Activating Compound | Comment | Organism | Structure |
---|---|---|---|
doxorubicin | treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug | Homo sapiens | |
gemcitabine | treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C149A | mutant has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition | Homo sapiens |
D32A | mutant is unable to bind NAD+, is enzymatically inactive and has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Homo sapiens | 5829 | - |
nucleus | - |
Homo sapiens | 5634 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
A-549 cell | - |
Homo sapiens | - |
liver | - |
Homo sapiens | - |
Subunits | Comment | Organism |
---|---|---|
More | recombinant GAPDH binds directly with high affinity to a single-stranded oligonucleotide comprising three telomeric DNA repeats. Nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding.The stoichiometry of the interaction is 2:1 DNA:GAPDH, and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide | Homo sapiens |