Search Results
Overview
| Uniprot ID | O15372 |
|---|---|
| Protein Name | Eukaryotic translation initiation factor 3 subunit H |
| Gene Name | EIF3H |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 165 | AQGSLSLKAYRLTPK |
| 188 | DFSPEALKKANITFE |
| 221 | LMWELEKKSAVADKH |
| 227 | KKSAVADKHELLSLA |
| 24 | STAGAAGKGKGKGGS |
| 274 | TSKQQQQKHQYQQRR |
| 28 | AAGKGKGKGGSGDSA |
| 5 | ***MASRKEGTGSTA |
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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0016282 | eukaryotic 43S preinitiation complex |
| Cellular Component | GO:0033290 | eukaryotic 48S preinitiation complex |
| Cellular Component | GO:0005852 | eukaryotic translation initiation factor 3 complex |
| Cellular Component | GO:0071541 | eukaryotic translation initiation factor 3 complex, eIF3m |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Molecular Function | GO:0140492 | metal-dependent deubiquitinase activity |
| Molecular Function | GO:0008237 | metallopeptidase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0003743 | translation initiation factor activity |
| Biological Process | GO:0001732 | formation of cytoplasmic translation initiation complex |
| Biological Process | GO:0032435 | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
| 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.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] 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.
[4] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[5] 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.