | |
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| RefSeq (mRNA) | |
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NM_001004019
NM_001165035
NM_001998 |
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| RefSeq (protein) | |
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NP_001004019
NP_001158507
NP_001989 |
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| Location (UCSC) | Chr 3: 13.55 – 13.64 Mb | Chr 6: 91.19 – 91.25 Mb |
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| PubMed search | [3] | [4] |
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| Wikidata |
| View/Edit Human | View/Edit Mouse |
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Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.[5][6]
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.[6]
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.[7]
Interactions
FBLN2 has been shown to interact with Laminin, alpha 1,[8][9] Laminin, alpha 5[8] and Perlecan.[10][11]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000163520 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000064080 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Zhang RZ, Pan TC, Zhang ZY, Mattei MG, Timpl R, Chu ML (January 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.
- ^ a b EntrezGene 2199 "FBLN2 fibulin 2 [ Homo sapiens (human) ]"
- ^ Sofela, Agbolahan A.; Hilton, David A.; Ammoun, Sylwia; Baiz, Daniele; Adams, Claire L.; Ercolano, Emanuela; Jenkinson, Michael D.; Kurian, Kathreena M.; Teo, Mario; Whitfield, Peter C.; Sahm, Felix; Hanemann, C. Oliver (8 January 2021). "Fibulin-2: A Novel Biomarker for Differentiating Grade II from Grade I Meningiomas". International Journal of Molecular Sciences. 22 (2): 560. doi:10.3390/ijms22020560. PMC 7827565. PMID 33429944.
- ^ a b Utani, A; Nomizu M; Yamada Y (January 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.
- ^ Talts, J F; Sasaki T; Miosge N; Göhring W; Mann K; Mayne R; Timpl R (November 2000). "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.
- ^ Hopf, M; Göhring W; Mann K; Timpl R (August 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.
- ^ Sasaki, T; Göhring W; Pan T C; Chu M L; Timpl R (December 1995). "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.
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.
- 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. S2CID 25996538.
- Collod G, Chu ML, Sasaki T, et al. (1997). "Fibulin-2: genetic mapping and exclusion as a candidate gene in Marfan syndrome type 2" (PDF). Eur. J. Hum. Genet. 4 (5): 292–5. doi:10.1159/000472216. PMID 8946175. S2CID 9891855.
- 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.
- 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. 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". Br. J. Haematol. 109 (2): 305–13. doi:10.1046/j.1365-2141.2000.02011.x. PMID 10848816. S2CID 37405859.
- 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. S2CID 45863539.
- 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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