| UniProt ID | NDUA5_HUMAN | |
|---|---|---|
| UniProt AC | Q16718 | |
| Protein Name | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 | |
| Gene Name | NDUFA5 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 116 | |
| 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 | MAGVLKKTTGLVGLAVCNTPHERLRILYTKILDVLEEIPKNAAYRKYTEQITNEKLAMVKAEPDVKKLEDQLQGGQLEEVILQAEHELNLARKMREWKLWEPLVEEPPADQWKWPI | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAGVLKKTT ------CCCCCCCCC | 19.46 | - | |
| 27 | Acetylation | PHERLRILYTKILDV HHHHHHHHHHHHHHH | 3.43 | 19608861 | |
| 28 | Phosphorylation | HERLRILYTKILDVL HHHHHHHHHHHHHHH | 12.01 | - | |
| 30 | Acetylation | RLRILYTKILDVLEE HHHHHHHHHHHHHHH | 27.93 | 19608861 | |
| 40 | Succinylation | DVLEEIPKNAAYRKY HHHHHCCCCHHHHHH | 65.95 | 23954790 | |
| 40 | Acetylation | DVLEEIPKNAAYRKY HHHHHCCCCHHHHHH | 65.95 | 26822725 | |
| 46 | Acetylation | PKNAAYRKYTEQITN CCCHHHHHHHHHHCH | 43.79 | 27452117 | |
| 46 | 2-Hydroxyisobutyrylation | PKNAAYRKYTEQITN CCCHHHHHHHHHHCH | 43.79 | - | |
| 55 | 2-Hydroxyisobutyrylation | TEQITNEKLAMVKAE HHHHCHHHHHHHCCC | 43.55 | - | |
| 55 | Acetylation | TEQITNEKLAMVKAE HHHHCHHHHHHHCCC | 43.55 | 27452117 | |
| 57 | Acetylation | QITNEKLAMVKAEPD HHCHHHHHHHCCCCC | 16.28 | 19608861 | |
| 60 | Sumoylation | NEKLAMVKAEPDVKK HHHHHHHCCCCCHHH | 33.67 | 19608861 | |
| 60 | Malonylation | NEKLAMVKAEPDVKK HHHHHHHCCCCCHHH | 33.67 | 26320211 | |
| 60 | Sumoylation | NEKLAMVKAEPDVKK HHHHHHHCCCCCHHH | 33.67 | - | |
| 60 | Acetylation | NEKLAMVKAEPDVKK HHHHHHHCCCCCHHH | 33.67 | 19608861 | |
| 60 | Succinylation | NEKLAMVKAEPDVKK HHHHHHHCCCCCHHH | 33.67 | 27452117 | |
| 66 | Acetylation | VKAEPDVKKLEDQLQ HCCCCCHHHHHHHHC | 60.05 | 25038526 | |
| 67 | Acetylation | KAEPDVKKLEDQLQG CCCCCHHHHHHHHCC | 57.89 | 25038526 | |
| 98 | Succinylation | ARKMREWKLWEPLVE HHHHHHHCCCCCCCC | 38.68 | - | |
| 98 | Succinylation | ARKMREWKLWEPLVE HHHHHHHCCCCCCCC | 38.68 | - | |
| 98 | Acetylation | ARKMREWKLWEPLVE HHHHHHHCCCCCCCC | 38.68 | 25038526 |
| 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 NDUA5_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NDUA5_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 NDUA5_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| DAZP2_HUMAN | DAZAP2 | physical | 16189514 | |
| NDUB1_HUMAN | NDUFB1 | physical | 16189514 | |
| CC85B_HUMAN | CCDC85B | physical | 16189514 | |
| A4_HUMAN | APP | physical | 21832049 | |
| NDUS3_HUMAN | NDUFS3 | physical | 22939629 | |
| NDUB9_HUMAN | NDUFB9 | physical | 22939629 | |
| NDUBA_HUMAN | NDUFB10 | physical | 22939629 | |
| RAB8A_HUMAN | RAB8A | physical | 27173435 | |
| WDR26_HUMAN | WDR26 | physical | 27173435 |
| 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. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-60, AND MASSSPECTROMETRY. | |