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Ephrin B1

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
EFNB1
Identifiers
AliasesEFNB1, CFND, CFNS, EFB1, EFL3, EPLG2, Elk-L, LERK2, ephrin B1
External IDsOMIM:300035;MGI:102708;HomoloGene:3263;GeneCards:EFNB1;OMA:EFNB1 - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for EFNB1
Genomic location for EFNB1
BandXq13.1Start68,829,021bp[1]
End68,842,160bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for EFNB1
Genomic location for EFNB1
BandX C3|X 43.22 cMStart98,179,736bp[2]
End98,192,597bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • ventricular zone

  • right lung

  • ganglionic eminence

  • mucosa of transverse colon

  • skin of abdomen

  • skin of leg

  • upper lobe of left lung

  • tibial nerve

  • apex of heart

  • ectocervix
Top expressed in
  • ventricular zone

  • Ileal epithelium

  • external carotid artery

  • lumbar spinal ganglion

  • internal carotid artery

  • Rostral migratory stream

  • renal corpuscle

  • lip

  • yolk sac

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

1947

13641

Ensembl

ENSG00000090776

ENSMUSG00000031217

UniProt

P98172

P52795

RefSeq (mRNA)

NM_004429

NM_010110

RefSeq (protein)

NP_004420

NP_034240

Location (UCSC)Chr X: 68.83 – 68.84 MbChr X: 98.18 – 98.19 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ephrin B1 is aprotein that in humans is encoded by theEFNB1gene.[5][6] It is a member of theephrin family. The encoded protein is atype I membrane protein and a ligand of Eph-relatedreceptor tyrosine kinases. It may play a role incell adhesion and function in the development or maintenance of the nervous system.[7]

Clinical significance

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Mutations in this protein are responsible for most cases ofcraniofrontonasal syndrome.[8][9][10]

Interactions

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EFNB1 has been shown tointeract withSDCBP.[11]

References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000090776Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000031217Ensembl, 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. ^Fletcher FA, Huebner K, Shaffer LG, Fairweather ND, Monaco AP, Muller U, Druck T, Simoneaux DK, Chelly J, Belmont JW, et al. (Jul 1995). "Assignment of the gene (EPLG2) encoding a high-affinity binding protein for the receptor tyrosine kinase Elk to a 200-kilobasepair region in human chromosome Xq12".Genomics.25 (1):334–5.doi:10.1016/0888-7543(95)80156-G.PMID 7774950.
  6. ^Shotelersuk V, Siriwan P, Ausavarat S (Mar 2006). "A novel mutation in EFNB1, probably with a dominant negative effect, underlying craniofrontonasal syndrome".Cleft Palate Craniofac J.43 (2):152–4.doi:10.1597/05-014.1.PMID 16526919.S2CID 10737616.
  7. ^"Entrez Gene: EFNB1 ephrin-B1".
  8. ^Wieland I, Weidner C, Ciccone R, et al. (December 2007). "Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome".Clin. Genet.72 (6):506–16.doi:10.1111/j.1399-0004.2007.00905.x.PMID 17941886.S2CID 33823266.
  9. ^Twigg SR, Kan R, Babbs C, Bochukova EG, Robertson SP, Wall SA, Morriss-Kay GM, Wilkie AO (Jun 2004)."Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome".Proc Natl Acad Sci U S A.101 (23):8652–7.Bibcode:2004PNAS..101.8652T.doi:10.1073/pnas.0402819101.PMC 423250.PMID 15166289.
  10. ^Wieland I, Jakubiczka S, Muschke P, Cohen M, Thiele H, Gerlach KL, Adams RH, Wieacker P (Jun 2004)."Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome".Am J Hum Genet.74 (6):1209–15.doi:10.1086/421532.PMC 1182084.PMID 15124102.
  11. ^Lin, D; Gish G D; Songyang Z; Pawson T (Feb 1999)."The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif".J. Biol. Chem.274 (6):3726–33.doi:10.1074/jbc.274.6.3726.ISSN 0021-9258.PMID 9920925.

Further reading

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External links

[edit]
Intercellular signaling peptides and proteins /ligands
Growth factors
Ephrin
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Angiopoietin
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LNGF (p75NTR)
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GFRα1
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Unsorted
SCF (c-Kit)
TGFβ
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VEGF
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