Ephrin B1

EFNB1
Identifiers
Aliases	EFNB1 , CFND, CFNS, EFB1, EFL3, EPLG2, Elk-L, LERK2, ephrin B1
External IDs	OMIM: 300035; MGI: 102708; HomoloGene: 3263; GeneCards: EFNB1; OMA:EFNB1 - orthologs
Gene location (Human) Chr. X chromosome (human) [1] Band Xq13.1 Start 68,829,021 bp [1] End 68,842,160 bp [1]
Gene location (Mouse) Chr. X chromosome (mouse) [2] Band X C3|X 43.22 cM Start 98,179,736 bp [2] End 98,192,597 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone right lung ganglionic eminence mucosa of transverse colon skin of abdomen skin of leg upper lobe of left lung tibial nerve apex of heart ectocervix Top expressed in ventricular zone Ileal epithelium external carotid artery lumbar spinal ganglion internal carotid artery Rostral migratory stream renal corpuscle lip yolk sac gastrula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding ephrin receptor binding protein tyrosine kinase activity Cellular component integral component of membrane nucleus extracellular exosome membrane membrane raft integral component of plasma membrane synapse cytoplasm plasma membrane Biological process positive regulation of T cell proliferation nervous system development cell-cell signaling T cell costimulation multicellular organism development neural crest cell migration cell differentiation cell adhesion embryonic pattern specification axon guidance ephrin receptor signaling pathway peptidyl-tyrosine phosphorylation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1947 13641 Ensembl ENSG00000090776 ENSMUSG00000031217 UniProt P98172 P52795 RefSeq (mRNA) NM_004429 NM_010110 RefSeq (protein) NP_004420 NP_034240 Location (UCSC) Chr X: 68.83 – 68.84 Mb Chr X: 98.18 – 98.19 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Ephrin B1 is a protein that in humans is encoded by the EFNB1 gene. ^{[5] [6]} 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. ^[7]

Clinical significance

Mutations in this protein are responsible for most cases of craniofrontonasal syndrome. ^{[8] [9] [10]}

Interactions

EFNB1 has been shown to interact with SDCBP. ^[11]

References

1. GRCh38: Ensembl release 89: ENSG00000090776 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031217 – 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. Fletcher FA, Huebner K, Shaffer LG, Fairweather ND, Monaco AP, Muller U, Druck T, Simoneaux DK, Chelly J, Belmont JW, et al. (Jul 1995). "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. doi:10.1016/0888-7543(95)80156-G. PMID   7774950.
6. Shotelersuk V, Siriwan P, Ausavarat S (Mar 2006). "A novel mutation in EFNB1, probably with a dominant negative effect, underlying craniofrontonasal syndrome". Cleft Palate Craniofac J. 43 (2): 152–4. doi:10.1597/05-014.1. PMID   16526919. S2CID   10737616.
7. "Entrez Gene: EFNB1 ephrin-B1".
8. Wieland I, Weidner C, Ciccone R, et al. (December 2007). "Contiguous gene deletions involving EFNB1, OPHN1, PJA1 and EDA in patients with craniofrontonasal syndrome". Clin. Genet. 72 (6): 506–16. doi:10.1111/j.1399-0004.2007.00905.x. PMID   17941886. S2CID   33823266.
9. Twigg SR, Kan R, Babbs C, Bochukova EG, Robertson SP, Wall SA, Morriss-Kay GM, Wilkie AO (Jun 2004). "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. Bibcode:2004PNAS..101.8652T. doi: 10.1073/pnas.0402819101 . PMC   423250 . PMID   15166289.
10. Wieland I, Jakubiczka S, Muschke P, Cohen M, Thiele H, Gerlach KL, Adams RH, Wieacker P (Jun 2004). "Mutations of the ephrin-B1 gene cause craniofrontonasal syndrome". Am J Hum Genet. 74 (6): 1209–15. doi:10.1086/421532. PMC   1182084 . PMID   15124102.
11. 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

• 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. S2CID   1278600.
• 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. 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. Vol. 196. pp. 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN   9780123646002. PMID   10730216.{{cite book}}: |journal= ignored (help)
• 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.
• 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.
• Davis S, Gale NW, Aldrich TH, et al. (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, et al. (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, 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.
• Böhme B, VandenBos T, Cerretti DP, et al. (1996). "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. doi: 10.1074/jbc.271.40.24747 . PMID   8798744.
• 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. Bibcode:1996Natur.383..722H. doi:10.1038/383722a0. hdl: 1807/9444 . PMID   8878483. S2CID   4349898.
• 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.
• Feldman GJ, Ward DE, Lajeunie-Renier E, et al. (1998). "A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22". Hum. Mol. Genet. 6 (11): 1937–41. doi: 10.1093/hmg/6.11.1937 . PMID   9302274.
• 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.
• Brückner K, Pablo Labrador J, Scheiffele P, et al. (1999). "EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains". Neuron. 22 (3): 511–24. 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 .