Search Results
Overview
| Uniprot ID | Q9UMS4 |
|---|---|
| Protein Name | Pre-mRNA-processing factor 19 |
| Gene Name | PRPF19 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 122 | RVIARLTKEVTAARE |
| 179 | IIQKLQDKATVLTTE |
| 192 | TERKKRGKTVPEELV |
| 244 | ILTGGADKNVVVFDK |
| 261 | EQILATLKGHTKKVT |
Function
Ubiquitin-protein ligase which is a core component of several complexes mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome (PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106, PubMed:30705154). Core component of the PRP19C/Prp19 complex/NTC/Nineteen complex which is part of the spliceosome and participates in its assembly, its remodeling and is required for its activity. During assembly of the spliceosome, mediates 'Lys-63'-linked polyubiquitination of the U4 spliceosomal protein PRPF3. Ubiquitination of PRPF3 allows its recognition by the U5 component PRPF8 and stabilizes the U4/U5/U6 tri-snRNP spliceosomal complex (PubMed:20595234). Recruited to RNA polymerase II C-terminal domain (CTD) and the pre-mRNA, it may also couple the transcriptional and spliceosomal machineries (PubMed:21536736). The XAB2 complex, which contains PRPF19, is also involved in pre-mRNA splicing, transcription and transcription-coupled repair (PubMed:17981804). Beside its role in pre-mRNA splicing PRPF19, as part of the PRP19-CDC5L complex, plays a role in the DNA damage response/DDR. It is recruited to the sites of DNA damage by the RPA complex where PRPF19 directly ubiquitinates RPA1 and RPA2. 'Lys-63'-linked polyubiquitination of the RPA complex allows the recruitment of the ATR-ATRIP complex and the activation of ATR, a master regulator of the DNA damage response (PubMed:24332808). May also play a role in DNA double-strand break (DSB) repair by recruiting the repair factor SETMAR to altered DNA (PubMed:18263876). As part of the PSO4 complex may also be involved in the DNA interstrand cross-links/ICLs repair process (PubMed:16223718). In addition, may also mediate 'Lys-48'-linked polyubiquitination of substrates and play a role in proteasomal degradation (PubMed:11435423). May play a role in the biogenesis of lipid droplets (By similarity). May play a role in neural differentiation possibly through its function as part of the spliceosome (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0000974 | Prp19 complex |
| Cellular Component | GO:0035861 | site of double-strand break |
| Cellular Component | GO:0005819 | spindle |
| Cellular Component | GO:0071006 | U2-type catalytic step 1 spliceosome |
| Cellular Component | GO:0071007 | U2-type catalytic step 2 spliceosome |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0061630 | ubiquitin protein ligase activity |
| Molecular Function | GO:0004842 | ubiquitin-protein transferase activity |
| Molecular Function | GO:0034450 | ubiquitin-ubiquitin ligase activity |
| Biological Process | GO:0000077 | DNA damage checkpoint signaling |
| Biological Process | GO:0006303 | double-strand break repair via nonhomologous end joining |
| Biological Process | GO:0008104 | intracellular protein localization |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0010498 | proteasomal protein catabolic process |
| Biological Process | GO:0070534 | protein K63-linked ubiquitination |
| Biological Process | GO:0000209 | protein polyubiquitination |
| Biological Process | GO:0000245 | spliceosomal complex assembly |
| Biological Process | GO:0000244 | spliceosomal tri-snRNP 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] 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] 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.