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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)
End	13,638,422 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	91,249,522 bp
RNA expression pattern
	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;
	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
	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
	2199
	14115
	ENSG00000163520
	ENSMUSG00000064080
	P98095
	P37889
	NM_001004019; NM_001165035; NM_001998
	NM_001081437; NM_007992
	NP_001004019; NP_001158507; NP_001989
	NP_001074906; NP_032018
	Wikidata
View/Edit Human	View/Edit Mouse

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.