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O75821 (EIF3G_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eukaryotic translation initiation factor 3 subunit G

Short name=eIF3g
Alternative name(s):
Eukaryotic translation initiation factor 3 RNA-binding subunit
Short name=eIF-3 RNA-binding subunit
Eukaryotic translation initiation factor 3 subunit 4
eIF-3-delta
eIF3 p42
eIF3 p44
Gene names
Name:EIF3G
Synonyms:EIF3S4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. 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 preinitiation 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. This subunit can bind 18S rRNA. HAMAP-Rule MF_03006

Subunit structure

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). Ref.1 Ref.2 Ref.6 Ref.7 Ref.10 Ref.11 Ref.13 Ref.15

Subcellular location

Cytoplasm By similarity. Nucleus. Cytoplasmperinuclear region. Note: Colocalizes with AIFM1 in the nucleus and perinuclear region. Ref.10

Post-translational modification

Phosphorylated. Phosphorylation is enhanced upon serum stimulation. Ref.13

Sequence similarities

Belongs to the eIF-3 subunit G family.

Contains 1 RRM (RNA recognition motif) domain.

Mass spectrometry

Molecular mass is 35639.8 Da from positions 1 - 320. Ref.13

Molecular mass is 35481.1±0.4 Da from positions 1 - 320. Determined by MALDI. Ref.15

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
Nucleus
   LigandRNA-binding
   Molecular functionInitiation factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

formation of translation preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

gene expression

Traceable author statement. Source: Reactome

regulation of translational initiation

Inferred from electronic annotation. Source: UniProtKB-HAMAP

translation

Traceable author statement. Source: Reactome

translational initiation

Inferred from direct assay Ref.12. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

eukaryotic 43S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic 48S preinitiation complex

Inferred from electronic annotation. Source: UniProtKB-HAMAP

eukaryotic translation initiation factor 3 complex

Inferred from direct assay Ref.13Ref.12Ref.15. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

translation initiation factor activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AIFM1O958319EBI-366632,EBI-356440
EIF3BP558844EBI-366632,EBI-366696

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 320319Eukaryotic translation initiation factor 3 subunit G HAMAP-Rule MF_03006
PRO_0000123510

Regions

Domain239 – 31779RRM

Amino acid modifications

Modified residue381Phosphothreonine Ref.14 Ref.17
Modified residue411Phosphothreonine Ref.13 Ref.14 Ref.17
Modified residue421Phosphoserine Ref.13 Ref.14 Ref.17

Experimental info

Sequence conflict2931A → R in AAC78728. Ref.1

Secondary structure

................. 320
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75821 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: 7D7226FEDE9D6FBB

FASTA32035,611
        10         20         30         40         50         60 
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG APLPPPKEVI 

        70         80         90        100        110        120 
NGNIKTVTEY KIDEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT 

       130        140        150        160        170        180 
TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK 

       190        200        210        220        230        240 
ELAEQLGLST GEKEKLPGEL EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT 

       250        260        270        280        290        300 
IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV 

       310        320 
SGFGYDHLIL NVEWAKPSTN 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3."
Block K.L., Vornlocher H.-P., Hershey J.W.B.
J. Biol. Chem. 273:31901-31908(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH EIF3A, RNA-BINDING.
[2]"Cloning and characterization of the p42 subunit of mammalian translation initiation factor 3 (eIF3): demonstration that eIF3 interacts with eIF5 in mammalian cells."
Bandyopadhyay A., Maitra U.
Nucleic Acids Res. 27:1331-1337(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH EIF5, RNA-BINDING.
[3]"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."
Chen W., Blough R.I., Winkelmann J.C.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Placenta.
[6]"Characterization of eIF3k: a newly discovered subunit of mammalian translation initiation factor eIF3."
Mayeur G.L., Fraser C.S., Peiretti F., Block K.L., Hershey J.W.B.
Eur. J. Biochem. 270:4133-4139(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3B.
[7]"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."
Fraser C.S., Lee J.Y., Mayeur G.L., Bushell M., Doudna J.A., Hershey J.W.B.
J. Biol. Chem. 279:8946-8956(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EIF3B.
[8]"Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association."
Kolupaeva V.G., Unbehaun A., Lomakin I.B., Hellen C.U.T., Pestova T.V.
RNA 11:470-486(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Apoptosis-inducing factor (AIF) inhibits protein synthesis by interacting with the eukaryotic translation initiation factor 3 subunit p44 (eIF3g)."
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.
FEBS Lett. 580:6375-6383(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH AIFM1.
[11]"Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit."
LeFebvre A.K., Korneeva N.L., Trutschl M., Cvek U., Duzan R.D., Bradley C.A., Hershey J.W.B., Rhoads R.E.
J. Biol. Chem. 281:22917-22932(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[12]"Reconstitution reveals the functional core of mammalian eIF3."
Masutani M., Sonenberg N., Yokoyama S., Imataka H.
EMBO J. 26:3373-3383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF THE EIF-3 COMPLEX.
[13]"Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry."
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.
Mol. Cell. Proteomics 6:1135-1146(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT THR-41 AND SER-42, MASS SPECTROMETRY.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3."
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.
Proc. Natl. Acad. Sci. U.S.A. 105:18139-18144(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3 COMPLEX, MASS SPECTROMETRY.
[16]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38; THR-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Structural roles for human translation factor eIF3 in initiation of protein synthesis."
Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., Nogales E.
Science 310:1513-1515(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
[22]"Solution structure of RNA binding domain in eukaryotic translation initiation factor 3 subunit 4."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 231-320.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U96074 mRNA. Translation: AAC78728.1.
AF020833 mRNA. Translation: AAB71866.1.
AF092453 Genomic DNA. Translation: AAG15396.1.
AF094850 mRNA. Translation: AAG15419.1.
BT006889 mRNA. Translation: AAP35535.1.
BC000733 mRNA. Translation: AAH00733.1.
BC008469 mRNA. Translation: AAH08469.1.
RefSeqNP_003746.2. NM_003755.3.
UniGeneHs.529059.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQ0NMR-A231-320[»]
ProteinModelPortalO75821.
SMRO75821. Positions 228-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114215. 41 interactions.
DIPDIP-31115N.
IntActO75821. 24 interactions.
MINTMINT-3001737.
STRING9606.ENSP00000253108.

PTM databases

PhosphoSiteO75821.

Proteomic databases

PaxDbO75821.
PeptideAtlasO75821.
PRIDEO75821.

Protocols and materials databases

DNASU8666.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253108; ENSP00000253108; ENSG00000130811.
GeneID8666.
KEGGhsa:8666.
UCSCuc002mnd.3. human.

Organism-specific databases

CTD8666.
GeneCardsGC19M010225.
HGNCHGNC:3274. EIF3G.
HPAHPA041997.
MIM603913. gene.
neXtProtNX_O75821.
PharmGKBPA162384827.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000239560.
HOVERGENHBG026850.
InParanoidO75821.
KOK03248.
OMAWKASNED.
OrthoDBEOG75QR4G.
PhylomeDBO75821.
TreeFamTF101516.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO75821.
BgeeO75821.
CleanExHS_EIF3G.
GenevestigatorO75821.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
HAMAPMF_03006. eIF3g.
InterProIPR017334. eIF3_g.
IPR024675. eIF3g_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERPTHR10352. PTHR10352. 1 hit.
PfamPF12353. eIF3g. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFPIRSF037949. Transl_init_eIF-3_RNA-bind. 1 hit.
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEIF3G. human.
EvolutionaryTraceO75821.
GeneWikiEIF3G.
GenomeRNAi8666.
NextBio32507.
PROO75821.
SOURCESearch...

Entry information

Entry nameEIF3G_HUMAN
AccessionPrimary (citable) accession number: O75821
Secondary accession number(s): O14801, Q969U5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: April 16, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Translation initiation factors

List of translation initiation factor entries

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM