Ephrin B2

EFNB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2HLE, 2I85, 2VSK, 2VSM, 2WO2, 3GXU, 4UF7
Identifiers
Aliases	EFNB2, EPLG5, HTKL, Htk-L, LERK5, ephrin B2
External IDs	MGI: 105097 HomoloGene: 3019 GeneCards: EFNB2
Gene ontology Molecular function • virus receptor activity • ephrin receptor binding • protein binding • receptor binding Cellular component • integral component of membrane • membrane • focal adhesion • plasma membrane • integral component of plasma membrane Biological process • cell differentiation • blood vessel morphogenesis • negative regulation of keratinocyte proliferation • regulation of chemotaxis • ephrin receptor signaling pathway • cell-cell signaling • anatomical structure morphogenesis • T cell costimulation • lymph vessel development • nervous system development • cell migration involved in sprouting angiogenesis • multicellular organism development • cell adhesion • nephric duct morphogenesis • angiogenesis • animal organ morphogenesis • viral entry into host cell • positive regulation of cardiac muscle cell differentiation • viral process • venous blood vessel morphogenesis • positive regulation of aorta morphogenesis • axon guidance Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	1948	13642
Ensembl	ENSG00000125266	ENSMUSG00000001300
UniProt	P52799	P52800
RefSeq (mRNA)	NM_004093	NM_010111
RefSeq (protein)	NP_004084.1	NP_034241.2
Location (UCSC)	Chr 13: 106.49 – 106.54 Mb	Chr 8: 8.62 – 8.66 Mb
PubMed search	[1]	[2]
Wikidata

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Ephrin-B2 is a protein that in humans is encoded by the EFNB2 gene.^[3]

Function

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 EFNB class ephrin which binds to the EPHB4 and EPHA3 receptors.^[4]

Interactions

EFNB2 has been shown to interact with EPHA3.^[5][6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Bonaldo MF, Yu MT, Jelenc P, Brown S, Su L, Lawton L, Deaven L, Efstratiadis A, Warburton D, Soares MB (Sep 1994). "Selection of cDNAs using chromosome-specific genomic clones: application to human chromosome 13". Human Molecular Genetics. 3 (9): 1663–73. doi:10.1093/hmg/3.9.1663. PMID 7833926.
4. "Entrez Gene: EFNB2 ephrin-B2".
5. Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ (Nov 1995). "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Molecular Immunology. 32 (16): 1197–205. doi:10.1016/0161-5890(95)00108-5. PMID 8559144.
6. Lackmann M, Mann RJ, Kravets L, Smith FM, Bucci TA, Maxwell KF, Howlett GJ, Olsson JE, Vanden Bos T, Cerretti DP, Boyd AW (Jun 1997). "Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor". The Journal of Biological Chemistry. 272 (26): 16521–30. doi:10.1074/jbc.272.26.16521. PMID 9195962.

Further reading

• Flanagan JG, Vanderhaeghen P (1998). "The ephrins and Eph receptors in neural development". Annual Review of Neuroscience. 21: 309–45. doi:10.1146/annurev.neuro.21.1.309. PMID 9530499.
• Zhou R (Mar 1998). "The Eph family receptors and ligands". Pharmacology & Therapeutics. 77 (3): 151–81. doi:10.1016/S0163-7258(97)00112-5. PMID 9576626.
• Holder N, Klein R (May 1999). "Eph receptors and ephrins: effectors of morphogenesis". Development. 126 (10): 2033–44. PMID 10207129.
• Wilkinson, David G. (2000). "Eph receptors and ephrins: Regulators of guidance and assembly". Int. Rev. Cytol. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. ISSN 0074-7696. PMID 10730216.
• Xu Q, Mellitzer G, Wilkinson DG (Jul 2000). "Roles of Eph receptors and ephrins in segmental patterning". Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 355 (1399): 993–1002. doi:10.1098/rstb.2000.0635. PMC 1692797. PMID 11128993.
• Wilkinson DG (Mar 2001). "Multiple roles of EPH receptors and ephrins in neural development". Nature Reviews. Neuroscience. 2 (3): 155–64. doi:10.1038/35058515. PMID 11256076.
• Bennett BD, Zeigler FC, Gu Q, Fendly B, Goddard AD, Gillett N, Matthews W (Mar 1995). "Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk". Proceedings of the National Academy of Sciences of the United States of America. 92 (6): 1866–70. doi:10.1073/pnas.92.6.1866. PMC 42383. PMID 7534404.
• Cerretti DP, Vanden Bos T, Nelson N, Kozlosky CJ, Reddy P, Maraskovsky E, Park LS, Lyman SD, Copeland NG, Gilbert DJ (Nov 1995). "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Molecular Immunology. 32 (16): 1197–205. doi:10.1016/0161-5890(95)00108-5. PMID 8559144.
• Cerretti DP, Lyman SD, Kozlosky CJ, Copeland NG, Gilbert DJ, Jenkins NA, Valentine V, Kirstein MN, Shapiro DN, Morris SW (Apr 1996). "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, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H, Wilkinson DG, Pawson T, Davis S, Yancopoulos GD (Jul 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.
• Holland SJ, Gale NW, Mbamalu G, Yancopoulos GD, Henkemeyer M, Pawson T (Oct 1996). "Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands". Nature. 383 (6602): 722–5. doi:10.1038/383722a0. PMID 8878483.
• Ephnomenclaturecommittee (Aug 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.
• Vogt T, Stolz W, Welsh J, Jung B, Kerbel RS, Kobayashi H, Landthaler M, McClelland M (Mar 1998). "Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased tumorigenicity and metastatic potential in human malignant melanomas". Clinical Cancer Research. 4 (3): 791–7. PMID 9533549.
• Wang HU, Chen ZF, Anderson DJ (May 1998). "Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4". Cell. 93 (5): 741–53. doi:10.1016/S0092-8674(00)81436-1. PMID 9630219.
• Nikolova Z, Djonov V, Zuercher G, Andres AC, Ziemiecki A (Sep 1998). "Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis". Journal of Cell Science. 111 (18): 2741–51. PMID 9718367.
• Torres R, Firestein BL, Dong H, Staudinger J, Olson EN, Huganir RL, Bredt DS, Gale NW, Yancopoulos GD (Dec 1998). "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands". Neuron. 21 (6): 1453–63. doi:10.1016/S0896-6273(00)80663-7. PMID 9883737.
• Lin D, Gish GD, Songyang Z, Pawson T (Feb 1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". The Journal of Biological Chemistry. 274 (6): 3726–33. doi:10.1074/jbc.274.6.3726. PMID 9920925.