Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Eukaryotic translation initiation factor 3 subunit F

Gene

EIF3F

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

  • IRES-dependent viral translational initiation Source: UniProtKB
  • protein deubiquitination Source: FlyBase
  • translational initiation Source: UniProtKB

Keywordsi

Molecular functionHydrolase, Initiation factor, Protease, Thiol protease
Biological processProtein biosynthesis, Ubl conjugation pathway

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
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

EuPathDBiHostDB:ENSG00000175390.12
HGNCiHGNC:3275 EIF3F
MIMi603914 gene
neXtProtiNX_O00303

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi8665
OpenTargetsiENSG00000175390
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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114214, 100 interactors
CORUMiO00303
DIPiDIP-35580N
IntActiO00303, 58 interactors
MINTiO00303
STRINGi9606.ENSP00000310040

Structurei

Secondary structure

1357
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi91 – 94Combined sources4
Helixi96 – 109Combined sources14
Beta strandi117 – 123Combined sources7
Beta strandi125 – 136Combined sources12
Beta strandi139 – 142Combined sources4
Beta strandi145 – 148Combined sources4
Helixi150 – 163Combined sources14
Beta strandi167 – 174Combined sources8
Helixi183 – 193Combined sources11
Beta strandi194 – 196Combined sources3
Beta strandi198 – 202Combined sources5
Beta strandi208 – 210Combined sources3
Beta strandi212 – 219Combined sources8
Beta strandi231 – 239Combined sources9
Helixi243 – 252Combined sources10
Turni253 – 256Combined sources4

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
Domaini92 – 222MPNPROSITE-ProRule annotationAdd BLAST131

Domaini

The MPN domain mediates deubiquitinating activity.

Sequence similaritiesi

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

Phylogenomic databases

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

Family and domain databases

CDDicd08064 MPN_eIF3f, 1 hit
HAMAPiMF_03005 eIF3f, 1 hit
InterProiView protein in InterPro
IPR027531 eIF3f
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR024969 Rpn11/EIF3F_C
PANTHERiPTHR10540:SF6 PTHR10540:SF6, 1 hit
PfamiView protein in Pfam
PF01398 JAB, 1 hit
PF13012 MitMem_reg, 1 hit
SMARTiView protein in SMART
SM00232 JAB_MPN, 1 hit
PROSITEiView protein in PROSITE
PS50249 MPN, 1 hit

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 dbSNP:rs1043738Ensembl.1
Natural variantiVAR_014452172W → L. Corresponds to variant dbSNP:rs1044058Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiEIF3F_HUMAN
AccessioniPrimary (citable) accession number: O00303
Secondary accession number(s): A8K0S2, Q6IB45, Q8N978
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: May 23, 2018
This is version 176 of the entry and version 1 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, Reference proteome

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health