UniProt ID | NDUA7_HUMAN | |
---|---|---|
UniProt AC | O95182 | |
Protein Name | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 7 | |
Gene Name | NDUFA7 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 113 | |
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 | MASATRLIQRLRNWASGHDLQGKLQLRYQEISKRTQPPPKLPVGPSHKLSNNYYCTRDGRRESVPPSIIMSSQKALVSGKPAESSAVAATEKKAVTPAPPIKRWELSSDQPYL | |
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 | ------MASATRLIQ ------CCHHHHHHH | 14.10 | - | |
3 | Phosphorylation | -----MASATRLIQR -----CCHHHHHHHH | 28.95 | 28270605 | |
5 | Phosphorylation | ---MASATRLIQRLR ---CCHHHHHHHHHH | 24.42 | 28270605 | |
12 | Methylation | TRLIQRLRNWASGHD HHHHHHHHHHHCCCC | 38.54 | 115484701 | |
23 | Ubiquitination | SGHDLQGKLQLRYQE CCCCCHHHHHHHHHH | 21.79 | 22817900 | |
32 | Phosphorylation | QLRYQEISKRTQPPP HHHHHHHHHHCCCCC | 18.48 | 23312004 | |
33 | 2-Hydroxyisobutyrylation | LRYQEISKRTQPPPK HHHHHHHHHCCCCCC | 66.19 | - | |
40 | Succinylation | KRTQPPPKLPVGPSH HHCCCCCCCCCCCCC | 71.80 | 27452117 | |
40 | Malonylation | KRTQPPPKLPVGPSH HHCCCCCCCCCCCCC | 71.80 | 26320211 | |
40 | Acetylation | KRTQPPPKLPVGPSH HHCCCCCCCCCCCCC | 71.80 | - | |
53 | Phosphorylation | SHKLSNNYYCTRDGR CCCCCCCEEECCCCC | 12.27 | 21945579 | |
54 | Phosphorylation | HKLSNNYYCTRDGRR CCCCCCEEECCCCCC | 6.89 | 21945579 | |
56 | Phosphorylation | LSNNYYCTRDGRRES CCCCEEECCCCCCCC | 18.70 | 21945579 | |
63 | Phosphorylation | TRDGRRESVPPSIIM CCCCCCCCCCHHHEE | 37.81 | 23312004 | |
67 | Phosphorylation | RRESVPPSIIMSSQK CCCCCCHHHEEECCE | 20.76 | 18691976 | |
78 | Phosphorylation | SSQKALVSGKPAESS ECCEEHHCCCCCCCC | 41.78 | 17081983 | |
80 | Malonylation | QKALVSGKPAESSAV CEEHHCCCCCCCCCC | 33.28 | 26320211 | |
80 | Acetylation | QKALVSGKPAESSAV CEEHHCCCCCCCCCC | 33.28 | 26051181 | |
84 | Phosphorylation | VSGKPAESSAVAATE HCCCCCCCCCCCCCC | 26.21 | 26437602 | |
85 | Phosphorylation | SGKPAESSAVAATEK CCCCCCCCCCCCCCC | 20.47 | - | |
90 | Phosphorylation | ESSAVAATEKKAVTP CCCCCCCCCCCCCCC | 38.30 | - | |
92 | 2-Hydroxyisobutyrylation | SAVAATEKKAVTPAP CCCCCCCCCCCCCCC | 41.50 | - | |
92 | Acetylation | SAVAATEKKAVTPAP CCCCCCCCCCCCCCC | 41.50 | 26051181 | |
96 | Phosphorylation | ATEKKAVTPAPPIKR CCCCCCCCCCCCCCC | 20.70 | 23312004 | |
102 | 2-Hydroxyisobutyrylation | VTPAPPIKRWELSSD CCCCCCCCCEECCCC | 58.18 | - |
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 NDUA7_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NDUA7_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 NDUA7_HUMAN !! |
Kegg Disease | ||||||
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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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Phosphorylation | |
Reference | PubMed |
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY. |