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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)

 EIF3G_HUMAN             Reviewed;         320 AA.
O75821; O14801; Q969U5;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
07-NOV-2018, entry version 188.
RecName: Full=Eukaryotic translation initiation factor 3 subunit G {ECO:0000255|HAMAP-Rule:MF_03006};
Short=eIF3g {ECO:0000255|HAMAP-Rule:MF_03006};
AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
Short=eIF-3 RNA-binding subunit {ECO:0000255|HAMAP-Rule:MF_03006};
AltName: Full=Eukaryotic translation initiation factor 3 subunit 4 {ECO:0000255|HAMAP-Rule:MF_03006};
AltName: Full=eIF-3-delta {ECO:0000255|HAMAP-Rule:MF_03006};
AltName: Full=eIF3 p42 {ECO:0000255|HAMAP-Rule:MF_03006};
AltName: Full=eIF3 p44 {ECO:0000255|HAMAP-Rule:MF_03006};
Name=EIF3G {ECO:0000255|HAMAP-Rule:MF_03006};
Synonyms=EIF3S4 {ECO:0000255|HAMAP-Rule:MF_03006};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF3A, AND RNA-BINDING.
PubMed=9822659; DOI=10.1074/jbc.273.48.31901;
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH
EIF5, AND RNA-BINDING.
PubMed=9973622; DOI=10.1093/nar/27.5.1331;
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Chen W., Blough R.I., Winkelmann J.C.;
"Molecular cloning, genomic structure and chromosomal localization of
a novel human RNA binding protein gene homologous to a tumor necrosis
factor alpha inducible transcript in mouse.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH EIF3B.
PubMed=14519125; DOI=10.1046/j.1432-1033.2003.03807.x;
Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.;
"Characterization of eIF3k: a newly discovered subunit of mammalian
translation initiation factor eIF3.";
Eur. J. Biochem. 270:4133-4139(2003).
[7]
INTERACTION WITH EIF3B.
PubMed=14688252; DOI=10.1074/jbc.M312745200;
Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A.,
Hershey J.W.B.;
"The j-subunit of human translation initiation factor eIF3 is required
for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal
subunits in vitro.";
J. Biol. Chem. 279:8946-8956(2004).
[8]
CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=15703437; DOI=10.1261/rna.7215305;
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T.,
Pestova T.V.;
"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits
and its role in ribosomal dissociation and anti-association.";
RNA 11:470-486(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH AIFM1.
PubMed=17094969; DOI=10.1016/j.febslet.2006.10.049;
Kim J.T., Kim K.D., Song E.Y., Lee H.G., Kim J.W., Kim J.W.,
Chae S.K., Kim E., Lee M.S., Yang Y., Lim J.S.;
"Apoptosis-inducing factor (AIF) inhibits protein synthesis by
interacting with the eukaryotic translation initiation factor 3
subunit p44 (eIF3g).";
FEBS Lett. 580:6375-6383(2006).
[11]
IDENTIFICATION IN THE EIF-3 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16766523; DOI=10.1074/jbc.M605418200;
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D.,
Bradley C.A., Hershey J.W.B., Rhoads R.E.;
"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e
subunit.";
J. Biol. Chem. 281:22917-22932(2006).
[12]
FUNCTION, AND CHARACTERIZATION OF THE EIF-3 COMPLEX.
PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
"Reconstitution reveals the functional core of mammalian eIF3.";
EMBO J. 26:3373-3383(2007).
[13]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT THR-41
AND SER-42, AND MASS SPECTROMETRY.
PubMed=17322308; DOI=10.1074/mcp.M600399-MCP200;
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,
Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
"Structural characterization of the human eukaryotic initiation factor
3 protein complex by mass spectrometry.";
Mol. Cell. Proteomics 6:1135-1146(2007).
[14]
FUNCTION (MICROBIAL INFECTION).
PubMed=18056426; DOI=10.1101/gad.439507;
Poyry T.A., Kaminski A., Connell E.J., Fraser C.S., Jackson R.J.;
"The mechanism of an exceptional case of reinitiation after
translation of a long ORF reveals why such events do not generally
occur in mammalian mRNA translation.";
Genes Dev. 21:3149-3162(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3
COMPLEX, AND MASS SPECTROMETRY.
PubMed=18599441; DOI=10.1073/pnas.0801313105;
Zhou M., Sandercock A.M., Fraser C.S., Ridlova G., Stephens E.,
Schenauer M.R., Yokoi-Fong T., Barsky D., Leary J.A., Hershey J.W.B.,
Doudna J.A., Robinson C.V.;
"Mass spectrometry reveals modularity and a complete subunit
interaction map of the eukaryotic translation factor eIF3.";
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-38; SER-223 AND
SER-264, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-189, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
INTERACTION WITH DHX33.
PubMed=26100019; DOI=10.1128/MCB.00315-15;
Zhang Y., You J., Wang X., Weber J.;
"The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
Mol. Cell. Biol. 35:2918-2931(2015).
[25]
FUNCTION, IDENTIFICATION IN THE EIF-3 COMPLEX, AND RNA-BINDING.
PubMed=25849773; DOI=10.1038/nature14267;
Lee A.S., Kranzusch P.J., Cate J.H.;
"eIF3 targets cell-proliferation messenger RNAs for translational
activation or repression.";
Nature 522:111-114(2015).
[26]
FUNCTION, AND RNA-BINDING.
PubMed=27462815; DOI=10.1038/nature18954;
Lee A.S., Kranzusch P.J., Doudna J.A., Cate J.H.;
"eIF3d is an mRNA cap-binding protein that is required for specialized
translation initiation.";
Nature 536:96-99(2016).
[27]
3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
PubMed=16322461; DOI=10.1126/science.1118977;
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.;
"Structural roles for human translation factor eIF3 in initiation of
protein synthesis.";
Science 310:1513-1515(2005).
[28]
STRUCTURE BY NMR OF 231-320.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA binding domain in eukaryotic translation
initiation factor 3 subunit 4.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: RNA-binding component of the eukaryotic translation
initiation factor 3 (eIF-3) complex, which is required for several
steps in the initiation of protein synthesis (PubMed:17581632,
PubMed:25849773, PubMed:27462815). The eIF-3 complex associates
with the 40S ribosome and facilitates the recruitment of eIF-1,
eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-
initiation complex (43S PIC). The eIF-3 complex stimulates mRNA
recruitment to the 43S PIC and scanning of the mRNA for AUG
recognition. The eIF-3 complex is also required for disassembly
and recycling of post-termination ribosomal complexes and
subsequently prevents premature joining of the 40S and 60S
ribosomal subunits prior to initiation (PubMed:17581632). The eIF-
3 complex specifically targets and initiates translation of a
subset of mRNAs involved in cell proliferation, including cell
cycling, differentiation and apoptosis, and uses different modes
of RNA stem-loop binding to exert either translational activation
or repression (PubMed:25849773). This subunit can bind 18S rRNA.
{ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17581632,
ECO:0000269|PubMed:25849773, ECO:0000269|PubMed:27462815}.
-!- FUNCTION: (Microbial infection) In case of FCV infection, plays a
role in the ribosomal termination-reinitiation event leading to
the translation of VP2 (PubMed:18056426).
{ECO:0000269|PubMed:18056426}.
-!- SUBUNIT: Component of the eukaryotic translation initiation factor
3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
C binds EIF3B of module A and EIF3H of module B, thereby linking
the three modules. EIF3J is a labile subunit that binds to the
eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
under conditions of nutrient depletion. Mitogenic stimulation
leads to binding and activation of a complex composed of MTOR and
RPTOR, leading to phosphorylation and release of RPS6KB1 and
binding of EIF4B to eIF-3. Interacts (via C-terminus) with AIFM1
(via N-terminus). Interacts with DHX33; the interaction is
independent of RNA (PubMed:26100019). {ECO:0000255|HAMAP-
Rule:MF_03006, ECO:0000269|PubMed:14519125,
ECO:0000269|PubMed:14688252, ECO:0000269|PubMed:16766523,
ECO:0000269|PubMed:17094969, ECO:0000269|PubMed:17322308,
ECO:0000269|PubMed:18599441, ECO:0000269|PubMed:25849773,
ECO:0000269|PubMed:26100019, ECO:0000269|PubMed:9822659,
ECO:0000269|PubMed:9973622}.
-!- INTERACTION:
Q96AP0:ACD; NbExp=2; IntAct=EBI-366632, EBI-717666;
O95831:AIFM1; NbExp=9; IntAct=EBI-366632, EBI-356440;
P55884:EIF3B; NbExp=9; IntAct=EBI-366632, EBI-366696;
Q13347:EIF3I; NbExp=2; IntAct=EBI-366632, EBI-354047;
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-366632, EBI-10175124;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-366632, EBI-618309;
Q9BRX2:PELO; NbExp=6; IntAct=EBI-366632, EBI-1043580;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03006}.
Nucleus {ECO:0000255|HAMAP-Rule:MF_03006,
ECO:0000269|PubMed:17094969}. Cytoplasm, perinuclear region
{ECO:0000255|HAMAP-Rule:MF_03006, ECO:0000269|PubMed:17094969}.
Note=Colocalizes with AIFM1 in the nucleus and perinuclear region.
-!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
stimulation. {ECO:0000255|HAMAP-Rule:MF_03006,
ECO:0000269|PubMed:17322308}.
-!- MASS SPECTROMETRY: Mass=35639.8; Method=Unknown; Range=1-320;
Evidence={ECO:0000269|PubMed:17322308};
-!- MASS SPECTROMETRY: Mass=35481.1; Mass_error=0.4; Method=MALDI;
Range=1-320; Evidence={ECO:0000269|PubMed:18599441};
-!- SIMILARITY: Belongs to the eIF-3 subunit G family.
{ECO:0000255|HAMAP-Rule:MF_03006}.
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EMBL; U96074; AAC78728.1; -; mRNA.
EMBL; AF020833; AAB71866.1; -; mRNA.
EMBL; AF092453; AAG15396.1; -; Genomic_DNA.
EMBL; AF094850; AAG15419.1; -; mRNA.
EMBL; BT006889; AAP35535.1; -; mRNA.
EMBL; BC000733; AAH00733.1; -; mRNA.
EMBL; BC008469; AAH08469.1; -; mRNA.
CCDS; CCDS12227.1; -.
RefSeq; NP_003746.2; NM_003755.4.
UniGene; Hs.529059; -.
PDB; 2CQ0; NMR; -; A=231-320.
PDB; 2MJC; NMR; -; A=150-179.
PDB; 5K0Y; EM; 5.80 A; M=103-140, O=239-315.
PDBsum; 2CQ0; -.
PDBsum; 2MJC; -.
PDBsum; 5K0Y; -.
ProteinModelPortal; O75821; -.
SMR; O75821; -.
BioGrid; 114215; 64.
CORUM; O75821; -.
DIP; DIP-31115N; -.
ELM; O75821; -.
IntAct; O75821; 42.
MINT; O75821; -.
STRING; 9606.ENSP00000253108; -.
MoonProt; O75821; -.
iPTMnet; O75821; -.
PhosphoSitePlus; O75821; -.
SwissPalm; O75821; -.
BioMuta; EIF3G; -.
EPD; O75821; -.
MaxQB; O75821; -.
PaxDb; O75821; -.
PeptideAtlas; O75821; -.
PRIDE; O75821; -.
ProteomicsDB; 50214; -.
TopDownProteomics; O75821; -.
DNASU; 8666; -.
Ensembl; ENST00000253108; ENSP00000253108; ENSG00000130811.
GeneID; 8666; -.
KEGG; hsa:8666; -.
UCSC; uc002mnd.4; human.
CTD; 8666; -.
DisGeNET; 8666; -.
EuPathDB; HostDB:ENSG00000130811.11; -.
GeneCards; EIF3G; -.
HGNC; HGNC:3274; EIF3G.
HPA; HPA041997; -.
MIM; 603913; gene.
neXtProt; NX_O75821; -.
OpenTargets; ENSG00000130811; -.
PharmGKB; PA162384827; -.
eggNOG; KOG0122; Eukaryota.
eggNOG; ENOG410Y3CW; LUCA.
GeneTree; ENSGT00510000047802; -.
HOGENOM; HOG000239560; -.
HOVERGEN; HBG026850; -.
InParanoid; O75821; -.
KO; K03248; -.
OMA; RKKWAKF; -.
OrthoDB; EOG091G0GSV; -.
PhylomeDB; O75821; -.
TreeFam; TF101516; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
ChiTaRS; EIF3G; human.
EvolutionaryTrace; O75821; -.
GeneWiki; EIF3G; -.
GenomeRNAi; 8666; -.
PRO; PR:O75821; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130811; Expressed in 238 organ(s), highest expression level in testis.
CleanEx; HS_EIF3G; -.
ExpressionAtlas; O75821; baseline and differential.
Genevisible; O75821; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016282; C:eukaryotic 43S preinitiation complex; IEA:UniProtKB-UniRule.
GO; GO:0033290; C:eukaryotic 48S preinitiation complex; IEA:UniProtKB-UniRule.
GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IEA:UniProtKB-UniRule.
GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
GO; GO:0075525; P:viral translational termination-reinitiation; IDA:UniProtKB.
CDD; cd12933; eIF3G; 1.
CDD; cd12408; RRM_eIF3G_like; 1.
Gene3D; 3.30.70.330; -; 1.
HAMAP; MF_03006; eIF3g; 1.
InterPro; IPR017334; eIF3_g.
InterPro; IPR024675; eIF3g_N.
InterPro; IPR034240; eIF3G_RRM.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR10352:SF0; PTHR10352:SF0; 1.
Pfam; PF12353; eIF3g; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Initiation factor; Nucleus; Phosphoprotein; Protein biosynthesis;
Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000255|HAMAP-
Rule:MF_03006,
ECO:0000269|PubMed:17322308}.
CHAIN 2 320 Eukaryotic translation initiation factor
3 subunit G.
/FTId=PRO_0000123510.
DOMAIN 239 317 RRM. {ECO:0000255|HAMAP-Rule:MF_03006}.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 38 38 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 41 41 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000255|HAMAP-Rule:MF_03006,
ECO:0000269|PubMed:17322308}.
MOD_RES 42 42 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000255|HAMAP-Rule:MF_03006,
ECO:0000269|PubMed:17322308}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 264 264 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CONFLICT 293 293 A -> R (in Ref. 1; AAC78728).
{ECO:0000305}.
STRAND 158 160 {ECO:0000244|PDB:2MJC}.
STRAND 162 164 {ECO:0000244|PDB:2MJC}.
HELIX 173 175 {ECO:0000244|PDB:2MJC}.
STRAND 236 245 {ECO:0000244|PDB:2CQ0}.
HELIX 252 256 {ECO:0000244|PDB:2CQ0}.
TURN 260 262 {ECO:0000244|PDB:2CQ0}.
STRAND 265 272 {ECO:0000244|PDB:2CQ0}.
STRAND 274 276 {ECO:0000244|PDB:2CQ0}.
STRAND 278 289 {ECO:0000244|PDB:2CQ0}.
HELIX 290 299 {ECO:0000244|PDB:2CQ0}.
TURN 300 302 {ECO:0000244|PDB:2CQ0}.
STRAND 311 316 {ECO:0000244|PDB:2CQ0}.
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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