EIF3G_HUMAN
ID EIF3G_HUMAN Reviewed; 320 AA.
AC O75821; O14801; Q969U5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF3g {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE Short=eIF-3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=Eukaryotic translation initiation factor 3 subunit 4 {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=eIF-3-delta {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=eIF3 p42 {ECO:0000255|HAMAP-Rule:MF_03006};
DE AltName: Full=eIF3 p44 {ECO:0000255|HAMAP-Rule:MF_03006};
GN Name=EIF3G {ECO:0000255|HAMAP-Rule:MF_03006};
GN Synonyms=EIF3S4 {ECO:0000255|HAMAP-Rule:MF_03006};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 translation
RT initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in
RT 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 a
RT novel human RNA binding protein gene homologous to a tumor necrosis factor
RT 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 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 project:
RT 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 for
RT the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits
RT 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., Pestova T.V.;
RT "Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and
RT 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT 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., Chae S.K.,
RA Kim E., Lee M.S., Yang Y., Lim J.S.;
RT "Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting
RT with the eukaryotic translation initiation factor 3 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 FUNCTION, AND 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 COMPLEX,
RP CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT THR-41 AND SER-42, AND
RP MASS SPECTROMETRY.
RX PubMed=17322308; DOI=10.1074/mcp.m600399-mcp200;
RA Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L., Hershey J.W.B.,
RA Doudna J.A., Robinson C.V., Leary J.A.;
RT "Structural characterization of the human eukaryotic initiation factor 3
RT protein complex by mass spectrometry.";
RL Mol. Cell. Proteomics 6:1135-1146(2007).
RN [14]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=18056426; DOI=10.1101/gad.439507;
RA Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
RT "The mechanism of an exceptional case of reinitiation after translation of
RT a long ORF reveals why such events do not generally occur in mammalian mRNA
RT translation.";
RL Genes Dev. 21:3149-3162(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [16]
RP IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX,
RP 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 interaction
RT map of the eukaryotic translation factor eIF3.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
RN [17]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [19]
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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., Buerckstuemmer T.,
RA 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 [21]
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., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-38; SER-223 AND
RP SER-264, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-189, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP INTERACTION WITH DHX33.
RX PubMed=26100019; DOI=10.1128/mcb.00315-15;
RA Zhang Y., You J., Wang X., Weber J.;
RT "The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
RL Mol. Cell. Biol. 35:2918-2931(2015).
RN [25]
RP FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, AND RNA-BINDING.
RX PubMed=25849773; DOI=10.1038/nature14267;
RA Lee A.S., Kranzusch P.J., Cate J.H.;
RT "eIF3 targets cell-proliferation messenger RNAs for translational
RT activation or repression.";
RL Nature 522:111-114(2015).
RN [26]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=27462815; DOI=10.1038/nature18954;
RA Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
RT "eIF3d is an mRNA cap-binding protein that is required for specialized
RT translation initiation.";
RL Nature 536:96-99(2016).
RN [27]
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 [28]
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: RNA-binding component of the eukaryotic translation
CC initiation factor 3 (eIF-3) complex, which is required for several
CC steps in the initiation of protein synthesis (PubMed:17581632,
CC PubMed:25849773, PubMed:27462815). The eIF-3 complex associates with
CC the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-
CC 2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex
CC (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC
CC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also
CC required for disassembly and recycling of post-termination ribosomal
CC complexes and subsequently prevents premature joining of the 40S and
CC 60S ribosomal subunits prior to initiation (PubMed:17581632). The eIF-3
CC complex specifically targets and initiates translation of a subset of
CC mRNAs involved in cell proliferation, including cell cycling,
CC differentiation and apoptosis, and uses different modes of RNA stem-
CC loop binding to exert either translational activation or repression
CC (PubMed:25849773). This subunit can bind 18S rRNA. {ECO:0000255|HAMAP-
CC Rule:MF_03006, ECO:0000269|PubMed:17581632,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
CC -!- FUNCTION: (Microbial infection) In case of FCV infection, plays a role
CC in the ribosomal termination-reinitiation event leading to the
CC translation of VP2 (PubMed:18056426). {ECO:0000269|PubMed:18056426}.
CC -!- SUBUNIT: Component of the eukaryotic translation initiation factor 3
CC (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B, EIF3C,
CC EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and
CC EIF3M. The eIF-3 complex appears to include 3 stable modules: module A
CC is composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A and
CC EIF3H of module B, thereby linking the three modules. EIF3J is a labile
CC subunit that binds to the eIF-3 complex via EIF3B. The eIF-3 complex
CC interacts with RPS6KB1 under conditions of nutrient depletion.
CC Mitogenic stimulation leads to binding and activation of a complex
CC composed of MTOR and RPTOR, leading to phosphorylation and release of
CC RPS6KB1 and binding of EIF4B to eIF-3. Interacts (via C-terminus) with
CC AIFM1 (via N-terminus). Interacts with DHX33; the interaction is
CC independent of RNA (PubMed:26100019). {ECO:0000255|HAMAP-Rule:MF_03006,
CC ECO:0000269|PubMed:14519125, ECO:0000269|PubMed:14688252,
CC ECO:0000269|PubMed:16766523, ECO:0000269|PubMed:17094969,
CC ECO:0000269|PubMed:17322308, ECO:0000269|PubMed:18599441,
CC ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:26100019,
CC ECO:0000269|PubMed:9822659, ECO:0000269|PubMed:9973622}.
CC -!- INTERACTION:
CC O75821; Q96AP0: ACD; NbExp=2; IntAct=EBI-366632, EBI-717666;
CC O75821; O95831: AIFM1; NbExp=9; IntAct=EBI-366632, EBI-356440;
CC O75821; P55884: EIF3B; NbExp=10; IntAct=EBI-366632, EBI-366696;
CC O75821; Q13347: EIF3I; NbExp=3; IntAct=EBI-366632, EBI-354047;
CC O75821; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-366632, EBI-10175124;
CC O75821; Q08379: GOLGA2; NbExp=3; IntAct=EBI-366632, EBI-618309;
CC O75821; P42858: HTT; NbExp=4; IntAct=EBI-366632, EBI-466029;
CC O75821; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-366632, EBI-16439278;
CC O75821; A9UHW6: MIF4GD; NbExp=2; IntAct=EBI-366632, EBI-373498;
CC O75821; A9UHW6-2: MIF4GD; NbExp=3; IntAct=EBI-366632, EBI-9118295;
CC O75821; Q9BRX2: PELO; NbExp=6; IntAct=EBI-366632, EBI-1043580;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}.
CC Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03006,
CC ECO:0000269|PubMed:17094969}. Note=Colocalizes with AIFM1 in the
CC nucleus and perinuclear region.
CC -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC stimulation. {ECO:0000255|HAMAP-Rule:MF_03006,
CC ECO:0000269|PubMed:17322308}.
CC -!- MASS SPECTROMETRY: Mass=35639.8; Method=Unknown;
CC Evidence={ECO:0000269|PubMed:17322308};
CC -!- MASS SPECTROMETRY: Mass=35481.1; Mass_error=0.4; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18599441};
CC -!- SIMILARITY: Belongs to the eIF-3 subunit G family. {ECO:0000255|HAMAP-
CC Rule:MF_03006}.
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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 CCDS; CCDS12227.1; -.
DR RefSeq; NP_003746.2; NM_003755.4.
DR PDB; 2CQ0; NMR; -; A=231-320.
DR PDB; 2MJC; NMR; -; A=150-179.
DR PDB; 5K0Y; EM; 5.80 A; M=103-140, O=239-315.
DR PDB; 6YBS; EM; 3.10 A; o=1-320.
DR PDB; 6ZMW; EM; 3.70 A; o=1-320.
DR PDBsum; 2CQ0; -.
DR PDBsum; 2MJC; -.
DR PDBsum; 5K0Y; -.
DR PDBsum; 6YBS; -.
DR PDBsum; 6ZMW; -.
DR AlphaFoldDB; O75821; -.
DR BMRB; O75821; -.
DR SMR; O75821; -.
DR BioGRID; 114215; 137.
DR ComplexPortal; CPX-6036; Eukaryotic translation initiation factor 3 complex.
DR CORUM; O75821; -.
DR DIP; DIP-31115N; -.
DR ELM; O75821; -.
DR IntAct; O75821; 68.
DR MINT; O75821; -.
DR STRING; 9606.ENSP00000253108; -.
DR MoonProt; O75821; -.
DR GlyGen; O75821; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; O75821; -.
DR MetOSite; O75821; -.
DR PhosphoSitePlus; O75821; -.
DR SwissPalm; O75821; -.
DR BioMuta; EIF3G; -.
DR EPD; O75821; -.
DR jPOST; O75821; -.
DR MassIVE; O75821; -.
DR MaxQB; O75821; -.
DR PaxDb; O75821; -.
DR PeptideAtlas; O75821; -.
DR PRIDE; O75821; -.
DR ProteomicsDB; 50214; -.
DR TopDownProteomics; O75821; -.
DR Antibodypedia; 12724; 286 antibodies from 30 providers.
DR DNASU; 8666; -.
DR Ensembl; ENST00000253108.9; ENSP00000253108.3; ENSG00000130811.12.
DR GeneID; 8666; -.
DR KEGG; hsa:8666; -.
DR MANE-Select; ENST00000253108.9; ENSP00000253108.3; NM_003755.5; NP_003746.2.
DR UCSC; uc002mnd.4; human.
DR CTD; 8666; -.
DR DisGeNET; 8666; -.
DR GeneCards; EIF3G; -.
DR HGNC; HGNC:3274; EIF3G.
DR HPA; ENSG00000130811; Low tissue specificity.
DR MIM; 603913; gene.
DR neXtProt; NX_O75821; -.
DR OpenTargets; ENSG00000130811; -.
DR PharmGKB; PA162384827; -.
DR VEuPathDB; HostDB:ENSG00000130811; -.
DR eggNOG; KOG0122; Eukaryota.
DR GeneTree; ENSGT00510000047802; -.
DR HOGENOM; CLU_034595_0_0_1; -.
DR InParanoid; O75821; -.
DR OMA; TTKCPFK; -.
DR OrthoDB; 1226059at2759; -.
DR PhylomeDB; O75821; -.
DR TreeFam; TF101516; -.
DR PathwayCommons; O75821; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; O75821; -.
DR SIGNOR; O75821; -.
DR BioGRID-ORCS; 8666; 694 hits in 1086 CRISPR screens.
DR ChiTaRS; EIF3G; human.
DR EvolutionaryTrace; O75821; -.
DR GeneWiki; EIF3G; -.
DR GenomeRNAi; 8666; -.
DR Pharos; O75821; Tbio.
DR PRO; PR:O75821; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75821; protein.
DR Bgee; ENSG00000130811; Expressed in granulocyte and 207 other tissues.
DR ExpressionAtlas; O75821; baseline and differential.
DR Genevisible; O75821; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IC:ComplexPortal.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
DR CDD; cd12933; eIF3G; 1.
DR CDD; cd12408; RRM_eIF3G_like; 1.
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; IPR034240; eIF3G_RRM.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
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 SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Initiation factor;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome;
KW RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006,
FT ECO:0000269|PubMed:17322308"
FT CHAIN 2..320
FT /note="Eukaryotic translation initiation factor 3 subunit
FT G"
FT /id="PRO_0000123510"
FT DOMAIN 239..317
FT /note="RRM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03006,
FT ECO:0000269|PubMed:17322308, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 293
FT /note="A -> R (in Ref. 1; AAC78728)"
FT /evidence="ECO:0000305"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2MJC"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:2MJC"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:2MJC"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 252..259
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 276..286
FT /evidence="ECO:0007829|PDB:6YBS"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:6YBS"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:6YBS"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:2CQ0"
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
