EIF2S3

Eukaryotic translation initiation factor 2, subunit 3 gamma, 52kDa

Identifiers

EIF2S3; EIF2; EIF2G; EIF2gamma

External IDs

OMIM: 300161 MGI: 1349431 HomoloGene: 37475 GeneCards: EIF2S3 Gene

Gene Ontology
Molecular function	• nucleotide binding • translation initiation factor activity • GTPase activity • GTP binding
Cellular component	• cytosolic small ribosomal subunit (sensu Eukaryota) • eukaryotic translation initiation factor 2 complex
Biological process	• translational initiation
Sources: Amigo / EGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr X:
23.98 - 24.01 Mb

Chr X:
90.44 - 90.47 Mb

PubMed search

[1]

[2]

Eukaryotic translation initiation factor 2 subunit 3 is a protein that in humans is encoded by the EIF2S3 gene.^[1]^[2]^[3]^[1]^[2]

1 Function
2 See also
3 References
4 Further reading

Function

Eukaryotic translation initiation factor 2 (EIF-2) 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. EIF-2 is composed of three subunits, alpha, beta, and gamma (this article), with the protein encoded by this gene representing the gamma subunit.^[3]

References

^ ^a ^b 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. PMID 8106381.
^ ^a ^b 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.
^ ^a ^b "Entrez Gene: EIF2S3 eukaryotic translation initiation factor 2, subunit 3 gamma, 52kDa". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1968.

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. 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. doi:10.1073/pnas.97.15.8566. 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. doi:10.1073/pnas.242603899. 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.
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. PMID 15489334.
Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
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. 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: 89. doi:10.1038/msb4100134. PMID 17353931.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic	PIF-1 · PIF-2 · PIF-3

Archaeal	aIF1 · aIF2 · aIF5 · aIF6

Eukaryotic	eIF1 (AX, AY, 1B) eIF2 (α, β, γ) eIF3 (A, B, C, D, F, G, H, I, J, K, M, S6) eIF4 (A2, A3, B, E1, E2, G1, G2, G3, H) eIF5 (A, A2, B) eIF6

Elongation factor

Prokaryotic (EF-Tu, EF-Ts, EF-G) · Archaeal (aEF-1, aEF-2) · Eukaryotic (EEF-1, EEF-2)

Release factor

Prokaryotic · Archaeal · Eukaryotic

Other

RPS1 · RPS2 · RPS3 · RPS4 · RPS5 · RPS6 · RPS7 · RPS8 · RPS9 · RPS10 · RPS11 · RPS12 · RPS13 · RPS14 · RPS15 · RPS16 · RPS17 · RPS18 · RPS19 · RPS20 · RPS21 · RPS22 · RPS23 · RPS24 · RPS25 · RPS26 · RPS27 · RPS28 · RPS29

Other concepts

Aminoacyl tRNA synthetase · Reading frame · Start codon · Shine-Dalgarno sequence/Kozak consensus sequence

This article on a gene on the X chromosome and/or its associated protein is a stub. You can help Wikipedia by expanding it.

Retrieved from "http://en.wikipedia.org/wiki/EIF2S3"

The information on this page is provieded by courtesy of wikipedia.

BROWSE:
You can alternatively just browse by the starting letter of the plant name
Click on any letter below, and it will show plants name starting with that letter

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z

EIF2S3

Contents

Function

See also

References

Further reading