Overview
| Uniprot ID | P41567 |
|---|
| Protein Name | Eukaryotic translation initiation factor 1 |
|---|
| Gene Name | EIF1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 42 |
IQQRNGRKTLTTVQG |
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:12435632, PubMed:14600024, PubMed:9732867). Together with eIF1A (EIF1AX), EIF1 facilitates scanning and is essential for start codon recognition on the basis of AUG nucleotide context and location relative to the 5'-cap (PubMed:12435632, PubMed:14600024, PubMed:9732867). Participates to initiation codon selection by influencing the conformation of the 40S ribosomal subunit and the positions of bound mRNA and initiator tRNA; this is possible after its binding to the interface surface of the platform of the 40S ribosomal subunit close to the P-site (PubMed:14600024). Together with eIF1A (EIF1AX), also regulates the opening and closing of the mRNA binding channel, which ensures mRNA recruitment, scanning and the fidelity of initiation codon selection (PubMed:9732867). Continuously monitors and protects against premature and partial base-pairing of codons in the 5'-UTR with the anticodon of initiator tRNA (PubMed:12435632, PubMed:9732867). Together with eIF1A (EIF1AX), acts for ribosomal scanning, promotion of the assembly of 48S complex at the initiation codon (43S PIC becomes 48S PIC after the start codon is reached), and dissociation of aberrant complexes (PubMed:9732867). Interacts with EIF4G1, which in a mutual exclusive interaction associates either with EIF1 or with EIF4E on a common binding site (PubMed:29987188). EIF4G1-EIF1 complex promotes ribosome scanning (on both short and long 5'UTR), leaky scanning (on short 5'UTR) which is the bypass of the initial start codon, and discrimination against cap-proximal AUG (PubMed:29987188). Is probably maintained within the 43S PIC in open conformation thanks to eIF1A-EIF5 interaction (PubMed:24319994). Once the correct start codon is reached, EIF1 is physically excluded from the decoding site, shifting the PIC into the closed conformation and arresting it at the start codon (PubMed:22813744)
Protein Sequence
10
MSAIQNLHSF
20
DPFADASKGD
30
DLLPAGTEDY
40
IHIRIQQRNG
50
RKTLTTVQGI
60
ADDYDKKKLV
70
KAFKKKFACN
80
GTVIEHPEYG
90
EVIQLQGDQR
100
KNICQFLVEI
110
GLAKDDQLKV
HGF
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0016282 |
eukaryotic 43S preinitiation complex |
| Cellular Component |
GO:0033290 |
eukaryotic 48S preinitiation complex |
| Cellular Component |
GO:0043614 |
multi-eIF complex |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0043024 |
ribosomal small subunit binding |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0008135 |
translation factor activity, RNA binding |
| Molecular Function |
GO:0003743 |
translation initiation factor activity |
| Biological Process |
GO:0006446 |
regulation of translational initiation |
| Biological Process |
GO:0006413 |
translational initiation |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.