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 | ||
|
* 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. |