EPH receptor B1

EPHB1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2DJS, 2EAO, 3ZFX
Identifiers
Aliases	EPHB1 , Ephb1, 9330129L11, AW488255, C130099E04Rik, Cek6, ENSMUSG00000074119, Elk, Elkh, Hek6, Net, EPHT2, EPH receptor B1, ELK, NET
External IDs	OMIM: 600600; MGI: 1096337; HomoloGene: 20936; GeneCards: EPHB1; OMA:EPHB1 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3q22.2 Start 134,795,260 bp [1] End 135,260,467 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 F1 Start 101,799,327 bp [2] End 102,231,892 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell ganglionic eminence Brodmann area 23 secondary oocyte cerebellum cerebellar cortex ventricular zone cerebellar hemisphere primary visual cortex right hemisphere of cerebellum Top expressed in otic vesicle lumbar subsegment of spinal cord otolith organ utricle inferior colliculi substantia nigra deep cerebellar nuclei superior colliculus Rostral migratory stream medial ganglionic eminence More reference expression data BioGPS n/a
Gene ontology Molecular function transferase activity nucleotide binding protein kinase activity kinase activity protein binding transmembrane receptor protein tyrosine kinase activity protein tyrosine kinase activity ATP binding ephrin receptor activity axon guidance receptor activity transmembrane-ephrin receptor activity protein-containing complex binding Cellular component integral component of membrane endosome cell projection early endosome membrane membrane integral component of plasma membrane extracellular region dendrite extracellular exosome endoplasmic reticulum cytosol plasma membrane axon cytoplasm filopodium tip membrane raft neuron projection receptor complex glutamatergic synapse Biological process phosphorylation transmembrane receptor protein tyrosine kinase signaling pathway nervous system development dendritic spine development cell-substrate adhesion regulation of JNK cascade protein phosphorylation cell adhesion regulation of neuron death regulation of ERK1 and ERK2 cascade protein autophosphorylation peptidyl-tyrosine phosphorylation immunological synapse formation axon guidance optic nerve morphogenesis central nervous system projection neuron axonogenesis retinal ganglion cell axon guidance ephrin receptor signaling pathway camera-type eye morphogenesis positive regulation of synapse assembly dendritic spine morphogenesis angiogenesis skeletal muscle satellite cell activation cranial nerve development neurogenesis establishment of cell polarity detection of temperature stimulus involved in sensory perception of pain cell chemotaxis neural precursor cell proliferation negative regulation of skeletal muscle satellite cell proliferation negative regulation of satellite cell differentiation modulation of chemical synaptic transmission Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2047 270190 Ensembl ENSG00000154928 ENSMUSG00000032537 UniProt P54762 Q8CBF3 RefSeq (mRNA) NM_004441 NM_001168296 NM_173447 RefSeq (protein) NP_004432 NP_001161768 NP_775623 Location (UCSC) Chr 3: 134.8 – 135.26 Mb Chr 9: 101.8 – 102.23 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ephrin type-B receptor 1 is a protein that in humans is encoded by the EPHB1 gene. ^{[5] [6]}

Function

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. ^[6]

Interactions

EPH receptor B1 has been shown to interact with:

• ACP1 ^[7]
• GRB7 ^[8] and
• NCK1 ^[9]
• Ephrin-B2 ^[10]

References

1. GRCh38: Ensembl release 89: ENSG00000154928 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000032537 – 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. Tang XX, Biegel JA, Nycum LM, Yoshioka A, Brodeur GM, Pleasure DE, Ikegaki N (1995). "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.
6. "Entrez Gene: EPHB1 EPH receptor B1".
7. Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (Mar 1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes Dev. 12 (5): 667–78. doi:10.1101/gad.12.5.667. PMC   316584 . PMID   9499402.
8. Han DC, Shen TL, Miao H, Wang B, Guan JL (Nov 2002). "EphB1 associates with Grb7 and regulates cell migration". J. Biol. Chem. 277 (47): 45655–61. doi: 10.1074/jbc.M203165200 . PMID   12223469.
9. Stein E, Huynh-Do U, Lane AA, Cerretti DP, Daniel TO (Jan 1998). "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase". J. Biol. Chem. 273 (3): 1303–8. doi: 10.1074/jbc.273.3.1303 . PMID   9430661.
10. Williams, SE; Mann, F; Erskine, L (2003). "Ephrin-B2 and EphB1 mediate retinal axon divergence at the optic chiasm". Neuron. 39 (6): 919–935. doi: 10.1016/j.neuron.2003.08.017 . PMID   12971893. S2CID   18565204.

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. doi:10.1016/S0163-7258(97)00112-5. PMID   9576626.
• Abrahamson DR, Robert B, Hyink DP, St John PL, Daniel TO (1998). "Origins and formation of microvasculature in the developing kidney". Kidney Int. Suppl. 67: S7-11. doi: 10.1046/j.1523-1755.1998.06702.x . PMID   9736245.
• Holder N, Klein R (1999). "Eph receptors and ephrins: effectors of morphogenesis". Development. 126 (10): 2033–44. doi:10.1242/dev.126.10.2033. PMID   10207129.
• Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly". Int. Rev. Cytol. International Review of Cytology. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN   9780123646002. PMID   10730216.
• Xu Q, Mellitzer G, Wilkinson DG (2000). "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. PMC   1692797 . PMID   11128993.
• Wilkinson DG (2001). "Multiple roles of EPH receptors and ephrins in neural development". Nat. Rev. Neurosci. 2 (3): 155–64. doi:10.1038/35058515. PMID   11256076. S2CID   205014301.
• 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.
• Davis S, Gale NW, Aldrich TH, Maisonpierre PC, Lhotak V, Pawson T, Goldfarb M, Yancopoulos GD (1994). "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity". Science. 266 (5186): 816–9. Bibcode:1994Sci...266..816D. doi:10.1126/science.7973638. PMID   7973638.
• Beckmann MP, Cerretti DP, Baum P, Vanden Bos T, James L, Farrah T, Kozlosky C, Hollingsworth T, Shilling H, Maraskovsky E (1994). "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors". EMBO J. 13 (16): 3757–62. doi:10.1002/j.1460-2075.1994.tb06685.x. PMC   395287 . PMID   8070404.
• Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ (1995). "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Mol. Immunol. 32 (16): 1197–205. doi:10.1016/0161-5890(95)00108-5. PMID   8559144.
• Gale NW, Holland SJ, Valenzuela DM, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H, Wilkinson DG, Pawson T, Davis S, Yancopoulos GD (1996). "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis". Neuron. 17 (1): 9–19. doi: 10.1016/S0896-6273(00)80276-7 . PMID   8755474. S2CID   1075856.
• 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. doi: 10.1074/jbc.271.38.23588 . PMID   8798570.
• Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi: 10.1101/gr.6.9.791 . PMID   8889548.
• Kozlosky CJ, VandenBos T, Park L, Cerretti DP, Carpenter MK (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.
• Ephnomenclaturecommittee (1997). "Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee". Cell. 90 (3): 403–4. doi: 10.1016/S0092-8674(00)80500-0 . PMID   9267020. S2CID   26773768.
• Stein E, Huynh-Do U, Lane AA, Cerretti DP, Daniel TO (1998). "Nck recruitment to Eph receptor, EphB1/ELK, couples ligand activation to c-Jun kinase". J. Biol. Chem. 273 (3): 1303–8. doi: 10.1074/jbc.273.3.1303 . PMID   9430661.
• Stein E, Lane AA, Cerretti DP, Schoecklmann HO, Schroff AD, Van Etten RL, Daniel TO (1998). "Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses". Genes Dev. 12 (5): 667–78. doi:10.1101/gad.12.5.667. PMC   316584 . PMID   9499402.