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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
'''EPH receptor A4''' ('''ephrin type-A receptor 4''') is a [[protein]] that in humans is encoded by the ''EPHA4'' [[gene]].<ref name="pmid9267020">{{cite journal | title = Unified nomenclature for Eph family receptors and their ligands, the ephrins. Eph Nomenclature Committee | journal = Cell | volume = 90 | issue = 3 | pages = 403–4 |date=Sep 1997 | pmid = 9267020 | pmc =  | doi =10.1016/S0092-8674(00)80500-0 | last1 =  Ephnomenclaturecommittee }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPHA4 EPH receptor A4| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2043| accessdate = }}</ref>
| image = PBB_Protein_EPHA4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b0x.
| PDB = {{PDB2|1b0x}}, {{PDB2|2hel}}
| Name = EPH receptor A4
| HGNCid = 3388
| Symbol = EPHA4
| AltSymbols =; HEK8; SEK; TYRO1
| OMIM = 602188
| ECnumber = 
| Homologene = 20933
| MGIid = 98277
| GeneAtlas_image1 = PBB_GE_EPHA4_206114_at_tn.png
| GeneAtlas_image2 = PBB_GE_EPHA4_gnf1h07687_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: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}} {{GNF_GO|id=GO:0007628 |text = adult walking behavior}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2043
    | Hs_Ensembl = ENSG00000116106
    | Hs_RefseqProtein = NP_004429
    | Hs_RefseqmRNA = NM_004438
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 221990993
    | Hs_GenLoc_end = 222145254
    | Hs_Uniprot = P54764
    | Mm_EntrezGene = 13838
    | Mm_Ensembl = ENSMUSG00000026235
    | Mm_RefseqmRNA = NM_007936
    | Mm_RefseqProtein = NP_031962
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 77250333
    | Mm_GenLoc_end = 77398236
    | Mm_Uniprot = Q3V1W9
  }}
}}
'''EPH receptor A4''', also known as '''EPHA4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EPHA4 EPH receptor A4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2043| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
{{PBB Summary
| section_title =  
| section_title =  
| summary_text = This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin 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.<ref name="entrez">{{cite web | title = Entrez Gene: EPHA4 EPH receptor A4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2043| accessdate = }}</ref>
| summary_text = This gene belongs to the [[ephrin]] receptor subfamily of the [[protein-tyrosine kinase]] family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the [[nervous system]]. Receptors in the EPH subfamily typically have a single [[kinase]] domain and an extracellular region containing a Cys-rich domain and 2 [[fibronectin]] type III repeats. The ephrin 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]].<ref name="entrez" />
 
In 2012, a publication in ''[[Nature Medicine]]'' revealed a connection between EPHA4 and the neurodegenerative disease [[Amyotrophic lateral sclerosis]] (ALS), where a defective gene allows ALS patients to live considerably longer than patients with an intact gene. This opens up for development of treatment for this currently untreatable disease.
}}
}}


==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; Chapter: 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=978-0-12-364600-2 }}
*{{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=Fox GM, Holst PL, Chute HT, ''et al.'' |title=cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases. |journal=Oncogene |volume=10 |issue= 5 |pages= 897-905 |year= 1995 |pmid= 7898931 |doi=  }}
*{{cite journal  | vauthors=Fox GM, Holst PL, Chute HT |title=cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases |journal=Oncogene |volume=10 |issue= 5 |pages= 897–905 |year= 1995 |pmid= 7898931 |doi=  |display-authors=etal}}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8 }}
*{{cite journal  | author=Ellis C, Kasmi F, Ganju P, ''et al.'' |title=A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn. |journal=Oncogene |volume=12 |issue= 8 |pages= 1727-36 |year= 1996 |pmid= 8622893 |doi=  }}
*{{cite journal  | vauthors=Ellis C, Kasmi F, Ganju P |title=A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn |journal=Oncogene |volume=12 |issue= 8 |pages= 1727–36 |year= 1996 |pmid= 8622893 |doi=  |display-authors=etal}}
*{{cite journal  | author=Gale NW, Holland SJ, Valenzuela DM, ''et al.'' |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=  }}
*{{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  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal  | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }}
*{{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=Aasheim HC, Terstappen LW, Logtenberg T |title=Regulated expression of the Eph-related receptor tyrosine kinase Hek11 in early human B lymphopoiesis |journal=Blood |volume=90 |issue= 9 |pages= 3613–22 |year= 1997 |pmid= 9345045 |doi=  }}
*{{cite journal  | author=Aasheim HC, Terstappen LW, Logtenberg T |title=Regulated expression of the Eph-related receptor tyrosine kinase Hek11 in early human B lymphopoiesis. |journal=Blood |volume=90 |issue= 9 |pages= 3613-22 |year= 1997 |pmid= 9345045 |doi=  }}
*{{cite journal  | vauthors=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3 |display-authors=etal}}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | vauthors=Bergemann AD, Zhang L, Chiang MK |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 |display-authors=etal}}
*{{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=Janis LS, Cassidy RM, Kromer LF |title=Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum |journal=J. Neurosci. |volume=19 |issue= 12 |pages= 4962–71 |year= 1999 |pmid= 10366629 |doi=  }}
*{{cite journal  | author=Janis LS, Cassidy RM, Kromer LF |title=Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum. |journal=J. Neurosci. |volume=19 |issue= 12 |pages= 4962-71 |year= 1999 |pmid= 10366629 |doi=  }}
}}
}}
{{refend}}
{{refend}}


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[[Category:Tyrosine kinase receptors]]
 
 
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Latest revision as of 11:03, 17 July 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

n/a

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RefSeq (mRNA)

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RefSeq (protein)

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

EPH receptor A4 (ephrin type-A receptor 4) is a protein that in humans is encoded by the EPHA4 gene.[1][2]

This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin 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.[2]

In 2012, a publication in Nature Medicine revealed a connection between EPHA4 and the neurodegenerative disease Amyotrophic lateral sclerosis (ALS), where a defective gene allows ALS patients to live considerably longer than patients with an intact gene. This opens up for development of treatment for this currently untreatable disease.

References

  1. ↑ Ephnomenclaturecommittee (Sep 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.
  2. ↑ 2.0 2.1 "Entrez Gene: EPHA4 EPH receptor A4".

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.
  • 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. PMID 10207129.
  • Wilkinson DG (2000). "Eph receptors and ephrins: regulators of guidance and assembly; Chapter: Eph receptors and ephrins: Regulators of guidance and assembly". Int. Rev. Cytol. International Review of Cytology. 196: 177–244. doi:10.1016/S0074-7696(00)96005-4. ISBN 978-0-12-364600-2. PMID 10730216.
  • 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.
  • Fox GM, Holst PL, Chute HT, et al. (1995). "cDNA cloning and tissue distribution of five human EPH-like receptor protein-tyrosine kinases". Oncogene. 10 (5): 897–905. PMID 7898931.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Ellis C, Kasmi F, Ganju P, et al. (1996). "A juxtamembrane autophosphorylation site in the Eph family receptor tyrosine kinase, Sek, mediates high affinity interaction with p59fyn". Oncogene. 12 (8): 1727–36. PMID 8622893.
  • 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.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Aasheim HC, Terstappen LW, Logtenberg T (1997). "Regulated expression of the Eph-related receptor tyrosine kinase Hek11 in early human B lymphopoiesis". Blood. 90 (9): 3613–22. PMID 9345045.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Bergemann AD, Zhang L, Chiang MK, et al. (1998). "Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube". Oncogene. 16 (4): 471–80. doi:10.1038/sj.onc.1201557. PMID 9484836.
  • Janis LS, Cassidy RM, Kromer LF (1999). "Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum". J. Neurosci. 19 (12): 4962–71. PMID 10366629.


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