P55010 · IF5_HUMAN
- ProteinEukaryotic translation initiation factor 5
- GeneEIF5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids431 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon (PubMed:11166181, PubMed:22813744, PubMed:24319994).
In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181).
During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744).
This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994).
When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181).
Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744).
This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744).
Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744).
In this complex, acts as a GTPase-activating protein, by promoting GTP hydrolysis by eIF2G (EIF2S3) (PubMed:11166181).
During scanning, interacts with both EIF1 (via its C-terminal domain (CTD)) and EIF1A (via its NTD) (PubMed:22813744).
This interaction with EIF1A contributes to the maintenance of EIF1 within the open 43S PIC (PubMed:24319994).
When start codon is recognized, EIF5, via its NTD, induces eIF2G (EIF2S3) to hydrolyze the GTP (PubMed:11166181).
Start codon recognition also induces a conformational change of the PIC to a closed state (PubMed:22813744).
This change increases the affinity of EIF5-CTD for EIF2-beta (EIF2S2), which allows the release, by an indirect mechanism, of EIF1 from the PIC (PubMed:22813744).
Finally, EIF5 stabilizes the PIC in its closed conformation (PubMed:22813744).
Features
Showing features for site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Cellular Component | synapse | |
Molecular Function | cadherin binding | |
Molecular Function | eukaryotic initiation factor eIF2 binding | |
Molecular Function | GDP-dissociation inhibitor activity | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activator activity | |
Molecular Function | RNA binding | |
Molecular Function | translation initiation factor activity | |
Biological Process | formation of cytoplasmic translation initiation complex | |
Biological Process | regulation of translational initiation | |
Biological Process | ribosome assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEukaryotic translation initiation factor 5
- Short nameseIF-5
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP55010
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 15 | Loss of ability to promote hydrolysis of GTP. | ||||
Sequence: R → M | ||||||
Mutagenesis | 305-306 | Disruption of binding to eIF1 and EIF2-beta (EIF2S2); when associated with 347-K-K-348. | ||||
Sequence: HN → DD | ||||||
Mutagenesis | 347-348 | Disruption of binding to eIF1 and EIF2-beta (EIF2S2); when associated with 305-D-D-306. | ||||
Sequence: EE → KK | ||||||
Natural variant | VAR_036467 | 418 | in a breast cancer sample; somatic mutation | |||
Sequence: K → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 455 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue, cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000212516 | 1-431 | UniProt | Eukaryotic translation initiation factor 5 | |||
Sequence: MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCELGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGNSCKACGYRGMLDTHHKLCTFILKNPPENSDSGTGKKEKEKKNRKGKDKENGSVSSSETPPPPPPPNEINPPPHTMEEEEDDDWGEDTTEEAQRRRMDEISDHAKVLTLSDDLERTIEERVNILFDFVKKKKEEGVIDSSDKEIVAEAERLDVKAMGPLVLTEVLFNEKIREQIKKYRRHFLRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASKKYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKAASVPKVETVKSDNKDDDIDIDAI | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 10 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 227 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 227 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 229 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 389 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 389 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 390 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 390 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 410 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 410 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 413 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 418 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 419 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 419 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the 43S pre-initiation complex (43S PIC), which is composed of the 40S ribosomal subunit, EIF1, eIF1A (EIF1AX), eIF3 complex, EIF5 and eIF2-GTP-initiator tRNA complex (eIF2 ternary complex). Interacts with eIF1A (EIF1AX) during scanning (PubMed:24319994).
Interacts through its C-terminal domain (CTD) with EIF1 or with eIF2-beta (EIF2S2) (mutually exclusive) through a common binding site (PubMed:21745818, PubMed:22813744).
Interacts through its C-terminal domain (CTD) with the CTD of EIF5B (PubMed:30211544).
Interacts with FMR1 isoform 6; this interaction occurs in a RNA-dependent manner (PubMed:24658146).
Interacts through its C-terminal domain (CTD) with EIF1 or with eIF2-beta (EIF2S2) (mutually exclusive) through a common binding site (PubMed:21745818, PubMed:22813744).
Interacts through its C-terminal domain (CTD) with the CTD of EIF5B (PubMed:30211544).
Interacts with FMR1 isoform 6; this interaction occurs in a RNA-dependent manner (PubMed:24658146).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P55010 | DUSP12 Q9UNI6 | 6 | EBI-286450, EBI-715161 | |
BINARY | P55010 | HTT P42858 | 3 | EBI-286450, EBI-466029 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 143-216 | Disordered | ||||
Sequence: KNPPENSDSGTGKKEKEKKNRKGKDKENGSVSSSETPPPPPPPNEINPPPHTMEEEEDDDWGEDTTEEAQRRRM | ||||||
Compositional bias | 150-171 | Basic and acidic residues | ||||
Sequence: DSGTGKKEKEKKNRKGKDKENG | ||||||
Compositional bias | 176-191 | Pro residues | ||||
Sequence: SETPPPPPPPNEINPP | ||||||
Domain | 233-392 | W2 | ||||
Sequence: ERTIEERVNILFDFVKKKKEEGVIDSSDKEIVAEAERLDVKAMGPLVLTEVLFNEKIREQIKKYRRHFLRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASKKYVSKELAKEIRVKAEPFIKWLKEAEEESSGG |
Sequence similarities
Belongs to the eIF-2-beta/eIF-5 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length431
- Mass (Da)49,223
- Last updated2003-01-10 v2
- ChecksumC6CCC3A255F9B9BC
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 60 | in Ref. 2; CAB45711 | ||||
Sequence: E → G | ||||||
Compositional bias | 150-171 | Basic and acidic residues | ||||
Sequence: DSGTGKKEKEKKNRKGKDKENG | ||||||
Compositional bias | 176-191 | Pro residues | ||||
Sequence: SETPPPPPPPNEINPP | ||||||
Sequence conflict | 203 | in Ref. 1; AAC50572 | ||||
Sequence: W → S | ||||||
Sequence conflict | 295 | in Ref. 2; CAB45711 | ||||
Sequence: K → E | ||||||
Sequence conflict | 311 | in Ref. 6; AAH32866 | ||||
Sequence: Q → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U49436 EMBL· GenBank· DDBJ | AAC50572.1 EMBL· GenBank· DDBJ | mRNA | ||
AL080102 EMBL· GenBank· DDBJ | CAB45711.1 EMBL· GenBank· DDBJ | mRNA | ||
AK026933 EMBL· GenBank· DDBJ | BAB15593.1 EMBL· GenBank· DDBJ | mRNA | ||
BX537367 EMBL· GenBank· DDBJ | CAD97610.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471061 EMBL· GenBank· DDBJ | EAW81809.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007728 EMBL· GenBank· DDBJ | AAH07728.1 EMBL· GenBank· DDBJ | mRNA | ||
BC032866 EMBL· GenBank· DDBJ | AAH32866.1 EMBL· GenBank· DDBJ | mRNA |