| UniProt ID | NDUA2_HUMAN | |
|---|---|---|
| UniProt AC | O43678 | |
| Protein Name | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 | |
| Gene Name | NDUFA2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 99 | |
| Subcellular Localization |
Mitochondrion inner membrane Peripheral membrane protein Matrix side . |
|
| Protein Description | Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.. | |
| Protein Sequence | MAAAAASRGVGAKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSDVQPKLWARYAFGQETNVPLNNFSADQVTRALENVLSGKA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAAAAASRG ------CHHHHHHCC | 13.05 | 1518044 | |
| 7 | Phosphorylation | -MAAAAASRGVGAKL -CHHHHHHCCCHHHH | 25.49 | 20068231 | |
| 8 | Methylation | MAAAAASRGVGAKLG CHHHHHHCCCHHHHC | 38.81 | 115383635 | |
| 13 | Acetylation | ASRGVGAKLGLREIR HHCCCHHHHCCHHHH | 36.84 | 25825284 | |
| 13 | Malonylation | ASRGVGAKLGLREIR HHCCCHHHHCCHHHH | 36.84 | 32601280 | |
| 27 | Phosphorylation | RIHLCQRSPGSQGVR HEEEHHCCCCCHHHH | 14.03 | 29214152 | |
| 46 | Malonylation | KRYVELKKANPDLPI HHHHHHHHHCCCCCE | 67.05 | 26320211 | |
| 64 | Acetylation | ECSDVQPKLWARYAF ECCCCCHHHHHHHHH | 39.30 | 25038526 | |
| 64 | Succinylation | ECSDVQPKLWARYAF ECCCCCHHHHHHHHH | 39.30 | - | |
| 64 | Succinylation | ECSDVQPKLWARYAF ECCCCCHHHHHHHHH | 39.30 | - | |
| 98 | Ubiquitination | LENVLSGKA------ HHHHHCCCC------ | 47.77 | 24816145 | |
| 98 | 2-Hydroxyisobutyrylation | LENVLSGKA------ HHHHHCCCC------ | 47.77 | - | |
| 98 | Acetylation | LENVLSGKA------ HHHHHCCCC------ | 47.77 | 25953088 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of NDUA2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NDUA2_HUMAN !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of NDUA2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
