Table 2.
Acetylated proteins in fibroblasts from PD patients with or without LRRK2 mutation.
| Protein ID | Protein Name | Subcellular Location | Ac-K Sites |
|---|---|---|---|
| P07355 | Annexin A2 | Extracellular space, Extracellular matrix | 10 |
| P04083 | Annexin A1 | Nucleus, Cytoplasm, Cell membrane | 1 |
| P08670 | Vimentin | Cytoplasm | 2 |
| Q9BQE3 | α-Tubulin 1C | Cytoplasm, Cytoskeleton | 1 |
| P68363 | α-Tubulin 1B | Cytoplasm, Cytoskeleton | 1 |
| P14618 | Pyruvate kinase | Cytoplasm, Nucleus | 2 |
| Q6PEY2 | α-Tubulin 3E | Cytoplasm, Cytoskeleton. | 1 |
| P08758 | Annexin A5 | – | 4 |
| P21333 | Filamin-A | Cytoplasm, Cell cortex, Cytoskeleton. | 1 |
| P62805 | Histone H4 | Nucleus, Chromosome | 4 |
| Q9GZZ1 | NAA50 | Cytoplasm | 2 |
| Q09472 | HAT p300 | Cytoplasm, Nucleus. | 5 |
| Q92793 | CBP | Cytoplasm, Nucleus. | 2 |
| Q99880 | H2B1L | Nucleus, Chromosome | 4 |
| P04406 | GAPDH | Cytoplasm, Cytoskeleton | 4 |
| P68371 | β-Tubulin 4B | Cytoplasm, Cytoskeleton, Nucleus | 1 |
| P07437 | β-Tubulin | Cytoplasm, Cytoskeleton. | 1 |
| P06733 | Alpha-enolase | Cytoplasm, Cell membrane | 4 |
| O43809 | CPSF5 | Nucleus | 1 |
| P62328 | Thymosin β-4 | Cytoplasm, Cytoskeleton. | 3 |
| P22392 | NME2 | Cytoplasm, Nucleus | 2 |
| Q15942 | Zyxin | Cytoplasm, Cytoskeleton, Nucleus, Cell junction | 2 |
| P21796 | VDAC1 | Outer mitochondrial membrane | 1 |
| P20962 | Parathymosin | Nucleus | 4 |
| P08559 | PDHA1 | Mitochondrial matrix | 4 |
| P06454 | Prothymosin α | Nucleus | 5 |
| P68871 | Hemoglobin β | – | 1 |
| P02042 | Hemoglobin Δ | – | 1 |
| P09972 | ALDOC | – | 1 |
| P04792 | Heat shock protein beta-1 | Cytoplasm, Nucleus | 1 |
| P06703 | Protein S100-A6 | Nucleus envelope, Cell membrane | 1 |
| P00338 | LDHA A | Cytoplasm | 4 |
We specified the subcellular location of proteins and the number of acetylation sites. Lines filled in blue represent the most relevant variations identified in PD models compared to control.