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Database: UniProt
Entry: O75821
LinkDB: O75821
Original site: O75821 
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   11-DEC-2019, entry version 198.
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       Q96AP0:ACD; NbExp=2; IntAct=EBI-366632, EBI-717666;
CC       O95831:AIFM1; NbExp=9; IntAct=EBI-366632, EBI-356440;
CC       P55884:EIF3B; NbExp=10; IntAct=EBI-366632, EBI-366696;
CC       Q13347:EIF3I; NbExp=3; IntAct=EBI-366632, EBI-354047;
CC       Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-366632, EBI-10175124;
CC       Q08379:GOLGA2; NbExp=3; IntAct=EBI-366632, EBI-618309;
CC       A9UHW6:MIF4GD; NbExp=2; IntAct=EBI-366632, EBI-373498;
CC       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}.
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   PDBsum; 2CQ0; -.
DR   PDBsum; 2MJC; -.
DR   PDBsum; 5K0Y; -.
DR   SMR; O75821; -.
DR   BioGrid; 114215; 85.
DR   CORUM; O75821; -.
DR   DIP; DIP-31115N; -.
DR   ELM; O75821; -.
DR   IntAct; O75821; 54.
DR   MINT; O75821; -.
DR   STRING; 9606.ENSP00000253108; -.
DR   MoonProt; O75821; -.
DR   iPTMnet; 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   DNASU; 8666; -.
DR   Ensembl; ENST00000253108; ENSP00000253108; ENSG00000130811.
DR   GeneID; 8666; -.
DR   KEGG; hsa:8666; -.
DR   UCSC; uc002mnd.4; human.
DR   CTD; 8666; -.
DR   DisGeNET; 8666; -.
DR   EuPathDB; HostDB:ENSG00000130811.11; -.
DR   GeneCards; EIF3G; -.
DR   HGNC; HGNC:3274; EIF3G.
DR   HPA; HPA041997; -.
DR   MIM; 603913; gene.
DR   neXtProt; NX_O75821; -.
DR   OpenTargets; ENSG00000130811; -.
DR   PharmGKB; PA162384827; -.
DR   eggNOG; KOG0122; Eukaryota.
DR   eggNOG; ENOG410Y3CW; LUCA.
DR   GeneTree; ENSGT00510000047802; -.
DR   HOGENOM; HOG000239560; -.
DR   InParanoid; O75821; -.
DR   KO; K03248; -.
DR   OMA; TTKCPFK; -.
DR   OrthoDB; 1226059at2759; -.
DR   PhylomeDB; O75821; -.
DR   TreeFam; TF101516; -.
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   ChiTaRS; EIF3G; human.
DR   EvolutionaryTrace; O75821; -.
DR   GeneWiki; EIF3G; -.
DR   GenomeRNAi; 8666; -.
DR   Pharos; O75821; Tbio.
DR   PRO; PR:O75821; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; O75821; protein.
DR   Bgee; ENSG00000130811; Expressed in 238 organ(s), highest expression level in testis.
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; IEA:UniProtKB-UniRule.
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   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   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         38
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:23186163"
FT   MOD_RES         41
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000255|HAMAP-
FT                   Rule:MF_03006, ECO:0000269|PubMed:17322308"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:18669648,
FT                   ECO:0000244|PubMed:19690332, ECO:0000255|HAMAP-
FT                   Rule:MF_03006, ECO:0000269|PubMed:17322308"
FT   MOD_RES         189
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:24275569"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         264
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   CONFLICT        293
FT                   /note="A -> R (in Ref. 1; AAC78728)"
FT                   /evidence="ECO:0000305"
FT   STRAND          158..160
FT                   /evidence="ECO:0000244|PDB:2MJC"
FT   STRAND          162..164
FT                   /evidence="ECO:0000244|PDB:2MJC"
FT   HELIX           173..175
FT                   /evidence="ECO:0000244|PDB:2MJC"
FT   STRAND          236..245
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   HELIX           252..256
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   TURN            260..262
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   STRAND          265..272
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   STRAND          274..276
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   STRAND          278..289
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   HELIX           290..299
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   TURN            300..302
FT                   /evidence="ECO:0000244|PDB:2CQ0"
FT   STRAND          311..316
FT                   /evidence="ECO:0000244|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
//
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