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]
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.
Publication
High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase.
GAPDH (D-glyceraldehyde-3-phosphate dehydrogenase) is a multifunctional protein that is a target for the design of antitrypanosomatid and anti-apoptosis drugs. Here, the first high-resolution (1.75 Angstroms) structure of a human GAPDH is reported. The structure shows that the intersubunit selectivity cleft that has been leveraged in the design of antitrypanosomatid compounds is closed in human GAPDH. Modeling of an anti-trypanosomatid GAPDH ... [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 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | 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