UniProt ID | NDUA2_MOUSE | |
---|---|---|
UniProt AC | Q9CQ75 | |
Protein Name | NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 | |
Gene Name | Ndufa2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 99 | |
Subcellular Localization |
Mitochondrion inner membrane Peripheral membrane protein Matrix side . |
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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 | MAAAAASRAVGAKLGLREIRVHLCQRSPGSQGVRDFIVQRYVELKKAHPNLPILIRECSEVQPKLWARYAFGQEKTVSLNNLSADEVTRAMQNVLSGKA | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAAAAASRA ------CHHHHHHHH | 13.05 | - | |
13 | Acetylation | ASRAVGAKLGLREIR HHHHHHHHHCCCCHH | 36.84 | 23864654 | |
13 | Malonylation | ASRAVGAKLGLREIR HHHHHHHHHCCCCHH | 36.84 | 26320211 | |
24 | S-nitrosocysteine | REIRVHLCQRSPGSQ CCHHHHHHHCCCCCH | 1.58 | - | |
24 | S-nitrosylation | REIRVHLCQRSPGSQ CCHHHHHHHCCCCCH | 1.58 | 21278135 | |
58 | S-nitrosocysteine | LPILIRECSEVQPKL CCEEEEECCCCCHHH | 2.78 | - | |
58 | S-nitrosylation | LPILIRECSEVQPKL CCEEEEECCCCCHHH | 2.78 | 21278135 | |
64 | Acetylation | ECSEVQPKLWARYAF ECCCCCHHHHHHHHH | 39.30 | 23576753 | |
64 | Succinylation | ECSEVQPKLWARYAF ECCCCCHHHHHHHHH | 39.30 | - | |
64 | Succinylation | ECSEVQPKLWARYAF ECCCCCHHHHHHHHH | 39.30 | 23806337 | |
75 | Acetylation | RYAFGQEKTVSLNNL HHHHCCCCEEECCCC | 46.46 | 23576753 | |
75 | Succinylation | RYAFGQEKTVSLNNL HHHHCCCCEEECCCC | 46.46 | 26388266 | |
76 | Phosphorylation | YAFGQEKTVSLNNLS HHHCCCCEEECCCCC | 17.99 | 27742792 | |
78 | Phosphorylation | FGQEKTVSLNNLSAD HCCCCEEECCCCCHH | 30.52 | 25521595 | |
83 | Phosphorylation | TVSLNNLSADEVTRA EEECCCCCHHHHHHH | 35.48 | 29899451 | |
98 | Succinylation | MQNVLSGKA------ HHHHHCCCC------ | 47.77 | 26388266 | |
98 | Acetylation | MQNVLSGKA------ HHHHHCCCC------ | 47.77 | 23576753 |
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 NDUA2_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 NDUA2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of NDUA2_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-64 AND LYS-75, AND MASSSPECTROMETRY. |