Full text data of EIF3G
EIF3G
(EIF3S4)
[Confidence: low (only semi-automatic identification from reviews)]
Eukaryotic translation initiation factor 3 subunit G; eIF3g (Eukaryotic translation initiation factor 3 RNA-binding subunit; eIF-3 RNA-binding subunit; Eukaryotic translation initiation factor 3 subunit 4; eIF-3-delta; eIF3 p42; eIF3 p44)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Eukaryotic translation initiation factor 3 subunit G; eIF3g (Eukaryotic translation initiation factor 3 RNA-binding subunit; eIF-3 RNA-binding subunit; Eukaryotic translation initiation factor 3 subunit 4; eIF-3-delta; eIF3 p42; eIF3 p44)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75821
ID EIF3G_HUMAN Reviewed; 320 AA.
AC O75821; O14801; Q969U5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G;
DE Short=eIF3g;
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit;
DE Short=eIF-3 RNA-binding subunit;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4;
DE AltName: Full=eIF-3-delta;
DE AltName: Full=eIF3 p42;
DE AltName: Full=eIF3 p44;
GN Name=EIF3G; Synonyms=EIF3S4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF3A, AND RNA-BINDING.
RX PubMed=9822659; DOI=10.1074/jbc.273.48.31901;
RA Block K.L., Vornlocher H.-P., Hershey J.W.B.;
RT "Characterization of cDNAs encoding the p44 and p35 subunits of human
RT translation initiation factor eIF3.";
RL J. Biol. Chem. 273:31901-31908(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
RP EIF5, AND RNA-BINDING.
RX PubMed=9973622; DOI=10.1093/nar/27.5.1331;
RA Bandyopadhyay A., Maitra U.;
RT "Cloning and characterization of the p42 subunit of mammalian
RT translation initiation factor 3 (eIF3): demonstration that eIF3
RT interacts with eIF5 in mammalian cells.";
RL Nucleic Acids Res. 27:1331-1337(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Chen W., Blough R.I., Winkelmann J.C.;
RT "Molecular cloning, genomic structure and chromosomal localization of
RT a novel human RNA binding protein gene homologous to a tumor necrosis
RT factor alpha inducible transcript in mouse.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH EIF3B.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [7]
RP INTERACTION WITH EIF3B.
RX PubMed=14688252; DOI=10.1074/jbc.M312745200;
RA Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
RA Hershey J.W.B.;
RT "The j-subunit of human translation initiation factor eIF3 is required
RT for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal
RT subunits in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [8]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
RA Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT and its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AIFM1.
RX PubMed=17094969; DOI=10.1016/j.febslet.2006.10.049;
RA Kim J.T., Kim K.D., Song E.Y., Lee H.G., Kim J.W., Kim J.W.,
RA Chae S.K., Kim E., Lee M.S., Yang Y., Lim J.S.;
RT "Apoptosis-inducing factor (AIF) inhibits protein synthesis by
RT interacting with the eukaryotic translation initiation factor 3
RT subunit p44 (eIF3g).";
RL FEBS Lett. 580:6375-6383(2006).
RN [11]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.M605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [12]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [13]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT THR-41
RP AND SER-42, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor
RT 3 protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit
RT interaction map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
RN [22]
RP STRUCTURE BY NMR OF 231-320.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in eukaryotic translation
RT initiation factor 3 subunit 4.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Component of the eukaryotic translation initiation
CC factor 3 (eIF-3) complex, which is required for several steps in
CC the initiation of protein synthesis. The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1,
CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly
CC and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation. This subunit can bind 18S
CC rRNA.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC C binds EIF3B of module A and EIF3H of module B, thereby linking
CC the three modules. EIF3J is a labile subunit that binds to the
CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3. Interacts (via C-terminus) with AIFM1
CC (via N-terminus).
CC -!- INTERACTION:
CC O95831:AIFM1; NbExp=9; IntAct=EBI-366632, EBI-356440;
CC P55884:EIF3B; NbExp=4; IntAct=EBI-366632, EBI-366696;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC Cytoplasm, perinuclear region. Note=Colocalizes with AIFM1 in the
CC nucleus and perinuclear region.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation.
CC -!- MASS SPECTROMETRY: Mass=35639.8; Method=Unknown; Range=1-320;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=35481.1; Mass_error=0.4; Method=MALDI;
CC Range=1-320; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; U96074; AAC78728.1; -; mRNA.
DR EMBL; AF020833; AAB71866.1; -; mRNA.
DR EMBL; AF092453; AAG15396.1; -; Genomic_DNA.
DR EMBL; AF094850; AAG15419.1; -; mRNA.
DR EMBL; BT006889; AAP35535.1; -; mRNA.
DR EMBL; BC000733; AAH00733.1; -; mRNA.
DR EMBL; BC008469; AAH08469.1; -; mRNA.
DR RefSeq; NP_003746.2; NM_003755.3.
DR UniGene; Hs.529059; -.
DR PDB; 2CQ0; NMR; -; A=231-320.
DR PDBsum; 2CQ0; -.
DR ProteinModelPortal; O75821; -.
DR SMR; O75821; 228-320.
DR DIP; DIP-31115N; -.
DR IntAct; O75821; 24.
DR MINT; MINT-3001737; -.
DR STRING; 9606.ENSP00000253108; -.
DR PhosphoSite; O75821; -.
DR PaxDb; O75821; -.
DR PeptideAtlas; O75821; -.
DR PRIDE; O75821; -.
DR DNASU; 8666; -.
DR Ensembl; ENST00000253108; ENSP00000253108; ENSG00000130811.
DR GeneID; 8666; -.
DR KEGG; hsa:8666; -.
DR UCSC; uc002mnd.3; human.
DR CTD; 8666; -.
DR GeneCards; GC19M010225; -.
DR HGNC; HGNC:3274; EIF3G.
DR HPA; HPA041997; -.
DR MIM; 603913; gene.
DR neXtProt; NX_O75821; -.
DR PharmGKB; PA162384827; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000239560; -.
DR HOVERGEN; HBG026850; -.
DR InParanoid; O75821; -.
DR KO; K03248; -.
DR OMA; WKASNED; -.
DR OrthoDB; EOG75QR4G; -.
DR PhylomeDB; O75821; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF3G; human.
DR EvolutionaryTrace; O75821; -.
DR GeneWiki; EIF3G; -.
DR GenomeRNAi; 8666; -.
DR NextBio; 32507; -.
DR PRO; PR:O75821; -.
DR ArrayExpress; O75821; -.
DR Bgee; O75821; -.
DR CleanEx; HS_EIF3G; -.
DR Genevestigator; O75821; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03006; eIF3g; 1; -.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10352; PTHR10352; 1.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 320 Eukaryotic translation initiation factor
FT 3 subunit G.
FT /FTId=PRO_0000123510.
FT DOMAIN 239 317 RRM.
FT MOD_RES 38 38 Phosphothreonine.
FT MOD_RES 41 41 Phosphothreonine.
FT MOD_RES 42 42 Phosphoserine.
FT CONFLICT 293 293 A -> R (in Ref. 1; AAC78728).
FT STRAND 236 245
FT HELIX 252 256
FT TURN 260 262
FT STRAND 265 272
FT STRAND 274 276
FT STRAND 278 289
FT HELIX 290 299
FT TURN 300 302
FT STRAND 311 316
SQ SEQUENCE 320 AA; 35611 MW; 7D7226FEDE9D6FBB CRC64;
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG APLPPPKEVI
NGNIKTVTEY KIDEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT
TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK
ELAEQLGLST GEKEKLPGEL EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT
IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
SGFGYDHLIL NVEWAKPSTN
//
ID EIF3G_HUMAN Reviewed; 320 AA.
AC O75821; O14801; Q969U5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 19-SEP-2002, sequence version 2.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G;
DE Short=eIF3g;
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit;
DE Short=eIF-3 RNA-binding subunit;
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4;
DE AltName: Full=eIF-3-delta;
DE AltName: Full=eIF3 p42;
DE AltName: Full=eIF3 p44;
GN Name=EIF3G; Synonyms=EIF3S4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF3A, AND RNA-BINDING.
RX PubMed=9822659; DOI=10.1074/jbc.273.48.31901;
RA Block K.L., Vornlocher H.-P., Hershey J.W.B.;
RT "Characterization of cDNAs encoding the p44 and p35 subunits of human
RT translation initiation factor eIF3.";
RL J. Biol. Chem. 273:31901-31908(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
RP EIF5, AND RNA-BINDING.
RX PubMed=9973622; DOI=10.1093/nar/27.5.1331;
RA Bandyopadhyay A., Maitra U.;
RT "Cloning and characterization of the p42 subunit of mammalian
RT translation initiation factor 3 (eIF3): demonstration that eIF3
RT interacts with eIF5 in mammalian cells.";
RL Nucleic Acids Res. 27:1331-1337(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Chen W., Blough R.I., Winkelmann J.C.;
RT "Molecular cloning, genomic structure and chromosomal localization of
RT a novel human RNA binding protein gene homologous to a tumor necrosis
RT factor alpha inducible transcript in mouse.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH EIF3B.
RX PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
RA Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
RT "Characterization of eIF3k: a newly discovered subunit of mammalian
RT translation initiation factor eIF3.";
RL Eur. J. Biochem. 270:4133-4139(2003).
RN [7]
RP INTERACTION WITH EIF3B.
RX PubMed=14688252; DOI=10.1074/jbc.M312745200;
RA Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
RA Hershey J.W.B.;
RT "The j-subunit of human translation initiation factor eIF3 is required
RT for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal
RT subunits in vitro.";
RL J. Biol. Chem. 279:8946-8956(2004).
RN [8]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=15703437; DOI=10.1261/rna.7215305;
RA Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
RA Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
RT and its role in ribosomal dissociation and anti-association.";
RL RNA 11:470-486(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH AIFM1.
RX PubMed=17094969; DOI=10.1016/j.febslet.2006.10.049;
RA Kim J.T., Kim K.D., Song E.Y., Lee H.G., Kim J.W., Kim J.W.,
RA Chae S.K., Kim E., Lee M.S., Yang Y., Lim J.S.;
RT "Apoptosis-inducing factor (AIF) inhibits protein synthesis by
RT interacting with the eukaryotic translation initiation factor 3
RT subunit p44 (eIF3g).";
RL FEBS Lett. 580:6375-6383(2006).
RN [11]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16766523; DOI=10.1074/jbc.M605418200;
RA LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
RA Bradley C.A., Hershey J.W.B., Rhoads R.E.;
RT "Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
RT subunit.";
RL J. Biol. Chem. 281:22917-22932(2006).
RN [12]
RP CHARACTERIZATION OF THE EIF-3 COMPLEX.
RX PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT "Reconstitution reveals the functional core of mammalian eIF3.";
RL EMBO J. 26:3373-3383(2007).
RN [13]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT THR-41
RP AND SER-42, AND MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
RA Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor
RT 3 protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42,
RP AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
RP COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=18599441; DOI=10.1073/pnas.0801313105;
RA Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
RA Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V.;
RT "Mass spectrometry reveals modularity and a complete subunit
RT interaction map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42,
RP AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [21]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=16322461; DOI=10.1126/science.1118977;
RA Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
RT "Structural roles for human translation factor eIF3 in initiation of
RT protein synthesis.";
RL Science 310:1513-1515(2005).
RN [22]
RP STRUCTURE BY NMR OF 231-320.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA binding domain in eukaryotic translation
RT initiation factor 3 subunit 4.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Component of the eukaryotic translation initiation
CC factor 3 (eIF-3) complex, which is required for several steps in
CC the initiation of protein synthesis. The eIF-3 complex associates
CC with the 40S ribosome and facilitates the recruitment of eIF-1,
CC eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC recruitment to the 43S PIC and scanning of the mRNA for AUG
CC recognition. The eIF-3 complex is also required for disassembly
CC and recycling of post-termination ribosomal complexes and
CC subsequently prevents premature joining of the 40S and 60S
CC ribosomal subunits prior to initiation. This subunit can bind 18S
CC rRNA.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC 3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC C binds EIF3B of module A and EIF3H of module B, thereby linking
CC the three modules. EIF3J is a labile subunit that binds to the
CC eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC under conditions of nutrient depletion. Mitogenic stimulation
CC leads to binding and activation of a complex composed of MTOR and
CC RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC binding of EIF4B to eIF-3. Interacts (via C-terminus) with AIFM1
CC (via N-terminus).
CC -!- INTERACTION:
CC O95831:AIFM1; NbExp=9; IntAct=EBI-366632, EBI-356440;
CC P55884:EIF3B; NbExp=4; IntAct=EBI-366632, EBI-366696;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC Cytoplasm, perinuclear region. Note=Colocalizes with AIFM1 in the
CC nucleus and perinuclear region.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation.
CC -!- MASS SPECTROMETRY: Mass=35639.8; Method=Unknown; Range=1-320;
CC Source=PubMed:17322308;
CC -!- MASS SPECTROMETRY: Mass=35481.1; Mass_error=0.4; Method=MALDI;
CC Range=1-320; Source=PubMed:18599441;
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR EMBL; U96074; AAC78728.1; -; mRNA.
DR EMBL; AF020833; AAB71866.1; -; mRNA.
DR EMBL; AF092453; AAG15396.1; -; Genomic_DNA.
DR EMBL; AF094850; AAG15419.1; -; mRNA.
DR EMBL; BT006889; AAP35535.1; -; mRNA.
DR EMBL; BC000733; AAH00733.1; -; mRNA.
DR EMBL; BC008469; AAH08469.1; -; mRNA.
DR RefSeq; NP_003746.2; NM_003755.3.
DR UniGene; Hs.529059; -.
DR PDB; 2CQ0; NMR; -; A=231-320.
DR PDBsum; 2CQ0; -.
DR ProteinModelPortal; O75821; -.
DR SMR; O75821; 228-320.
DR DIP; DIP-31115N; -.
DR IntAct; O75821; 24.
DR MINT; MINT-3001737; -.
DR STRING; 9606.ENSP00000253108; -.
DR PhosphoSite; O75821; -.
DR PaxDb; O75821; -.
DR PeptideAtlas; O75821; -.
DR PRIDE; O75821; -.
DR DNASU; 8666; -.
DR Ensembl; ENST00000253108; ENSP00000253108; ENSG00000130811.
DR GeneID; 8666; -.
DR KEGG; hsa:8666; -.
DR UCSC; uc002mnd.3; human.
DR CTD; 8666; -.
DR GeneCards; GC19M010225; -.
DR HGNC; HGNC:3274; EIF3G.
DR HPA; HPA041997; -.
DR MIM; 603913; gene.
DR neXtProt; NX_O75821; -.
DR PharmGKB; PA162384827; -.
DR eggNOG; COG0724; -.
DR HOGENOM; HOG000239560; -.
DR HOVERGEN; HBG026850; -.
DR InParanoid; O75821; -.
DR KO; K03248; -.
DR OMA; WKASNED; -.
DR OrthoDB; EOG75QR4G; -.
DR PhylomeDB; O75821; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; EIF3G; human.
DR EvolutionaryTrace; O75821; -.
DR GeneWiki; EIF3G; -.
DR GenomeRNAi; 8666; -.
DR NextBio; 32507; -.
DR PRO; PR:O75821; -.
DR ArrayExpress; O75821; -.
DR Bgee; O75821; -.
DR CleanEx; HS_EIF3G; -.
DR Genevestigator; O75821; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IEA:UniProtKB-HAMAP.
DR GO; GO:0006446; P:regulation of translational initiation; IEA:UniProtKB-HAMAP.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR Gene3D; 3.30.70.330; -; 1.
DR HAMAP; MF_03006; eIF3g; 1; -.
DR InterPro; IPR017334; eIF3_g.
DR InterPro; IPR024675; eIF3g_N.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR10352; PTHR10352; 1.
DR Pfam; PF12353; eIF3g; 1.
DR Pfam; PF00076; RRM_1; 1.
DR PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 1.
DR SMART; SM00360; RRM; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
KW Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 320 Eukaryotic translation initiation factor
FT 3 subunit G.
FT /FTId=PRO_0000123510.
FT DOMAIN 239 317 RRM.
FT MOD_RES 38 38 Phosphothreonine.
FT MOD_RES 41 41 Phosphothreonine.
FT MOD_RES 42 42 Phosphoserine.
FT CONFLICT 293 293 A -> R (in Ref. 1; AAC78728).
FT STRAND 236 245
FT HELIX 252 256
FT TURN 260 262
FT STRAND 265 272
FT STRAND 274 276
FT STRAND 278 289
FT HELIX 290 299
FT TURN 300 302
FT STRAND 311 316
SQ SEQUENCE 320 AA; 35611 MW; 7D7226FEDE9D6FBB CRC64;
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG APLPPPKEVI
NGNIKTVTEY KIDEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT
TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK
ELAEQLGLST GEKEKLPGEL EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT
IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
SGFGYDHLIL NVEWAKPSTN
//
MIM
603913
*RECORD*
*FIELD* NO
603913
*FIELD* TI
*603913 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT G; EIF3G
;;EIF3-p42;;
EIF3-p44;;
read moreEUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 4, FORMERLY; EIF3S4,
FORMERLY
*FIELD* TX
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits in mammals. See p66
(EIF3S7; 603915). By searching an EST database with partial protein
sequences of the human eIF3-p44 and eIF3-p35 (603910) subunits, Block et
al. (1998) isolated cDNAs encoding these 2 proteins. The predicted
320-amino acid p44 protein contains an RRM (RNA recognition motif) near
the C terminus. Sequence analysis indicated that human p44 shares 97%
protein sequence identity with the predicted mouse p44 homolog and 33%
identity with the S. cerevisiae eIF3-p33 subunit. Using Northwestern
blots, Block et al. (1998) demonstrated that p44 binds RNA, as do eIF3
subunits p170 (602039) and p66. On Far Western blots, the p44 protein
interacted strong and specifically with p170, and weakly with p116
(603917)/p110 (603916), p66, p40 (603912), and itself. Northern blot
analysis revealed that p44 is expressed as an approximately 1.4-kb mRNA
in HeLa cells.
Independently, Bandyopadhyay and Maitra (1999) cloned cDNAs encoding
p44, which they called p42. When expressed in mammalian cells,
epitope-tagged p42 was incorporated into endogenous eIF3. The authors
found that a major fraction of endogenous eIF5 was associated with eIF3,
leading them to suggest that a specific interaction between these 2
initiation factors may play an important role in the function of eIF5
during translation initiation.
*FIELD* RF
1. Bandyopadhyay, A.; Maitra, U.: Cloning and characterization of
the p42 subunit of mammalian translation initiation factor 3 (eIF3):
demonstration that eIF3 interacts with eIF5 in mammalian cells. Nucleic
Acids Res. 27: 1331-1337, 1999.
2. Block, K. L.; Vornlocher, H.-P.; Hershey, J. W. B.: Characterization
of cDNAs encoding the p44 and p35 subunits of human translation initiation
factor eIF3. J. Biol. Chem. 273: 31901-31908, 1998.
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 10/02/2007
alopez: 6/17/1999
*RECORD*
*FIELD* NO
603913
*FIELD* TI
*603913 EUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT G; EIF3G
;;EIF3-p42;;
EIF3-p44;;
read moreEUKARYOTIC TRANSLATION INITIATION FACTOR 3, SUBUNIT 4, FORMERLY; EIF3S4,
FORMERLY
*FIELD* TX
Eukaryotic initiation factor-3 (eIF3) is the largest of the eIFs and
consists of at least 10 nonidentical subunits in mammals. See p66
(EIF3S7; 603915). By searching an EST database with partial protein
sequences of the human eIF3-p44 and eIF3-p35 (603910) subunits, Block et
al. (1998) isolated cDNAs encoding these 2 proteins. The predicted
320-amino acid p44 protein contains an RRM (RNA recognition motif) near
the C terminus. Sequence analysis indicated that human p44 shares 97%
protein sequence identity with the predicted mouse p44 homolog and 33%
identity with the S. cerevisiae eIF3-p33 subunit. Using Northwestern
blots, Block et al. (1998) demonstrated that p44 binds RNA, as do eIF3
subunits p170 (602039) and p66. On Far Western blots, the p44 protein
interacted strong and specifically with p170, and weakly with p116
(603917)/p110 (603916), p66, p40 (603912), and itself. Northern blot
analysis revealed that p44 is expressed as an approximately 1.4-kb mRNA
in HeLa cells.
Independently, Bandyopadhyay and Maitra (1999) cloned cDNAs encoding
p44, which they called p42. When expressed in mammalian cells,
epitope-tagged p42 was incorporated into endogenous eIF3. The authors
found that a major fraction of endogenous eIF5 was associated with eIF3,
leading them to suggest that a specific interaction between these 2
initiation factors may play an important role in the function of eIF5
during translation initiation.
*FIELD* RF
1. Bandyopadhyay, A.; Maitra, U.: Cloning and characterization of
the p42 subunit of mammalian translation initiation factor 3 (eIF3):
demonstration that eIF3 interacts with eIF5 in mammalian cells. Nucleic
Acids Res. 27: 1331-1337, 1999.
2. Block, K. L.; Vornlocher, H.-P.; Hershey, J. W. B.: Characterization
of cDNAs encoding the p44 and p35 subunits of human translation initiation
factor eIF3. J. Biol. Chem. 273: 31901-31908, 1998.
*FIELD* CD
Rebekah S. Rasooly: 6/16/1999
*FIELD* ED
mgross: 10/02/2007
alopez: 6/17/1999