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Protein

Eukaryotic translation initiation factor 3 subunit F

Gene

EIF3F

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).UniRule annotation3 Publications
Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.1 Publication

Catalytic activityi

Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).1 Publication

GO - Molecular functioni

  • thiol-dependent ubiquitin-specific protease activity Source: FlyBase
  • translation initiation factor activity Source: UniProtKB
  • translation initiation factor binding Source: GO_Central

GO - Biological processi

  • formation of translation preinitiation complex Source: UniProtKB-HAMAP
  • IRES-dependent viral translational initiation Source: UniProtKB
  • protein deubiquitination Source: FlyBase
  • regulation of translational initiation Source: UniProtKB-HAMAP
  • translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Initiation factor, Protease, Thiol protease

Keywords - Biological processi

Protein biosynthesis, Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175390-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.
SIGNORiO00303.

Protein family/group databases

MEROPSiM67.974.

Names & Taxonomyi

Protein namesi
Recommended name:
Eukaryotic translation initiation factor 3 subunit FUniRule annotation
Short name:
eIF3fUniRule annotation
Alternative name(s):
Deubiquitinating enzyme eIF3f (EC:3.4.19.12)
Eukaryotic translation initiation factor 3 subunit 5UniRule annotation
eIF-3-epsilonUniRule annotation
eIF3 p47UniRule annotation
Gene namesi
Name:EIF3FUniRule annotation
Synonyms:EIF3S5UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3275. EIF3F.

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi8665.
OpenTargetsiENSG00000175390.
ENSG00000280606.
PharmGKBiPA162384806.

Chemistry databases

ChEMBLiCHEMBL2062352.

Polymorphism and mutation databases

BioMutaiEIF3F.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedUniRule annotation1 Publication
ChainiPRO_00002139642 – 357Eukaryotic translation initiation factor 3 subunit FAdd BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineUniRule annotation1 Publication1
Modified residuei46Phosphoserine; by CDK11; in vitroUniRule annotation1 Publication1
Modified residuei238N6-acetyllysineCombined sources1
Modified residuei258PhosphoserineUniRule annotationCombined sources1 Publication1

Post-translational modificationi

Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO00303.
MaxQBiO00303.
PaxDbiO00303.
PeptideAtlasiO00303.
PRIDEiO00303.

PTM databases

iPTMnetiO00303.
PhosphoSitePlusiO00303.
SwissPalmiO00303.

Expressioni

Gene expression databases

BgeeiENSG00000175390.
CleanExiHS_EIF3F.
ExpressionAtlasiO00303. baseline and differential.
GenevisibleiO00303. HS.

Organism-specific databases

HPAiHPA049250.

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 RNF139; the interaction leads to protein translation inhibitions in a ubiquitination-dependent manner. Interacts with DTX1, the interaction is required for deubiquitinating activity towards NOTCH1.UniRule annotation7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDK11BP211273EBI-711990,EBI-1298
EIF3BP558844EBI-711990,EBI-366696
EIF3MQ7L2H76EBI-711990,EBI-353901
FBXO32Q969P57EBI-711990,EBI-2932534
GLE1Q53GS72EBI-711990,EBI-1955541
MSH4O154576EBI-711990,EBI-6092777
ORFQ9Q2G43EBI-711990,EBI-6248094From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114214. 90 interactors.
DIPiDIP-35580N.
IntActiO00303. 35 interactors.
MINTiMINT-5000761.
STRINGi9606.ENSP00000310040.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-F1-257[»]
3J8Celectron microscopy-F1-257[»]
ProteinModelPortaliO00303.
SMRiO00303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini87 – 196MPNUniRule annotationAdd BLAST110

Domaini

The MPN domain mediates deubiquitinating activity.

Sequence similaritiesi

Belongs to the eIF-3 subunit F family.UniRule annotation
Contains 1 MPN (JAB/Mov34) domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG2975. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00530000063075.
HOGENOMiHOG000241154.
HOVERGENiHBG107843.
InParanoidiO00303.
KOiK03249.
OMAiRECNNPI.
OrthoDBiEOG091G0EMR.
PhylomeDBiO00303.
TreeFamiTF101517.

Family and domain databases

CDDicd08064. MPN_eIF3f. 1 hit.
HAMAPiMF_03005. eIF3f. 1 hit.
InterProiIPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O00303-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA
60 70 80 90 100
AAAAATAAPG QTPASAQAPA QTPAPALPGP ALPGPFPGGR VVRLHPVILA
110 120 130 140 150
SIVDSYERRN EGAARVIGTL LGTVDKHSVE VTNCFSVPHN ESEDEVAVDM
160 170 180 190 200
EFAKNMYELH KKVSPNELIL GWYATGHDIT EHSVLIHEYY SREAPNPIHL
210 220 230 240 250
TVDTSLQNGR MSIKAYVSTL MGVPGRTMGV MFTPLTVKYA YYDTERIGVD
260 270 280 290 300
LIMKTCFSPN RVIGLSSDLQ QVGGASARIQ DALSTVLQYA EDVLSGKVSA
310 320 330 340 350
DNTVGRFLMS LVNQVPKIVP DDFETMLNSN INDLLMVTYL ANLTQSQIAL

NEKLVNL
Length:357
Mass (Da):37,564
Last modified:July 1, 1997 - v1
Checksum:i8A70FC6E2BF07737
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50 – 56Missing in BAC04577 (PubMed:14702039).Curated7

Mass spectrometryi

Molecular mass is 37554.8 Da from positions 1 - 357. 1 Publication
Molecular mass is 37475.6±0.2 Da from positions 1 - 357. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02926739P → L.Corresponds to variant rs1043738dbSNPEnsembl.1
Natural variantiVAR_014452172W → L.Corresponds to variant rs1044058dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94855 mRNA. Translation: AAD03467.1.
AK095574 mRNA. Translation: BAC04577.1.
AK289637 mRNA. Translation: BAF82326.1.
AK291354 mRNA. Translation: BAF84043.1.
BT006894 mRNA. Translation: AAP35540.1.
CR456959 mRNA. Translation: CAG33240.1.
BC000490 mRNA. Translation: AAH00490.1.
CCDSiCCDS7785.1.
RefSeqiNP_003745.1. NM_003754.2.
UniGeneiHs.516023.

Genome annotation databases

EnsembliENST00000309828; ENSP00000310040; ENSG00000175390.
ENST00000533626; ENSP00000431800; ENSG00000175390.
ENST00000626223; ENSP00000485772; ENSG00000280606.
ENST00000628056; ENSP00000486798; ENSG00000280606.
GeneIDi8665.
KEGGihsa:8665.
UCSCiuc001mfw.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U94855 mRNA. Translation: AAD03467.1.
AK095574 mRNA. Translation: BAC04577.1.
AK289637 mRNA. Translation: BAF82326.1.
AK291354 mRNA. Translation: BAF84043.1.
BT006894 mRNA. Translation: AAP35540.1.
CR456959 mRNA. Translation: CAG33240.1.
BC000490 mRNA. Translation: AAH00490.1.
CCDSiCCDS7785.1.
RefSeqiNP_003745.1. NM_003754.2.
UniGeneiHs.516023.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J8Belectron microscopy-F1-257[»]
3J8Celectron microscopy-F1-257[»]
ProteinModelPortaliO00303.
SMRiO00303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114214. 90 interactors.
DIPiDIP-35580N.
IntActiO00303. 35 interactors.
MINTiMINT-5000761.
STRINGi9606.ENSP00000310040.

Chemistry databases

ChEMBLiCHEMBL2062352.

Protein family/group databases

MEROPSiM67.974.

PTM databases

iPTMnetiO00303.
PhosphoSitePlusiO00303.
SwissPalmiO00303.

Polymorphism and mutation databases

BioMutaiEIF3F.

Proteomic databases

EPDiO00303.
MaxQBiO00303.
PaxDbiO00303.
PeptideAtlasiO00303.
PRIDEiO00303.

Protocols and materials databases

DNASUi8665.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309828; ENSP00000310040; ENSG00000175390.
ENST00000533626; ENSP00000431800; ENSG00000175390.
ENST00000626223; ENSP00000485772; ENSG00000280606.
ENST00000628056; ENSP00000486798; ENSG00000280606.
GeneIDi8665.
KEGGihsa:8665.
UCSCiuc001mfw.5. human.

Organism-specific databases

CTDi8665.
DisGeNETi8665.
GeneCardsiEIF3F.
HGNCiHGNC:3275. EIF3F.
HPAiHPA049250.
MIMi603914. gene.
neXtProtiNX_O00303.
OpenTargetsiENSG00000175390.
ENSG00000280606.
PharmGKBiPA162384806.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2975. Eukaryota.
COG1310. LUCA.
GeneTreeiENSGT00530000063075.
HOGENOMiHOG000241154.
HOVERGENiHBG107843.
InParanoidiO00303.
KOiK03249.
OMAiRECNNPI.
OrthoDBiEOG091G0EMR.
PhylomeDBiO00303.
TreeFamiTF101517.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175390-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.
SIGNORiO00303.

Miscellaneous databases

GeneWikiiEIF3F.
GenomeRNAii8665.
PROiO00303.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175390.
CleanExiHS_EIF3F.
ExpressionAtlasiO00303. baseline and differential.
GenevisibleiO00303. HS.

Family and domain databases

CDDicd08064. MPN_eIF3f. 1 hit.
HAMAPiMF_03005. eIF3f. 1 hit.
InterProiIPR027531. eIF3f.
IPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamiPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTiSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEIF3F_HUMAN
AccessioniPrimary (citable) accession number: O00303
Secondary accession number(s): A8K0S2, Q6IB45, Q8N978
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: November 30, 2016
This is version 164 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, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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.