EPH receptor A1

Protein-coding gene in the species Homo sapiens
EPHA1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2K1K, 2K1L, 3HIL, 3KKA

Identifiers
AliasesEPHA1, Epha1, 5730453L17Rik, AL033318, Eph, Esk, EPHT, EPHT1, EPH receptor A1, EPH
External IDsOMIM: 179610; MGI: 107381; HomoloGene: 3835; GeneCards: EPHA1; OMA:EPHA1 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for EPHA1
Genomic location for EPHA1
Band7q34-q35Start143,390,289 bp[1]
End143,408,856 bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for EPHA1
Genomic location for EPHA1
Band6|6 B2.1Start42,335,421 bp[2]
End42,350,202 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • skin of leg

  • skin of abdomen

  • right uterine tube

  • right lobe of liver

  • minor salivary glands

  • vagina

  • left lobe of thyroid gland

  • ectocervix

  • mucosa of transverse colon

  • right lung
Top expressed in
  • lip

  • tail of embryo

  • esophagus

  • embryo

  • epiblast

  • female urethra

  • right kidney

  • ascending aorta

  • male urethra

  • genital tubercle
More reference expression data
BioGPS
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
SpeciesHumanMouse
Entrez

2041

13835

Ensembl

ENSG00000146904
ENSG00000284816

ENSMUSG00000029859

UniProt

P21709

Q60750

RefSeq (mRNA)

NM_005232

NM_023580

RefSeq (protein)

NP_005223

NP_076069

Location (UCSC)Chr 7: 143.39 – 143.41 MbChr 6: 42.34 – 42.35 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c ENSG00000284816 GRCh38: Ensembl release 89: ENSG00000146904, ENSG00000284816 – Ensembl, May 2017
  2. ^ a b c 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.
  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.
  6. ^ a b "Entrez Gene: EPHA1 EPH receptor A1".

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 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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  • 1x5a: The solution structure of the second fibronectin type III domain of mouse Ephrin type-A receptor 1
    1x5a: The solution structure of the second fibronectin type III domain of mouse Ephrin type-A receptor 1
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Growth factor receptors
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