Search Results
Overview
| Uniprot ID | Q14692 |
|---|---|
| Protein Name | Ribosome biogenesis protein BMS1 homolog |
| Gene Name | BMS1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1172 | HIPKALQKALPFKNK |
| 43 | DARKRNPKAFAVQSA |
| 565 | SDRVNLEKSLLMKKA |
| 674 | WKEDLSRKAAEAFLR |
| 857 | DLKGEMQKQAQLNRA |
Function
GTPase required for the synthesis of 40S ribosomal subunits and for processing of pre-ribosomal RNA (pre-rRNA) at sites A0, A1, and A2. Controls access of pre-rRNA intermediates to RCL1 during ribosome biogenesis by binding RCL1 in a GTP-dependent manner, and delivering it to pre-ribosomes. GTP-binding and/or GTP hydrolysis may induce conformational rearrangements within the BMS1-RCL1 complex allowing the interaction of RCL1 with its RNA substrate. Required for RCL1 import into the nucleus
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0030686 | 90S preribosome |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0032040 | small-subunit processome |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0000479 | endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| Biological Process | GO:0030490 | maturation of SSU-rRNA |
| Biological Process | GO:0000462 | maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) |
| Biological Process | GO:0042274 | ribosomal small subunit biogenesis |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[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.