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Ephrin-A5
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| PDB rendering based on 1shw. The Protein Data Bank ( PDB) is a repository for 3-D structural data of Proteins and Nucleic acids These data typically obtained by X-ray crystallography | ||
| Available structures: 1shw, 1shx | ||
| Identifiers | ||
| Symbol(s) | EFNA5; AF1; EFL5; EPLG7; GLC1M; LERK7; RAGS | |
| External IDs | OMIM: 601535 MGI: 107444 HomoloGene: 1482 | |
| RNA expression pattern | ||
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| Orthologs | ||
| Human | Mouse | |
| Entrez | 1946 | 13640 |
| Ensembl | ENSG00000184349 | ENSMUSG00000048915 |
| Uniprot | P52803 | O08543 |
| Refseq | NM_001962 (mRNA) NP_001953 (protein) |
NM_010109 (mRNA) NP_034239 (protein) |
| Location | Chr 5: 106.74 - 107.03 Mb | Chr 17: 62.29 - 62.57 Mb |
| Pubmed search | [1] | [2] |
Ephrin-A5, also known as EFNA5, is a human gene. The Human Genome Organisation (HUGO is an organization involved in the Human Genome Project, a project about mapping the human genome The Mouse Genome Informatics (MGI website is run by The Jackson Laboratory. HomoloGene, a tool of the National Center for Biotechnology Information (NCBI is a system for automated detection of homologs (similarity attributable to descent The Entrez Global Query Cross-Database Search System is a powerful Federated search engine or Web portal that allows users to search many discrete Health sciences Ensembl is a joint scientific project between the European Bioinformatics Institute and the Wellcome Trust Sanger Institute, which was launched in 1999 in response to the imminent UniProt is the uni versal prot ein resource a central repository of Protein data created by combining Swiss-Prot, TrEMBL PubMed is a free search engine for accessing the MEDLINE database of citations and abstracts of biomedical research articles History See also History of genetics The existence of genes was first suggested by Gregor Mendel (1822-1884 who in the 1860s studied inheritance [1]
Ephrin-A5, a member of the ephrin gene family, prevents axon bundling in cocultures of cortical neurons with astrocytes, a model of late stage nervous system development and differentiation. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are similarly divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. [1]