| UniProt ID | ATG8_YEAST | |
|---|---|---|
| UniProt AC | P38182 | |
| Protein Name | Autophagy-related protein 8 | |
| Gene Name | ATG8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 117 | |
| Subcellular Localization |
Cytoplasmic vesicle, cvt vesicle membrane Lipid-anchor. Cytoplasmic vesicle, autophagosome membrane Lipid-anchor. Vacuole membrane Lipid-anchor. Membrane-associated through a lipid anchor. This association needs the 2 ubiquitin-like systems requir |
|
| Protein Description | Ubiquitin-like modifier involved in cytoplasm to vacuole transport (Cvt) vesicles and autophagosomes formation. With ATG4, mediates the delivery of the vesicles and autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Moreover not only conjugation, but also subsequent ATG8-PE deconjugation is an important step required to facilitate multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. Plays also a role in regulation of filamentous growth.. | |
| Protein Sequence | MKSTFKSEYPFEKRKAESERIADRFKNRIPVICEKAEKSDIPEIDKRKYLVPADLTVGQFVYVIRKRIMLPPEKAIFIFVNDTLPPTAALMSAIYQEHKDKDGFLYVTYSGENTFGR | |
| 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 |
|---|---|---|---|---|---|
| 116 | Phosphatidylethanolamine amidation | YSGENTFGR------ ECCCCCCCC------ | 32.14 | 11100732 |
| 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 ATG8_YEAST !! | ||||||
* 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 ATG8_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Lipoprotein | |
| Reference | PubMed |
| "A ubiquitin-like system mediates protein lipidation."; Ichimura Y., Kirisako T., Takao T., Satomi Y., Shimonishi Y.,Ishihara N., Mizushima N., Tanida I., Kominami E., Ohsumi M., Noda T.,Ohsumi Y.; Nature 408:488-492(2000). Cited for: FUNCTION, INTERACTION WITH ATG3 AND ATG7, AND LIPIDATION. | |
