Search Results
Overview
| Uniprot ID | Q9Y450 |
|---|---|
| Protein Name | HBS1-like protein |
| Gene Name | HBS1L |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 140 | EATVSTGKIAKGKPV |
| 143 | VSTGKIAKGKPVDSQ |
| 161 | SESEIVPKVAKMTVS |
| 164 | EIVPKVAKMTVSGKK |
| 236 | SSTPAPVKKSGKLRQ |
| 237 | STPAPVKKSGKLRQQ |
| 294 | INKRTMHKYEQESKK |
| 622 | RLISVLNKSTGEVTK |
Function
GTPase component of the Pelota-HBS1L complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:21448132, PubMed:23667253, PubMed:27863242). The Pelota-HBS1L complex recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel (PubMed:27863242). Following mRNA extraction from stalled ribosomes by the SKI complex, the Pelota-HBS1L complex promotes recruitment of ABCE1, which drives the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway (PubMed:21448132, PubMed:32006463)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0022626 | cytosolic ribosome |
| Cellular Component | GO:1990533 | Dom34-Hbs1 complex |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0003746 | translation elongation factor activity |
| Biological Process | GO:0070966 | nuclear-transcribed mRNA catabolic process, no-go decay |
| Biological Process | GO:0006417 | regulation of translation |
| Biological Process | GO:0072344 | rescue of stalled cytosolic ribosome |
| Biological Process | GO:0032790 | ribosome disassembly |
| Biological Process | GO:0007165 | signal transduction |
| Biological Process | GO:0006412 | translation |
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] 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.
[3] 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.
[4] 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.