Search Results
Overview
| Uniprot ID | Q8WWY3 |
|---|---|
| Protein Name | U4/U6 small nuclear ribonucleoprotein Prp31 |
| Gene Name | PRPF31 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 298 | AARLVAAKCTLAARV |
| 417 | TQVNEATKARISKTL |
| 422 | ATKARISKTLQRTLQ |
| 430 | TLQRTLQKQSVVYGG |
| 438 | QSVVYGGKSTIRDRS |
Function
Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11867543, PubMed:20118938, PubMed:28781166). Required for the assembly of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome (PubMed:11867543)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015030 | Cajal body |
| Cellular Component | GO:0071339 | MLL1 complex |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0071011 | precatalytic spliceosome |
| Cellular Component | GO:0097526 | spliceosomal tri-snRNP complex |
| Cellular Component | GO:0071005 | U2-type precatalytic spliceosome |
| Cellular Component | GO:0005684 | U2-type spliceosomal complex |
| Cellular Component | GO:0005687 | U4 snRNP |
| Cellular Component | GO:0046540 | U4/U6 x U5 tri-snRNP complex |
| Cellular Component | GO:0005690 | U4atac snRNP |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0030674 | protein-macromolecule adaptor activity |
| Molecular Function | GO:0043021 | ribonucleoprotein complex binding |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0070990 | snRNP binding |
| Molecular Function | GO:0030621 | U4 snRNA binding |
| Molecular Function | GO:0030622 | U4atac snRNA binding |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0071166 | ribonucleoprotein complex localization |
| 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] 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] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.
[6] 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.