UniProt ID | ATG18_YEAST | |
---|---|---|
UniProt AC | P43601 | |
Protein Name | Autophagy-related protein 18 {ECO:0000303|PubMed:14536056} | |
Gene Name | ATG18 {ECO:0000303|PubMed:14536056} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 500 | |
Subcellular Localization |
Preautophagosomal structure membrane Peripheral membrane protein . Vacuole membrane Peripheral membrane protein . Endosome membrane Peripheral membrane protein . Requires VAC7 for vacuole membrane localization. Under mid-log phase growth, local |
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Protein Description | The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). May negatively regulate FAB1 activity by sequestering or masking VAC7 from FAB1. Necessary for proper vacuole morphology. Plays an important role in osmotically-induced vacuole fragmentation. Required for cytoplasm to vacuole transport (Cvt) vesicle formation, pexophagy and starvation-induced autophagy. Involved in correct ATG9 trafficking to the pre-autophagosomal structure. Might also be involved in premeiotic DNA replication. With ATG2, protects ATG8 from ATG4-mediated cleavage.. | |
Protein Sequence | MSDSSPTINFINFNQTGTCISLGTSKGFKIFNCEPFGKFYSEDSGGYAIVEMLFSTSLLALVGIGDQPALSPRRLRIINTKKHSIICEVTFPTSILSVKMNKSRLVVLLQEQIYIYDINTMRLLHTIETNPNPRGLMAMSPSVANSYLVYPSPPKVINSEIKAHATTNNITLSVGGNTETSFKRDQQDAGHSDISDLDQYSSFTKRDDADPTSSNGGNSSIIKNGDVIVFNLETLQPTMVIEAHKGEIAAMAISFDGTLMATASDKGTIIRVFDIETGDKIYQFRRGTYATRIYSISFSEDSQYLAVTGSSKTVHIFKLGHSMSNNKLDSDDSNMEEAAADDSSLDTTSIDALSDEENPTRLAREPYVDASRKTMGRMIRYSSQKLSRRAARTLGQIFPIKVTSLLESSRHFASLKLPVETNSHVMTISSIGSPIDIDTSEYPELFETGNSASTESYHEPVMKMVPIRVVSSDGYLYNFVMDPERGGDCLILSQYSILMD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
114 | Phosphorylation | VLLQEQIYIYDINTM EEEECEEEEEECCHH | 7.98 | 29688323 | |
116 | Phosphorylation | LQEQIYIYDINTMRL EECEEEEEECCHHEE | 8.19 | 29688323 | |
120 | Phosphorylation | IYIYDINTMRLLHTI EEEEECCHHEEEEEE | 12.19 | 29688323 | |
140 | Phosphorylation | PRGLMAMSPSVANSY CCCEEECCHHHCCEE | 12.41 | 27017623 | |
152 | Phosphorylation | NSYLVYPSPPKVINS CEEEEECCCCCEECC | 35.83 | 27017623 | |
159 | Phosphorylation | SPPKVINSEIKAHAT CCCCEECCEEEEEEE | 29.58 | 27017623 | |
166 | Phosphorylation | SEIKAHATTNNITLS CEEEEEEECCCEEEE | 21.86 | 27017623 | |
167 | Phosphorylation | EIKAHATTNNITLSV EEEEEEECCCEEEEE | 27.35 | 27017623 | |
171 | Phosphorylation | HATTNNITLSVGGNT EEECCCEEEEECCCH | 18.33 | 27017623 | |
178 | Phosphorylation | TLSVGGNTETSFKRD EEEECCCHHHCCCHH | 43.87 | 27017623 | |
180 | Phosphorylation | SVGGNTETSFKRDQQ EECCCHHHCCCHHHC | 37.11 | 27017623 | |
181 | Phosphorylation | VGGNTETSFKRDQQD ECCCHHHCCCHHHCC | 23.65 | 27017623 | |
192 | Phosphorylation | DQQDAGHSDISDLDQ HHCCCCCCCCHHHHH | 35.40 | 22369663 | |
195 | Phosphorylation | DAGHSDISDLDQYSS CCCCCCCHHHHHHHC | 36.79 | 22369663 | |
201 | Phosphorylation | ISDLDQYSSFTKRDD CHHHHHHHCCCCCCC | 17.22 | 28889911 | |
202 | Phosphorylation | SDLDQYSSFTKRDDA HHHHHHHCCCCCCCC | 31.81 | 30377154 | |
212 | Phosphorylation | KRDDADPTSSNGGNS CCCCCCCCCCCCCCC | 45.38 | 27017623 | |
214 | Phosphorylation | DDADPTSSNGGNSSI CCCCCCCCCCCCCCE | 41.81 | 27017623 | |
254 | Phosphorylation | EIAAMAISFDGTLMA CEEEEEEEECCEEEE | 14.03 | 29688323 | |
258 | Phosphorylation | MAISFDGTLMATASD EEEEECCEEEEEECC | 18.40 | 29688323 | |
262 | Phosphorylation | FDGTLMATASDKGTI ECCEEEEEECCCCCE | 16.84 | 29688323 | |
264 | Phosphorylation | GTLMATASDKGTIIR CEEEEEECCCCCEEE | 35.18 | 29688323 | |
268 | Phosphorylation | ATASDKGTIIRVFDI EEECCCCCEEEEEEE | 20.97 | 29688323 | |
280 | Acetylation | FDIETGDKIYQFRRG EEECCCCEEEEECCC | 44.66 | 24489116 | |
347 | Phosphorylation | ADDSSLDTTSIDALS HCCCCCCCCCHHHCC | 27.95 | 28889911 | |
354 | Phosphorylation | TTSIDALSDEENPTR CCCHHHCCCCCCCCH | 44.70 | 22753491 | |
367 | Phosphorylation | TRLAREPYVDASRKT CHHHCCCCCCCCHHH | 13.25 | 28889911 | |
371 | Phosphorylation | REPYVDASRKTMGRM CCCCCCCCHHHHHHH | 29.82 | 28889911 | |
381 | Phosphorylation | TMGRMIRYSSQKLSR HHHHHHHHHHHHHHH | 11.18 | 23749301 | |
383 | Phosphorylation | GRMIRYSSQKLSRRA HHHHHHHHHHHHHHH | 23.54 | 23749301 | |
385 | Acetylation | MIRYSSQKLSRRAAR HHHHHHHHHHHHHHH | 50.83 | 25381059 | |
393 | Phosphorylation | LSRRAARTLGQIFPI HHHHHHHHHHHHCCE | 30.43 | 21126336 | |
404 | Phosphorylation | IFPIKVTSLLESSRH HCCEEHHHHHHCCCC | 33.66 | 30377154 |
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 ATG18_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATG18_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 ATG18_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASSSPECTROMETRY. |