| UniProt ID | NDUAA_MOUSE | |
|---|---|---|
| UniProt AC | Q99LC3 | |
| Protein Name | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial | |
| Gene Name | Ndufa10 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 355 | |
| Subcellular Localization | Mitochondrion matrix . | |
| 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 | MALRLLRLVPASAPARGLAAGAQRVGRIHTSVHCKLRYGLLAAILGDKTTKKLHEYSRVITVDGNICSGKNKLAKEIAQQLGMKHYPEAGIQYSSTTTGDGRPLDIEFSGSCSLEKFYDDPKSNDGNSYRLQSWLYASRLLQYADALEHLLSTGQGVVLERSIYSDFVFLEAMYNQGYIRKQCVDHYNEIKRLTLPEYLPPHAVIYIDVPVPEVQSRIQKKGDPHEMKVTSAYLQDIENAYKKTFLPKMSEMCEVLVYDSWEAEDPTKVVEDIEYLKYNKGPWLKQDDWTFHYLRMLVQDKTEVLNYTTIPVYLPEITIGAHQGSRIYNSFRELPGRKYAPGYNAEVGDKWIWLK | |
| 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 |
|---|---|---|---|---|---|
| 67 | S-nitrosocysteine | ITVDGNICSGKNKLA EEECCCCCCCCHHHH | 5.21 | - | |
| 67 | S-palmitoylation | ITVDGNICSGKNKLA EEECCCCCCCCHHHH | 5.21 | 28526873 | |
| 67 | S-nitrosylation | ITVDGNICSGKNKLA EEECCCCCCCCHHHH | 5.21 | 22588120 | |
| 72 | Acetylation | NICSGKNKLAKEIAQ CCCCCCHHHHHHHHH | 53.99 | 24062335 | |
| 75 | Acetylation | SGKNKLAKEIAQQLG CCCHHHHHHHHHHHC | 61.15 | 24062335 | |
| 75 | Succinylation | SGKNKLAKEIAQQLG CCCHHHHHHHHHHHC | 61.15 | 26388266 | |
| 84 | Acetylation | IAQQLGMKHYPEAGI HHHHHCCCCCCCCCE | 37.88 | 24062335 | |
| 112 | S-nitrosocysteine | DIEFSGSCSLEKFYD EEEEECCEEEEEECC | 6.50 | - | |
| 112 | S-nitrosylation | DIEFSGSCSLEKFYD EEEEECCEEEEEECC | 6.50 | 21278135 | |
| 122 | Acetylation | EKFYDDPKSNDGNSY EEECCCCCCCCCCCH | 69.73 | 23576753 | |
| 122 | Succinylation | EKFYDDPKSNDGNSY EEECCCCCCCCCCCH | 69.73 | - | |
| 122 | Ubiquitination | EKFYDDPKSNDGNSY EEECCCCCCCCCCCH | 69.73 | - | |
| 122 | Succinylation | EKFYDDPKSNDGNSY EEECCCCCCCCCCCH | 69.73 | 23806337 | |
| 181 | Acetylation | YNQGYIRKQCVDHYN HHCCCCHHHHHHCHH | 38.19 | 16916647 | |
| 183 | S-nitrosocysteine | QGYIRKQCVDHYNEI CCCCHHHHHHCHHHH | 4.33 | - | |
| 183 | S-nitrosylation | QGYIRKQCVDHYNEI CCCCHHHHHHCHHHH | 4.33 | 21278135 | |
| 191 | Acetylation | VDHYNEIKRLTLPEY HHCHHHHHHCCCCCC | 34.87 | 23864654 | |
| 228 | Acetylation | KGDPHEMKVTSAYLQ CCCHHHHHCCHHHHH | 39.10 | 24062335 | |
| 230 | Phosphorylation | DPHEMKVTSAYLQDI CHHHHHCCHHHHHHH | 11.34 | 29899451 | |
| 231 | Phosphorylation | PHEMKVTSAYLQDIE HHHHHCCHHHHHHHH | 20.22 | 20495213 | |
| 233 | Phosphorylation | EMKVTSAYLQDIENA HHHCCHHHHHHHHHH | 12.50 | 29899451 | |
| 242 | Succinylation | QDIENAYKKTFLPKM HHHHHHHHHHCHHHH | 42.82 | 26388266 | |
| 242 | Acetylation | QDIENAYKKTFLPKM HHHHHHHHHHCHHHH | 42.82 | 23864654 | |
| 243 | Succinylation | DIENAYKKTFLPKMS HHHHHHHHHCHHHHH | 31.65 | 26388266 | |
| 243 | Acetylation | DIENAYKKTFLPKMS HHHHHHHHHCHHHHH | 31.65 | 130453 | |
| 250 | Phosphorylation | KTFLPKMSEMCEVLV HHCHHHHHHCCEEEE | 28.45 | 24652937 | |
| 277 | Succinylation | VEDIEYLKYNKGPWL EEEHHHHEECCCCCC | 45.97 | 23954790 | |
| 277 | Acetylation | VEDIEYLKYNKGPWL EEEHHHHEECCCCCC | 45.97 | 23864654 | |
| 277 | Ubiquitination | VEDIEYLKYNKGPWL EEEHHHHEECCCCCC | 45.97 | - | |
| 285 | Succinylation | YNKGPWLKQDDWTFH ECCCCCCCCCCHHHH | 48.05 | - | |
| 285 | Succinylation | YNKGPWLKQDDWTFH ECCCCCCCCCCHHHH | 48.05 | 23806337 | |
| 285 | Acetylation | YNKGPWLKQDDWTFH ECCCCCCCCCCHHHH | 48.05 | 23806337 | |
| 318 | Phosphorylation | PVYLPEITIGAHQGS CEECCEEEEECCCCC | 16.23 | - | |
| 325 | Phosphorylation | TIGAHQGSRIYNSFR EEECCCCCHHHHCHH | 14.66 | - | |
| 338 | Ubiquitination | FRELPGRKYAPGYNA HHCCCCCCCCCCCCC | 52.24 | 27667366 | |
| 350 | Succinylation | YNAEVGDKWIWLK-- CCCCCCCEEEEEC-- | 34.35 | 23806337 | |
| 350 | Acetylation | YNAEVGDKWIWLK-- CCCCCCCEEEEEC-- | 34.35 | 16916647 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 250 | S | Phosphorylation | Kinase | PINK1 | Q99MQ3 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 242 | K | Acetylation |
| - |
| 250 | S | Phosphorylation |
| 24652937 |
* 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 NDUAA_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of NDUAA_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-181; LYS-242 ANDLYS-350, AND MASS SPECTROMETRY. | |