EIF2S3

Protein-coding gene in humans
EIF2S3
Identifiers
AliasesEIF2S3, EIF2, EIF2G, EIF2gamma, eIF-2gA, eukaryotic translation initiation factor 2 subunit gamma, MRXSBRK, MEHMO
External IDsOMIM: 300161; MGI: 1349431; HomoloGene: 90888; GeneCards: EIF2S3; OMA:EIF2S3 - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for EIF2S3
Genomic location for EIF2S3
BandXp22.11Start24,054,946 bp[1]
End24,078,810 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for EIF2S3
Genomic location for EIF2S3
BandX C3|X 41.52 cMStart93,232,313 bp[2]
End93,256,468 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • germinal epithelium

  • parietal pleura

  • skin of arm

  • visceral pleura

  • tibia

  • mucosa of ileum

  • monocyte

  • epithelium of nasopharynx

  • palpebral conjunctiva

  • epithelium of colon
Top expressed in
  • molar

  • maxillary prominence

  • genital tubercle

  • mandibular prominence

  • hand

  • epiblast

  • foot

  • ventricular zone

  • medial ganglionic eminence

  • atrium
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GTP binding
  • translation factor activity, RNA binding
  • protein binding
  • translation initiation factor activity
  • GTPase activity
  • cadherin binding
Cellular component
  • cytoplasm
  • cytosol
  • extracellular exosome
  • nucleus
  • eukaryotic translation initiation factor 2 complex
Biological process
  • translational initiation
  • transmembrane transport
  • protein biosynthesis
  • formation of translation preinitiation complex
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1968

26905

Ensembl

ENSG00000130741

ENSMUSG00000035150

UniProt

P41091

Q9Z0N1

RefSeq (mRNA)

NM_001415

NM_012010

RefSeq (protein)

NP_001406

NP_036140

Location (UCSC)Chr X: 24.05 – 24.08 MbChr X: 93.23 – 93.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Eukaryotic translation initiation factor 2 subunit 3 (eIF2γ) is a protein that in humans is encoded by the EIF2S3 gene.[5][6][7]

Function

Eukaryotic translation initiation factor 2 (eIF2) functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA and binding to a 40S ribosomal subunit. eIF2 is composed of three subunits, alpha (α), beta (β), and gamma (γ, this article), with the protein encoded by this gene representing the gamma subunit.[7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000130741 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000035150 – 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. ^ Gaspar NJ, Kinzy TG, Scherer BJ, Humbelin M, Hershey JW, Merrick WC (Mar 1994). "Translation initiation factor eIF-2. Cloning and expression of the human cDNA encoding the gamma-subunit". J Biol Chem. 269 (5): 3415–22. doi:10.1016/S0021-9258(17)41878-3. PMID 8106381.
  6. ^ Ehrmann IE, Ellis PS, Mazeyrat S, Duthie S, Brockdorff N, Mattei MG, Gavin MA, Affara NA, Brown GM, Simpson E, Mitchell MJ, Scott DM (Dec 1998). "Characterization of genes encoding translation initiation factor eIF-2gamma in mouse and human: sex chromosome localization, escape from X-inactivation and evolution". Hum Mol Genet. 7 (11): 1725–37. doi:10.1093/hmg/7.11.1725. PMID 9736774.
  7. ^ a b "Entrez Gene: EIF2S3 eukaryotic translation initiation factor 2, subunit 3 gamma, 52kDa".

Further reading

  • Ray MK, Chakraborty A, Datta B, et al. (1993). "Characteristics of the eukaryotic initiation factor 2 associated 67-kDa polypeptide". Biochemistry. 32 (19): 5151–9. doi:10.1021/bi00070a026. PMID 8098621.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Brand SR, Kobayashi R, Mathews MB (1997). "The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR". J. Biol. Chem. 272 (13): 8388–95. doi:10.1074/jbc.272.13.8388. PMID 9079663.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Cai R, Carpick B, Chun RF, et al. (2000). "HIV-I TAT inhibits PKR activity by both RNA-dependent and RNA-independent mechanisms". Arch. Biochem. Biophys. 373 (2): 361–7. doi:10.1006/abbi.1999.1583. PMID 10620360.
  • Ben-Asouli Y, Banai Y, Hauser H, Kaempfer R (2000). "Recognition of 5'-terminal TAR structure in human immunodeficiency virus-1 mRNA by eukaryotic translation initiation factor 2". Nucleic Acids Res. 28 (4): 1011–8. doi:10.1093/nar/28.4.1011. PMC 102579. PMID 10648795.
  • Kruger M, Beger C, Li QX, et al. (2000). "Identification of eIF2Bgamma and eIF2gamma as cofactors of hepatitis C virus internal ribosome entry site-mediated translation using a functional genomics approach". Proc. Natl. Acad. Sci. U.S.A. 97 (15): 8566–71. Bibcode:2000PNAS...97.8566K. doi:10.1073/pnas.97.15.8566. PMC 26988. PMID 10900014.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • Filippova GN, Cheng MK, Moore JM, et al. (2005). "Boundaries between chromosomal domains of X inactivation and escape bind CTCF and lack CpG methylation during early development". Dev. Cell. 8 (1): 31–42. doi:10.1016/j.devcel.2004.10.018. PMID 15669143.
  • Marques AC, Dupanloup I, Vinckenbosch N, et al. (2006). "Emergence of young human genes after a burst of retroposition in primates". PLOS Biol. 3 (11): e357. doi:10.1371/journal.pbio.0030357. PMC 1251493. PMID 16201836.
  • Suragani RN, Kamindla R, Ehtesham NZ, Ramaiah KV (2006). "Interaction of recombinant human eIF2 subunits with eIF2B and eIF2alpha kinases". Biochem. Biophys. Res. Commun. 338 (4): 1766–72. doi:10.1016/j.bbrc.2005.10.150. PMID 16288713.
  • Mikami S, Masutani M, Sonenberg N, et al. (2006). "An efficient mammalian cell-free translation system supplemented with translation factors". Protein Expr. Purif. 46 (2): 348–57. doi:10.1016/j.pep.2005.09.021. PMID 16289705.
  • Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell. Proteomics. 6 (4): 575–88. doi:10.1074/mcp.M600249-MCP200. PMID 17220478.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • v
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  • e
Proteins
Initiation factor
Bacterial
Mitochondrial
Archaeal
  • aIF1
  • aIF2
  • aIF5
  • aIF6
Eukaryotic
eIF1
eIF2
eIF3
eIF4
eIF5
eIF6
Elongation factor
Bacterial/​Mitochondrial
Archaeal/​Eukaryotic
Release factor
Ribosomal Proteins
Cytoplasmic
60S subunit
40S subunit
Mitochondrial
39S subunit
28S subunit
Other concepts


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