UniProt ID | NDUA9_MOUSE | |
---|---|---|
UniProt AC | Q9DC69 | |
Protein Name | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 9, mitochondrial | |
Gene Name | Ndufa9 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 377 | |
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 | MAAAVRFRVVRALPMSRPAITAAATSVFCGSSHRQLHHAVIPHGKGGRSSVSGVVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDVYDIMHLRLMGDLGQLTFLEWDARDKDSIRKAVQHSNVVINLIGREWETRNFDFEDVFVNIPRAIAQASKEAGVERFIHVSHLNASMKSSSKSLRSKAVGEKEVRSVFPEAIIIRPSDIFGREDRFLNHFANYRWFLAVPLVSLGFKTVKQPVYVADVSKGIVNATKDPDAVGKTFAFTGPNRYLLFHLVKYIFGMTHRTFIPYPLPLFVYSWIGKLFGLSPFEPWTTKDKVERIHISDVMPTDLPGLEDLGVQPTPLELKSIEVLRRHRTYRWLSSEIEETKPAKTVNY | |
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 |
---|---|---|---|---|---|
16 | Phosphorylation | VVRALPMSRPAITAA EEECCCCCCHHHHHH | 32.92 | 22802335 | |
21 | Phosphorylation | PMSRPAITAAATSVF CCCCHHHHHHHCEEC | 16.61 | 22802335 | |
68 | Phosphorylation | ATGFLGRYVVNHLGR CCCHHHHHHHHHHHC | 13.62 | 27180971 | |
86 | S-palmitoylation | QVIIPYRCDVYDIMH EEEEEECCCHHHHHH | 3.24 | 26165157 | |
86 | S-nitrosocysteine | QVIIPYRCDVYDIMH EEEEEECCCHHHHHH | 3.24 | - | |
86 | S-nitrosylation | QVIIPYRCDVYDIMH EEEEEECCCHHHHHH | 3.24 | 21278135 | |
113 | Acetylation | LEWDARDKDSIRKAV EEECCCCHHHHHHHH | 48.07 | 23201123 | |
156 | O-linked_Glycosylation | PRAIAQASKEAGVER HHHHHHHHHHHCCCE | 20.96 | 15066235 | |
157 | Acetylation | RAIAQASKEAGVERF HHHHHHHHHHCCCEE | 55.38 | 23806337 | |
157 | Succinylation | RAIAQASKEAGVERF HHHHHHHHHHCCCEE | 55.38 | 23806337 | |
173 | Phosphorylation | HVSHLNASMKSSSKS EHHHHCHHHCCCCHH | 26.18 | - | |
175 | Succinylation | SHLNASMKSSSKSLR HHHCHHHCCCCHHHH | 44.69 | - | |
175 | Acetylation | SHLNASMKSSSKSLR HHHCHHHCCCCHHHH | 44.69 | 23806337 | |
175 | Succinylation | SHLNASMKSSSKSLR HHHCHHHCCCCHHHH | 44.69 | 23806337 | |
189 | Acetylation | RSKAVGEKEVRSVFP HHHHHCHHHHHHHCC | 56.43 | 23576753 | |
189 | Succinylation | RSKAVGEKEVRSVFP HHHHHCHHHHHHHCC | 56.43 | 26388266 | |
193 | Phosphorylation | VGEKEVRSVFPEAII HCHHHHHHHCCCEEE | 33.03 | 24719451 | |
237 | Ubiquitination | SLGFKTVKQPVYVAD HCCCCCCCCCEEEEE | 54.86 | 27667366 | |
254 | Ubiquitination | KGIVNATKDPDAVGK CCCCCCCCCCCCCCC | 65.93 | 22790023 | |
254 | Acetylation | KGIVNATKDPDAVGK CCCCCCCCCCCCCCC | 65.93 | 23201123 | |
261 | Succinylation | KDPDAVGKTFAFTGP CCCCCCCCEEEECCC | 33.59 | 23954790 | |
316 | Acetylation | PFEPWTTKDKVERIH CCCCCCCCCCEEEEE | 48.45 | 23954790 | |
370 | Acetylation | SSEIEETKPAKTVNY HHHHCCCCCCCCCCC | 46.38 | 23576753 | |
373 | Acetylation | IEETKPAKTVNY--- HCCCCCCCCCCC--- | 62.63 | 24062335 |
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 NDUA9_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NDUA9_MOUSE !! |
* 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 NDUA9_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NDUA9_MOUSE !! |
Kegg Drug | ||||||
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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-370, AND MASS SPECTROMETRY. |