Search Results
Overview
| Uniprot ID | O43768 |
|---|---|
| Protein Name | Alpha-endosulfine |
| Gene Name | ENSA |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 107 | PQDLPQRKSSLVTSK |
| 114 | KSSLVTSKLAGGQVE |
| 40 | EEAKLKAKYPSLGQK |
| 47 | KYPSLGQKPGGSDFL |
| 56 | GGSDFLMKRLQKGQK |
| 63 | KRLQKGQKYFDSGDY |
| 74 | SGDYNMAKAKMKNKQ |
| 76 | DYNMAKAKMKNKQLP |
| 80 | AKAKMKNKQLPSAGP |
| 89 | LPSAGPDKNLVTGDH |
Function
Protein phosphatase inhibitor that specifically inhibits protein phosphatase 2A (PP2A) during mitosis. When phosphorylated at Ser-67 during mitosis, specifically interacts with PPP2R2D (PR55-delta) and inhibits its activity, leading to inactivation of PP2A, an essential condition to keep cyclin-B1-CDK1 activity high during M phase (By similarity). Also acts as a stimulator of insulin secretion by interacting with sulfonylurea receptor (ABCC8), thereby preventing sulfonylurea from binding to its receptor and reducing K(ATP) channel currents
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005654 | nucleoplasm |
| Molecular Function | GO:0008200 | ion channel inhibitor activity |
| Molecular Function | GO:0019212 | phosphatase inhibitor activity |
| Molecular Function | GO:0019870 | potassium channel inhibitor activity |
| Molecular Function | GO:0051721 | protein phosphatase 2A binding |
| Molecular Function | GO:0004864 | protein phosphatase inhibitor activity |
| Molecular Function | GO:0019888 | protein phosphatase regulator activity |
| Molecular Function | GO:0005102 | signaling receptor binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0000086 | G2/M transition of mitotic cell cycle |
| Biological Process | GO:0000278 | mitotic cell cycle |
| Biological Process | GO:0050796 | regulation of insulin secretion |
| Biological Process | GO:0007584 | response to nutrient |
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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[4] 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.
[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.