EPH receptor A4

EPHA4
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2LW8, 2WO1, 2WO2, 2WO3, 3CKH, 3GXU, 4BK4, 4BK5, 4BKA, 4BKF, 4M4P, 4M4R, 4W4Z, 4W50, 5JR2
Identifiers
Aliases	EPHA4, Epha4, 2900005C20Rik, AI385584, Cek8, Hek8, Sek, Sek1, Tyro1, rb, EPH receptor A4, HEK8, SEK, TYRO1, EK8
External IDs	MGI: 98277 HomoloGene: 20933 GeneCards: EPHA4
Gene location (Human)
Chr.	Chromosome 2 (human)[1]
End	221,574,202 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	77,515,088 bp[2]
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• transferase activity; • protein kinase activity; • nucleotide binding; • GPI-linked ephrin receptor activity; • ephrin receptor binding; • DH domain binding; • transmembrane-ephrin receptor activity; • kinase activity; • protein binding; • identical protein binding; • transmembrane receptor protein tyrosine kinase activity; • PH domain binding; • protein tyrosine kinase activity; • ATP binding; • ephrin receptor activity;
Cellular component	• cytoplasm; • axon terminus; • integral component of membrane; • cell body; • perikaryon; • postsynaptic membrane; • Golgi apparatus; • endosome; • cell projection; • early endosome membrane; • membrane; • postsynaptic density; • filopodium; • neuromuscular junction; • plasma membrane; • dendritic spine; • axonal growth cone; • integral component of plasma membrane; • synapse; • cell surface; • mitochondrial outer membrane; • cell junction; • axon; • dendrite; • early endosome; • endoplasmic reticulum;
Biological process	• negative regulation of axon regeneration; • fasciculation of motor neuron axon; • phosphorylation; • transmembrane receptor protein tyrosine kinase signaling pathway; • positive regulation of JUN kinase activity; • regulation of GTPase activity; • nervous system development; • regulation of axonogenesis; • multicellular organism development; • protein phosphorylation; • regulation of astrocyte differentiation; • cell adhesion; • positive regulation of dendrite morphogenesis; • nephric duct morphogenesis; • protein autophosphorylation; • corticospinal tract morphogenesis; • peptidyl-tyrosine phosphorylation; • fasciculation of sensory neuron axon; • motor neuron axon guidance; • positive regulation of Rho guanyl-nucleotide exchange factor activity; • regulation of dendritic spine morphogenesis; • glial cell migration; • adult walking behavior; • axon guidance; • ephrin receptor signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	2043
	13838
	ENSG00000116106
	ENSMUSG00000026235
	P54764
	Q03137
	NM_001304536; NM_001304537; NM_004438; NM_001363748
	NM_007936
	NP_001291465; NP_001291466; NP_004429; NP_001350677
	NP_031962
	Wikidata
View/Edit Human	View/Edit Mouse

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

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 2 3 GRCh38: Ensembl release 89: ENSG00000116106 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026235 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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.
1 2 "Entrez Gene: EPHA4 EPH receptor A4".

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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000116106 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026235 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[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.

[entrez-6] 1 2 "Entrez Gene: EPHA4 EPH receptor A4".

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme 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)

EPH receptor A4

References

Further reading