Search Results
Overview
| Uniprot ID | P48047 |
|---|---|
| Protein Name | ATP synthase peripheral stalk subunit OSCP, mitochondrial |
| Gene Name | ATP5PO |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 158 | EATLSELKTVLKSFL |
| 162 | SELKTVLKSFLSQGQ |
| 172 | LSQGQVLKLEAKTDP |
| 176 | QVLKLEAKTDPSILG |
| 199 | KYVDMSVKTKIQKLG |
| 51 | ALYSAASKQNKLEQV |
| 54 | SAASKQNKLEQVEKE |
| 60 | NKLEQVEKELLRVAQ |
| 70 | LRVAQILKEPKVAAS |
| 73 | AQILKEPKVAASVLN |
| 84 | SVLNPYVKRSIKVKS |
| 90 | VKRSIKVKSLNDITA |
| 98 | SLNDITAKERFSPLT |
Function
Subunit OSCP, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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 (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). 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 (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0009986 | cell surface |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0045259 | proton-transporting ATP synthase complex |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:1903924 | estradiol binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Molecular Function | GO:0046933 | proton-transporting ATP synthase activity, rotational mechanism |
| Biological Process | GO:0006754 | ATP biosynthetic process |
| Biological Process | GO:0071320 | cellular response to cAMP |
| Biological Process | GO:0071345 | cellular response to cytokine stimulus |
| Biological Process | GO:0015986 | proton motive force-driven ATP synthesis |
| Biological Process | GO:0042776 | proton motive force-driven mitochondrial ATP synthesis |
| Biological Process | GO:1902600 | proton transmembrane transport |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[3] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.