Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa, also known as EIF2S1, 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]
The translation initiation factor eIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, eIF2, and GTP. eIF2 is composed of 3 nonidentical subunits, alpha (36 kD), beta (38 kD, MIM 603908), and gamma (52 kD, MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of eIF2-alpha (Ernst et al. , 1987). [supplied by OMIM][1]
References
Further reading
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- Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank. ". Gene 150 (2): 243–50. PMID 7821789.
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- Dever TE, Chen JJ, Barber GN, et al. (1993). "Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast. ". Proc. Natl. Acad. Sci. U. S. A. 90 (10): 4616–20. PMID 8099443.
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- Ting NS, Kao PN, Chan DW, et al. (1998). "DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. ". J. Biol. Chem. 273 (4): 2136–45. PMID 9442054.
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