Search Results
Overview
| Uniprot ID | O43290 |
|---|---|
| Protein Name | U4/U6.U5 tri-snRNP-associated protein 1 |
| Gene Name | SART1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 170 | QREELREKLAAAKEK |
| 183 | EKRLLNQKLGKIKTL |
| 302 | VDKERAEKNVELRKK |
| 309 | KNVELRKKKPDYLPY |
| 336 | KPRSILSKYDEELEG |
| 657 | LLETTVQKVARVKAP |
| 666 | ARVKAPNKSLPSAVY |
Function
Plays a role in mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. May also bind to DNA
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015030 | Cajal body |
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0071005 | U2-type precatalytic spliceosome |
| Cellular Component | GO:0046540 | U4/U6 x U5 tri-snRNP complex |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0000481 | maturation of 5S rRNA |
| Biological Process | GO:0045292 | mRNA cis splicing, via spliceosome |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0045585 | positive regulation of cytotoxic T cell differentiation |
| Biological Process | GO:0000387 | spliceosomal snRNP assembly |
| Biological Process | GO:0000244 | spliceosomal tri-snRNP complex assembly |
| Biological Process | GO:0000388 | spliceosome conformational change to release U4 (or U4atac) and U1 (or U11) |
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] 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.
[3] 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.
[4] 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.
[5] 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.
[6] 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.
[7] 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.
[8] 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.