Ephrin B1: Difference between revisions

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==Interactions==
==Interactions==
EFNB1 has been shown to [[Protein-protein interaction|interact]] with [[SDCBP]].<ref name=pmid9920925>{{cite journal |last=Lin |first=D |author2=Gish G D |author3=Songyang Z |author4=Pawson T  |date=Feb 1999 |title=The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif |journal=J. Biol. Chem. |volume=274 |issue=6 |pages=3726–33 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9920925 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.274.6.3726 }}</ref>
EFNB1 has been shown to [[Protein-protein interaction|interact]] with [[SDCBP]].<ref name=pmid9920925>{{cite journal |last=Lin |first=D |author2=Gish G D |author3=Songyang Z |author4=Pawson T  |date=Feb 1999 |title=The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif |journal=J. Biol. Chem. |volume=274 |issue=6 |pages=3726–33 | issn = 0021-9258| pmid = 9920925 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1074/jbc.274.6.3726 }}</ref>


==References==
==References==
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*{{cite journal  | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151–81 |year= 1998 |pmid= 9576626 |doi=10.1016/S0163-7258(97)00112-5  }}
*{{cite journal  | author=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151–81 |year= 1998 |pmid= 9576626 |doi=10.1016/S0163-7258(97)00112-5  }}
*{{cite journal  | vauthors=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |pmid= 10207129 |doi=  }}
*{{cite journal  | vauthors=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis. |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |pmid= 10207129 |doi=  }}
*{{cite journal | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue=  |pages= 177–244 |year= 2000 |pmid= 10730216 |doi=10.1016/S0074-7696(00)96005-4  }}
*{{cite book | author=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly. |journal=Int. Rev. Cytol. |volume=196 |issue=  |pages= 177–244 |year= 2000 |pmid= 10730216 |doi=10.1016/S0074-7696(00)96005-4  |series=International Review of Cytology |isbn=9780123646002 }}
*{{cite journal  | vauthors=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond. B Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635  | pmc=1692797 }}
*{{cite journal  | vauthors=Xu Q, Mellitzer G, Wilkinson DG |title=Roles of Eph receptors and ephrins in segmental patterning. |journal=Philos. Trans. R. Soc. Lond. B Biol. Sci. |volume=355 |issue= 1399 |pages= 993–1002 |year= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635  | pmc=1692797 }}
*{{cite journal  | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=10.1038/35058515  }}
*{{cite journal  | author=Wilkinson DG |title=Multiple roles of EPH receptors and ephrins in neural development. |journal=Nat. Rev. Neurosci. |volume=2 |issue= 3 |pages= 155–64 |year= 2001 |pmid= 11256076 |doi=10.1038/35058515  }}
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*{{cite journal  | vauthors=Gale NW, Holland SJ, Valenzuela DM |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=10.1016/S0896-6273(00)80276-7  |display-authors=etal}}
*{{cite journal  | vauthors=Gale NW, Holland SJ, Valenzuela DM |title=Eph receptors and ligands comprise two major specificity subclasses and are reciprocally compartmentalized during embryogenesis. |journal=Neuron |volume=17 |issue= 1 |pages= 9–19 |year= 1996 |pmid= 8755474 |doi=10.1016/S0896-6273(00)80276-7  |display-authors=etal}}
*{{cite journal  | vauthors=Böhme B, VandenBos T, Cerretti DP |title=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. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24747–52 |year= 1996 |pmid= 8798744 |doi=10.1074/jbc.271.40.24747  |display-authors=etal}}
*{{cite journal  | vauthors=Böhme B, VandenBos T, Cerretti DP |title=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. |journal=J. Biol. Chem. |volume=271 |issue= 40 |pages= 24747–52 |year= 1996 |pmid= 8798744 |doi=10.1074/jbc.271.40.24747  |display-authors=etal}}
*{{cite journal  | vauthors=Holland SJ, Gale NW, Mbamalu G |title=Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. |journal=Nature |volume=383 |issue= 6602 |pages= 722–5 |year= 1996 |pmid= 8878483 |doi= 10.1038/383722a0 |display-authors=etal|bibcode=1996Natur.383..722H }}
*{{cite journal  | vauthors=Holland SJ, Gale NW, Mbamalu G |title=Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. |journal=Nature |volume=383 |issue= 6602 |pages= 722–5 |year= 1996 |pmid= 8878483 |doi= 10.1038/383722a0 |display-authors=etal|bibcode=1996Natur.383..722H |hdl=1807/9444 }}
*{{cite journal  | author= Ephnomenclaturecommittee|title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=10.1016/S0092-8674(00)80500-0  }}
*{{cite journal  | author= Ephnomenclaturecommittee|title=Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee. |journal=Cell |volume=90 |issue= 3 |pages= 403–4 |year= 1997 |pmid= 9267020 |doi=10.1016/S0092-8674(00)80500-0  }}
*{{cite journal  | vauthors=Feldman GJ, Ward DE, Lajeunie-Renier E |title=A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1937–41 |year= 1998 |pmid= 9302274 |doi=10.1093/hmg/6.11.1937  |display-authors=etal}}
*{{cite journal  | vauthors=Feldman GJ, Ward DE, Lajeunie-Renier E |title=A novel phenotypic pattern in X-linked inheritance: craniofrontonasal syndrome maps to Xp22. |journal=Hum. Mol. Genet. |volume=6 |issue= 11 |pages= 1937–41 |year= 1998 |pmid= 9302274 |doi=10.1093/hmg/6.11.1937  |display-authors=etal}}

Latest revision as of 22:06, 3 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

Ephrin-B1 is a protein that in humans is encoded by the EFNB1 gene.[1][2]

This gene encodes 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]

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. 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.
  2. 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.
  3. "Entrez Gene: EFNB1 ephrin-B1".
  4. 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.
  5. 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.
  6. 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.
  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