O00303 · EIF3F_HUMAN
- ProteinEukaryotic translation initiation factor 3 subunit F
- GeneEIF3F
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids357 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
Deubiquitinates activated NOTCH1, promoting its nuclear import, thereby acting as a positive regulator of Notch signaling.
Catalytic activity
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | eukaryotic 43S preinitiation complex | |
Cellular Component | eukaryotic 48S preinitiation complex | |
Cellular Component | eukaryotic translation initiation factor 3 complex | |
Cellular Component | eukaryotic translation initiation factor 3 complex, eIF3m | |
Cellular Component | membrane | |
Cellular Component | synapse | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | identical protein binding | |
Molecular Function | metal-dependent deubiquitinase activity | |
Molecular Function | translation initiation factor activity | |
Molecular Function | translation initiation factor binding | |
Biological Process | formation of cytoplasmic translation initiation complex | |
Biological Process | IRES-dependent viral translational initiation | |
Biological Process | proteolysis | |
Biological Process | translational initiation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 3 subunit F
- Short nameseIF3f
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00303
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Intellectual developmental disorder, autosomal recessive 67 (MRT67)
- Note
- DescriptionA form of intellectual disability, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. Some MRT67 patients manifest seizures and sensorineural hearing loss.
- See alsoMIM:618295
Natural variants in MRT67
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081783 | 232 | F>V | in MRT67; decreased protein abundance; dbSNP:rs141976414 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_029267 | 39 | in dbSNP:rs1043738 | |||
Sequence: P → L | ||||||
Natural variant | VAR_014452 | 172 | in dbSNP:rs1044058 | |||
Sequence: W → L | ||||||
Natural variant | VAR_081783 | 232 | in MRT67; decreased protein abundance; dbSNP:rs141976414 | |||
Sequence: F → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 393 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000213964 | 2-357 | UniProt | Eukaryotic translation initiation factor 3 subunit F | |||
Sequence: ATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPALPGPFPGGRVVRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMGVPGRTMGVMFTPLTVKYAYYDTERIGVDLIMKTCFSPNRVIGLSSDLQQVGGASARIQDALSTVLQYAEDVLSGKVSADNTVGRFLMSLVNQVPKIVPDDFETMLNSNINDLLMVTYLANLTQSQIALNEKLVNL | |||||||
Modified residue | 46 | UniProt | Phosphoserine; by CDK11; in vitro | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 238 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 258 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation is enhanced upon serum stimulation. Phosphorylated during apoptosis by caspase-processed CDK11.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
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.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-82 | Disordered | ||||
Sequence: MATPAVPVSAPPATPTPVPAAAPASVPAPTPAPAAAPVPAAAPASSSDPAAAAAATAAPGQTPASAQAPAQTPAPALPGPAL | ||||||
Compositional bias | 8-38 | Pro residues | ||||
Sequence: VSAPPATPTPVPAAAPASVPAPTPAPAAAPV | ||||||
Domain | 92-222 | MPN | ||||
Sequence: VRLHPVILASIVDSYERRNEGAARVIGTLLGTVDKHSVEVTNCFSVPHNESEDEVAVDMEFAKNMYELHKKVSPNELILGWYATGHDITEHSVLIHEYYSREAPNPIHLTVDTSLQNGRMSIKAYVSTLMG |
Domain
The MPN domain mediates deubiquitinating activity.
Sequence similarities
Belongs to the eIF-3 subunit F family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length357
- Mass (Da)37,564
- Last updated1997-07-01 v1
- Checksum8A70FC6E2BF07737
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YDT6 | H0YDT6_HUMAN | EIF3F | 359 | ||
A0A1W2PP79 | A0A1W2PP79_HUMAN | EIF3F | 172 | ||
E9PQV8 | E9PQV8_HUMAN | EIF3F | 55 | ||
A0A7I2YQA0 | A0A7I2YQA0_HUMAN | EIF3F | 218 | ||
A0A7I2V4S2 | A0A7I2V4S2_HUMAN | EIF3F | 124 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 8-38 | Pro residues | ||||
Sequence: VSAPPATPTPVPAAAPASVPAPTPAPAAAPV | ||||||
Sequence conflict | 50-56 | in Ref. 2; BAC04577 | ||||
Sequence: Missing |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U94855 EMBL· GenBank· DDBJ | AAD03467.1 EMBL· GenBank· DDBJ | mRNA | ||
AK095574 EMBL· GenBank· DDBJ | BAC04577.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289637 EMBL· GenBank· DDBJ | BAF82326.1 EMBL· GenBank· DDBJ | mRNA | ||
AK291354 EMBL· GenBank· DDBJ | BAF84043.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006894 EMBL· GenBank· DDBJ | AAP35540.1 EMBL· GenBank· DDBJ | mRNA | ||
CR456959 EMBL· GenBank· DDBJ | CAG33240.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000490 EMBL· GenBank· DDBJ | AAH00490.1 EMBL· GenBank· DDBJ | mRNA |