| UniProt ID | ATP5I_HUMAN | |
|---|---|---|
| UniProt AC | P56385 | |
| Protein Name | ATP synthase subunit e, mitochondrial | |
| Gene Name | ATP5I | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 69 | |
| 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 | MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARELAEDDSILK | |
| 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 |
|---|---|---|---|---|---|
| 8 | Phosphorylation | MVPPVQVSPLIKLGR CCCCCCCCHHHHHCH | 9.26 | 26074081 | |
| 12 | Ubiquitination | VQVSPLIKLGRYSAL CCCCHHHHHCHHHHH | 53.20 | 24816145 | |
| 17 | O-linked_Glycosylation | LIKLGRYSALFLGVA HHHHCHHHHHHHHHH | 19.69 | 30379171 | |
| 25 | Phosphorylation | ALFLGVAYGATRYNY HHHHHHHHCHHHHHC | 12.60 | - | |
| 28 | Phosphorylation | LGVAYGATRYNYLKP HHHHHCHHHHHCCCH | 29.35 | - | |
| 30 | Phosphorylation | VAYGATRYNYLKPRA HHHCHHHHHCCCHHH | 12.10 | 22817900 | |
| 32 | Phosphorylation | YGATRYNYLKPRAEE HCHHHHHCCCHHHHH | 13.73 | 22817900 | |
| 34 | Succinylation | ATRYNYLKPRAEEER HHHHHCCCHHHHHHH | 23.30 | 23954790 | |
| 34 | Ubiquitination | ATRYNYLKPRAEEER HHHHHCCCHHHHHHH | 23.30 | - | |
| 34 | Acetylation | ATRYNYLKPRAEEER HHHHHCCCHHHHHHH | 23.30 | 25825284 | |
| 48 | 2-Hydroxyisobutyrylation | RRIAAEEKKKQDELK HHHHHHHHHHHHHHH | 57.69 | - | |
| 49 | Ubiquitination | RIAAEEKKKQDELKR HHHHHHHHHHHHHHH | 59.97 | 24816145 | |
| 50 | Ubiquitination | IAAEEKKKQDELKRI HHHHHHHHHHHHHHH | 74.23 | 24816145 | |
| 55 | Ubiquitination | KKKQDELKRIARELA HHHHHHHHHHHHHHH | 39.45 | 25015289 | |
| 55 | 2-Hydroxyisobutyrylation | KKKQDELKRIARELA HHHHHHHHHHHHHHH | 39.45 | - | |
| 66 | Phosphorylation | RELAEDDSILK---- HHHHHHCCCCC---- | 41.99 | 25850435 | |
| 69 | Acetylation | AEDDSILK------- HHHCCCCC------- | 57.53 | 68909 | |
| 69 | Ubiquitination | AEDDSILK------- HHHCCCCC------- | 57.53 | 24816145 |
| 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 ATP5I_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATP5I_HUMAN !! | ||||||
* 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_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| RS16_HUMAN | RPS16 | physical | 22939629 | |
| RS21_HUMAN | RPS21 | physical | 22939629 | |
| RER1_HUMAN | RER1 | physical | 26344197 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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