EIF2A

Eukaryotic translation initiation factor 2A (eIF2A) is a protein that in humans is encoded by the EIF2A gene.[5][6][7] The eIF2A protein is not to be confused with eIF2α, a subunit of the heterotrimeric eIF2 complex. Instead, eIF2A functions by a separate mechanism in eukaryotic translation.

EIF2A
Identifiers
Aliases	EIF2A, EIF-2A, MST089, MSTP004, MSTP089, CDA02, eukaryotic translation initiation factor 2A
External IDs	OMIM: 609234 MGI: 1098684 HomoloGene: 5969 GeneCards: EIF2A
Gene location (Human) Chr. Chromosome 3 (human)[1] Band 3q25.1 Start 150,546,678 bp[1] End 150,586,016 bp[1]
Gene location (Mouse) Chr. Chromosome 3 (mouse)[2] Band 3 D|3 28.58 cM Start 58,525,821 bp[2] End 58,557,501 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • ribosome binding • tRNA binding • GO:0001948 protein binding • translation initiation factor activity • mRNA binding • cadherin binding Cellular component • cytoplasm • eukaryotic translation initiation factor 2 complex • blood microparticle • extracellular • cytosolic small ribosomal subunit Biological process • translational initiation • protein phosphorylation • SREBP signaling pathway • positive regulation of signal transduction • ribosome assembly • regulation of translation • protein biosynthesis • response to amino acid starvation Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	83939	229317
Ensembl	ENSG00000144895	ENSMUSG00000027810
UniProt	Q9BY44	Q8BJW6
RefSeq (mRNA)	NM_032025 NM_001319043 NM_001319044 NM_001319045 NM_001319046	NM_001005509
RefSeq (protein)	NP_001305972 NP_001305973 NP_001305974 NP_001305975 NP_114414	NP_001005509
Location (UCSC)	Chr 3: 150.55 – 150.59 Mb	Chr 3: 58.53 – 58.56 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

eIF2A is a 65 kDa protein that catalyzes the formation of puromycin-sensitive 80S preinitiation complexes (Zoll et al., 2002).[supplied by OMIM][7] It may be important for translation initiation mediated by the HCV IRES under stress conditions, but this result has been debated.[8][9]

See also

• eIF2

References

1. GRCh38: Ensembl release 89: ENSG00000144895 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000027810 - 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. Zoll WL, Horton LE, Komar AA, Hensold JO, Merrick WC (Oct 2002). "Characterization of mammalian eIF2A and identification of the yeast homolog". The Journal of Biological Chemistry. 277 (40): 37079–87. doi:10.1074/jbc.M207109200. PMID 12133843.
6. Merrick WC (Jun 1992). "Mechanism and regulation of eukaryotic protein synthesis". Microbiological Reviews. 56 (2): 291–315. PMC 372869. PMID 1620067.
7. "Entrez Gene: EIF2A eukaryotic translation initiation factor 2A, 38kDa".
8. Kim JH, Park SM, Park JH, Keum SJ, Jang SK (Jun 2011). "eIF2A mediates translation of hepatitis C viral mRNA under stress conditions". The EMBO Journal. 30 (12): 2454–64. doi:10.1038/emboj.2011.146. PMC 3116280. PMID 21556050.
9. Jaafar ZA, Oguro A, Nakamura Y, Kieft JS (December 2016). "Translation initiation by the hepatitis C virus IRES requires eIF1A and ribosomal complex remodeling". eLife. 5: e21198. doi:10.7554/elife.21198. PMC 5238962. PMID 28009256.

Further reading

• Koumenis C, Naczki C, Koritzinsky M, Rastani S, Diehl A, Sonenberg N, Koromilas A, Wouters BG (Nov 2002). "Regulation of protein synthesis by hypoxia via activation of the endoplasmic reticulum kinase PERK and phosphorylation of the translation initiation factor eIF2alpha". Molecular and Cellular Biology. 22 (21): 7405–16. doi:10.1128/MCB.22.21.7405-7416.2002. PMC 135664. PMID 12370288.
• Page AB, Owen CR, Kumar R, Miller JM, Rafols JA, White BC, DeGracia DJ, Krause GS (Jul 2003). "Persistent eIF2alpha(P) is colocalized with cytoplasmic cytochrome c in vulnerable hippocampal neurons after 4 hours of reperfusion following 10-minute complete brain ischemia". Acta Neuropathologica. 106 (1): 8–16. doi:10.1007/s00401-003-0693-2. PMID 12687390.
• Ito T, Marintchev A, Wagner G (Sep 2004). "Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B". Structure. 12 (9): 1693–704. doi:10.1016/j.str.2004.07.010. PMID 15341733.
• Weiser DC, Sikes S, Li S, Shenolikar S (Nov 2004). "The inhibitor-1 C terminus facilitates hormonal regulation of cellular protein phosphatase-1: functional implications for inhibitor-1 isoforms". The Journal of Biological Chemistry. 279 (47): 48904–14. doi:10.1074/jbc.M404416200. PMID 15345721.
• Komar AA, Gross SR, Barth-Baus D, Strachan R, Hensold JO, Goss Kinzy T, Merrick WC (Apr 2005). "Novel characteristics of the biological properties of the yeast Saccharomyces cerevisiae eukaryotic initiation factor 2A". The Journal of Biological Chemistry. 280 (16): 15601–11. doi:10.1074/jbc.M413728200. PMID 15718232.
• Wang J, Laschinger C, Zhao XH, Mak B, Seth A, McCulloch CA (Apr 2005). "Mechanical force activates eIF-2alpha phospho-kinases in fibroblast". Biochemical and Biophysical Research Communications. 330 (1): 123–30. doi:10.1016/j.bbrc.2005.02.140. PMID 15781241.
• Gorrini C, Loreni F, Gandin V, Sala LA, Sonenberg N, Marchisio PC, Biffo S (Jun 2005). "Fibronectin controls cap-dependent translation through beta1 integrin and eukaryotic initiation factors 4 and 2 coordinated pathways". Proceedings of the National Academy of Sciences of the United States of America. 102 (26): 9200–5. doi:10.1073/pnas.0409513102. PMC 1166589. PMID 15961545.
• Su Q, Wang S, Baltzis D, Qu LK, Wong AH, Koromilas AE (Jan 2006). "Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase". Proceedings of the National Academy of Sciences of the United States of America. 103 (1): 63–8. doi:10.1073/pnas.0508207103. PMC 1324992. PMID 16373505.
• Squatrito M, Mancino M, Sala L, Draetta GF (Jun 2006). "Ebp1 is a dsRNA-binding protein associated with ribosomes that modulates eIF2alpha phosphorylation". Biochemical and Biophysical Research Communications. 344 (3): 859–68. doi:10.1016/j.bbrc.2006.03.205. PMID 16631606.
• Scheuner D, Patel R, Wang F, Lee K, Kumar K, Wu J, Nilsson A, Karin M, Kaufman RJ (Jul 2006). "Double-stranded RNA-dependent protein kinase phosphorylation of the alpha-subunit of eukaryotic translation initiation factor 2 mediates apoptosis". The Journal of Biological Chemistry. 281 (30): 21458–68. doi:10.1074/jbc.M603784200. PMID 16717090.
• Mazroui R, Sukarieh R, Bordeleau ME, Kaufman RJ, Northcote P, Tanaka J, Gallouzi I, Pelletier J (Oct 2006). "Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylation". Molecular Biology of the Cell. 17 (10): 4212–9. doi:10.1091/mbc.E06-04-0318. PMC 1635342. PMID 16870703.
• Fribley AM, Evenchik B, Zeng Q, Park BK, Guan JY, Zhang H, Hale TJ, Soengas MS, Kaufman RJ, Wang CY (Oct 2006). "Proteasome inhibitor PS-341 induces apoptosis in cisplatin-resistant squamous cell carcinoma cells by induction of Noxa". The Journal of Biological Chemistry. 281 (42): 31440–7. doi:10.1074/jbc.M604356200. PMID 16928686.
• Fritsch RM, Schneider G, Saur D, Scheibel M, Schmid RM (Aug 2007). "Translational repression of MCL-1 couples stress-induced eIF2 alpha phosphorylation to mitochondrial apoptosis initiation". The Journal of Biological Chemistry. 282 (31): 22551–62. doi:10.1074/jbc.M702673200. PMID 17553788.
• Nayak R, Pintel DJ (Nov 2007). "Adeno-associated viruses can induce phosphorylation of eIF2alpha via PKR activation, which can be overcome by helper adenovirus type 5 virus-associated RNA". Journal of Virology. 81 (21): 11908–16. doi:10.1128/JVI.01132-07. PMC 2168773. PMID 17715234.