EPHA7: Difference between revisions

EPHA7
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2REI, 3DKO, 3H8M, 3NRU
Identifiers
Aliases	EPHA7, EHK-3, EHK3, EK11, HEK11, EPH receptor A7
External IDs	OMIM: 602190; MGI: 95276; HomoloGene: 20935; GeneCards: EPHA7; OMA:EPHA7 - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	93,419,559 bp
Gene location (Mouse)
Chr.	Chromosome 4 (mouse)
End	28,967,499 bp
RNA expression pattern
	Top expressed in
	endothelial cell; ; Brodmann area 23; ; middle temporal gyrus; ; muscle layer of sigmoid colon; ; ganglionic eminence; ; ventricular zone; ; caput epididymis; ; primary visual cortex; ; gastric mucosa; ; epithelium of colon;
	Top expressed in
	vestibular membrane of cochlear duct; ; dentate gyrus; ; Region I of hippocampus proper; ; hippocampus proper; ; dentate gyrus of hippocampal formation granule cell; ; CA3 field; ; genital tubercle; ; atrioventricular valve; ; habenula; ; atrium;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; nucleotide binding; protein kinase activity; GPI-linked ephrin receptor activity; ephrin receptor binding; kinase activity; protein binding; transmembrane receptor protein tyrosine kinase activity; protein tyrosine kinase activity; ATP binding; axon guidance receptor activity; ephrin receptor activity; chemorepellent activity; receptor tyrosine kinase; transmembrane signaling receptor activity; transmembrane-ephrin receptor activity;
Cellular component	integral component of membrane; postsynaptic membrane; membrane; neuromuscular junction; plasma membrane; integral component of plasma membrane; soma; dendrite; Schaffer collateral - CA1 synapse; hippocampal mossy fiber to CA3 synapse; glutamatergic synapse; integral component of postsynaptic specialization membrane; integral component of postsynaptic density membrane; cytoplasm; neuron projection; receptor complex;
Biological process	apoptotic process; positive regulation of protein phosphorylation; regulation of protein autophosphorylation; phosphorylation; transmembrane receptor protein tyrosine kinase signaling pathway; ephrin receptor signaling pathway; negative regulation of synapse assembly; regulation of cysteine-type endopeptidase activity involved in apoptotic process; nervous system development; branching morphogenesis of a nerve; multicellular organism development; protein phosphorylation; negative regulation of collateral sprouting; positive regulation of neuron apoptotic process; brain development; nephric duct morphogenesis; regulation of cell-cell adhesion; regulation of ERK1 and ERK2 cascade; positive regulation of apoptotic process; peptidyl-tyrosine phosphorylation; regulation of peptidyl-tyrosine phosphorylation; retinal ganglion cell axon guidance; negative chemotaxis; regulation of postsynapse organization; negative regulation of signal transduction; cell differentiation; negative regulation of apoptotic process; positive regulation of ERK1 and ERK2 cascade; axon guidance;
	Sources:Amigo / QuickGO
Orthologs
	2045
	13841
	ENSG00000135333
	ENSMUSG00000028289
	Q15375
	Q61772
	NM_001288629; NM_001288630; NM_004440
	NM_001122889; NM_001290434; NM_010141
NP_001275558; NP_001275559; NP_004431; NP_001363394; NP_001363395;
	NP_001363396; NP_001363397; NP_001363398; NP_001363399; NP_001363400
	NP_001116361; NP_001277363; NP_034271
	Wikidata
View/Edit Human	View/Edit Mouse

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Latest revision as of 08:44, 24 December 2023

Ephrin type-A receptor 7 is a protein that in humans is encoded by the EPHA7 gene.^[5]^[6]

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.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000135333 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000028289 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. S2CID 26773768.
^ ^a ^b "Entrez Gene: EPHA7 EPH receptor A7".

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. doi:10.1242/dev.126.10.2033. PMID 10207129.
Wilkinson DG (2000). "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. S2CID 205014301.
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.
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. S2CID 1075856.
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.
Ciossek T, Ullrich A (1997). "Identification of Elf-1 and B61 as high affinity ligands for the receptor tyrosine kinase MDK1". Oncogene. 14 (1): 35–43. doi:10.1038/sj.onc.1200800. PMID 9010230. S2CID 24727040.
Hock B, Böhme B, Karn T, et al. (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. Bibcode:1998PNAS...95.9779H. doi:10.1073/pnas.95.17.9779. PMC 21413. PMID 9707552.
Bianchi LM, Liu H (1999). "Comparison of ephrin-A ligand and EphA receptor distribution in the developing inner ear". Anat. Rec. 254 (1): 127–34. doi:10.1002/(SICI)1097-0185(19990101)254:1<127::AID-AR16>3.0.CO;2-Q. PMID 9892426.
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. doi:10.1523/JNEUROSCI.19-12-04962.1999. PMC 6782661. PMID 10366629.
Stubbs J, Palmer A, Vidovic M, Marotte LR (2000). "Graded expression of EphA3 in the retina and ephrin-A2 in the superior colliculus during initial development of coarse topography in the wallaby retinocollicular projection". Eur. J. Neurosci. 12 (10): 3626–36. doi:10.1046/j.1460-9568.2000.00251.x. PMID 11029633. S2CID 37988439.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000135333 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000028289 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9267020-5] 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. S2CID 26773768.

[entrez-6] "Entrez Gene: EPHA7 EPH receptor A7".

[1]

[2]

[3]

[4]

[5]

[6]

@@ Line 1: / Line 1: @@
+{{cs1 config|name-list-style=vanc}}
-{{PBB|geneid=2045}}
+{{Short description|Protein-coding gene in the species Homo sapiens}}
-'''Ephrin type-A receptor 7''' is a [[protein]] that in humans is encoded by the ''EPHA7'' [[gene]].<ref name="pmid9267020">{{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 | month = Sep | pmid = 9267020 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPHA7 EPH receptor A7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2045| accessdate = }}</ref>
+{{Infobox_gene}}
+'''Ephrin type-A receptor 7''' is a [[protein]] that in humans is encoded by the ''EPHA7'' [[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 | doi =10.1016/S0092-8674(00)80500-0 | last1 =  Ephnomenclaturecommittee  | s2cid = 26773768 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: EPHA7 EPH receptor A7| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2045}}</ref>
+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" />
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
-{{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.<ref name="entrez">{{cite web | title = Entrez Gene: EPHA7 EPH receptor A7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2045| accessdate = }}</ref>
-}}
 ==References==
 {{reflist}}
 ==Further reading==
 {{refbegin | 2}}
+*{{cite journal  | vauthors=Flanagan JG, Vanderhaeghen P |title=The ephrins and Eph receptors in neural development |journal=Annu. Rev. Neurosci. |volume=21 |pages= 309–45 |year= 1998 |pmid= 9530499 |doi= 10.1146/annurev.neuro.21.1.309 }}
-{{PBB_Further_reading
+*{{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  }}
-| 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=Holder N, Klein R |title=Eph receptors and ephrins: effectors of morphogenesis |journal=Development |volume=126 |issue= 10 |pages= 2033–44 |year= 1999 |doi=10.1242/dev.126.10.2033 |pmid= 10207129 }}
-*{{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=Wilkinson DG |title=Eph receptors and ephrins: regulators of guidance and assembly |journal=Int. Rev. Cytol. |volume=196 |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=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= 2001 |pmid= 11128993 |doi= 10.1098/rstb.2000.0635  | pmc=1692797 }}
-*{{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=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  |s2cid=205014301 }}
-*{{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=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 |display-authors=etal}}
-*{{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  | 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  |s2cid=1075856 |display-authors=etal|doi-access=free }}
-*{{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=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  |doi-access=free }}
-*{{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=10.1016/S0896-6273(00)80276-7  }}
+*{{cite journal  | vauthors=Ciossek T, Ullrich A |title=Identification of Elf-1 and B61 as high affinity ligands for the receptor tyrosine kinase MDK1 |journal=Oncogene |volume=14 |issue= 1 |pages= 35–43 |year= 1997 |pmid= 9010230 |doi= 10.1038/sj.onc.1200800 |s2cid=24727040 |doi-access=  }}
-*{{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=10.1101/gr.6.9.791  }}
+*{{cite journal  | vauthors=Hock B, Böhme B, Karn T |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=10.1073/pnas.95.17.9779  | pmc=21413  |bibcode=1998PNAS...95.9779H |display-authors=etal|doi-access=free }}
-*{{cite journal  | author=Ciossek T, Ullrich A |title=Identification of Elf-1 and B61 as high affinity ligands for the receptor tyrosine kinase MDK1. |journal=Oncogene |volume=14 |issue= 1 |pages= 35–43 |year= 1997 |pmid= 9010230 |doi= 10.1038/sj.onc.1200800 }}
+*{{cite journal  | vauthors=Bianchi LM, Liu H |title=Comparison of ephrin-A ligand and EphA receptor distribution in the developing inner ear |journal=Anat. Rec. |volume=254 |issue= 1 |pages= 127–34 |year= 1999 |pmid= 9892426 |doi=10.1002/(SICI)1097-0185(19990101)254:1<127::AID-AR16>3.0.CO;2-Q  |doi-access=free }}
-*{{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=10.1073/pnas.95.17.9779  }}
+*{{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=  10.1523/JNEUROSCI.19-12-04962.1999|pmc=6782661 }}
-*{{cite journal  | author=Bianchi LM, Liu H |title=Comparison of ephrin-A ligand and EphA receptor distribution in the developing inner ear. |journal=Anat. Rec. |volume=254 |issue= 1 |pages= 127–34 |year= 1999 |pmid= 9892426 |doi=10.1002/(SICI)1097-0185(19990101)254:1<127::AID-AR16>3.0.CO;2-Q  }}
+*{{cite journal  | vauthors=Stubbs J, Palmer A, Vidovic M, Marotte LR |title=Graded expression of EphA3 in the retina and ephrin-A2 in the superior colliculus during initial development of coarse topography in the wallaby retinocollicular projection |journal=Eur. J. Neurosci. |volume=12 |issue= 10 |pages= 3626–36 |year= 2000 |pmid= 11029633 |doi=10.1046/j.1460-9568.2000.00251.x  |s2cid=37988439 }}
-*{{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=  }}
-*{{cite journal  | author=Stubbs J, Palmer A, Vidovic M, Marotte LR |title=Graded expression of EphA3 in the retina and ephrin-A2 in the superior colliculus during initial development of coarse topography in the wallaby retinocollicular projection. |journal=Eur. J. Neurosci. |volume=12 |issue= 10 |pages= 3626–36 |year= 2000 |pmid= 11029633 |doi=10.1046/j.1460-9568.2000.00251.x  }}
-}}
 {{refend}}
-{{gene-6-stub}}
 {{Tyrosine kinases}}
+{{Enzymes}}
+{{Growth factor receptor modulators}}
+{{Portal bar|Biology|border=no}}
+[[Category:Tyrosine kinase receptors]]
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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)