Ephrin B1

Short description: Protein-coding gene in the species Homo sapiens

Generic protein structure example

Ephrin B1 is a protein that in humans is encoded by the EFNB1 gene.[1][2] It is a member of the ephrin family. The encoded protein is a type I membrane protein and a ligand of Eph-related receptor tyrosine kinases. It may play a role in cell adhesion and function in the development or maintenance of the nervous system.[3]

## Contents

* 1 Clinical significance
* 2 Interactions
* 3 References
* 4 Further reading
* 5 External links

## Clinical significance

Mutations in this protein are responsible for most cases of craniofrontonasal syndrome.[4][5][6]

## Interactions

EFNB1 has been shown to interact with SDCBP.[7]

## References

1. ↑ "Assignment of the gene (EPLG2) encoding a high-affinity binding protein for the receptor tyrosine kinase Elk to a 200-kilobasepair region in human chromosome Xq12". Genomics 25 (1): 334–5. Jul 1995. doi:10.1016/0888-7543(95)80156-G. PMID 7774950.
2. ↑ "A novel mutation in EFNB1, probably with a dominant negative effect, underlying craniofrontonasal syndrome". Cleft Palate Craniofac J 43 (2): 152–4. Mar 2006. doi:10.1597/05-014.1. PMID 16526919.
3. ↑ "Entrez Gene: EFNB1 ephrin-B1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1947.
4. ↑ "Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome". Clin. Genet. 72 (6): 506–16. December 2007. doi:10.1111/j.1399-0004.2007.00905.x. PMID 17941886.
5. ↑ "Mutations of ephrin-B1 (EFNB1), a marker of tissue boundary formation, cause craniofrontonasal syndrome". Proc Natl Acad Sci U S A 101 (23): 8652–7. Jun 2004. doi:10.1073/pnas.0402819101. PMID 15166289. Bibcode: 2004PNAS..101.8652T.
6. ↑ "Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome". Am J Hum Genet 74 (6): 1209–15. Jun 2004. doi:10.1086/421532. PMID 15124102.
7. ↑ Lin, D; Gish G D; Songyang Z; Pawson T (Feb 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. ISSN 0021-9258. PMID 9920925.

## Further reading

* "The ephrins and Eph receptors in neural development.". Annu. Rev. Neurosci. 21: 309–45. 1998. 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.
* "Eph receptors and ephrins: effectors of morphogenesis.". Development 126 (10): 2033–44. 1999. 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.
* "Roles of Eph receptors and ephrins in segmental patterning.". Philos. Trans. R. Soc. Lond. B Biol. Sci. 355 (1399): 993–1002. 2001. doi:10.1098/rstb.2000.0635. 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.
* "Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity.". Science 266 (5186): 816–9. 1994. doi:10.1126/science.7973638. PMID 7973638. Bibcode: 1994Sci...266..816D.
* "Molecular characterization of a family of ligands for eph-related tyrosine kinase receptors.". EMBO J. 13 (16): 3757–62. 1994. doi:10.1002/j.1460-2075.1994.tb06685.x. PMID 8070404.
* "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. 1997. doi:10.1006/geno.1996.0192. PMID 8660976. https://zenodo.org/record/1229677.
* "Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis.". Neuron 17 (1): 9–19. 1996. doi:10.1016/S0896-6273(00)80276-7. PMID 8755474.
* "Cell-cell adhesion mediated by binding of membrane-anchored ligand LERK-2 to the EPH-related receptor human embryonal kinase 2 promotes tyrosine kinase activity.". J. Biol. Chem. 271 (40): 24747–52. 1996. doi:10.1074/jbc.271.40.24747. PMID 8798744.
* "Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands.". Nature 383 (6602): 722–5. 1996. doi:10.1038/383722a0. PMID 8878483. Bibcode: 1996Natur.383..722H.
* 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.
* "A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22.". Hum. Mol. Genet. 6 (11): 1937–41. 1998. doi:10.1093/hmg/6.11.1937. PMID 9302274.
* "PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands.". Neuron 21 (6): 1453–63. 1999. doi:10.1016/S0896-6273(00)80663-7. PMID 9883737.
* "The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif.". J. Biol. Chem. 274 (6): 3726–33. 1999. doi:10.1074/jbc.274.6.3726. PMID 9920925.
* "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains.". Neuron 22 (3): 511–24. 1999. doi:10.1016/S0896-6273(00)80706-0. PMID 10197531.

## External links

* Overview of all the structural information available in the PDB for UniProt: P98172 (Human Ephrin-B1) at the PDBe-KB.
* Overview of all the structural information available in the PDB for UniProt: P52795 (Mouse Ephrin-B1) at the PDBe-KB.

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