EPHA7

Ephrin type-A receptor 7 is a protein that in humans is encoded by the EPHA7 gene.

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) Band 6q16.1 Start 93,240,020 bp End 93,419,559 bp
Gene location (Mouse) Chr. Chromosome 4 (mouse) Band 4 A4|4 12.42 cM Start 28,813,131 bp End 28,967,499 bp
RNA expression pattern Bgee Human Mouse (ortholog) 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 BioGPS 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 Species Human Mouse Entrez 2045 13841 Ensembl ENSG00000135333 ENSMUSG00000028289 UniProt Q15375 Q61772 RefSeq (mRNA) NM_001288629 NM_001288630 NM_004440 NM_001122889 NM_001290434 NM_010141 RefSeq (protein) 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 Location (UCSC) Chr 6: 93.24 – 93.42 Mb Chr 4: 28.81 – 28.97 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

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. 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.