Ephrin B2

Ephrin-B2 is a protein that in humans is encoded by the EFNB2 gene.

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	OMIM: 600527; MGI: 105097; HomoloGene: 3019; GeneCards: EFNB2; OMA:EFNB2 - orthologs
Gene location (Human) Chr. Chromosome 13 (human) Band 13q33.3 Start 106,489,745 bp End 106,535,662 bp
Gene location (Mouse) Chr. Chromosome 8 (mouse) Band 8 A1.1|8 3.42 cM Start 8,667,434 bp End 8,711,242 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence mucosa of sigmoid colon visceral pleura amniotic fluid parietal pleura periodontal fiber secondary oocyte nipple hair follicle Top expressed in lumbar spinal ganglion medullary collecting duct renal corpuscle hair follicle Rostral migratory stream right lung left lung ganglionic eminence vas deferens vestibular membrane of cochlear duct More reference expression data BioGPS More reference expression data
Gene ontology Molecular function virus receptor activity protein binding signaling receptor binding ephrin receptor binding protein tyrosine kinase activity Cellular component integral component of membrane membrane focal adhesion plasma membrane integral component of plasma membrane Schaffer collateral - CA1 synapse glutamatergic synapse integral component of presynaptic membrane integral component of postsynaptic density membrane Biological process cell differentiation blood vessel morphogenesis negative regulation of keratinocyte proliferation regulation of chemotaxis 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 positive regulation of cell population proliferation ephrin receptor signaling pathway axon guidance negative regulation of neuron projection development peptidyl-tyrosine phosphorylation presynapse assembly regulation of postsynaptic membrane neurotransmitter receptor levels regulation of postsynaptic neurotransmitter receptor internalization positive regulation of neuron death Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1948 13642 Ensembl ENSG00000125266 ENSMUSG00000001300 UniProt P52799 P52800 RefSeq (mRNA) NM_004093 NM_001372056 NM_001372057 NM_001372058 NM_010111 NM_001368299 RefSeq (protein) NP_004084 NP_001358985 NP_001358986 NP_001358987 NP_034241 NP_001355228 Location (UCSC) Chr 13: 106.49 – 106.54 Mb Chr 8: 8.67 – 8.71 Mb PubMed search
Wikidata
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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.

Cancer

EFNB2 gene has been observed progressively downregulated in Human papillomavirus-positive neoplastic keratinocytes derived from uterine cervical preneoplastic lesions at different levels of malignancy. For this reason, EFNB2 is likely to be associated with tumorigenesis and may be a potential prognostic marker for uterine cervical preneoplastic lesions progression.

Interactions

EFNB2 has been shown to interact with EPHA3 and EPHB1 in optic chiasm development.

EFNB2 has also been shown to serve as a receptor for Hendra Virus and Nipah Virus, mediating entry into the cell during infection.

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. doi:10.1242/dev.126.10.2033. PMID 10207129.
• Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly". 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 (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. S2CID 205014301.
• 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. Bibcode:1995PNAS...92.1866B. 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. Bibcode:1996Natur.383..722H. doi:10.1038/383722a0. hdl:1807/9444. PMID 8878483. S2CID 4349898.
• 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. doi:10.1242/jcs.111.18.2741. 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.