| UniProt ID | ATG11_YEAST | |
|---|---|---|
| UniProt AC | Q12527 | |
| Protein Name | Autophagy-related protein 11 | |
| Gene Name | ATG11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1178 | |
| Subcellular Localization |
Preautophagosomal structure membrane Peripheral membrane protein. Vacuole membrane Peripheral membrane protein. During pexophagy, accumulates in the vacuolar membrane region, where the peroxisomes contact the vacuole. ATG11 localization is dependen |
|
| Protein Description | Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation, through its interaction with ATG32. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for ATG9 anterograde transport from the mitochondria to the PAS. Recruits also the ATG19-prAPE1 complex to the PAS. Required for the Cvt vesicles completion. Plays a significant role in life span extension.. | |
| Protein Sequence | MADADEYSTAPTQQEITPLQTTATIINAISGECITTNVDFFVSLDKFKQFIARKWKIPPDQLLILLPYGNKLKPSMFKELLINRSFTLNDFYVYDRRLFSLVSKPTPTNLLTSKDSNPMNSPNSNDLTETLEYLIKNSHISQYQGSDTIMIKPMPSPLEDADVDLSRLNYHSVTSLLTTNLGWLSALEIDVHYFKSLIPDIIAHIKRIFDGLTVCSQYLKLYCFDVESLYNSNVQFLNQLVDNGMTSKWEKCFNDTLSKLTALEGDSLQKFINIESLLENEKSVKILNHSINGKLNKIKREIDENASFRDIITVNIDRLRQMFTPNESKFELEDQMAESFEVLVSEMRTRSRNVLDKEEEEFNSQEFLKSMNVMLEKDKKESVKTLFTISQALYSQIGELIDLKKSLQKHAVAILGNIAFTQMEILGIKRLLLNECNKDLELYKKYEVEFAQVEDLPLIYGLYLIEKYRRLSWFQQILSFISNFNQDLELFKQNELRTRNKWVKNFGSIATVFCEDLLSSSDFKRLNEYHSHTSPPNEDEEDENENSIANYRQDLVKVSQAIDNYMTQIKETDVSEPIIDLLSKTLFETKRFHIIYSNFKNNNNNSSNGNSISPEGSIALKSDDVVKGYKTRIKKLESLLHEFQYSDIGHWPQGVLNTHLKPFRGSATSINKKKFLGASVLLEPANISEVNIDSVSQANNHQIQELESNVDDLLHQLQLLKEENNRKSMQISEMGKKISDLEVEKTAYRETLTNLNQELARLTNEEQSHRTEIFTLNASFKKQLNDIISQDNEKIEKLTGDYDDVSKSRERLQMDLDESNKKHEQEVNLLKADIERLGKQIVTSEKSYAETNSSSMEKGEKFETIPLAEDPGRENQISAYTQTLQDRIFDIISTNIFILENIGLLLTFDNNNNIQIRRVKGLKKGTAQSNILDESTQMLDAHDNSLIKSPVFQKLKDEYELIKSVANGSEKDTQQSIFLGNITQLYDNKLYEVAVIRRFKDIETLAKKLTKENKIKRTLLERFQREKVTLRNFQIGDLALFLPTRENVNSVGSMSSSTSSLSSSFSSVDLSTPPPLDAMSIQSSPSVIHSNVINQASISGRDKNKLMRPWAAFTAFEESTRYFLKDEKGLTKGKEWFVGRIVTLEHFVADSPSNNPFRLPKGSVWFQVTAVVVSYQGV | |
| 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 |
|---|---|---|---|---|---|
| 124 | Phosphorylation | NPMNSPNSNDLTETL CCCCCCCCCCHHHHH | 34.80 | 21551504 | |
| 128 | Phosphorylation | SPNSNDLTETLEYLI CCCCCCHHHHHHHHH | 29.77 | 24961812 | |
| 130 | Phosphorylation | NSNDLTETLEYLIKN CCCCHHHHHHHHHHC | 21.47 | 24961812 | |
| 370 | Phosphorylation | NSQEFLKSMNVMLEK CHHHHHHHHHHHHHH | 20.10 | 19795423 | |
| 547 | Phosphorylation | EEDENENSIANYRQD CCCCCCCCHHHHHHH | 19.52 | 24961812 | |
| 551 | Phosphorylation | NENSIANYRQDLVKV CCCCHHHHHHHHHHH | 10.71 | 24961812 | |
| 606 | Phosphorylation | FKNNNNNSSNGNSIS CCCCCCCCCCCCCCC | 27.57 | 23749301 | |
| 607 | Phosphorylation | KNNNNNSSNGNSISP CCCCCCCCCCCCCCC | 51.37 | 22369663 | |
| 611 | Phosphorylation | NNSSNGNSISPEGSI CCCCCCCCCCCCCCE | 26.33 | 22369663 | |
| 613 | Phosphorylation | SSNGNSISPEGSIAL CCCCCCCCCCCCEEE | 19.40 | 22369663 | |
| 617 | Phosphorylation | NSISPEGSIALKSDD CCCCCCCCEEECCCH | 11.74 | 22369663 | |
| 666 | Phosphorylation | HLKPFRGSATSINKK CCCCCCCCCCCCCCC | 24.90 | 21551504 | |
| 668 | Phosphorylation | KPFRGSATSINKKKF CCCCCCCCCCCCCCC | 31.66 | 21551504 | |
| 739 | Phosphorylation | SEMGKKISDLEVEKT HHHHHHHHHHHHHHH | 45.05 | 27017623 | |
| 789 | Phosphorylation | KQLNDIISQDNEKIE HHHHHHHHCCHHHHH | 31.64 | 29136822 | |
| 808 | Phosphorylation | DYDDVSKSRERLQMD CHHHHHHHHHHHHCC | 31.69 | 27214570 | |
| 846 | Ubiquitination | KQIVTSEKSYAETNS HHHHHCCCCCCCCCC | 48.83 | 23749301 | |
| 853 | Phosphorylation | KSYAETNSSSMEKGE CCCCCCCCCHHCCCC | 31.07 | 28889911 | |
| 926 | Phosphorylation | VKGLKKGTAQSNILD ECCCCCCCCHHCCCC | 30.33 | 22369663 | |
| 929 | Phosphorylation | LKKGTAQSNILDEST CCCCCCHHCCCCHHH | 24.31 | 22369663 | |
| 935 | Phosphorylation | QSNILDESTQMLDAH HHCCCCHHHHHHHCC | 24.49 | 22369663 | |
| 936 | Phosphorylation | SNILDESTQMLDAHD HCCCCHHHHHHHCCC | 18.89 | 22369663 | |
| 945 | Phosphorylation | MLDAHDNSLIKSPVF HHHCCCCCCCCCHHH | 37.21 | 22369663 |
| 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 ATG11_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATG11_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 ATG11_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-613 AND SER-935, ANDMASS SPECTROMETRY. | |
