Search Results
Overview
| Uniprot ID | O15381 |
|---|---|
| Protein Name | Nuclear valosin-containing protein-like |
| Gene Name | NVL |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 129 | SLLSLYRKGNPDSVS |
| 156 | STPRISSKTGSIPLK |
| 218 | SLLESDMKRKGKLKN |
| 28 | LTSNKCGKYVDIGVL |
| 85 | LEDEHLAKRARQGEE |
Function
Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT (PubMed:22226966). Involved in both early and late stages of the pre-rRNA processing pathways (PubMed:26166824). Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucleolus (PubMed:15469983, PubMed:16782053, PubMed:26456651, PubMed:29107693). Catalyzes the release of specific assembly factors, such as WDR74, from pre-60S ribosomal particles through the ATPase activity (PubMed:26456651, PubMed:28416111, PubMed:29107693)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005697 | telomerase holoenzyme complex |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:1990275 | preribosome binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0032092 | positive regulation of protein binding |
| Biological Process | GO:0032206 | positive regulation of telomere maintenance |
| Biological Process | GO:1904749 | regulation of protein localization to nucleolus |
| Biological Process | GO:0042273 | ribosomal large subunit biogenesis |
| Biological Process | GO:0042254 | ribosome biogenesis |
| Biological Process | GO:0006364 | rRNA processing |
| Biological Process | GO:1905323 | telomerase holoenzyme complex assembly |
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] 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.