EIF2S2

From Wikipedia, the free encyclopedia

Eukaryotic translation initiation factor 2, subunit 2 beta, 38kDa

Identifiers

EIF2S2; EIF2; EIF2B; EIF2beta; PPP1R67; eIF-2-beta

External IDs

OMIM: 603908 MGI: 1914454 HomoloGene: 2904 GeneCards: EIF2S2 Gene

Gene Ontology
Molecular function	• RNA binding • translation initiation factor activity • protein binding • translation factor activity, nucleic acid binding • metal ion binding
Cellular component	• cytosol • eukaryotic translation initiation factor 2 complex
Biological process	• translation • translational initiation • gene expression • cellular protein metabolic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 20:
32.68 – 32.7 Mb

Chr 2:
154.87 – 154.89 Mb

PubMed search

Eukaryotic translation initiation factor 2 subunit 2 is a protein that in humans is encoded by the EIF2S2 gene.^[1]^[1]^[2]

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 (this article), and gamma, with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the EIF-2 complex for another round of initiation.^[2]

Regulation

Both eIF2-alpha and eIF2-beta expression is regulated by the NRF1 transcription factor.^[3]

References

↑ 1.0 1.1 Pathak VK, Nielsen PJ, Trachsel H, Hershey JW (Sep 1988). "Structure of the beta subunit of translational initiation factor eIF-2". Cell 54 (5): 633–9. doi:10.1016/S0092-8674(88)80007-2. PMID 3044606.
↑ 2.0 2.1 "Entrez Gene: EIF2S2 eukaryotic translation initiation factor 2, subunit 2 beta, 38kDa".
↑ Chiorini JA, Miyamoto S, Harkin SJ, Safer B (February 1999). "Genomic cloning and characterization of the human eukaryotic initiation factor-2beta promoter". J. Biol. Chem. 274 (7): 4195–201. doi:10.1074/jbc.274.7.4195. PMID 9933616.

Welsh GI, Price NT, Bladergroen BA et al. (1994). "Identification of novel phosphorylation sites in the beta-subunit of translation initiation factor eIF-2". Biochem. Biophys. Res. Commun. 201 (3): 1279–88. doi:10.1006/bbrc.1994.1843. PMID 8024572.
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.
Das S, Maiti T, Das K, Maitra U (1998). "Specific interaction of eukaryotic translation initiation factor 5 (eIF5) with the beta-subunit of eIF2". J. Biol. Chem. 272 (50): 31712–8. doi:10.1074/jbc.272.50.31712. PMID 9395514.
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. doi:10.1074/jbc.273.4.2136. PMID 9442054.
Kimball SR, Heinzinger NK, Horetsky RL, Jefferson LS (1998). "Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B". J. Biol. Chem. 273 (5): 3039–44. doi:10.1074/jbc.273.5.3039. PMID 9446619.
Chiorini JA, Miyamoto S, Harkin SJ, Safer B (1999). "Genomic cloning and characterization of the human eukaryotic initiation factor-2beta promoter". J. Biol. Chem. 274 (7): 4195–201. doi:10.1074/jbc.274.7.4195. PMID 9933616.
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.
Das S, Maitra U (2000). "Mutational Analysis of Mammalian Translation Initiation Factor 5 (eIF5): Role of Interaction between the β Subunit of eIF2 and eIF5 in eIF5 Function In Vitro and In Vivo". Mol. Cell. Biol. 20 (11): 3942–50. doi:10.1128/MCB.20.11.3942-3950.2000. PMC 85746. PMID 10805737.
Gomez E, Pavitt GD (2000). "Identification of Domains and Residues within the ɛ Subunit of Eukaryotic Translation Initiation Factor 2B (eIF2Bɛ) Required for Guanine Nucleotide Exchange Reveals a Novel Activation Function Promoted by eIF2B Complex Formation". Mol. Cell. Biol. 20 (11): 3965–76. doi:10.1128/MCB.20.11.3965-3976.2000. PMC 85753. PMID 10805739.
Das S, Ghosh R, Maitra U (2001). "Eukaryotic translation initiation factor 5 functions as a GTPase-activating protein". J. Biol. Chem. 276 (9): 6720–6. doi:10.1074/jbc.M008863200. PMID 11092890.
Reichman TW, Muñiz LC, Mathews MB (2002). "The RNA Binding Protein Nuclear Factor 90 Functions as Both a Positive and Negative Regulator of Gene Expression in Mammalian Cells". Mol. Cell. Biol. 22 (1): 343–56. doi:10.1128/MCB.22.1.343-356.2002. PMC 134226. PMID 11739746.
Deloukas P, Matthews LH, Ashurst J et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Kebache S, Zuo D, Chevet E, Larose L (2002). "Modulation of protein translation by Nck-1". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5406–11. doi:10.1073/pnas.082483399. PMC 122782. PMID 11959995.
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. PMC 139241. PMID 12477932.
Llorens F, Roher N, Miró FA et al. (2004). "Eukaryotic translation-initiation factor eIF2beta binds to protein kinase CK2: effects on CK2alpha activity". Biochem. J. 375 (Pt 3): 623–31. doi:10.1042/BJ20030915. PMC 1223719. PMID 12901717.
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. doi:10.1038/nature03207. PMID 15635413.
Stelzl U, Worm U, Lalowski M et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.

Protein biosynthesis: translation (prokaryotic, eukaryotic)

Ribosomal proteins

Initiation factor

Prokaryotic

Archaeal

aIF1
aIF2
aIF5
aIF6

Eukaryotic

eIF1	EIF1AX AY 1B

eIF2	EIF2S1 EIF2S2 EIF2S3 EIF2B1 EIF2B2 EIF2B3 EIF2B4 EIF2B5 EIF-2 kinase

eIF3	EIF3A B C D F G H I J K M S6

eIF4	EIF4A2 A3 B E1 E2 G1 G2 G3 H

eIF5	EIF5A A2 B

eIF6	EIF6

Elongation factor

Prokaryotic	EF-Tu EF-Ts EF-G

Archaeal	aEF-1, aEF-2

Eukaryotic	EEF-1 EEF1A1 EEF1A2 EEF1A3 EEF1B1 EEF1B2 EEF1B3 EEF1B4 EEF1D EEF1E1 EEF1G EEF2

Release factor

Other

Other concepts

see also disorders of translation and posttranslational modification
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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EIF2S2

Function

Regulation

See also

References

Further reading