Search Results
Overview
| Uniprot ID | P36873 |
|---|---|
| Protein Name | Serine/threonine-protein phosphatase PP1-gamma catalytic subunit |
| Gene Name | PPP1CC |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 238 | VVAKFLHKHDLDLIC |
| 319 | PPRGMITKQAKK*** |
| 322 | GMITKQAKK****** |
| 41 | EIRGLCLKSREIFLS |
Function
Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets (PubMed:17936702, PubMed:25012651). Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Dephosphorylates RPS6KB1 (PubMed:17936702). Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). In balance with CSNK1D and CSNK1E, determines the circadian period length, through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation (PubMed:21712997). May dephosphorylate CSNK1D and CSNK1E (By similarity). Regulates the recruitment of the SKA complex to kinetochores (PubMed:28982702). Dephosphorylates the 'Ser-418' residue of FOXP3 in regulatory T-cells (Treg) from patients with rheumatoid arthritis, thereby inactivating FOXP3 and rendering Treg cells functionally defective (PubMed:23396208). Together with PPP1CA (PP1-alpha subunit), dephosphorylates IFIH1/MDA5 and RIG-I leading to their activation and a functional innate immune response (PubMed:23499489). Core component of the SHOC2-MRAS-PP1c (SMP) holophosphatase complex that regulates the MAPK pathway activation (PubMed:35768504, PubMed:35831509). The SMP complex specifically dephosphorylates the inhibitory phosphorylation at 'Ser-259' of RAF1 kinase, 'Ser-365' of BRAF kinase and 'Ser-214' of ARAF kinase, stimulating their kinase activities (PubMed:35768504, PubMed:35831509). Dephosphorylates MKI67 at the onset of anaphase (PubMed:25012651). The SMP complex enhances the dephosphorylation activity and substrate specificity of PP1c (PubMed:35768504, PubMed:35831509)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0032154 | cleavage furrow |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0043197 | dendritic spine |
| Cellular Component | GO:0005925 | focal adhesion |
| Cellular Component | GO:0098978 | glutamatergic synapse |
| Cellular Component | GO:0000776 | kinetochore |
| Cellular Component | GO:0005815 | microtubule organizing center |
| Cellular Component | GO:0030496 | midbody |
| Cellular Component | GO:0005741 | mitochondrial outer membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005730 | nucleolus |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0098793 | presynapse |
| Cellular Component | GO:0032991 | protein-containing complex |
| Cellular Component | GO:0072357 | PTW/PP1 phosphatase complex |
| Molecular Function | GO:0005521 | lamin binding |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0016791 | phosphatase activity |
| Molecular Function | GO:0004721 | phosphoprotein phosphatase activity |
| Molecular Function | GO:0019904 | protein domain specific binding |
| Molecular Function | GO:0019901 | protein kinase binding |
| Molecular Function | GO:0008157 | protein phosphatase 1 binding |
| Molecular Function | GO:0004722 | protein serine/threonine phosphatase activity |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0032922 | circadian regulation of gene expression |
| Biological Process | GO:0043153 | entrainment of circadian clock by photoperiod |
| Biological Process | GO:0005977 | glycogen metabolic process |
| Biological Process | GO:0000165 | MAPK cascade |
| Biological Process | GO:0000070 | mitotic sister chromatid segregation |
| Biological Process | GO:0030182 | neuron differentiation |
| Biological Process | GO:0060252 | positive regulation of glial cell proliferation |
| Biological Process | GO:0046579 | positive regulation of Ras protein signal transduction |
| Biological Process | GO:0006470 | protein dephosphorylation |
| Biological Process | GO:0042752 | regulation of circadian rhythm |
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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[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] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[5] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.
[6] 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.