| Tbio | Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial |
Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the beta subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Sep 2016]
Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the beta subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene. [provided by RefSeq, Sep 2016]
Comments
| Disease | Target Count | Z-score | Confidence |
|---|---|---|---|
| Disease Progression | 136 | 0.0 | 0.0 |
| Retinitis Pigmentosa | 226 | 0.0 | 4.0 |
| Retinitis Pigmentosa 46 | 1 | 0.0 | 0.0 |
| Stomach Neoplasms | 300 | 0.0 | 0.0 |
| Disease | Target Count | P-value |
|---|---|---|
| malignant mesothelioma | 3232 | 5.9e-07 |
| psoriasis | 6694 | 2.9e-05 |
| Multiple myeloma | 1332 | 1.8e-04 |
| ovarian cancer | 8520 | 1.8e-04 |
| osteosarcoma | 7950 | 9.4e-04 |
| Waldenstrons macroglobulinemia | 765 | 9.1e-03 |
| Disease | log2 FC | p |
|---|---|---|
| malignant mesothelioma | 1.300 | 5.9e-07 |
| Multiple myeloma | 1.506 | 1.8e-04 |
| osteosarcoma | -1.049 | 9.4e-04 |
| ovarian cancer | 1.100 | 1.8e-04 |
| psoriasis | 1.800 | 2.9e-05 |
| Waldenstrons macroglobulinemia | 1.071 | 9.1e-03 |
| Species | Source | Disease |
|---|---|---|
| OMA EggNOG | ||
| Inparanoid OMA EggNOG | ||
| Inparanoid OMA EggNOG | ||
| Inparanoid OMA EggNOG | ||
| Inparanoid OMA EggNOG | ||
| Inparanoid OMA EggNOG | ||
| Inparanoid OMA EggNOG | ||
| OMA EggNOG | ||
| OMA EggNOG | ||
| Inparanoid OMA | ||
| Inparanoid OMA | ||
| Inparanoid OMA | ||
| Inparanoid OMA |
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEV 1 - 70 FKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFA 71 - 140 NVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGR 141 - 210 GKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNL 211 - 280 AAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVK 281 - 350 KVIKVGKVRTRDMGGYSTTTDFIKSVIGHLQTKGS 351 - 385 //
