Search Results
Overview
| Uniprot ID | O14974 |
|---|---|
| Protein Name | Protein phosphatase 1 regulatory subunit 12A |
| Gene Name | PPP1R12A |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 320 | SQKTFKNKETLIIEP |
| 413 | TPTSPIKKFPTTATK |
| 420 | KFPTTATKISPKEEE |
| 442 | TWRLGLRKTGSYGAL |
| 532 | SSSYTRRKWEDDLKK |
| 551 | NEGSTYHKSCSFGRR |
Function
Key regulator of protein phosphatase 1C (PPP1C). Mediates binding to myosin. As part of the PPP1C complex, involved in dephosphorylation of PLK1. Capable of inhibiting HIF1AN-dependent suppression of HIF1A activity
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0031672 | A band |
| Cellular Component | GO:0015629 | actin cytoskeleton |
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0043292 | contractile muscle fiber |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0000776 | kinetochore |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0072357 | PTW/PP1 phosphatase complex |
| Cellular Component | GO:0001725 | stress fiber |
| Cellular Component | GO:0030018 | Z disc |
| Molecular Function | GO:0071889 | 14-3-3 protein binding |
| Molecular Function | GO:0004857 | enzyme inhibitor activity |
| Molecular Function | GO:0017020 | myosin phosphatase regulator activity |
| Molecular Function | GO:0019208 | phosphatase regulator activity |
| Molecular Function | GO:0019901 | protein kinase binding |
| Biological Process | GO:0007098 | centrosome cycle |
| Biological Process | GO:0000278 | mitotic cell cycle |
| Biological Process | GO:0043086 | negative regulation of catalytic activity |
| Biological Process | GO:0048812 | neuron projection morphogenesis |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006470 | protein dephosphorylation |
| Biological Process | GO:0030155 | regulation of cell adhesion |
| Biological Process | GO:0007165 | signal transduction |
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] 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.
[5] 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.