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Protein

Eukaryotic translation initiation factor 3 subunit G

Gene

EIF3G

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation3 Publications
(Microbial infection) In case of FCV infection, plays a role in the ribosomal termination-reinitiation event leading to the translation of VP2 (PubMed:18056426).1 Publication

GO - Molecular functioni

  • RNA binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB-KW

GO - Biological processi

  • translational initiation Source: UniProtKB
  • viral translational termination-reinitiation Source: UniProtKB

Keywordsi

Molecular functionInitiation factor, RNA-binding
Biological processProtein biosynthesis

Enzyme and pathway databases

ReactomeiR-HSA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-HSA-72649. Translation initiation complex formation.
R-HSA-72689. Formation of a pool of free 40S subunits.
R-HSA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-HSA-72702. Ribosomal scanning and start codon recognition.
R-HSA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit GUniRule annotation
Short name:
eIF3gUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 RNA-binding subunitUniRule annotation
Short name:
eIF-3 RNA-binding subunitUniRule annotation
Eukaryotic translation initiation factor 3 subunit 4UniRule annotation
eIF-3-deltaUniRule annotation
eIF3 p42UniRule annotation
eIF3 p44UniRule annotation
Gene namesi
Name:EIF3GUniRule annotation
Synonyms:EIF3S4UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000130811.11.
HGNCiHGNC:3274. EIF3G.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi8666.
OpenTargetsiENSG00000130811.
PharmGKBiPA162384827.

Polymorphism and mutation databases

BioMutaiEIF3G.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotation1 Publication
ChainiPRO_00001235102 – 320Eukaryotic translation initiation factor 3 subunit GAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei8PhosphoserineCombined sources1
Modified residuei11PhosphoserineCombined sources1
Modified residuei38PhosphothreonineCombined sources1
Modified residuei41PhosphothreonineUniRule annotationCombined sources1 Publication1
Modified residuei42PhosphoserineUniRule annotationCombined sources1 Publication1
Modified residuei189PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1
Modified residuei264PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO75821.
MaxQBiO75821.
PaxDbiO75821.
PeptideAtlasiO75821.
PRIDEiO75821.
TopDownProteomicsiO75821.

PTM databases

iPTMnetiO75821.
PhosphoSitePlusiO75821.
SwissPalmiO75821.

Expressioni

Gene expression databases

BgeeiENSG00000130811.
CleanExiHS_EIF3G.
ExpressionAtlasiO75821. baseline and differential.
GenevisibleiO75821. HS.

Organism-specific databases

HPAiHPA041997.

Interactioni

Subunit structurei

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).UniRule annotation9 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi114215. 58 interactors.
CORUMiO75821.
DIPiDIP-31115N.
ELMiO75821.
IntActiO75821. 41 interactors.
MINTiMINT-3001737.
STRINGi9606.ENSP00000253108.

Structurei

Secondary structure

1320
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi158 – 160Combined sources3
Beta strandi162 – 164Combined sources3
Helixi173 – 175Combined sources3
Beta strandi236 – 245Combined sources10
Helixi252 – 256Combined sources5
Turni260 – 262Combined sources3
Beta strandi265 – 272Combined sources8
Beta strandi274 – 276Combined sources3
Beta strandi278 – 289Combined sources12
Helixi290 – 299Combined sources10
Turni300 – 302Combined sources3
Beta strandi311 – 316Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CQ0NMR-A231-320[»]
2MJCNMR-A150-179[»]
5K0Yelectron microscopy5.80M103-140[»]
O239-315[»]
ProteinModelPortaliO75821.
SMRiO75821.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75821.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini239 – 317RRMUniRule annotationAdd BLAST79

Sequence similaritiesi

Belongs to the eIF-3 subunit G family.UniRule annotation

Phylogenomic databases

eggNOGiKOG0122. Eukaryota.
ENOG410Y3CW. LUCA.
GeneTreeiENSGT00510000047802.
HOGENOMiHOG000239560.
HOVERGENiHBG026850.
InParanoidiO75821.
KOiK03248.
OMAiKMDGFGF.
OrthoDBiEOG091G0GSV.
PhylomeDBiO75821.
TreeFamiTF101516.

Family and domain databases

CDDicd12933. eIF3G. 1 hit.
cd12408. RRM_eIF3G_like. 1 hit.
HAMAPiMF_03006. eIF3g. 1 hit.
InterProiView protein in InterPro
IPR017334. eIF3_g.
IPR024675. eIF3g_N.
IPR034240. eIF3G_RRM.
IPR000504. RRM_dom.
PANTHERiPTHR10352:SF4. PTHR10352:SF4. 1 hit.
PfamiView protein in Pfam
PF12353. eIF3g. 1 hit.
PF00076. RRM_1. 1 hit.
SMARTiView protein in SMART
SM00360. RRM. 1 hit.
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiView protein in PROSITE
PS50102. RRM. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLATGD TSPEPELLPG
60 70 80 90 100
APLPPPKEVI NGNIKTVTEY KIDEDGKKFK IVRTFRIETR KASKAVARRK
110 120 130 140 150
NWKKFGNSEF DPPGPNVATT TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK
160 170 180 190 200
GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK ELAEQLGLST GEKEKLPGEL
210 220 230 240 250
EPVQATQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT IRVTNLSEDT
260 270 280 290 300
RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
310 320
SGFGYDHLIL NVEWAKPSTN
Length:320
Mass (Da):35,611
Last modified:September 19, 2002 - v2
Checksum:i7D7226FEDE9D6FBB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti293A → R in AAC78728 (PubMed:9822659).Curated1

Mass spectrometryi

Molecular mass is 35639.8 Da from positions 1 - 320. 1 Publication
Molecular mass is 35481.1±0.4 Da from positions 1 - 320. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12227.1.
RefSeqiNP_003746.2. NM_003755.4.
UniGeneiHs.529059.

Genome annotation databases

EnsembliENST00000253108; ENSP00000253108; ENSG00000130811.
GeneIDi8666.
KEGGihsa:8666.
UCSCiuc002mnd.4. human.

Similar proteinsi

Entry informationi

Entry nameiEIF3G_HUMAN
AccessioniPrimary (citable) accession number: O75821
Secondary accession number(s): O14801, Q969U5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 19, 2002
Last modified: September 27, 2017
This is version 178 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Translation initiation factors
    List of translation initiation factor entries
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families