Search Results
Overview
| Uniprot ID | P41091 |
|---|---|
| Protein Name | Eukaryotic translation initiation factor 2 subunit 3 |
| Gene Name | EIF2S3 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 183 | AIEIMKLKHILILQN |
| 196 | QNKIDLVKESQAKEQ |
| 266 | IRSFDVNKPGCEVDD |
| 421 | GGRVSAVKADLGKIV |
| 59 | HGKSTVVKAISGVHT |
| 90 | YANAKIYKLDDPSCP |
Function
Member of the eIF2 complex that functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA (PubMed:31836389). This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form the 43S pre-initiation complex (43S PIC) (By similarity). Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF2 and release of an eIF2-GDP binary complex (By similarity). In order for eIF2 to recycle and catalyze another round of initiation, the GDP bound to eIF2 must exchange with GTP by way of a reaction catalyzed by eIF-2B (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0006446 | regulation of translational initiation |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005850 | eukaryotic translation initiation factor 2 complex |
| Cellular Component | GO:0070062 | extracellular exosome |
| Molecular Function | GO:0045296 | cadherin binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:1990856 | methionyl-initiator methionine tRNA binding |
| Molecular Function | GO:0008135 | translation factor activity, RNA binding |
| Molecular Function | GO:0003743 | translation initiation factor activity |
| Biological Process | GO:0002183 | cytoplasmic translational initiation |
| Biological Process | GO:0001731 | formation of translation preinitiation complex |
| Biological Process | GO:0006413 | translational initiation |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[2] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.