EIF2S2

Protein-coding gene in the species Homo sapiens
EIF2S2
Identifiers
AliasesEIF2S2, EIF2, EIF2B, EIF2beta, PPP1R67, eIF-2-beta, eukaryotic translation initiation factor 2 subunit beta
External IDsOMIM: 603908; MGI: 1914454; HomoloGene: 2904; GeneCards: EIF2S2; OMA:EIF2S2 - orthologs
Gene location (Human)
Chromosome 20 (human)
Chr.Chromosome 20 (human)[1]
Chromosome 20 (human)
Genomic location for EIF2S2
Genomic location for EIF2S2
Band20q11.22Start34,088,309 bp[1]
End34,112,243 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for EIF2S2
Genomic location for EIF2S2
Band2 H1|2 76.89 cMStart154,713,330 bp[2]
End154,734,855 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cartilage tissue

  • oral cavity

  • glutes

  • right ventricle

  • trabecular bone

  • deltoid muscle

  • muscle of arm

  • biceps brachii

  • mucosa of sigmoid colon

  • triceps brachii muscle
Top expressed in
  • morula

  • blastocyst

  • yolk sac

  • tail of embryo

  • embryo

  • genital tubercle

  • muscle of thigh

  • embryo

  • spermatocyte

  • ventricular zone
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • translation factor activity, RNA binding
  • protein binding
  • translation initiation factor activity
  • metal ion binding
  • RNA binding
  • mRNA binding
  • translation initiation factor binding
Cellular component
  • cytoplasm
  • cytosol
  • nucleus
  • eukaryotic translation initiation factor 2 complex
Biological process
  • translational initiation
  • male germ cell proliferation
  • male gonad development
  • in utero embryonic development
  • transmembrane transport
  • protein biosynthesis
  • formation of translation preinitiation complex
  • formation of cytoplasmic translation initiation complex
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8894

67204

Ensembl

ENSG00000125977

ENSMUSG00000074656

UniProt

P20042

Q99L45

RefSeq (mRNA)

NM_003908
NM_001316363
NM_001316364

NM_026030

RefSeq (protein)

NP_001303292
NP_001303293
NP_003899

NP_080306

Location (UCSC)Chr 20: 34.09 – 34.11 MbChr 2: 154.71 – 154.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Eukaryotic translation initiation factor 2 subunit 2 (eIF2β) is a protein that in humans is encoded by the EIF2S2 gene.[5][6]

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, this article), and gamma (γ), with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the eIF2 complex for another round of initiation.[6]

Regulation

Both eIF2α and eIF2β expression is regulated by the NRF1 transcription factor.[7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000125977 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074656 – 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. ^ 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. S2CID 54414457.
  6. ^ a b "Entrez Gene: EIF2S2 eukaryotic translation initiation factor 2, subunit 2 beta, 38kDa".
  7. ^ 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.

Further reading

  • 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. Bibcode:2001Natur.414..865D. 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. Bibcode:2002PNAS...99.5406K. 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
  • 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. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070. S2CID 8235923.
  • v
  • t
  • 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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