Search Results
Overview
| Uniprot ID | O43172 |
|---|---|
| Protein Name | U4/U6 small nuclear ribonucleoprotein Prp4 |
| Gene Name | PRPF4 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 147 | VGTDALKKTKKDDEK |
| 15 | STQATKTKAPDDLVA |
| 26 | DLVAPVVKKPHIYYG |
| 27 | LVAPVVKKPHIYYGS |
| 45 | KERERLAKGESGILG |
| 53 | GESGILGKDGLKAGI |
Function
Plays a role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0015030 | Cajal body |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005681 | spliceosomal complex |
| Cellular Component | GO:0097525 | spliceosomal snRNP complex |
| Cellular Component | GO:0071005 | U2-type precatalytic spliceosome |
| Cellular Component | GO:0071001 | U4/U6 snRNP |
| Cellular Component | GO:0046540 | U4/U6 x U5 tri-snRNP complex |
| Molecular Function | GO:0030621 | U4 snRNA binding |
| Molecular Function | GO:0017070 | U6 snRNA binding |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0006396 | RNA processing |
| Biological Process | GO:0008380 | RNA splicing |
| Biological Process | GO:0000375 | RNA splicing, via transesterification reactions |
| Biological Process | GO:0000245 | spliceosomal complex assembly |
| 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] 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.
[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] 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.
[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.