UniProt ID | ATP5I_MOUSE | |
---|---|---|
UniProt AC | Q06185 | |
Protein Name | ATP synthase subunit e, mitochondrial | |
Gene Name | Atp5i | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 71 | |
Subcellular Localization | Mitochondrion. Mitochondrion inner membrane. | |
Protein Description | Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.. | |
Protein Sequence | MVPPVQVSPLIKFGRYSALIIGMAYGAKRYSYLKPRAEEERRIAAEEKKRLDELKRIERELAEAQDDSILK | |
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 |
---|---|---|---|---|---|
8 | Phosphorylation | MVPPVQVSPLIKFGR CCCCCCCCHHHHCCC | 9.26 | 27841257 | |
25 | Phosphorylation | ALIIGMAYGAKRYSY HHHHHHHHCHHHHHC | 14.55 | - | |
28 | Acetylation | IGMAYGAKRYSYLKP HHHHHCHHHHHCCCC | 47.72 | 2388355 | |
28 | Succinylation | IGMAYGAKRYSYLKP HHHHHCHHHHHCCCC | 47.72 | 26388266 | |
30 | Phosphorylation | MAYGAKRYSYLKPRA HHHCHHHHHCCCCHH | 10.85 | 23140645 | |
31 | Phosphorylation | AYGAKRYSYLKPRAE HHCHHHHHCCCCHHH | 28.20 | 23140645 | |
32 | Phosphorylation | YGAKRYSYLKPRAEE HCHHHHHCCCCHHHH | 15.15 | 26032504 | |
34 | Acetylation | AKRYSYLKPRAEEER HHHHHCCCCHHHHHH | 24.99 | 23576753 | |
34 | Ubiquitination | AKRYSYLKPRAEEER HHHHHCCCCHHHHHH | 24.99 | 27667366 | |
48 | Acetylation | RRIAAEEKKRLDELK HHHHHHHHHHHHHHH | 34.40 | 23864654 | |
68 | Phosphorylation | LAEAQDDSILK---- HHHHHCCCCCC---- | 37.80 | 25521595 | |
71 | Acetylation | AQDDSILK------- HHCCCCCC------- | 57.53 | 23864654 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ATP5I_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATP5I_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 ATP5I_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ATP5I_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32, AND MASSSPECTROMETRY. |