EPH receptor B1

EPH receptor B1
PDB rendering based on 2djs.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 2djs​
Identifiers
Symbols	EPHB1 ; NET; ELK; EPHT2; FLJ37986; Hek6
External IDs	Template:OMIM5 Template:MGI HomoloGene: 20936
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
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

EPH receptor B1, also known as EPHB1, is a human gene.

Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. 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. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.

Further reading

• 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.
• Abrahamson DR, Robert B, Hyink DP; et al. (1998). "Origins and formation of microvasculature in the developing kidney". Kidney Int. Suppl. 67: S7–11. PMID 9736245.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Multiple names: authors list (link)
• Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. PMID 11256076.
• Larose L, Gish G, Shoelson S, Pawson T (1993). "Identification of residues in the beta platelet-derived growth factor receptor that confer specificity for binding to phospholipase C-gamma 1". Oncogene. 8 (9): 2493–9. PMID 7689724.CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Cerretti DP, Vanden Bos T, Nelson N; et al. (1996). "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Mol. Immunol. 32 (16): 1197–205. PMID 8559144.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Tang XX, Biegel JA, Nycum LM; et al. (1996). "cDNA cloning, molecular characterization, and chromosomal localization of NET(EPHT2), a human EPH-related receptor protein-tyrosine kinase gene preferentially expressed in brain". Genomics. 29 (2): 426–37. doi:10.1006/geno.1995.9985. PMID 8666391.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Stein E, Cerretti DP, Daniel TO (1996). "Ligand activation of ELK receptor tyrosine kinase promotes its association with Grb10 and Grb2 in vascular endothelial cells". J. Biol. Chem. 271 (38): 23588–93. PMID 8798570.CS1 maint: Multiple names: authors list (link)
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.CS1 maint: Multiple names: authors list (link)
• Kozlosky CJ, VandenBos T, Park L; et al. (1997). "LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain". Cytokine. 9 (8): 540–9. doi:10.1006/cyto.1997.0199. PMID 9245480.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell. 90 (3): 403–4. 1997. PMID 9267020.
• Stein E, Huynh-Do U, Lane AA; et al. (1998). "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase". J. Biol. Chem. 273 (3): 1303–8. PMID 9430661.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Stein E, Lane AA, Cerretti DP; et al. (1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes Dev. 12 (5): 667–78. PMID 9499402.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)