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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Ephrin type-B receptor 3''' is a [[protein]] that in humans is encoded by the ''EPHB3'' [[gene]].<ref name="pmid8397371">{{cite journal | vauthors = Böhme B, Holtrich U, Wolf G, Luzius H, Grzeschik KH, Strebhardt K, Rübsamen-Waigmann H | title = PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2 | journal = Oncogene | volume = 8 | issue = 10 | pages = 2857–62 | date = Oct 1993 | pmid = 8397371 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPHB3 EPH receptor B3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2049| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = EPH receptor B3
| HGNCid = 3394
| Symbol = EPHB3
| AltSymbols =; ETK2; HEK2; TYRO6
| OMIM = 601839
| ECnumber = 
| Homologene = 20938
| MGIid = 104770
| GeneAtlas_image1 = PBB_GE_EPHB3_1438_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPHB3_204600_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005003 |text = ephrin receptor activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008046 |text = axon guidance receptor activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007411 |text = axon guidance}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2049
    | Hs_Ensembl = ENSG00000182580
    | Hs_RefseqProtein = NP_004434
    | Hs_RefseqmRNA = NM_004443
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 185762281
    | Hs_GenLoc_end = 185782889
    | Hs_Uniprot = P54753
    | Mm_EntrezGene = 13845
    | Mm_Ensembl = ENSMUSG00000005958
    | Mm_RefseqmRNA = NM_010143
    | Mm_RefseqProtein = NP_034273
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 21118777
    | Mm_GenLoc_end = 21137287
    | Mm_Uniprot = Q60669
  }}
}}
'''EPH receptor B3''', also known as '''EPHB3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPHB3 EPH receptor B3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2049| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. 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. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. 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. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.<ref name="entrez">{{cite web | title = Entrez Gene: EPHB3 EPH receptor B3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2049| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
EPHB3 has been shown to [[Protein-protein interaction|interact]] with [[MLLT4]]<ref name=pmid9707552>{{cite journal | vauthors = Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K | title = PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor | journal = [[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] | volume = 95 | issue = 17 | pages = 9779–84 | date = Aug 1998 | pmid = 9707552 | pmc = 21413 | doi = 10.1073/pnas.95.17.9779 }}</ref> and [[RAS p21 protein activator 1]].<ref name=pmid9674711>{{cite journal | vauthors = Hock B, Böhme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K | title = Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions | journal = Oncogene | volume = 17 | issue = 2 | pages = 255–60 | date = Jul 1998 | pmid = 9674711 | doi = 10.1038/sj.onc.1201907 }}</ref>
{{refbegin | 2}}
 
{{PBB_Further_reading
== References ==
| citations =
{{reflist}}
*{{cite journal | author=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development. |journal=Annu. Rev. Neurosci. |volume=21 |issue=  |pages= 309-45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
 
*{{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= }}
== Further reading ==
*{{cite journal | author=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=  }}
{{refbegin|35em}}
*{{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= }}
* {{cite journal | vauthors = Flanagan JG, Vanderhaeghen P | title = The ephrins and Eph receptors in neural development. | journal = Annu. Rev. Neurosci. | volume = 21 | issue =  | pages = 309–45 | year = 1998 | pmid = 9530499 | doi = 10.1146/annurev.neuro.21.1.309 }}
*{{cite journal | author=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 }}
* {{cite journal | vauthors = 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=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= }}
* {{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=Böhme B, Holtrich U, Wolf G, ''et al.'' |title=PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2. |journal=Oncogene |volume=8 |issue= 10 |pages= 2857-62 |year= 1993 |pmid= 8397371 |doi=  }}
* {{cite journal | vauthors = 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 journal | author=Böhme B, VandenBos T, Cerretti DP, ''et al.'' |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= }}
* {{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 | pmc = 1692797 | doi = 10.1098/rstb.2000.0635 }}
*{{cite journal | author= |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= }}
* {{cite journal | vauthors = 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=Bergemann AD, Zhang L, Chiang MK, ''et al.'' |title=Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. |journal=Oncogene |volume=16 |issue= 4 |pages= 471-80 |year= 1998 |pmid= 9484836 |doi= 10.1038/sj.onc.1201557 }}
* {{cite journal | vauthors = Böhme B, VandenBos T, Cerretti DP, Park LS, Holtrich U, Rübsamen-Waigmann H, Strebhardt K | 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 }}
*{{cite journal | author=Hock B, Böhme B, Karn T, ''et al.'' |title=Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. |journal=Oncogene |volume=17 |issue= 2 |pages= 255-60 |year= 1998 |pmid= 9674711 |doi= 10.1038/sj.onc.1201907 }}
* {{cite journal | vauthors = 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=Hock B, Böhme B, Karn T, ''et al.'' |title=PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 17 |pages= 9779-84 |year= 1998 |pmid= 9707552 |doi= }}
* {{cite journal | vauthors = Bergemann AD, Zhang L, Chiang MK, Brambilla R, Klein R, Flanagan JG | title = Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. | journal = Oncogene | volume = 16 | issue = 4 | pages = 471–80 | year = 1998 | pmid = 9484836 | doi = 10.1038/sj.onc.1201557 }}
*{{cite journal | author=Ciossek T, Monschau B, Kremoser C, ''et al.'' |title=Eph receptor-ligand interactions are necessary for guidance of retinal ganglion cell axons in vitro. |journal=Eur. J. Neurosci. |volume=10 |issue= 5 |pages= 1574-80 |year= 1998 |pmid= 9751130 |doi= }}
* {{cite journal | vauthors = Hock B, Böhme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K | title = Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions. | journal = Oncogene | volume = 17 | issue = 2 | pages = 255–60 | year = 1998 | pmid = 9674711 | doi = 10.1038/sj.onc.1201907 }}
*{{cite journal | author=Adams RH, Wilkinson GA, Weiss C, ''et al.'' |title=Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. |journal=Genes Dev. |volume=13 |issue= 3 |pages= 295-306 |year= 1999 |pmid= 9990854 |doi= }}
* {{cite journal | vauthors = Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K | title = PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor. | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 95 | issue = 17 | pages = 9779–84 | year = 1998 | pmid = 9707552 | pmc = 21413 | doi = 10.1073/pnas.95.17.9779 }}
}}
* {{cite journal | vauthors = Ciossek T, Monschau B, Kremoser C, Löschinger J, Lang S, Müller BK, Bonhoeffer F, Drescher U | title = Eph receptor-ligand interactions are necessary for guidance of retinal ganglion cell axons in vitro. | journal = Eur. J. Neurosci. | volume = 10 | issue = 5 | pages = 1574–80 | year = 1998 | pmid = 9751130 | doi = 10.1046/j.1460-9568.1998.00180.x }}
* {{cite journal | vauthors = Adams RH, Wilkinson GA, Weiss C, Diella F, Gale NW, Deutsch U, Risau W, Klein R | title = Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. | journal = Genes Dev. | volume = 13 | issue = 3 | pages = 295–306 | year = 1999 | pmid = 9990854 | pmc = 316426 | doi = 10.1101/gad.13.3.295 }}
{{refend}}
{{refend}}


{{protein-stub}}
{{Tyrosine kinases}}
{{WikiDoc Sources}}
{{Enzymes}}
{{Growth factor receptor modulators}}
{{Portal bar|Molecular and Cellular Biology|border=no}}
 
[[Category:Tyrosine kinase receptors]]
 
 
{{gene-3-stub}}

Latest revision as of 05:02, 25 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ephrin type-B receptor 3 is a protein that in humans is encoded by the EPHB3 gene.[1][2]

Function

Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. 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. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.[2]

Interactions

EPHB3 has been shown to interact with MLLT4[3] and RAS p21 protein activator 1.[4]

References

  1. ↑ Böhme B, Holtrich U, Wolf G, Luzius H, Grzeschik KH, Strebhardt K, Rübsamen-Waigmann H (Oct 1993). "PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2". Oncogene. 8 (10): 2857–62. PMID 8397371.
  2. ↑ 2.0 2.1 "Entrez Gene: EPHB3 EPH receptor B3".
  3. ↑ Hock B, Böhme B, Karn T, Yamamoto T, Kaibuchi K, Holtrich U, Holland S, Pawson T, Rübsamen-Waigmann H, Strebhardt K (Aug 1998). "PDZ-domain-mediated interaction of the Eph-related receptor tyrosine kinase EphB3 and the ras-binding protein AF6 depends on the kinase activity of the receptor". Proc. Natl. Acad. Sci. U.S.A. 95 (17): 9779–84. doi:10.1073/pnas.95.17.9779. PMC 21413. PMID 9707552.
  4. ↑ Hock B, Böhme B, Karn T, Feller S, Rübsamen-Waigmann H, Strebhardt K (Jul 1998). "Tyrosine-614, the major autophosphorylation site of the receptor tyrosine kinase HEK2, functions as multi-docking site for SH2-domain mediated interactions". Oncogene. 17 (2): 255–60. doi:10.1038/sj.onc.1201907. PMID 9674711.

Further reading


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