HCSGD entry for GAPDH
1. General information
| Official gene symbol | GAPDH |
|---|---|
| Entrez ID | 2597 |
| Gene full name | glyceraldehyde-3-phosphate dehydrogenase |
| Other gene symbols | G3PD GAPD |
| 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:0000226 | Microtubule cytoskeleton organization | ISS | biological_process |
| GO:0004365 | Glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity | IEA ISS NAS | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005634 | Nucleus | ISS | cellular_component |
| GO:0005737 | Cytoplasm | IDA ISS | cellular_component |
| GO:0005811 | Lipid particle | IDA | cellular_component |
| GO:0005829 | Cytosol | ISS TAS | cellular_component |
| GO:0005886 | Plasma membrane | IDA | cellular_component |
| GO:0005975 | Carbohydrate metabolic process | TAS | biological_process |
| GO:0006006 | Glucose metabolic process | TAS | biological_process |
| GO:0006094 | Gluconeogenesis | TAS | biological_process |
| GO:0006096 | Glycolysis | IEA TAS | biological_process |
| GO:0008017 | Microtubule binding | ISS | molecular_function |
| GO:0015630 | Microtubule cytoskeleton | ISS | cellular_component |
| GO:0017148 | Negative regulation of translation | IDA IMP | biological_process |
| GO:0030529 | Ribonucleoprotein complex | IDA | cellular_component |
| GO:0035605 | Peptidyl-cysteine S-nitrosylase activity | ISS | molecular_function |
| GO:0035606 | Peptidyl-cysteine S-trans-nitrosylation | ISS | biological_process |
| GO:0042802 | Identical protein binding | IPI | molecular_function |
| GO:0044281 | Small molecule metabolic process | TAS | biological_process |
| GO:0048471 | Perinuclear region of cytoplasm | IEA | cellular_component |
| GO:0050661 | NADP binding | IEA | molecular_function |
| GO:0050821 | Protein stabilization | ISS | biological_process |
| GO:0051287 | NAD binding | IEA | molecular_function |
| GO:0051402 | Neuron apoptotic process | ISS | biological_process |
| GO:0070062 | Extracellular vesicular exosome | IDA | cellular_component |
| GO:0071346 | Cellular response to interferon-gamma | IDA | biological_process |
| GO:0097452 | GAIT complex | IDA | cellular_component |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.6220259831 | 0.6195471791 | 0.9999902473 | 1.0000000000 |
- 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 | Up | 0.0754951013 |
| GSE13712_SHEAR | Down | -0.0205366245 |
| GSE13712_STATIC | Down | -0.0706865108 |
| GSE19018 | Up | 0.6401458027 |
| GSE19899_A1 | Down | -0.2006719248 |
| GSE19899_A2 | Down | -0.1013600889 |
| PubMed_21979375_A1 | Up | 0.6237454841 |
| PubMed_21979375_A2 | Down | -0.0445247671 |
| GSE35957 | Down | -0.1551622854 |
| GSE36640 | Down | -0.4384799235 |
| GSE54402 | Up | 0.1147460325 |
| GSE9593 | Up | 0.0048188683 |
| GSE43922 | Down | -0.1016243637 |
| GSE24585 | Up | 0.0591464643 |
| GSE37065 | Up | 0.0248665019 |
| GSE28863_A1 | Up | 0.0025803377 |
| GSE28863_A2 | Up | 0.0777591374 |
| GSE28863_A3 | Up | 0.1236546487 |
| GSE28863_A4 | Up | 0.0766822030 |
| GSE48662 | Down | -0.2483593251 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Name | Drug | Accession number |
|---|---|---|
| NADH | DB00157 | NUTR00041 | DB01907 | EXPT02287 | DB03527 |
| Adenosine-5-Diphosphoribose | DB02059 | EXPT00544 |
| Thionicotinamide-Adenine-Dinucleotide | DB03893 | EXPT02928 |
| 4-(2-AMINOETHYL)BENZENESULFONYL FLUORIDE | DB07347 | - |
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
|---|---|---|---|---|---|
| hsa-miR-29c-3p | MIMAT0000681 | MIRT001929 | Luciferase reporter assay | Non-Functional MTI | 18390668 |
| hsa-miR-644a | MIMAT0003314 | MIRT007162 | Luciferase reporter assay//qRT-PCR//Western blot | Functional MTI | 23091630 |
| hsa-miR-1229-3p | MIMAT0005584 | MIRT036280 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-877-3p | MIMAT0004950 | MIRT036904 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-423-5p | MIMAT0004748 | MIRT038105 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-342-5p | MIMAT0004694 | MIRT038226 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-296-3p | MIMAT0004679 | MIRT038345 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-106b-3p | MIMAT0004672 | MIRT038579 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-29b-2-5p | MIMAT0004515 | MIRT038710 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-766-3p | MIMAT0003888 | MIRT039028 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-769-3p | MIMAT0003887 | MIRT039090 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-615-3p | MIMAT0003283 | MIRT039782 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-501-5p | MIMAT0002872 | MIRT041139 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-484 | MIMAT0002174 | MIRT041819 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-324-3p | MIMAT0000762 | MIRT042878 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-331-3p | MIMAT0000760 | MIRT043451 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-320a | MIMAT0000510 | MIRT044658 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-149-5p | MIMAT0000450 | MIRT045446 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-23b-3p | MIMAT0000418 | MIRT046276 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-96-5p | MIMAT0000095 | MIRT048718 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-93-5p | MIMAT0000093 | MIRT048761 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-92a-3p | MIMAT0000092 | MIRT049457 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-25-3p | MIMAT0000081 | MIRT050206 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-17-3p | MIMAT0000071 | MIRT050751 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-17-5p | MIMAT0000070 | MIRT050952 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-let-7b-5p | MIMAT0000063 | MIRT052138 | 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: 11 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 24853433 | We found that radiation induced the expression and activation of glyceraldehyde-3-phosphate dehydrogenase that has an important role in glycolysis |
| 23377192 | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) plays a central role in glycolysis |
| 23377192 | Knockdown of GAPDH by RNA interference induced the accelerated senescent phenotype in A549 cells, suggesting that GAPDH is a potential molecular target for combination chemotherapy |
| 23377192 | Our study identified the antimetabolite drugs active in senescent cells that can be used in combination with GAPDH inhibitors in cancer treatment |
| 22847419 | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) induces cancer cell senescence by interacting with telomerase RNA component |
| 22847419 | Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a key mediator of many oxidative stress responses, involving GAPDH nuclear translocation and induction of cell death |
| 22847419 | We report here that GAPDH interacts with the telomerase RNA component (TERC), inhibits telomerase activity, and induces telomere shortening and breast cancer cell senescence |
| 22847419 | The Rossmann fold containing NAD(+) binding region on GAPDH is responsible for the interaction with TERC, whereas a lysine residue in the GAPDH catalytic domain is required for inhibiting telomerase activity and disrupting telomere maintenance |
| 22847419 | Furthermore, the GAPDH substrate glyceraldehyde-3-phosphate (G3P) and the nitric oxide donor S-nitrosoglutathione (GSNO) both negatively regulate GAPDH inhibition of telomerase activity |
| 22847419 | Thus, we demonstrate that GAPDH is regulated to target the telomerase complex, resulting in an arrest of telomere maintenance and cancer cell proliferation |
| 22067611 | Also examined were the expression of genes involved in proliferation and mineralization such as human alkaline phosphatase (ALP), beta-actin, collagen 1 (col-1), core binding factor (cbfa-1), dentin matrix protein (DMP-1), dentin sialophosphoprotein (DSPP), GAPDH, hTERT, osteocalcin (OCN), osteopontin (OPN) as well as oncoproteins involved in senescence (p16, p21 and p53) using RT-PCR |
| 21895736 | GAPDH: a common enzyme with uncommon functions |
| 21895736 | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has long been recognized as an important enzyme for energy metabolism and the production of ATP and pyruvate through anaerobic glycolysis in the cytoplasm |
| 21895736 | Recent studies have shown that GAPDH has multiple functions independent of its role in energy metabolism |
| 21895736 | Although increased GAPDH gene expression and enzymatic function is associated with cell proliferation and tumourigenesis, conditions such as oxidative stress impair GAPDH catalytic activity and lead to cellular aging and apoptosis |
| 21895736 | The mechanism(s) underlying the effects of GAPDH on cellular proliferation remains unclear, yet much evidence has been accrued that demonstrates a variety of interacting partners for GAPDH, including proteins, various RNA species and telomeric DNA |
| 21895736 | The present mini review summarizes recent findings relating to the extraglycolytic functions of GAPDH and highlights the significant role this enzyme plays in regulating both cell survival and apoptotic death |
| 21749859 | Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) is a pivotal glycolytic enzyme, and a signaling molecule which acts at the interface between stress factors and the cellular apoptotic machinery |
| 21749859 | Earlier, we found that knockdown of GAPDH in human carcinoma cell lines resulted in cell proliferation arrest and chemoresistance to S phase-specific cytotoxic agents |
| 21749859 | To elucidate the mechanism by which GAPDH depletion arrests cell proliferation, we examined the effect of GAPDH knockdown on human carcinoma cells A549 |
| 21749859 | Rescue experiments using metabolic and genetic models confirmed that GAPDH has important regulatory functions linking the energy metabolism and the cell cycle networks |
| 21749859 | Induction of senescence in LKB1-deficient non-small cell lung cancer cells via GAPDH depletion suggests a novel strategy to control tumor cell proliferation |
| 20707929 | Effect of experimental treatment on GAPDH mRNA expression as a housekeeping gene in human diploid fibroblasts |
| 20707929 | The purpose of this study was to determine the effect of different experimental treatments on the expression of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) mRNA so that the reliability of GAPDH as reference gene for quantitative real time RT-PCR in human diploid fibroblasts (HDFs) can be validated |
| 20707929 | Total RNA concentration and purity were determined prior to GAPDH mRNA quantification |
| 20707929 | Standard curve of GAPDH expression in serial diluted total RNA, melting curve analysis and agarose gel electrophoresis were used to determine the reliability of GAPDH as reference gene |
| 20707929 | However the expression level of GAPDH was consistent in all treatment groups |
| 20707929 | CONCLUSION: The study demonstrated that GAPDH is reliable as reference gene for quantitative gene expression analysis in HDFs |
| 19458325 | RESULTS: Several large fragments of typical cytosolic proteins, such as GAPDH, triosephosphate isomerase, and M2-type pyruvate kinase increased approximately two- to threefold in the prematurely senescent ARPE-19 cells |
| 7857667 | IgG binding, creatinine, and glyceraldehyde-3-phosphate dehydrogenase are normal |
| 3179456 | Treatments were assessed for their ability to induce in vitro the following changes observed in normal erythrocytes aged in vivo: 1 increased breakdown of band 3 as detected by immunoblotting, 2 decrease in anion transport efficiency as detected with a sulfate self-exchange assay, 3 decrease in total glyceraldehyde 3-phosphate dehydrogenase activity with an increase in membrane-bound activity, and 4 increase in the binding of autologous IgG as detected with a protein A binding assay |
| 3458208 | Results of our studies indicate that erythrocytes of all ages from vitamin E-deficient rats behave like old erythrocytes from normal rats, as determined by their susceptibility to phagocytosis, IgG binding, anion transport ability, and glyceraldehyde-3-phosphate dehydrogenase activity |
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