EPH receptor A2: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''EPH receptor A2''' ('''ephrin type-A receptor 2''') is a [[protein]] that in humans is encoded by the ''EPHA2'' [[gene]].<ref name="pmid9119409">{{cite journal | vauthors = Sulman EP, Tang XX, Allen C, Biegel JA, Pleasure DE, Brodeur GM, Ikegaki N | title = ECK, a human EPH-related gene, maps to 1p36.1, a common region of alteration in human cancers | journal = Genomics | volume = 40 | issue = 2 | pages = 371–4  | date = April 1997 | pmid = 9119409 | pmc = | doi = 10.1006/geno.1996.4569 }}</ref><ref name="entrez"/>
| update_page = yes
| require_manual_inspection = no
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_EPHA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mqb.
| PDB = {{PDB2|1mqb}}
| Name = EPH receptor A2
| HGNCid = 3386
| Symbol = EPHA2
| AltSymbols =; ECK
| OMIM = 176946
| ECnumber = 
| Homologene = 20929
| MGIid = 95278
| GeneAtlas_image1 = PBB_GE_EPHA2_203499_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: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}} {{GNF_GO|id=GO:0016021 |text = integral to 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:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0030182 |text = neuron differentiation}} {{GNF_GO|id=GO:0048013 |text = ephrin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1969
    | Hs_Ensembl = ENSG00000142627
    | Hs_RefseqProtein = NP_004422
    | Hs_RefseqmRNA = NM_004431
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 16323419
    | Hs_GenLoc_end = 16355169
    | Hs_Uniprot = P29317
    | Mm_EntrezGene = 13836
    | Mm_Ensembl = ENSMUSG00000006445
    | Mm_RefseqmRNA = XM_982454
    | Mm_RefseqProtein = XP_987548
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 140573316
    | Mm_GenLoc_end = 140601454
    | Mm_Uniprot = Q3UNI2
  }}
}}
'''EPH receptor A2''', also known as '''EPHA2''', is a human [[gene]].<ref>{{cite web | title = Entrez Gene: EPHA2 EPH receptor A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1969| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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. This gene encodes a protein that binds ephrin-A ligands.<ref name="entrez">{{cite web | title = Entrez Gene: EPHA2 EPH receptor A2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1969| accessdate = }}</ref>
{{PBB_Summary
| 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. This gene encodes a protein that binds ephrin-A ligands.<ref name="entrez">{{cite web | title = Entrez Gene: EPHA2 EPH receptor A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1969| accessdate = }}</ref>
}}


==References==
==Clinical significance==
{{reflist|2}}
It may be implicated in BRAF mutated melanomas becoming resistant to BRAF-inhibitors and [[MEK inhibitor]]s.<ref>{{cite web |url=http://www.oncotherapynetwork.com/skin-cancer-melanoma-targets/counteracting-drug-resistance-melanoma |title=Counteracting Drug Resistance in Melanoma |year=2015 }}</ref> It also the receptor by which [[Kaposi sarcoma-associated herpesvirus]] (KSHV) enters host cells and small molecule inhibitors of EphA2 have shown some ability to block KSHV entry into human cells.<ref>{{cite journal | vauthors = Hahn AS, Kaufmann JK, Wies E, Naschberger E, Panteleev-Ivlev J, Schmidt K, Holzer A, Schmidt M, Chen J, König S, Ensser A, Myoung J, Brockmeyer NH, Stürzl M, Fleckenstein B, Neipel F | title = The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's sarcoma–associated herpesvirus | journal = Nat. Med. | volume = 18 | issue = 6 | pages = 961–6 | year = 2012 | pmid = 22635007 | pmc = 3645317 | doi = 10.1038/nm.2805 }}</ref>
 
== Interactions ==
 
EPH receptor A2 has been shown to [[Protein-protein interaction|interact]] with:
* [[ACP1]]<ref name = pmid12167657>{{cite journal | vauthors = Kikawa KD, Vidale DR, Van Etten RL, Kinch MS | title = Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation | journal = J. Biol. Chem. | volume = 277 | issue = 42 | pages = 39274–9  | date = October 2002 | pmid = 12167657 | doi = 10.1074/jbc.M207127200 }}</ref>
* [[Grb2]],<ref name = pmid12400011>{{cite journal | vauthors = Pratt RL, Kinch MS | title = Activation of the EphA2 tyrosine kinase stimulates the MAP/ERK kinase signaling cascade | journal = Oncogene | volume = 21 | issue = 50 | pages = 7690–9  | date = October 2002 | pmid = 12400011 | doi = 10.1038/sj.onc.1205758 }}</ref>
* [[PIK3R1]],<ref name = pmid7982920>{{cite journal | vauthors = Pandey A, Lazar DF, Saltiel AR, Dixit VM | title = Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity | journal = J. Biol. Chem. | volume = 269 | issue = 48 | pages = 30154–7  | date = December 1994 | pmid = 7982920 | doi =  }}</ref>  and
* [[SHC1]].<ref name = pmid12400011/>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 }}
| citations =
* {{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=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 = 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=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 | 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=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 = 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 = 2000 | pmid = 11128993 | pmc = 1692797 | doi = 10.1098/rstb.2000.0635 }}
*{{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 = 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=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 = Kinch MS, Carles-Kinch K | title = Overexpression and functional alterations of the EphA2 tyrosine kinase in cancer | journal = Clin. Exp. Metastasis | volume = 20 | issue = 1 | pages = 59–68 | year = 2003 | pmid = 12650608 | doi = 10.1023/A:1022546620495 }}
*{{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 = Walker-Daniels J, Hess AR, Hendrix MJ, Kinch MS | title = Differential regulation of EphA2 in normal and malignant cells | journal = Am. J. Pathol. | volume = 162 | issue = 4 | pages = 1037–42 | year = 2003 | pmid = 12651595 | pmc = 1851246 | doi = 10.1016/S0002-9440(10)63899-0 }}
*{{cite journal | author=Kinch MS, Carles-Kinch K |title=Overexpression and functional alterations of the EphA2 tyrosine kinase in cancer. |journal=Clin. Exp. Metastasis |volume=20 |issue= 1 |pages= 59-68 |year= 2003 |pmid= 12650608 |doi= }}
* {{cite journal | vauthors = Lindberg RA, Hunter T | title = cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases | journal = Mol. Cell. Biol. | volume = 10 | issue = 12 | pages = 6316–24 | year = 1990 | pmid = 2174105 | pmc = 362907 | doi =  }}
*{{cite journal | author=Walker-Daniels J, Hess AR, Hendrix MJ, Kinch MS |title=Differential regulation of EphA2 in normal and malignant cells. |journal=Am. J. Pathol. |volume=162 |issue= 4 |pages= 1037-42 |year= 2003 |pmid= 12651595 |doi= }}
* {{cite journal | vauthors = Pandey A, Shao H, Marks RM, Polverini PJ, Dixit VM | title = Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-alpha-induced angiogenesis | journal = Science | volume = 268 | issue = 5210 | pages = 567–9 | year = 1995 | pmid = 7536959 | doi = 10.1126/science.7536959 }}
*{{cite journal | author=Lindberg RA, Hunter T |title=cDNA cloning and characterization of eck, an epithelial cell receptor protein-tyrosine kinase in the eph/elk family of protein kinases. |journal=Mol. Cell. Biol. |volume=10 |issue= 12 |pages= 6316-24 |year= 1991 |pmid= 2174105 |doi=  }}
* {{cite journal | vauthors = Pandey A, Duan H, Dixit VM | title = Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase | journal = J. Biol. Chem. | volume = 270 | issue = 33 | pages = 19201–4 | year = 1995 | pmid = 7543898 | doi = 10.1074/jbc.270.33.19201 }}
*{{cite journal | author=Pandey A, Shao H, Marks RM, ''et al.'' |title=Role of B61, the ligand for the Eck receptor tyrosine kinase, in TNF-alpha-induced angiogenesis. |journal=Science |volume=268 |issue= 5210 |pages= 567-9 |year= 1995 |pmid= 7536959 |doi= }}
* {{cite journal | vauthors = Ruiz JC, Robertson EJ | title = The expression of the receptor-protein tyrosine kinase gene, eck, is highly restricted during early mouse development | journal = Mech. Dev. | volume = 46 | issue = 2 | pages = 87–100 | year = 1994 | pmid = 7918100 | doi = 10.1016/0925-4773(94)90078-7 }}
*{{cite journal | author=Pandey A, Duan H, Dixit VM |title=Characterization of a novel Src-like adapter protein that associates with the Eck receptor tyrosine kinase. |journal=J. Biol. Chem. |volume=270 |issue= 33 |pages= 19201-4 |year= 1995 |pmid= 7543898 |doi= }}
* {{cite journal | vauthors = Davis S, Gale NW, Aldrich TH, Maisonpierre PC, Lhotak V, Pawson T, Goldfarb M, Yancopoulos GD | title = Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity | journal = Science | volume = 266 | issue = 5186 | pages = 816–9 | year = 1994 | pmid = 7973638 | doi = 10.1126/science.7973638 }}
*{{cite journal | author=Ruiz JC, Robertson EJ |title=The expression of the receptor-protein tyrosine kinase gene, eck, is highly restricted during early mouse development. |journal=Mech. Dev. |volume=46 |issue= 2 |pages= 87-100 |year= 1994 |pmid= 7918100 |doi= }}
* {{cite journal | vauthors = Pandey A, Lazar DF, Saltiel AR, Dixit VM | title = Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity | journal = J. Biol. Chem. | volume = 269 | issue = 48 | pages = 30154–7 | year = 1994 | pmid = 7982920 | doi =  }}
*{{cite journal | author=Davis S, Gale NW, Aldrich TH, ''et al.'' |title=Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity. |journal=Science |volume=266 |issue= 5186 |pages= 816-9 |year= 1994 |pmid= 7973638 |doi= }}
* {{cite journal | vauthors = Ganju P, Shigemoto K, Brennan J, Entwistle A, Reith AD | title = The Eck receptor tyrosine kinase is implicated in pattern formation during gastrulation, hindbrain segmentation and limb development | journal = Oncogene | volume = 9 | issue = 6 | pages = 1613–24 | year = 1994 | pmid = 8183555 | doi =  }}
*{{cite journal | author=Pandey A, Lazar DF, Saltiel AR, Dixit VM |title=Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity. |journal=J. Biol. Chem. |volume=269 |issue= 48 |pages= 30154-7 |year= 1994 |pmid= 7982920 |doi=  }}
* {{cite journal | vauthors = Gale NW, Holland SJ, Valenzuela DM, Flenniken A, Pan L, Ryan TE, Henkemeyer M, Strebhardt K, Hirai H, Wilkinson DG, Pawson T, Davis S, Yancopoulos GD | 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 }}
*{{cite journal | author=Ganju P, Shigemoto K, Brennan J, ''et al.'' |title=The Eck receptor tyrosine kinase is implicated in pattern formation during gastrulation, hindbrain segmentation and limb development. |journal=Oncogene |volume=9 |issue= 6 |pages= 1613-24 |year= 1994 |pmid= 8183555 |doi=  }}
* {{cite journal | vauthors = Kozlosky CJ, VandenBos T, Park L, Cerretti DP, Carpenter MK | title = LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain | journal = Cytokine | volume = 9 | issue = 8 | pages = 540–9 | year = 1997 | pmid = 9245480 | doi = 10.1006/cyto.1997.0199 }}
*{{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 = 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=Sulman EP, Tang XX, Allen C, ''et al.'' |title=ECK, a human EPH-related gene, maps to 1p36.1, a common region of alteration in human cancers. |journal=Genomics |volume=40 |issue= 2 |pages= 371-4 |year= 1997 |pmid= 9119409 |doi= 10.1006/geno.1996.4569 }}
*{{cite journal | author=Kozlosky CJ, VandenBos T, Park L, ''et al.'' |title=LERK-7: a ligand of the Eph-related kinases is developmentally regulated in the brain. |journal=Cytokine |volume=9 |issue= 8 |pages= 540-9 |year= 1997 |pmid= 9245480 |doi= 10.1006/cyto.1997.0199 }}
*{{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= }}
}}
{{refend}}
{{refend}}


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Revision as of 05:01, 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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EPH receptor A2 (ephrin type-A receptor 2) is a protein that in humans is encoded by the EPHA2 gene.[1][2]

Function

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. This gene encodes a protein that binds ephrin-A ligands.[2]

Clinical significance

It may be implicated in BRAF mutated melanomas becoming resistant to BRAF-inhibitors and MEK inhibitors.[3] It also the receptor by which Kaposi sarcoma-associated herpesvirus (KSHV) enters host cells and small molecule inhibitors of EphA2 have shown some ability to block KSHV entry into human cells.[4]

Interactions

EPH receptor A2 has been shown to interact with:

References

  1. ↑ Sulman EP, Tang XX, Allen C, Biegel JA, Pleasure DE, Brodeur GM, Ikegaki N (April 1997). "ECK, a human EPH-related gene, maps to 1p36.1, a common region of alteration in human cancers". Genomics. 40 (2): 371–4. doi:10.1006/geno.1996.4569. PMID 9119409.
  2. ↑ 2.0 2.1 "Entrez Gene: EPHA2 EPH receptor A2".
  3. ↑ "Counteracting Drug Resistance in Melanoma". 2015.
  4. ↑ Hahn AS, Kaufmann JK, Wies E, Naschberger E, Panteleev-Ivlev J, Schmidt K, Holzer A, Schmidt M, Chen J, König S, Ensser A, Myoung J, Brockmeyer NH, Stürzl M, Fleckenstein B, Neipel F (2012). "The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's sarcoma–associated herpesvirus". Nat. Med. 18 (6): 961–6. doi:10.1038/nm.2805. PMC 3645317. PMID 22635007.
  5. ↑ Kikawa KD, Vidale DR, Van Etten RL, Kinch MS (October 2002). "Regulation of the EphA2 kinase by the low molecular weight tyrosine phosphatase induces transformation". J. Biol. Chem. 277 (42): 39274–9. doi:10.1074/jbc.M207127200. PMID 12167657.
  6. ↑ 6.0 6.1 Pratt RL, Kinch MS (October 2002). "Activation of the EphA2 tyrosine kinase stimulates the MAP/ERK kinase signaling cascade". Oncogene. 21 (50): 7690–9. doi:10.1038/sj.onc.1205758. PMID 12400011.
  7. ↑ Pandey A, Lazar DF, Saltiel AR, Dixit VM (December 1994). "Activation of the Eck receptor protein tyrosine kinase stimulates phosphatidylinositol 3-kinase activity". J. Biol. Chem. 269 (48): 30154–7. PMID 7982920.

Further reading


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