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 | ||
* 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. |