GAPDH
Gene Ontology Biological Process
- carbohydrate metabolic process [TAS]
- cellular response to interferon-gamma [IDA]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [TAS]
- microtubule cytoskeleton organization [ISS]
- negative regulation of translation [IDA, IMP]
- neuron apoptotic process [ISS]
- peptidyl-cysteine S-trans-nitrosylation [ISS]
- protein stabilization [ISS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- GAIT complex [IDA]
- cytoplasm [IDA, ISS]
- cytosol [IDA, ISS, TAS]
- extracellular vesicular exosome [IDA]
- intracellular membrane-bounded organelle [IDA]
- lipid particle [IDA]
- membrane [IDA]
- microtubule cytoskeleton [ISS]
- nuclear membrane [IDA]
- nucleus [IDA, ISS]
- plasma membrane [IDA]
- ribonucleoprotein complex [IDA]
- vesicle [IDA]
GAPDH
Gene Ontology Biological Process
- carbohydrate metabolic process [TAS]
- cellular response to interferon-gamma [IDA]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [TAS]
- microtubule cytoskeleton organization [ISS]
- negative regulation of translation [IDA, IMP]
- neuron apoptotic process [ISS]
- peptidyl-cysteine S-trans-nitrosylation [ISS]
- protein stabilization [ISS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- GAIT complex [IDA]
- cytoplasm [IDA, ISS]
- cytosol [IDA, ISS, TAS]
- extracellular vesicular exosome [IDA]
- intracellular membrane-bounded organelle [IDA]
- lipid particle [IDA]
- membrane [IDA]
- microtubule cytoskeleton [ISS]
- nuclear membrane [IDA]
- nucleus [IDA, ISS]
- plasma membrane [IDA]
- ribonucleoprotein complex [IDA]
- vesicle [IDA]
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Characterization of heparin-induced glyceraldehyde-3-phosphate dehydrogenase early amyloid-like oligomers and their implication in α-synuclein aggregation.
Lewy bodies and Lewy neurites, neuropathological hallmarks of several neurological diseases, are mainly made of filamentous assemblies of α-synuclein. However, other macromolecules including Tau, ubiquitin, glyceraldehyde-3-phosphate dehydrogenase, and glycosaminoglycans are routinely found associated with these amyloid deposits. Glyceraldehyde-3-phosphate dehydrogenase is a glycolytic enzyme that can form fibrillar aggregates in the presence of acidic membranes, but its role in Parkinson disease ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| GAPDH GAPDH | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 3559297 | |
| GAPDH GAPDH | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | - | |
| GAPDH GAPDH | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3706718 | |
| GAPDH GAPDH | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | - | |
| GAPDH GAPDH | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | High | - | BioGRID | - |
Curated By
- BioGRID