EPHA7

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

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)[1] Band 6q16.1 Start 93,240,020 bp[1] End 93,419,559 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 A4|4 12.42 cM Start 28,813,131 bp[2] End 28,967,499 bp[2]
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 [3] [4]
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.^[6]