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{{Infobox_gene}}
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'''Ephrin type-B receptor 4''' is a [[protein]] that in humans is encoded by the ''EPHB4'' [[gene]].<ref name="pmid8188704">{{cite journal | vauthors = Bennett BD, Wang Z, Kuang WJ, Wang A, Groopman JE, Goeddel DV, Scadden DT | title = Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily | journal = J Biol Chem | volume = 269 | issue = 19 | pages = 14211–8 |date=Jun 1994 | pmid = 8188704 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPHB4 EPH receptor B4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2050| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_EPHB4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2bba.
| PDB = {{PDB2|2bba}}, {{PDB2|2hle}}
| Name = EPH receptor B4
| HGNCid = 3395
| Symbol = EPHB4
| AltSymbols =; HTK; MYK1; TYRO11
| OMIM = 600011
| ECnumber = 
| Homologene = 20939
| MGIid = 104757
| GeneAtlas_image1 = PBB_GE_EPHB4_202894_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPHB4_216680_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005003 |text = ephrin receptor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{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:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}} {{GNF_GO|id=GO:0048168 |text = regulation of neuronal synaptic plasticity}} {{GNF_GO|id=GO:0048170 |text = positive regulation of long-term neuronal synaptic plasticity}} {{GNF_GO|id=GO:0050770 |text = regulation of axonogenesis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2050
    | Hs_Ensembl = ENSG00000196411
    | Hs_RefseqProtein = NP_004435
    | Hs_RefseqmRNA = NM_004444
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 100238123
    | Hs_GenLoc_end = 100263079
    | Hs_Uniprot = P54760
    | Mm_EntrezGene = 13846
    | Mm_Ensembl = ENSMUSG00000029710
    | Mm_RefseqmRNA = NM_010144
    | Mm_RefseqProtein = NP_034274
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 137579897
    | Mm_GenLoc_end = 137604298
    | Mm_Uniprot = Q3V1K8
  }}
}}
'''EPH receptor B4''', also known as '''EPHB4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPHB4 EPH receptor B4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2050| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 binds to ephrin-B2 and plays an essential role in vascular development.<ref name="entrez">{{cite web | title = Entrez Gene: EPHB4 EPH receptor B4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2050| accessdate = }}</ref>
| 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 binds to [[EFNB2|ephrin-B2]] and plays an essential role in vascular development.<ref name="entrez">{{cite web | title = Entrez Gene: EPHB4 EPH receptor B4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2050| accessdate = }}</ref><ref name="GERETYETAL">{{cite journal  | vauthors=Gerety SS, Wang HU, Chen ZF, Anderson DJ |title=Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development. |journal=Mol. Cell |volume=4 |issue= 3 |pages= 403–14 |year= 1999 |pmid= 10518221 |doi=10.1016/S1097-2765(00)80342-1  }}</ref>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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  | 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=Zhou R |title=The Eph family receptors and ligands. |journal=Pharmacol. Ther. |volume=77 |issue= 3 |pages= 151-81 |year= 1998 |pmid= 9576626 |doi=  }}
*{{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=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=  }}
*{{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 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=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=  }}
*{{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=Andres AC, Reid HH, Zürcher G, ''et al.'' |title=Expression of two novel eph-related receptor protein tyrosine kinases in mammary gland development and carcinogenesis. |journal=Oncogene |volume=9 |issue= 5 |pages= 1461-7 |year= 1994 |pmid= 8152808 |doi=  }}
*{{cite journal  | vauthors=Andres AC, Reid HH, Zürcher G |title=Expression of two novel eph-related receptor protein tyrosine kinases in mammary gland development and carcinogenesis. |journal=Oncogene |volume=9 |issue= 5 |pages= 1461–7 |year= 1994 |pmid= 8152808 |doi=  |display-authors=etal}}
*{{cite journal  | author=Bennett BD, Wang Z, Kuang WJ, ''et al.'' |title=Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily. |journal=J. Biol. Chem. |volume=269 |issue= 19 |pages= 14211-8 |year= 1994 |pmid= 8188704 |doi= }}
*{{cite journal  | vauthors=Berclaz G, Andres AC, Albrecht D |title=Expression of the receptor protein tyrosine kinase myk-1/htk in normal and malignant mammary epithelium. |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue= 3 |pages= 869–75 |year= 1996 |pmid= 8831703 |doi= 10.1006/bbrc.1996.1442 |display-authors=etal}}
*{{cite journal  | author=Berclaz G, Andres AC, Albrecht D, ''et al.'' |title=Expression of the receptor protein tyrosine kinase myk-1/htk in normal and malignant mammary epithelium. |journal=Biochem. Biophys. Res. Commun. |volume=226 |issue= 3 |pages= 869-75 |year= 1996 |pmid= 8831703 |doi= 10.1006/bbrc.1996.1442 }}
*{{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= |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=Nikolova Z, Djonov V, Zuercher G |title=Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis. |journal=J. Cell Sci. |volume=111 |issue=  18|pages= 2741–51 |year= 1998 |pmid= 9718367 |doi=  |display-authors=etal}}
*{{cite journal  | author=Nikolova Z, Djonov V, Zuercher G, ''et al.'' |title=Cell-type specific and estrogen dependent expression of the receptor tyrosine kinase EphB4 and its ligand ephrin-B2 during mammary gland morphogenesis. |journal=J. Cell. Sci. |volume=111 ( Pt 18) |issue=  |pages= 2741-51 |year= 1998 |pmid= 9718367 |doi=  }}
*{{cite journal  | vauthors=Tang XX, Brodeur GM, Campling BG, Ikegaki N |title=Coexpression of transcripts encoding EPHB receptor protein tyrosine kinases and their ephrin-B ligands in human small cell lung carcinoma. |journal=Clin. Cancer Res. |volume=5 |issue= 2 |pages= 455–60 |year= 1999 |pmid= 10037197 |doi=  }}
*{{cite journal  | author=Tang XX, Brodeur GM, Campling BG, Ikegaki N |title=Coexpression of transcripts encoding EPHB receptor protein tyrosine kinases and their ephrin-B ligands in human small cell lung carcinoma. |journal=Clin. Cancer Res. |volume=5 |issue= 2 |pages= 455-60 |year= 1999 |pmid= 10037197 |doi=  }}
*{{cite journal  | vauthors=Dalva MB, Takasu MA, Lin MZ |title=EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. |journal=Cell |volume=103 |issue= 6 |pages= 945–56 |year= 2001 |pmid= 11136979 |doi=10.1016/S0092-8674(00)00197-5 |display-authors=etal}}
*{{cite journal  | author=Gerety SS, Wang HU, Chen ZF, Anderson DJ |title=Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development. |journal=Mol. Cell |volume=4 |issue= 3 |pages= 403-14 |year= 1999 |pmid= 10518221 |doi=  }}
*{{cite journal  | vauthors=Wilson MD, Riemer C, Martindale DW |title=Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. |journal=Nucleic Acids Res. |volume=29 |issue= 6 |pages= 1352–65 |year= 2001 |pmid= 11239002 |doi=10.1093/nar/29.6.1352 | pmc=29746  |display-authors=etal}}
*{{cite journal  | author=Dalva MB, Takasu MA, Lin MZ, ''et al.'' |title=EphB receptors interact with NMDA receptors and regulate excitatory synapse formation. |journal=Cell |volume=103 |issue= 6 |pages= 945-56 |year= 2001 |pmid= 11136979 |doi=  }}
*{{cite journal  | author=Wilson MD, Riemer C, Martindale DW, ''et al.'' |title=Comparative analysis of the gene-dense ACHE/TFR2 region on human chromosome 7q22 with the orthologous region on mouse chromosome 5. |journal=Nucleic Acids Res. |volume=29 |issue= 6 |pages= 1352-65 |year= 2001 |pmid= 11239002 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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[[Category:Tyrosine kinase receptors]]
 
 
{{gene-7-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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PubMed searchn/an/a
Wikidata
View/Edit Human

Ephrin type-B receptor 4 is a protein that in humans is encoded by the EPHB4 gene.[1][2]

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 binds to ephrin-B2 and plays an essential role in vascular development.[2][3]

References

  1. ↑ Bennett BD, Wang Z, Kuang WJ, Wang A, Groopman JE, Goeddel DV, Scadden DT (Jun 1994). "Cloning and characterization of HTK, a novel transmembrane tyrosine kinase of the EPH subfamily". J Biol Chem. 269 (19): 14211–8. PMID 8188704.
  2. ↑ 2.0 2.1 "Entrez Gene: EPHB4 EPH receptor B4".
  3. ↑ Gerety SS, Wang HU, Chen ZF, Anderson DJ (1999). "Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development". Mol. Cell. 4 (3): 403–14. doi:10.1016/S1097-2765(00)80342-1. PMID 10518221.

Further reading


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