Search Results
Overview
| Uniprot ID | Q8N0X7 |
|---|---|
| Protein Name | Spartin |
| Gene Name | SPART |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 377 | KQLDQGNKDVRHKGK |
| 390 | GKRGKRAKDTSSEEV |
| 447 | KGAEITGKAIQKGAS |
| 475 | EVSPAVTKGLYIAKQ |
| 481 | TKGLYIAKQATGGAA |
| 514 | KELAPHVKKHGSKLV |
| 519 | HVKKHGSKLVPESLK |
| 615 | GIKAMVKKTATQTGH |
Function
Lipophagy receptor that plays an important role in lipid droplet (LD) turnover in motor neurons (PubMed:37443287). Localizes to LDs and interacts with components of the autophagy machinery, such as MAP1LC3A/C proteins to deliver LDs to autophagosomes for degradation via lipophagy (PubMed:37443287). Lipid transfer protein required for lipid droplet degradation, including by lipophagy (PubMed:38190532). Can bind and transfer all lipid species found in lipid droplets, from phospholipids to triglycerides and sterol esters but the direction of lipid transfer by spartin and its cargos are unknown (PubMed:38190532). May be implicated in endosomal trafficking, or microtubule dynamics, or both. Participates in cytokinesis (PubMed:20719964)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005811 | lipid droplet |
| Cellular Component | GO:0030496 | midbody |
| Cellular Component | GO:0005741 | mitochondrial outer membrane |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0045202 | synapse |
| Molecular Function | GO:0008289 | lipid binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0051301 | cell division |
| Biological Process | GO:0016042 | lipid catabolic process |
| Biological Process | GO:0006869 | lipid transport |
| Biological Process | GO:0061724 | lipophagy |
| Biological Process | GO:0061952 | midbody abscission |
| Biological Process | GO:0030514 | negative regulation of BMP signaling pathway |
| Biological Process | GO:0051881 | regulation of mitochondrial membrane potential |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[3] 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.