Primary Information | |
|---|---|
| BoMiProt ID | Bomi6522 |
| Protein Name | Isocitrate dehydrogenase [NAD] subunit beta, mitochondrial/Isocitric dehydrogenase subunit beta/NAD(+)-isocitrate dehydrogenase subunit 1 |
| Organism | Bos taurus |
| Uniprot ID | O77784 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_001139344.1 |
| Aminoacid Length | 385 |
| Molecular Weight | 42497 |
| FASTA Sequence | Download |
| Gene Name | IDH3B |
| Gene ID | 613338 |
| Protein Existence Status | reviewed |
Secondary Information | |
| Protein Function | It is involved in facilitating the assembly and ensuring the activity of the enzyme catalyzing the decarboxylation of isocitrate into α-ketoglutarate. |
| Biochemical Properties | Bovine NAD(+)-dependent isocitrate dehydrogenase contain four subunits of approx. 40 kDa (subunits 1-4) possessing different peptide maps and electrophoretic properties |
| PTMs | Acetylation |
| Linking IDs | Bomi6522 |
| Bibliography | Weiss, C., Zeng, Y., Huang, J., Sobocka, M. B., & Rushbrook, J. I. (2000). Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing and tissue-dependent expression of subunit 1. Biochemistry, 39(7), 1807–1816. https://doi.org/10.1021/bi991691i |
| Protein Function | It is involved in facilitating the assembly and ensuring the activity of the enzyme catalyzing the decarboxylation of isocitrate into α-ketoglutarate. |
| Biochemical Properties | Bovine NAD(+)-dependent isocitrate dehydrogenase contain four subunits of approx. 40 kDa (subunits 1-4) possessing different peptide maps and electrophoretic properties |
| PTMs | Acetylation |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | NA |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| Linking IDs | |
| Bibliography | Weiss, C., Zeng, Y., Huang, J., Sobocka, M. B., & Rushbrook, J. I. (2000). Bovine NAD+-dependent isocitrate dehydrogenase: alternative splicing and tissue-dependent expression of subunit 1. Biochemistry, 39(7), 1807–1816. https://doi.org/10.1021/bi991691i |