Search Results
Overview
| Uniprot ID | P05141 |
|---|---|
| Protein Name | ADP/ATP translocase 2 |
| Gene Name | SLC25A5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 105 | IFLGGVDKRTQFWLY |
| 147 | RLAADVGKAGAEREF |
| 163 | GLGDCLVKIYKSDGI |
| 166 | DCLVKIYKSDGIKGL |
| 23 | GVAAAISKTAVAPIE |
| 245 | MMMQSGRKGTDIMYT |
| 268 | IARDEGGKAFFKGAW |
| 272 | EGGKAFFKGAWSNVL |
| 33 | VAPIERVKLLLQVQH |
| 43 | LQVQHASKQITADKQ |
| 63 | DCVVRIPKEQGVLSF |
| 92 | QALNFAFKDKYKQIF |
| 94 | LNFAFKDKYKQIFLG |
| 96 | FAFKDKYKQIFLGGV |
Function
ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (By similarity). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate-binding site intermittently exposed to either the cytosolic (c-state) or matrix (m-state) side of the inner mitochondrial membrane (By similarity). In addition to its ADP:ATP antiporter activity, also involved in mitochondrial uncoupling and mitochondrial permeability transition pore (mPTP) activity (By similarity). Plays a role in mitochondrial uncoupling by acting as a proton transporter: proton transport uncouples the proton flows via the electron transport chain and ATP synthase to reduce the efficiency of ATP production and cause mitochondrial thermogenesis (By similarity). Proton transporter activity is inhibited by ADP:ATP antiporter activity, suggesting that SLC25A5/ANT2 acts as a master regulator of mitochondrial energy output by maintaining a delicate balance between ATP production (ADP:ATP antiporter activity) and thermogenesis (proton transporter activity) (By similarity). Proton transporter activity requires free fatty acids as cofactor, but does not transport it (By similarity). Probably mediates mitochondrial uncoupling in tissues that do not express UCP1 (By similarity). Also plays a key role in mPTP opening, a non-specific pore that enables free passage of the mitochondrial membranes to solutes of up to 1.5 kDa, and which contributes to cell death (PubMed:31883789). It is however unclear if SLC25A5/ANT2 constitutes a pore-forming component of mPTP or regulates it (By similarity). Acts as a regulator of mitophagy independently of ADP:ATP antiporter activity: promotes mitophagy via interaction with TIMM44, leading to inhibit the presequence translocase TIMM23, thereby promoting stabilization of PINK1 (By similarity). As part of the mitotic spindle-associated MMXD complex it may play a role in chromosome segregation (PubMed:20797633)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0042645 | mitochondrial nucleoid |
| Cellular Component | GO:0005757 | mitochondrial permeability transition pore complex |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0071817 | MMXD complex |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0000295 | adenine nucleotide transmembrane transporter activity |
| Molecular Function | GO:0015207 | adenine transmembrane transporter activity |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0005471 | ATP:ADP antiporter activity |
| Molecular Function | GO:0017077 | oxidative phosphorylation uncoupler activity |
| Molecular Function | GO:0015078 | proton transmembrane transporter activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:1990845 | adaptive thermogenesis |
| Biological Process | GO:0051503 | adenine nucleotide transport |
| Biological Process | GO:0030183 | B cell differentiation |
| Biological Process | GO:0007059 | chromosome segregation |
| Biological Process | GO:0030218 | erythrocyte differentiation |
| Biological Process | GO:0140021 | mitochondrial ADP transmembrane transport |
| Biological Process | GO:1990544 | mitochondrial ATP transmembrane transport |
| Biological Process | GO:1901029 | negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway |
| Biological Process | GO:0008284 | positive regulation of cell population proliferation |
| Biological Process | GO:1901526 | positive regulation of mitophagy |
| Biological Process | GO:0046902 | regulation of mitochondrial membrane permeability |
Reference
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[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
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[7] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[8] 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.
[9] 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.