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Protein

Eukaryotic translation initiation factor 3 subunit E

Gene

EIF3E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (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). Required for nonsense-mediated mRNA decay (NMD); may act in conjunction with UPF2 to divert mRNAs from translation to the NMD pathway (PubMed:17468741). May interact with MCM7 and EPAS1 and regulate the proteasome-mediated degradation of these proteins (PubMed:17310990, PubMed:17324924).UniRule annotation6 Publications

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • translation initiation factor activity Source: UniProtKB

GO - Biological processi

  • formation of translation preinitiation complex Source: UniProtKB-HAMAP
  • negative regulation of translational initiation Source: UniProtKB
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  • regulation of translational initiation Source: UniProtKB
  • translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Initiation factor

Keywords - Biological processi

Protein biosynthesis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104408-MONOMER.
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 EUniRule annotation
Short name:
eIF3eUniRule annotation
Alternative name(s):
Eukaryotic translation initiation factor 3 subunit 6UniRule annotation
Viral integration site protein INT-6 homolog
eIF-3 p48UniRule annotation
Gene namesi
Name:EIF3EUniRule annotation
Synonyms:EIF3S6UniRule annotation, INT6UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3277. EIF3E.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • eukaryotic 43S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic 48S preinitiation complex Source: UniProtKB-HAMAP
  • eukaryotic translation initiation factor 3 complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi312L → D: Promotes nuclear accumulation. 1 Publication1

Organism-specific databases

DisGeNETi3646.
OpenTargetsiENSG00000104408.
PharmGKBiPA27705.

Polymorphism and mutation databases

BioMutaiEIF3E.
DMDMi41019126.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotationCombined sources2 Publications
ChainiPRO_00001235152 – 445Eukaryotic translation initiation factor 3 subunit EAdd BLAST444

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineUniRule annotationCombined sources2 Publications1
Modified residuei399PhosphoserineCombined sources1
Modified residuei439PhosphothreonineBy similarity1
Modified residuei442PhosphoserineCombined sources1
Modified residuei445PhosphotyrosineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP60228.
MaxQBiP60228.
PaxDbiP60228.
PeptideAtlasiP60228.
PRIDEiP60228.

PTM databases

iPTMnetiP60228.
PhosphoSitePlusiP60228.
SwissPalmiP60228.

Expressioni

Tissue specificityi

Ubiquitously expressed. Expressed at highest levels in appendix, lymph, pancreas, skeletal muscle, spleen and thymus.2 Publications

Gene expression databases

BgeeiENSG00000104408.
CleanExiHS_EIF3E.
ExpressionAtlasiP60228. baseline and differential.
GenevisibleiP60228. HS.

Organism-specific databases

HPAiHPA023973.

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 with COPS3, COPS6, COPS7 (COPS7A or COPS7B), EIF4G1, EPAS1, MCM7, NCBP1, PSMC6, TRIM27 and UPF2. Interacts with the HTLV-1 protein Tax-1. Interacts with IFIT1 and IFIT2.UniRule annotation16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C4orf19Q8IY423EBI-347740,EBI-10216552
EPAS1Q9981410EBI-347740,EBI-447470
ORFQ9Q2G45EBI-347740,EBI-6248094From a different organism.
RUNDC3AQ59EK94EBI-347740,EBI-747225
TRIM27P143737EBI-347740,EBI-719493
ZDHHC17Q8IUH52EBI-347740,EBI-524753

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109857. 100 interactors.
DIPiDIP-32691N.
IntActiP60228. 46 interactors.
MINTiMINT-153842.
STRINGi9606.ENSP00000220849.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-E1-395[»]
3J8Celectron microscopy-E1-395[»]
ProteinModelPortaliP60228.
SMRiP60228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini290 – 395PCIUniRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 128Sufficient for interaction with EPAS11 PublicationAdd BLAST125
Regioni9 – 195Sufficient for interaction with TRIM271 PublicationAdd BLAST187
Regioni351 – 445Sufficient for interaction with MCM71 PublicationAdd BLAST95

Sequence similaritiesi

Belongs to the eIF-3 subunit E family.UniRule annotation
Contains 1 PCI domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG2758. Eukaryota.
ENOG410XQK5. LUCA.
GeneTreeiENSGT00390000002661.
HOVERGENiHBG001097.
InParanoidiP60228.
KOiK03250.
OMAiKGTNMVD.
OrthoDBiEOG091G075K.
PhylomeDBiP60228.
TreeFamiTF101518.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03004. eIF3e. 1 hit.
InterProiIPR016650. eIF3e.
IPR019010. eIF3e_N.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10317. PTHR10317. 1 hit.
PfamiPF09440. eIF3_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view]
PIRSFiPIRSF016255. eIF3e_su6. 1 hit.
SMARTiSM01186. eIF3_N. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P60228-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM
60 70 80 90 100
VDFAMDVYKN LYSDDIPHAL REKRTTVVAQ LKQLQAETEP IVKMFEDPET
110 120 130 140 150
TRQMQSTRDG RMLFDYLADK HGFRQEYLDT LYRYAKFQYE CGNYSGAAEY
160 170 180 190 200
LYFFRVLVPA TDRNALSSLW GKLASEILMQ NWDAAMEDLT RLKETIDNNS
210 220 230 240 250
VSSPLQSLQQ RTWLIHWSLF VFFNHPKGRD NIIDLFLYQP QYLNAIQTMC
260 270 280 290 300
PHILRYLTTA VITNKDVRKR RQVLKDLVKV IQQESYTYKD PITEFVECLY
310 320 330 340 350
VNFDFDGAQK KLRECESVLV NDFFLVACLE DFIENARLFI FETFCRIHQC
360 370 380 390 400
ISINMLADKL NMTPEEAERW IVNLIRNARL DAKIDSKLGH VVMGNNAVSP
410 420 430 440
YQQVIEKTKS LSFRSQMLAM NIEKKLNQNS RSEAPNWATQ DSGFY
Length:445
Mass (Da):52,221
Last modified:January 16, 2004 - v1
Checksum:iA5368651DD0DDD0C
GO

Mass spectrometryi

Molecular mass is 52131.8 Da from positions 1 - 445. 1 Publication
Molecular mass is 52133.4±0.2 Da from positions 1 - 445. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_046480185A → V.1 PublicationCorresponds to variant rs17856554dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54562 mRNA. Translation: AAC51760.1.
U94174
, U94162, U94163, U94164, U94165, U94166, U94167, U94168, U94169, U94170, U94171, U94172, U94173 Genomic DNA. Translation: AAC51917.1.
U94175 mRNA. Translation: AAC51919.1.
U62962 mRNA. Translation: AAB58251.1.
U85947 mRNA. Translation: AAB88873.1.
CR542275 mRNA. Translation: CAG47071.1.
CH471060 Genomic DNA. Translation: EAW91918.1.
BC000734 mRNA. Translation: AAH00734.1.
BC008419 mRNA. Translation: AAH08419.1.
BC016706 mRNA. Translation: AAH16706.1.
BC017887 mRNA. Translation: AAH17887.1.
BC021679 mRNA. Translation: AAH21679.1.
CCDSiCCDS6308.1.
RefSeqiNP_001559.1. NM_001568.2.
UniGeneiHs.405590.

Genome annotation databases

EnsembliENST00000220849; ENSP00000220849; ENSG00000104408.
GeneIDi3646.
KEGGihsa:3646.
UCSCiuc003ymu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U54562 mRNA. Translation: AAC51760.1.
U94174
, U94162, U94163, U94164, U94165, U94166, U94167, U94168, U94169, U94170, U94171, U94172, U94173 Genomic DNA. Translation: AAC51917.1.
U94175 mRNA. Translation: AAC51919.1.
U62962 mRNA. Translation: AAB58251.1.
U85947 mRNA. Translation: AAB88873.1.
CR542275 mRNA. Translation: CAG47071.1.
CH471060 Genomic DNA. Translation: EAW91918.1.
BC000734 mRNA. Translation: AAH00734.1.
BC008419 mRNA. Translation: AAH08419.1.
BC016706 mRNA. Translation: AAH16706.1.
BC017887 mRNA. Translation: AAH17887.1.
BC021679 mRNA. Translation: AAH21679.1.
CCDSiCCDS6308.1.
RefSeqiNP_001559.1. NM_001568.2.
UniGeneiHs.405590.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-E1-395[»]
3J8Celectron microscopy-E1-395[»]
ProteinModelPortaliP60228.
SMRiP60228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109857. 100 interactors.
DIPiDIP-32691N.
IntActiP60228. 46 interactors.
MINTiMINT-153842.
STRINGi9606.ENSP00000220849.

PTM databases

iPTMnetiP60228.
PhosphoSitePlusiP60228.
SwissPalmiP60228.

Polymorphism and mutation databases

BioMutaiEIF3E.
DMDMi41019126.

Proteomic databases

EPDiP60228.
MaxQBiP60228.
PaxDbiP60228.
PeptideAtlasiP60228.
PRIDEiP60228.

Protocols and materials databases

DNASUi3646.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000220849; ENSP00000220849; ENSG00000104408.
GeneIDi3646.
KEGGihsa:3646.
UCSCiuc003ymu.4. human.

Organism-specific databases

CTDi3646.
DisGeNETi3646.
GeneCardsiEIF3E.
HGNCiHGNC:3277. EIF3E.
HPAiHPA023973.
MIMi602210. gene.
neXtProtiNX_P60228.
OpenTargetsiENSG00000104408.
PharmGKBiPA27705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2758. Eukaryota.
ENOG410XQK5. LUCA.
GeneTreeiENSGT00390000002661.
HOVERGENiHBG001097.
InParanoidiP60228.
KOiK03250.
OMAiKGTNMVD.
OrthoDBiEOG091G075K.
PhylomeDBiP60228.
TreeFamiTF101518.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000104408-MONOMER.
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.

Miscellaneous databases

ChiTaRSiEIF3E. human.
GeneWikiiEIF3S6.
GenomeRNAii3646.
PROiP60228.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000104408.
CleanExiHS_EIF3E.
ExpressionAtlasiP60228. baseline and differential.
GenevisibleiP60228. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
HAMAPiMF_03004. eIF3e. 1 hit.
InterProiIPR016650. eIF3e.
IPR019010. eIF3e_N.
IPR000717. PCI_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10317. PTHR10317. 1 hit.
PfamiPF09440. eIF3_N. 1 hit.
PF01399. PCI. 1 hit.
[Graphical view]
PIRSFiPIRSF016255. eIF3e_su6. 1 hit.
SMARTiSM01186. eIF3_N. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3E_HUMAN
AccessioniPrimary (citable) accession number: P60228
Secondary accession number(s): O43902
, Q64058, Q64059, Q64252, Q6FG33, Q8WVK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: November 30, 2016
This is version 149 of the entry and version 1 of the sequence. [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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Translation initiation factors
    List of translation initiation factor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.