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FBLN1

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens

FBLN1
Identifiers
AliasesFBLN1, FBLN, FIBL1, fibulin 1
External IDsOMIM:135820;MGI:95487;HomoloGene:21295;GeneCards:FBLN1;OMA:FBLN1 - orthologs
Gene location (Human)
Chromosome 22 (human)
Chr.Chromosome 22 (human)[1]
Chromosome 22 (human)
Genomic location for FBLN1
Genomic location for FBLN1
Band22q13.31Start45,502,238bp[1]
End45,601,135bp[1]
Gene location (Mouse)
Chromosome 15 (mouse)
Chr.Chromosome 15 (mouse)[2]
Chromosome 15 (mouse)
Genomic location for FBLN1
Genomic location for FBLN1
Band15|15 E2Start85,090,150bp[2]
End85,170,736bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • canal of the cervix

  • gallbladder

  • vena cava

  • pericardium

  • gastric mucosa

  • ectocervix

  • vagina

  • left uterine tube

  • right auricle

  • tendon of biceps brachii
Top expressed in
  • aortic valve

  • otic vesicle

  • ascending aorta

  • otic placode

  • ciliary body

  • external carotid artery

  • saccule

  • mandibular prominence

  • internal carotid artery

  • maxillary prominence
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2192

14114

Ensembl

ENSG00000077942

ENSMUSG00000006369

UniProt

P23142

Q08879

RefSeq (mRNA)

NM_006487
NM_001996
NM_006485
NM_006486

NM_010180
NM_001347088

RefSeq (protein)

NP_001987
NP_006476
NP_006477
NP_006478

NP_001334017
NP_034310

Location (UCSC)Chr 22: 45.5 – 45.6 MbChr 15: 85.09 – 85.17 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

FBLN1 is the gene encodingfibulin-1, an extracellular matrix and plasma protein.[5][6][7]

Function

[edit]

Fibulin-1 is a secretedglycoprotein that is found in association withextracellular matrix structures includingfibronectin-containing fibers,elastin-containing fibers andbasement membranes. Fibulin-1 binds to a number of extracellular matrix constituents includingfibronectin,[7]nidogen-1, and theproteoglycan,versican.[7][8] Fibulin-1 is also a blood protein capable of binding tofibrinogen.[9]

Structure

[edit]

Fibulin-1 has modular domain structure and includes a series of nineepidermal growth factor-like modules followed by afibulin-type module, a module found in all members of the fibulin gene family.[6]

The human fibulin-1 gene, FBLN1, encodes foursplice variants designated fibulin-1A, B, C and D, which differ in theircarboxy terminal regions. In mouse, chicken and the nematode,C. elegans, only two fibulin-1 variants are produced, fibulin-1C and fibulin-1D.[5]

Interactions

[edit]

FBLN1 has been shown tointeract with:

See also

[edit]

References

[edit]
  1. ^abcGRCh38: Ensembl release 89: ENSG00000077942Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000006369Ensembl, 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. ^ab"Entrez Gene: FBLN1 fibulin 1".
  6. ^abArgraves WS, Tran H, Burgess WH, Dickerson K (Dec 1990)."Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure".The Journal of Cell Biology.111 (6 Pt 2):3155–64.doi:10.1083/jcb.111.6.3155.PMC 2116371.PMID 2269669.
  7. ^abcBalbona K, Tran H, Godyna S, Ingham KC, Strickland DK, Argraves WS (Oct 1992)."Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin".The Journal of Biological Chemistry.267 (28):20120–5.doi:10.1016/S0021-9258(19)88674-X.PMID 1400330.
  8. ^Timpl R, Sasaki T, Kostka G, Chu ML (Jun 2003). "Fibulins: a versatile family of extracellular matrix proteins".Nature Reviews Molecular Cell Biology.4 (6):479–89.doi:10.1038/nrm1130.PMID 12778127.S2CID 8442153.
  9. ^abArgraves WS, Tanaka A, Smith EP, Twal WO, Argraves KM, Fan D, Haudenschild CC (Nov 2009). "Fibulin-1 and fibrinogen in human atherosclerotic lesions".Histochemistry and Cell Biology.132 (5):559–65.doi:10.1007/s00418-009-0628-7.PMID 19693531.S2CID 13501440.
  10. ^Perbal B, Martinerie C, Sainson R, Werner M, He B, Roizman B (Feb 1999)."The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling".Proceedings of the National Academy of Sciences of the United States of America.96 (3):869–74.Bibcode:1999PNAS...96..869P.doi:10.1073/pnas.96.3.869.PMC 15317.PMID 9927660.
  11. ^Ohsawa I, Takamura C, Kohsaka S (Mar 2001). "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function".Journal of Neurochemistry.76 (5):1411–20.doi:10.1046/j.1471-4159.2001.00144.x.PMID 11238726.S2CID 83321033.
  12. ^Adam S, Göhring W, Wiedemann H, Chu ML, Timpl R, Kostka G (Sep 1997). "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules".Journal of Molecular Biology.272 (2):226–36.doi:10.1006/jmbi.1997.1244.PMID 9299350.
  13. ^Tran H, VanDusen WJ, Argraves WS (Sep 1997)."The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains".The Journal of Biological Chemistry.272 (36):22600–6.doi:10.1074/jbc.272.36.22600.PMID 9278415.
  14. ^Pan TC, Kluge M, Zhang RZ, Mayer U, Timpl R, Chu ML (Aug 1993)."Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands".European Journal of Biochemistry.215 (3):733–40.doi:10.1111/j.1432-1033.1993.tb18086.x.PMID 8354280.
  15. ^Deeney JT, Tornheim K, Korchak HM, Prentki M, Corkey BE (Oct 1992)."Acyl-CoA esters modulate intracellular Ca2+ handling by permeabilized clonal pancreatic beta-cells".The Journal of Biological Chemistry.267 (28):19840–5.doi:10.1016/S0021-9258(19)88631-3.PMID 1400300.

Further reading

[edit]
Cell membrane
Adhesion molecules
Calcium channels
Calcium pumps
GPCRs
Annexins
Intracellularsignaling
Second messengers
Intracellular channels
Intracellular pumps
Sensors andchelators
Calcium-dependentchaperones
Calcium-dependentkinases
Calcium-dependentproteases
Indirect regulators
Extracellularchelators
Extracellular matrix proteins
Secreted hormones
Calcium-bindingdomains
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