EIF2S3

Identifiers

EIF2S3, EIF2, EIF2G, EIF2gamma, eIF-2gA, eukaryotic translation initiation factor 2 subunit gamma, MRXSBRK, MEHMO

External IDs

OMIM: 300161 MGI: 1349431 HomoloGene: 90888 GeneCards: EIF2S3

Gene location (Human)

Chr.	X chromosome (human)^[1]

Band	Xp22.11	Start	24,054,946 bp^[1]
Band	Xp22.11	End	24,078,810 bp^[1]

Gene location (Mouse)

Chr.	X chromosome (mouse)^[2]

Band	X C3\|X 41.52 cM	Start	93,232,313 bp^[2]
Band	X C3\|X 41.52 cM	End	93,256,468 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

germinal epithelium

parietal pleura

visceral pleura

tibia

monocyte

palpebral conjunctiva

endometrium

lymph node

body of pancreas

tibialis anterior muscle

Top expressed in

molar

maxillary prominence

hand

foot

medial ganglionic eminence

atrium

abdominal wall

renal corpuscle

yolk sac

somite

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

Species

Human

Mouse

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 Mb

Chr X: 93.23 – 93.26 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/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]

References

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.

Protein biosynthesis: translation (bacterial, archaeal, eukaryotic)

Proteins

Initiation factor

Bacterial

Mitochondrial

MTIF1
MTIF2
MTIF3

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	eIF1 B SUI1 family eIF1A Y
eIF2	α kinase β γ eIF2A eIF2B 1 2 3 4 5 eIF2D
eIF3	A B C D E F G H I J K L M
eIF4	A 1 2 3 E1 2 3 G 1 2 3 B H
eIF5	EIF5 EIF5A 2 5B
eIF6	EIF6

Elongation factor

Bacterial/Mitochondrial	EF-Tu EF-Ts EF-G EF-4 EF-P TSFM GFM1 GFM2
Archaeal/Eukaryotic	a/eEF-1 A1 2 3 B P1 P2 P3 D E G a/eEF-2

Release factor

Class 1
- eRF1
Class 2/RF3
- GSPT1
- GSPT2

Ribosomal Proteins

Cytoplasmic

60S subunit	RPL3 RPL4 RPL5 RPL6 RPL7 RPL7A RPL8 RPL9 RPL10 RPL10A RPL10-like RPL11 RPL12 RPL13 RPL13A RPL14 RPL15 RPL17 RPL18 RPL18A RPL19 RPL21 RPL22 RPL23 RPL23A RPL24 RPL26 RPL27 RPL27A RPL28 RPL29 RPL30 RPL31 RPL32 RPL34 RPL35 RPL35A RPL36 RPL36A RPL37 RPL37A RPL38 RPL39 RPL40 RPL41 RPLP0 RPLP1 RPLP2 RRP15-like RSL24D1
40S subunit	RPSA RPS2 RPS3 RPS3A RPS4 (RPS4X, RPS4Y1, RPS4Y2) RPS5 RPS6 RPS7 RPS8 RPS9 RPS10 RPS11 RPS12 RPS13 RPS14 RPS15 RPS15A RPS16 RPS17 RPS18 RPS19 RPS20 RPS21 RPS23 RPS24 RPS25 RPS26 RPS27 RPS27A RPS28 RPS29 RPS30 RACK1

Mitochondrial

39S subunit	MRPL1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42
28S subunit	MRPS1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35

Other concepts

Function

See also

References

Further reading