| UniProt ID | ATG3_YEAST | |
|---|---|---|
| UniProt AC | P40344 | |
| Protein Name | Autophagy-related protein 3 | |
| Gene Name | ATG3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 310 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | E2 conjugating enzyme required for the cytoplasm to vacuole transport (Cvt) and autophagy. 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. Responsible for the E2-like covalent binding of phosphatidylethanolamine to the C-terminal Gly of ATG8. The ATG12-ATG5 conjugate plays a role of an E3 and promotes the transfer of ATG8 from ATG3 to phosphatidylethanolamine (PE). This step is required for the membrane association of ATG8. The formation of the ATG8-phosphatidylethanolamine conjugate is essential for autophagy and for the cytoplasm to vacuole transport (Cvt). The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy.. | |
| Protein Sequence | MIRSTLSSWREYLTPITHKSTFLTTGQITPEEFVQAGDYLCHMFPTWKWNEESSDISYRDFLPKNKQFLIIRKVPCDKRAEQCVEVEGPDVIMKGFAEDGDEDDVLEYIGSETEHVQSTPAGGTKDSSIDDIDELIQDMEIKEEDENDDTEEFNAKGGLAKDMAQERYYDLYIAYSTSYRVPKMYIVGFNSNGSPLSPEQMFEDISADYRTKTATIEKLPFYKNSVLSVSIHPCKHANVMKILLDKVRVVRQRRRKELQEEQELDGVGDWEDLQDDIDDSLRVDQYLIVFLKFITSVTPSIQHDYTMEGW | |
| 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 |
|---|---|---|---|---|---|
| 19 | Acetylation | YLTPITHKSTFLTTG HHCCCCCCCCCCCCC | 42.41 | 22539722 | |
| 48 | Acetylation | CHMFPTWKWNEESSD HHCCCCCCCCCCCCC | 42.49 | 22539722 | |
| 108 | Phosphorylation | DEDDVLEYIGSETEH CCCCHHHHCCCCCCC | 13.35 | 22369663 | |
| 111 | Phosphorylation | DVLEYIGSETEHVQS CHHHHCCCCCCCEEC | 31.61 | 22369663 | |
| 113 | Phosphorylation | LEYIGSETEHVQSTP HHHCCCCCCCEECCC | 32.84 | 21440633 | |
| 118 | Phosphorylation | SETEHVQSTPAGGTK CCCCCEECCCCCCCC | 34.96 | 22369663 | |
| 119 | Phosphorylation | ETEHVQSTPAGGTKD CCCCEECCCCCCCCC | 10.48 | 22369663 | |
| 124 | Phosphorylation | QSTPAGGTKDSSIDD ECCCCCCCCCCCCHH | 30.66 | 22369663 | |
| 127 | Phosphorylation | PAGGTKDSSIDDIDE CCCCCCCCCCHHHHH | 30.65 | 21551504 | |
| 150 | Phosphorylation | EEDENDDTEEFNAKG CCCCCCCHHHHHHHC | 40.03 | 28889911 | |
| 183 | Acetylation | STSYRVPKMYIVGFN ECCCCCCCEEEEEEC | 41.29 | 22539722 | |
| 218 | Acetylation | TKTATIEKLPFYKNS CCEEEEEECCCCCCC | 58.57 | 24489116 |
| 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 ATG3_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 ATG3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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