EPH receptor A1

EPHA1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2K1K, 2K1L, 3HIL, 3KKA
Identifiers
Aliases	EPHA1, Epha1, 5730453L17Rik, AL033318, Eph, Esk, EPHT, EPHT1, EPH receptor A1, EPH
External IDs	OMIM: 179610 MGI: 107381 HomoloGene: 3835 GeneCards: EPHA1
Gene location (Human)
Chr.	Chromosome 7 (human)
End	143,408,856 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	42,350,202 bp
RNA expression pattern
	Top expressed in
	skin of abdomen; ; right uterine tube; ; right lobe of liver; ; minor salivary gland; ; vagina; ; left lobe of thyroid gland; ; right lung; ; right lobe of thyroid gland; ; body of stomach; ; upper lobe of left lung;
	Top expressed in
	lip; ; esophagus; ; female urethra; ; ascending aorta; ; male urethra; ; jejunum; ; duodenum; ; aortic valve; ; yolk sac; ; proximal tubule;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity; protein kinase activity; nucleotide binding; transmembrane-ephrin receptor activity; kinase activity; transmembrane receptor protein tyrosine kinase activity; protein tyrosine kinase activity; ATP binding; protein kinase binding; ephrin receptor activity; receptor tyrosine kinase; transmembrane signaling receptor activity;
Cellular component	integral component of membrane; membrane; plasma membrane; integral component of plasma membrane; cytoplasm; neuron projection; receptor complex;
Biological process	somatic stem cell population maintenance; negative regulation of protein kinase activity; activation of GTPase activity; phosphorylation; transmembrane receptor protein tyrosine kinase signaling pathway; positive regulation of cell-matrix adhesion; positive regulation of cell migration; regulation of GTPase activity; positive regulation of angiogenesis; protein phosphorylation; cell surface receptor signaling pathway; negative regulation of cell migration; cell adhesion; angiogenesis; positive regulation of cell population proliferation; protein autophosphorylation; peptidyl-tyrosine phosphorylation; substrate adhesion-dependent cell spreading; positive regulation of stress fiber assembly; ephrin receptor signaling pathway; 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
	2041
	13835
	ENSG00000146904; ENSG00000284816
	ENSMUSG00000029859
	P21709
	Q60750
	NM_005232
	NM_023580
	NP_005223
	NP_076069
	Wikidata
View/Edit Human	View/Edit Mouse

EPH receptor A1 (ephrin type-A receptor 1) is a protein that in humans is encoded by the EPHA1 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. This gene is expressed in some human cancer cell lines and has been implicated in carcinogenesis.^[6]

References

1 2 3 ENSG00000284816 GRCh38: Ensembl release 89: ENSG00000146904, ENSG00000284816 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029859 - 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.
1 2 "Entrez Gene: EPHA1 EPH receptor A1".

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 9780123646002. 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.
Hirai H, Maru Y, Hagiwara K, et al. (1988). "A novel putative tyrosine kinase receptor encoded by the eph gene". Science. 238 (4834): 1717–20. doi:10.1126/science.2825356. PMID 2825356.
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.
Owshalimpur D, Kelley MJ (1999). "Genomic structure of the EPHA1 receptor tyrosine kinase gene". Mol. Cell. Probes. 13 (3): 169–73. doi:10.1006/mcpr.1999.0228. PMID 10369740.
Kalo MS, Pasquale EB (October 1999). "Signal transfer by eph receptors". Cell and Tissue Research. 298 (1): 1–9. doi:10.1007/pl00008807. PMID 10502115. S2CID 1241074.
Coulthard MG, Lickliter JD, Subanesan N, et al. (2002). "Characterization of the Epha1 receptor tyrosine kinase: expression in epithelial tissues". Growth Factors. 18 (4): 303–17. doi:10.3109/08977190109029118. PMID 11519828. S2CID 43039239.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.

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[refGRCh38Ensembl-1] 1 2 3 ENSG00000284816 GRCh38: Ensembl release 89: ENSG00000146904, ENSG00000284816 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029859 - 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] 1 2 "Entrez Gene: EPHA1 EPH receptor A1".

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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)

References

Further reading