Ephrin A1

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Ephrin-A1
Identifiers
Symbols EFNA1 ; B61; ECKLG; EFL1; EPLG1; LERK1; TNFAIP4
External IDs Template:OMIM5 Template:MGI HomoloGene3262
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Ephrin-A1, also known as EFNA1, is a human gene.[1]

This gene encodes a member of the ephrin (EPH) family. The ephrins and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. This gene encodes an EFNA class ephrin which binds to the EPHA2, EPHA4, EPHA5, EPHA6, and EPHA7 receptors. Two transcript variants that encode different isoforms were identified through sequence analysis.[1]

References

  1. 1.0 1.1 "Entrez Gene: EFNA1 ephrin-A1".

Further reading

  • Pandey A, Lindberg RA, Dixit VM (1996). "Cell signalling. Receptor orphans find a family". Curr. Biol. 5 (9): 986–9. PMID 8542290.
  • Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development". Annu. Rev. Neurosci. 21: 309–45. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499.
  • Zhou R (1998). "The Eph family receptors and ligands". Pharmacol. Ther. 77 (3): 151–81. PMID 9576626.
  • Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis". Development. 126 (10): 2033–44. PMID 10207129.
  • Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly". Int. Rev. Cytol. 196: 177–244. PMID 10730216.
  • Xu Q, Mellitzer G, Wilkinson DG (2001). "Roles of Eph receptors and ephrins in segmental patterning". Philos. Trans. R. Soc. Lond., B, Biol. Sci. 355 (1399): 993–1002. doi:10.1098/rstb.2000.0635. PMID 11128993.
  • Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. PMID 11256076.
  • Holzman LB, Marks RM, Dixit VM (1990). "A novel immediate-early response gene of endothelium is induced by cytokines and encodes a secreted protein". Mol. Cell. Biol. 10 (11): 5830–8. PMID 2233719.
  • Mahadevan D, Thanki N, Singh J; et al. (1995). "Structural studies on the PH domains of Db1, Sos1, IRS-1, and beta ARK1 and their differential binding to G beta gamma subunits". Biochemistry. 34 (28): 9111–7. PMID 7619809.
  • Kozlosky CJ, Maraskovsky E, McGrew JT; et al. (1995). "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins". Oncogene. 10 (2): 299–306. PMID 7838529.
  • Davis S, Gale NW, Aldrich TH; et al. (1994). "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science. 266 (5186): 816–9. PMID 7973638.
  • Beckmann MP, Cerretti DP, Baum P; et al. (1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors". EMBO J. 13 (16): 3757–62. PMID 8070404.
  • Cerretti DP, Lyman SD, Kozlosky CJ; et al. (1997). "The genes encoding the eph-related receptor tyrosine kinase ligands LERK-1 (EPLG1, Epl1), LERK-3 (EPLG3, Epl3), and LERK-4 (EPLG4, Epl4) are clustered on human chromosome 1 and mouse chromosome 3". Genomics. 33 (2): 277–82. doi:10.1006/geno.1996.0192. PMID 8660976.
  • Gale NW, Holland SJ, Valenzuela DM; et al. (1996). "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron. 17 (1): 9–19. PMID 8755474.
  • "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell. 90 (3): 403–4. 1997. PMID 9267020.
  • Nagel W, Schilcher P, Zeitlmann L, Kolanus W (1998). "The PH domain and the polybasic c domain of cytohesin-1 cooperate specifically in plasma membrane association and cellular function". Mol. Biol. Cell. 9 (8): 1981–94. PMID 9693361.

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