FBLN2

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
Gene location (Human)
Chr.Chromosome 3 (human)[1]
Band3p25.1Start13,549,125 bp[1]
End13,638,422 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 6: 91.21 – 91.27 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]

Interactions

FBLN2 has been shown to interact with Laminin, alpha 1,[7][8] Laminin, alpha 5[7] and Perlecan.[9][10]

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References

  1. GRCh38: Ensembl release 89: ENSG00000163520 - Ensembl, May 2017
  2. 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. "Entrez Gene: FBLN2 fibulin 2".
  7. 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. ISSN 0021-9258. PMID 9006922.
  8. 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. ISSN 0021-9258. PMID 10934193.
  9. 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. ISSN 0022-2836. PMID 11493006.
  10. 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. ISSN 0022-2836. PMID 7500359.

Further reading


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