Fibulin-2 is a protein that in humans is encoded by the FBLN2 gene.[5][6]

FBLN2
Identifiers
AliasesFBLN2, fibulin 2
External IDsOMIM: 135821 MGI: 95488 HomoloGene: 1514 GeneCards: FBLN2
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 MbChr 6: 91.19 – 91.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 edit

FBLN2 has been shown to interact with Laminin, alpha 1,[8][9] Laminin, alpha 5[8] and Perlecan.[10][11]

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163520 - Ensembl, May 2017
  2. ^ a b c 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.
  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.
  6. ^ a b 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.
  8. ^ 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.
  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.
  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.
  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.

Further reading edit