HCSGD entry for PPP2R4
1. General information
| Official gene symbol | PPP2R4 |
|---|---|
| Entrez ID | 5524 |
| Gene full name | protein phosphatase 2A activator, regulatory subunit 4 |
| Other gene symbols | PP2A PR53 PTPA |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
This gene isn't in Literature mining network.
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0000159 | Protein phosphatase type 2A complex | TAS | cellular_component |
| GO:0000413 | Protein peptidyl-prolyl isomerization | IBA | biological_process |
| GO:0003755 | Peptidyl-prolyl cis-trans isomerase activity | IBA | molecular_function |
| GO:0005102 | Receptor binding | IPI | molecular_function |
| GO:0005524 | ATP binding | IDA | molecular_function |
| GO:0005634 | Nucleus | IDA | cellular_component |
| GO:0005730 | Nucleolus | IDA | cellular_component |
| GO:0005737 | Cytoplasm | IDA | cellular_component |
| GO:0006200 | ATP catabolic process | IDA | biological_process |
| GO:0006457 | Protein folding | IEA | biological_process |
| GO:0008160 | Protein tyrosine phosphatase activator activity | IDA | molecular_function |
| GO:0008601 | Protein phosphatase type 2A regulator activity | IDA TAS | molecular_function |
| GO:0016887 | ATPase activity | IDA | molecular_function |
| GO:0019211 | Phosphatase activator activity | IEA | molecular_function |
| GO:0030472 | Mitotic spindle organization in nucleus | IBA | biological_process |
| GO:0032515 | Negative regulation of phosphoprotein phosphatase activity | IDA | biological_process |
| GO:0032516 | Positive regulation of phosphoprotein phosphatase activity | IDA | biological_process |
| GO:0034704 | Calcium channel complex | IDA | cellular_component |
| GO:0035307 | Positive regulation of protein dephosphorylation | IDA | biological_process |
| GO:0035308 | Negative regulation of protein dephosphorylation | IDA | biological_process |
| GO:0042803 | Protein homodimerization activity | IDA | molecular_function |
| GO:0043065 | Positive regulation of apoptotic process | IDA | biological_process |
| GO:0043666 | Regulation of phosphoprotein phosphatase activity | IDA | biological_process |
| GO:0046982 | Protein heterodimerization activity | TAS | molecular_function |
| GO:0051721 | Protein phosphatase 2A binding | IDA | molecular_function |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.8881721059 | 0.1173538923 | 0.9999902473 | 0.6574750638 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
| Data source | Up or down | Log fold change |
|---|---|---|
| GSE11954 | Down | -0.1421512631 |
| GSE13712_SHEAR | Down | -0.0785977861 |
| GSE13712_STATIC | Up | 0.0472321519 |
| GSE19018 | Up | 0.0083949910 |
| GSE19899_A1 | Down | -0.0394899115 |
| GSE19899_A2 | Up | 0.4400738957 |
| PubMed_21979375_A1 | Up | 0.8125207993 |
| PubMed_21979375_A2 | Up | 0.4245288576 |
| GSE35957 | Down | -0.4033823743 |
| GSE36640 | Down | -0.1771920317 |
| GSE54402 | Down | -0.1485546407 |
| GSE9593 | Down | -0.3251404207 |
| GSE43922 | Down | -0.0109015821 |
| GSE24585 | Down | -0.2597574339 |
| GSE37065 | Down | -0.2599065881 |
| GSE28863_A1 | Down | -0.0733818178 |
| GSE28863_A2 | Down | -0.2181473293 |
| GSE28863_A3 | Down | -0.3989303737 |
| GSE28863_A4 | Up | 0.0234615023 |
| GSE48662 | Up | 0.0223006215 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-30a-5p | MIMAT0000087 | MIRT005188 | pSILAC//Proteomics;Other | Functional MTI (Weak) | 18668040 |
| hsa-miR-326 | MIMAT0000756 | MIRT043628 | CLASH | Functional MTI (Weak) | 23622248 |
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- mirRecord
No target information from mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 9 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 26657292 | Mitochondrial reactive oxygen species perturb AKT/cyclin D1 cell cycle signaling via oxidative inactivation of PP2A in lowdose irradiated human fibroblasts |
| 26657292 | Excess ROS promoted oxidative inactivation of protein phosphatase PP2A which in turn led to disruption of normal negative feed-back control of AKT/cyclin D1 signaling in cells treated with long-term FR |
| 25341065 | Like A1AT, protein phosphatase 2A (PP2A), a major serine-threonine phosphatase, regulates similar biologic processes and plays a key role in chronic obstructive pulmonary disease |
| 25341065 | OBJECTIVES: Given their common effects, this study investigated whether A1AT acts via PP2A to alter tumor necrosis factor (TNF) signaling, inflammation, and proteolytic responses in this disease |
| 25341065 | METHODS: PP2A activity was measured in peripheral blood neutrophils from A1AT-deficient (PiZZ) and healthy (PiMM) individuals and in alveolar macrophages from normal (60 mg/kg) and high-dose (120 mg/kg) A1AT-treated PiZZ subjects |
| 25341065 | PP2A activation was assessed in human neutrophils, airway epithelial cells, and peripheral blood monocytes treated with plasma purified A1AT protein |
| 25341065 | Similarly, lung PP2A activity was measured in mice administered intranasal A1AT |
| 25341065 | PP2A was silenced in lung epithelial cells treated with A1AT and matrix metalloproteinase and cytokine production was then measured following TNF-alpha stimulation |
| 25341065 | MEASUREMENTS AND MAIN RESULTS: PP2A was significantly lower in neutrophils isolated from PiZZ compared with PiMM subjects |
| 25341065 | A1AT protein activated PP2A in human alveolar macrophages, monocytes, neutrophils, airway epithelial cells, and in mouse lungs |
| 25341065 | CONCLUSIONS: Together, these data indicate that A1AT modulates PP2A to counter inflammatory and proteolytic responses induced by TNF signaling in the lung |
| 24295239 | In addition, we demonstrate that FADD phosphorylation and the recruitment of PP2A and FADD to PKCbeta are induced responses to oxidative stress, and that the extent of FADD phosphorylation in wild-type mice was augmented during aging, accompanied by impairment of the interaction between PKCbeta and PP2A |
| 22961627 | In addition, we found that PP2A prevented the interaction of hTERT with 14-3-3theta signaling protein, an hTERT binding partner that is required for nuclear localization of hTERT |
| 22961627 | Activation of PP2A by overexpression of PP2AC or PR65 led to cytoplasmic accumulation of hTERT, which was reversed by treatment with PP2A inhibitor okadaic acid |
| 22961627 | Together, these observations suggest that PP2A regulates hTERT subcellular localization, in addition to its inhibitory effects on telomerase activity |
| 22665485 | STRN4 (Zinedin) is a regulatory subunit of protein phosphatase 2A (PP2A) and was recently shown to be a component of a novel protein complex called striatin-interacting phosphatase and kinase (STRIPAK) |
| 22665485 | In addition, STRN4 reduced MINK1 activity in the presence of catalytic and structural subunits of PP2A |
| 17658517 | Cells were induced to senescence by inhibition of phosphatase activity (VHR, MKP3, or PP2A) without additional cellular stress |
| 15843932 | Among these strains, short telomeres were found in the sit4 disruptant that lacks one form of protein phosphatase 2A (PP2A) |
| 15843932 | These observations suggest that the PP2A pathway regulates life span in yeast |
| 15034937 | Using bioinformatics-, Western-blotting-, yeast-two-hybrid-system-, polymerase chain reaction (PCR)-, and fluorescence microscopy-analyses, we demonstrate here that the neuroprotective protein p60TRP (p60-transcription-regulator-protein) is a basic helix-loop-helix (bHLH) domain-containing member of a new protein family that interacts with the Ran-binding-protein-5 (RanBP5) and the protein-phosphatase-2A (PP2A) |
| 12676512 | However, the mechanisms how ceramide directly activates enzymes such as JNK and PP2A are still not clear |
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