EFNB2

Ephrin-B2

PDB rendering based on 1iko.

Available structures
PDB	2HLE, 2I85, 2VSK, 2VSM, 2WO2, 3GXU

Identifiers

Symbols

EFNB2; EPLG5; HTKL; Htk-L; LERK5; MGC126226; MGC126227; MGC126228

External IDs

OMIM: 600527 MGI: 105097 HomoloGene: 3019 GeneCards: EFNB2 Gene

Gene Ontology
Molecular function	• ephrin receptor binding
Cellular component	• plasma membrane • integral to plasma membrane
Biological process	• lymph vessel development • Notch signaling pathway • cell-cell signaling • multicellular organismal development • nervous system development • anatomical structure morphogenesis • organ morphogenesis • cell differentiation • interspecies interaction between organisms
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 13:
107.14 – 107.19 Mb

Chr 8:
8.62 – 8.66 Mb

PubMed search

[1]

[2]

Ephrin-B2 is a protein that in humans is encoded by the EFNB2 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 EFNB class ephrin which binds to the EPHB4 and EPHA3 receptors.^[2]

Interactions

EFNB2 has been shown to interact with EPHA3.^[3]^[4]

References

^ Bonaldo MF, Yu MT, Jelenc P, Brown S, Su L, Lawton L, Deaven L, Efstratiadis A, Warburton D, Soares MB (Feb 1995). "Selection of cDNAs using chromosome-specific genomic clones: application to human chromosome 13". Hum Mol Genet 3 (9): 1663–73. doi:10.1093/hmg/3.9.1663. PMID 7833926.
^ "Entrez Gene: EFNB2 ephrin-B2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1948.
^ Cerretti, D P; Vanden Bos T, Nelson N, Kozlosky C J, Reddy P, Maraskovsky E, Park L S, Lyman S D, Copeland N G, Gilbert D J (Nov. 1995). "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine kinases". Mol. Immunol. (ENGLAND) 32 (16): 1197–205. doi:10.1016/0161-5890(95)00108-5. ISSN 0161-5890. PMID 8559144.
^ Lackmann, M; Mann R J, Kravets L, Smith F M, Bucci T A, Maxwell K F, Howlett G J, Olsson J E, Vanden Bos T, Cerretti D P, Boyd A W (Jun. 1997). "Ligand for EPH-related kinase (LERK) 7 is the preferred high affinity ligand for the HEK receptor". J. Biol. Chem. (UNITED STATES) 272 (26): 16521–30. doi:10.1074/jbc.272.26.16521. ISSN 0021-9258. PMID 9195962.

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.
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. "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 (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. PMC 1692797. PMID 11128993. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1692797.
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.
Bennett BD, Zeigler FC, Gu Q, et al. (1995). "Molecular cloning of a ligand for the EPH-related receptor protein-tyrosine kinase Htk". Proc. Natl. Acad. Sci. U.S.A. 92 (6): 1866–70. doi:10.1073/pnas.92.6.1866. PMC 42383. PMID 7534404. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=42383.
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. doi:10.1016/0161-5890(95)00108-5. PMID 8559144.
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. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474.
Holland SJ, Gale NW, Mbamalu G, et al. (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, (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, et al. (1998). "Overexpression of Lerk-5/Eplg5 messenger RNA: a novel marker for increased tumorigenicity and metastatic potential in human malignant melanomas". Clin. Cancer Res. 4 (3): 791–7. PMID 9533549.
Wang HU, Chen ZF, Anderson DJ (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, et al. (1998). "Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis". J. Cell. Sci. 111 ( Pt 18): 2741–51. PMID 9718367.
Torres R, Firestein BL, Dong H, et al. (1999). "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 (1999). "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif". J. Biol. Chem. 274 (6): 3726–33. doi:10.1074/jbc.274.6.3726. PMID 9920925.

PDB gallery

1iko: CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN

1kgy: Crystal Structure of the EphB2-ephrinB2 complex

2hle: Structural and biophysical characterization of the EPHB4-EPHRINB2 protein protein interaction and receptor specificity

Intercellular signaling peptides and proteins / ligands

Growth factors	Endothelial growth factor • Epidermal growth factor • Fibroblast growth factor • Nerve growth factor • Platelet-derived growth factor • Transforming growth factor beta superfamily

Ephrin	EFNA1 • EFNA2 • EFNA3 • EFNA4 • EFNA5 • EFNB1 • EFNB2 • EFNB3

Other	Adipokine • Agouti signaling protein • Agouti-related protein • Angiogenic protein • CCN intercellular signaling protein (Cysteine-rich protein 61, Connective tissue growth factor, Nephroblastoma overexpressed protein) • Cytokine • Endothelin (EDN1, EDN2, EDN3) • Hedgehog protein • Interferon • Kinin • Parathyroid hormone-related protein • Semaphorin • Somatomedin • Tolloid-like metalloproteinase • Tumor necrosis factor • Wnt protein

see also extracellular ligand disorders B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

EFNB2

Interactions

References

Further reading