Search Results
Overview
| Uniprot ID | Q13356 |
|---|---|
| Protein Name | RING-type E3 ubiquitin-protein ligase PPIL2 |
| Gene Name | PPIL2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 235 | PEKKKVDKLNAAHYS |
| 454 | QERKTQLKVAPETKV |
| 462 | VAPETKVKSSQPQAG |
| 482 | TFRQGVGKYINPAAT |
| 490 | YINPAATKRAAEEEP |
| 507 | SATVPMSKKKPSRGF |
| 508 | ATVPMSKKKPSRGFG |
Function
Has a ubiquitin-protein ligase activity acting as an E3 ubiquitin protein ligase or as an ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on substrates. By mediating 'Lys-48'-linked polyubiquitination of proteins could target them for proteasomal degradation (PubMed:11435423). May also function as a chaperone, playing a role in transport to the cell membrane of BSG/Basigin for instance (PubMed:15946952). Probable inactive PPIase with no peptidyl-prolyl cis-trans isomerase activity (PubMed:20676357). As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0071013 | catalytic step 2 spliceosome |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005796 | Golgi lumen |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0061630 | ubiquitin protein ligase activity |
| Molecular Function | GO:0034450 | ubiquitin-ubiquitin ligase activity |
| Biological Process | GO:0000398 | mRNA splicing, via spliceosome |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0072659 | protein localization to plasma membrane |
| Biological Process | GO:0000209 | protein polyubiquitination |
Reference
[1] 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.
[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] 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.
[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.