FBLN2

FBLN2
Identifiers
Aliases	FBLN2 , fibulin 2
External IDs	OMIM: 135821 MGI: 95488 HomoloGene: 1514 GeneCards: FBLN2
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 coronary artery; ; subcutaneous adipose tissue; ; abdominal fat; ; left coronary artery; ; vena cava; ; saphenous vein; ; pericardium; ; tibial nerve; ; stromal cell of endometrium; ; synovial joint;
	Top expressed in
	belly cord; ; external carotid artery; ; internal carotid artery; ; ankle joint; ; plantaris muscle; ; pericardium; ; molar; ; lip; ; basilar part of occipital bone; ; atrium;
	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

Last updated March 04, 2023

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]

Related Research Articles

Nidogen-1 (NID-1), formerly known as entactin, is a protein that in humans is encoded by the NID1 gene. Both nidogen-1 and nidogen-2 are essential components of the basement membrane alongside other components such as type IV collagen, proteoglycans, laminin and fibronectin.

<span class="mw-page-title-main">Laminin</span> Protein in the extracellular matrix

Laminins are a family of glycoproteins of the extracellular matrix of all animals. They are major components of the basal lamina, the protein network foundation for most cells and organs. The laminins are an important and biologically active part of the basal lamina, influencing cell differentiation, migration, and adhesion.

<span class="mw-page-title-main">Endostatin</span>

Endostatin is a naturally occurring, 20-kDa C-terminal fragment derived from type XVIII collagen. It is reported to serve as an anti-angiogenic agent, similar to angiostatin and thrombospondin.

Perlecan (PLC) also known as basement membrane-specific heparan sulfate proteoglycan core protein (HSPG) or heparan sulfate proteoglycan 2 (HSPG2), is a protein that in humans is encoded by the HSPG2 gene. The HSPG2 gene codes for a 4,391 amino acid protein with a molecular weight of 468,829. It is one of the largest known proteins.

Fibulin (FY-beau-lin) is the prototypic member of a multigene family, currently with seven members. Fibulin-1 is a calcium-binding glycoprotein. In vertebrates, fibulin-1 is found in blood and extracellular matrices. In the extracellular matrix, fibulin-1 associates with basement membranes and elastic fibers. The association with these matrix structures is mediated by its ability to interact with numerous extracellular matrix constituents including fibronectin, proteoglycans, laminins and tropoelastin. In blood, fibulin-1 binds to fibrinogen and incorporates into clots.

FBLN1 is the gene encoding fibulin-1, an extracellular matrix and plasma protein.

Tenascin C (TN-C) is a glycoprotein that in humans is encoded by the TNC gene. It is expressed in the extracellular matrix of various tissues during development, disease or injury, and in restricted neurogenic areas of the central nervous system. Tenascin-C is the founding member of the tenascin protein family. In the embryo it is made by migrating cells like the neural crest; it is also abundant in developing tendons, bone and cartilage.

Collagen alpha-1(XVIII) chain is a protein that in humans is encoded by the COL18A1 gene.

Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene.

Laminin subunit alpha-3 is a protein that in humans is encoded by the LAMA3 gene.

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

Laminin subunit gamma-1 is a protein that in humans is encoded by the LAMC1 gene.

Laminin subunit beta-1 is a protein that in humans is encoded by the LAMB1 gene.

Laminin subunit alpha-2 is a protein that in humans is encoded by the LAMA2 gene.

Collagen alpha-6(IV) chain is a protein that in humans is encoded by the COL4A6 gene.

EGF-containing fibulin-like extracellular matrix protein 1 is a protein that in humans is encoded by the EFEMP1 gene.

EGF-containing fibulin-like extracellular matrix protein 2 is a protein that in humans is encoded by the EFEMP2 gene.

Collagen alpha-1(XIII) chain is a protein that in humans is encoded by the COL13A1 gene.

Prolargin is a protein that in humans is encoded by the PRELP gene.

Nidogen-2, also known as osteonidogen, is a basal lamina protein of the nidogen family. It was the second nidogen to be described after nidogen-1 (entactin). Both play key roles during late embryonic development. In humans it is encoded by the NID2 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000163520 - Ensembl, May 2017
1 2 3 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.
1 2 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.
1 2 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.

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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000163520 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000064080 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7806230-5] 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.

[entrez-6] 1 2 EntrezGene 2199 "FBLN2 fibulin 2 [ Homo sapiens (human) ]"

[7] 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.

[pmid9006922-8] 1 2 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.

[pmid10934193-9] 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.

[pmid11493006-10] 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.

[pmid7500359-11] 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.

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FBLN2

Contents

Interactions

Related Research Articles

References

Further reading