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Protein

Eukaryotic translation initiation factor 3 subunit G

Gene

Eif3g

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-RNO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-RNO-72649. Translation initiation complex formation.
R-RNO-72689. Formation of a pool of free 40S subunits.
R-RNO-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-RNO-72702. Ribosomal scanning and start codon recognition.
R-RNO-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:Eif3g
Synonyms:Eif3s4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi1307191. Eif3g.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation
  • Cytoplasmperinuclear region UniRule annotation

  • Note: Colocalizes with AIFM1 in the nucleus and perinuclear region.UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 320319Eukaryotic translation initiation factor 3 subunit GPRO_0000365396Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111PhosphoserineBy similarity
Modified residuei38 – 381PhosphothreonineUniRule annotationBy similarity
Modified residuei41 – 411PhosphothreonineCombined sources
Modified residuei42 – 421PhosphoserineCombined sources
Modified residuei189 – 1891PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is enhanced upon serum stimulation.UniRule annotation

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ5RK09.
PRIDEiQ5RK09.

PTM databases

iPTMnetiQ5RK09.
PhosphoSiteiQ5RK09.

Expressioni

Gene expression databases

GenevisibleiQ5RK09. RN.

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) (By similarity).UniRule annotation

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027986.

Structurei

3D structure databases

ProteinModelPortaliQ5RK09.
SMRiQ5RK09. Positions 228-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini239 – 31779RRMUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the eIF-3 subunit G family.UniRule annotation
Contains 1 RRM (RNA recognition motif) domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG0122. Eukaryota.
ENOG410Y3CW. LUCA.
GeneTreeiENSGT00510000047802.
HOGENOMiHOG000239560.
HOVERGENiHBG026850.
InParanoidiQ5RK09.
KOiK03248.
OMAiIVRTYKI.
OrthoDBiEOG75QR4G.
PhylomeDBiQ5RK09.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_03006. eIF3g.
InterProiIPR017334. eIF3_g.
IPR024675. eIF3g_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR10352. PTHR10352. 2 hits.
PfamiPF12353. eIF3g. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF037949. Transl_init_eIF-3_RNA-bind. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q5RK09-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLPTGD TSPEPELLPG
60 70 80 90 100
DPLPPPKEVI NGNIKTVTEY KVEEDGKKFK 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
EPVQAAQNKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT IRVTNLSEDT
260 270 280 290 300
RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
310 320
SGFGYDHLIL NVEWAKPSTN
Length:320
Mass (Da):35,651
Last modified:December 21, 2004 - v1
Checksum:i25773AB587192BE5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473993 Genomic DNA. Translation: EDL78343.1.
BC086383 mRNA. Translation: AAH86383.1.
RefSeqiNP_001013113.1. NM_001013095.1.
UniGeneiRn.107880.

Genome annotation databases

EnsembliENSRNOT00000027985; ENSRNOP00000027986; ENSRNOG00000020619.
GeneIDi298700.
KEGGirno:298700.
UCSCiRGD:1307191. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473993 Genomic DNA. Translation: EDL78343.1.
BC086383 mRNA. Translation: AAH86383.1.
RefSeqiNP_001013113.1. NM_001013095.1.
UniGeneiRn.107880.

3D structure databases

ProteinModelPortaliQ5RK09.
SMRiQ5RK09. Positions 228-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000027986.

PTM databases

iPTMnetiQ5RK09.
PhosphoSiteiQ5RK09.

Proteomic databases

PaxDbiQ5RK09.
PRIDEiQ5RK09.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000027985; ENSRNOP00000027986; ENSRNOG00000020619.
GeneIDi298700.
KEGGirno:298700.
UCSCiRGD:1307191. rat.

Organism-specific databases

CTDi8666.
RGDi1307191. Eif3g.

Phylogenomic databases

eggNOGiKOG0122. Eukaryota.
ENOG410Y3CW. LUCA.
GeneTreeiENSGT00510000047802.
HOGENOMiHOG000239560.
HOVERGENiHBG026850.
InParanoidiQ5RK09.
KOiK03248.
OMAiIVRTYKI.
OrthoDBiEOG75QR4G.
PhylomeDBiQ5RK09.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ5RK09.

Gene expression databases

GenevisibleiQ5RK09. RN.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
HAMAPiMF_03006. eIF3g.
InterProiIPR017334. eIF3_g.
IPR024675. eIF3g_N.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PANTHERiPTHR10352. PTHR10352. 2 hits.
PfamiPF12353. eIF3g. 1 hit.
PF00076. RRM_1. 1 hit.
[Graphical view]
PIRSFiPIRSF037949. Transl_init_eIF-3_RNA-bind. 1 hit.
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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: Ovary.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiEIF3G_RAT
AccessioniPrimary (citable) accession number: Q5RK09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: December 21, 2004
Last modified: June 8, 2016
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.