Search Results
Overview
| Uniprot ID | P23284 |
|---|---|
| Protein Name | Peptidyl-prolyl cis-trans isomerase B |
| Gene Name | PPIB |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 116 | RGDGTGGKSIYGERF |
| 129 | RFPDENFKLKHYGPG |
| 131 | PDENFKLKHYGPGWV |
| 165 | KTAWLDGKHVVFGKV |
| 171 | GKHVVFGKVLEGMEV |
| 186 | VRKVESTKTDSRDKP |
| 195 | DSRDKPLKDVIIADC |
| 209 | CGKIEVEKPFAIAKE |
| 215 | EKPFAIAKE****** |
| 67 | VIFGLFGKTVPKTVD |
| 71 | LFGKTVPKTVDNFVA |
| 84 | VALATGEKGFGYKNS |
| 89 | GEKGFGYKNSKFHRV |
| 98 | SKFHRVIKDFMIQGG |
Function
Peptidyl-prolyl cis-trans isomerase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0034663 | endoplasmic reticulum chaperone complex |
| Cellular Component | GO:0005788 | endoplasmic reticulum lumen |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0042470 | melanosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0005790 | smooth endoplasmic reticulum |
| Molecular Function | GO:0016018 | cyclosporin A binding |
| Molecular Function | GO:0003755 | peptidyl-prolyl cis-trans isomerase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0070063 | RNA polymerase binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0060348 | bone development |
| Biological Process | GO:0044829 | host-mediated activation of viral genome replication |
| Biological Process | GO:0044794 | host-mediated activation of viral process |
| Biological Process | GO:0030593 | neutrophil chemotaxis |
| Biological Process | GO:0040018 | positive regulation of multicellular organism growth |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0050821 | protein stabilization |
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] 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.
[6] 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.
[7] 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.