UniProt ID | ATG20_YEAST | |
---|---|---|
UniProt AC | Q07528 | |
Protein Name | Autophagy-related protein 20 | |
Gene Name | ATG20 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 640 | |
Subcellular Localization |
Endosome membrane Peripheral membrane protein. Preautophagosomal structure membrane Peripheral membrane protein. |
|
Protein Description | Required for cytoplasm to vacuole transport (Cvt), pexophagy and mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Functions in protein retrieval from the endocytic pathway. Required for proper sorting of the v-SNARE protein SNC1.. | |
Protein Sequence | MSDLNDVQENAKLNSETRNTGKAEPPHGTTEYVAEAEISKNGVGSPKKSPKKGKVGKGDNNKVETELVHTALLEKDNPFMEEGPTGFTKSALLEIPGMRSHNLKNPNEDYEDDSEGLLPLNQESNAETCRTSLSGSINSMNGETSASEEPSVSNRKKSARIHILEAKRVSEGQGRAYIAYVIQFENSTVQRRYSDFESLRSILIRLFPMTLIPPIPEKQSIKNYGKSITGSSSKYLLPSEGSGSVDLSLSVIHASVNNSDEKLIRHRIRMLTEFLNKLLTNEEITKTSIITDFLDPNNHNWHEFVNSSSTFSSLPKSILQCNPLDPTNTTRIHAMLPIPGSSSQLLLNKESNDKKMDKERSKSFTNIEQDYKQYENLLDNGIYKYNRRTTKTYHDLKSDYNEIGEVFAQFAHEQAQVGELAEQLSYLSNAFSGSSISLEKLVGRLYYNINEPLNESVHMATSARELIKYRKLKYLQNEMIKKSLNSKRAQLEKLEAQNNEYKDVDKIIDNEMSKSHTINLERPNNNTGSGGKSYGGKLFNGFNKLASMVKDSVKYQETDPHTASINLKKEIEQLSESLEVTENDLEVISKVIKNDQLPKFSKEREVDLSEILKHYSRYMRNYARQNLEIWKEVKRHQDFA | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSDLNDVQE ------CCCHHHHHH | 51.29 | 30377154 | |
2 | Acetylation | ------MSDLNDVQE ------CCCHHHHHH | 51.29 | 22814378 | |
45 | Phosphorylation | ISKNGVGSPKKSPKK HHCCCCCCCCCCCCC | 31.01 | 16445868 | |
49 | Phosphorylation | GVGSPKKSPKKGKVG CCCCCCCCCCCCCCC | 48.34 | 16445868 | |
70 | Phosphorylation | VETELVHTALLEKDN CCHHHHHHHHHCCCC | 16.12 | 24961812 | |
90 | Phosphorylation | GPTGFTKSALLEIPG CCCCCCHHHHHCCCC | 22.53 | 28152593 | |
110 | Phosphorylation | LKNPNEDYEDDSEGL CCCCCCCCCCCCCCC | 18.32 | 28889911 | |
114 | Phosphorylation | NEDYEDDSEGLLPLN CCCCCCCCCCCCCCC | 45.98 | 30377154 | |
131 | Phosphorylation | SNAETCRTSLSGSIN CCCCHHHHHHCCCHH | 35.85 | 29688323 | |
132 | Phosphorylation | NAETCRTSLSGSINS CCCHHHHHHCCCHHC | 10.94 | 23749301 | |
134 | Phosphorylation | ETCRTSLSGSINSMN CHHHHHHCCCHHCCC | 30.20 | 29688323 | |
136 | Phosphorylation | CRTSLSGSINSMNGE HHHHHCCCHHCCCCC | 18.41 | 19779198 | |
139 | Phosphorylation | SLSGSINSMNGETSA HHCCCHHCCCCCCCC | 16.38 | 23749301 | |
144 | Phosphorylation | INSMNGETSASEEPS HHCCCCCCCCCCCCC | 30.87 | 23749301 | |
145 | Phosphorylation | NSMNGETSASEEPSV HCCCCCCCCCCCCCC | 26.04 | 23749301 | |
147 | Phosphorylation | MNGETSASEEPSVSN CCCCCCCCCCCCCCC | 42.11 | 29688323 | |
151 | Phosphorylation | TSASEEPSVSNRKKS CCCCCCCCCCCCCCC | 41.27 | 29688323 | |
153 | Phosphorylation | ASEEPSVSNRKKSAR CCCCCCCCCCCCCCE | 34.94 | 29688323 | |
218 | Acetylation | LIPPIPEKQSIKNYG CCCCCCCCHHHHHCC | 43.95 | 24489116 | |
361 | Phosphorylation | KKMDKERSKSFTNIE HHCCHHHHHHCCCHH | 33.47 | 17563356 | |
363 | Phosphorylation | MDKERSKSFTNIEQD CCHHHHHHCCCHHHH | 38.25 | 22369663 | |
365 | Phosphorylation | KERSKSFTNIEQDYK HHHHHHCCCHHHHHH | 42.23 | 22369663 | |
371 | Phosphorylation | FTNIEQDYKQYENLL CCCHHHHHHHHHHHH | 10.33 | 19779198 | |
513 | Phosphorylation | KIIDNEMSKSHTINL HHHCCCHHHCCEEEE | 25.48 | 21440633 | |
515 | Phosphorylation | IDNEMSKSHTINLER HCCCHHHCCEEEEEC | 20.68 | 21440633 | |
517 | Phosphorylation | NEMSKSHTINLERPN CCHHHCCEEEEECCC | 20.74 | 24961812 | |
537 | Acetylation | GGKSYGGKLFNGFNK CCCCHHHHCCCCHHH | 45.61 | 25381059 | |
547 | Phosphorylation | NGFNKLASMVKDSVK CCHHHHHHHHHHHHC | 34.25 | 28747907 | |
552 | Phosphorylation | LASMVKDSVKYQETD HHHHHHHHHCCCCCC | 18.13 | 28747907 | |
555 | Phosphorylation | MVKDSVKYQETDPHT HHHHHHCCCCCCCCC | 14.93 | 28747907 | |
562 | Phosphorylation | YQETDPHTASINLKK CCCCCCCCCCCHHHH | 27.73 | 28747907 | |
613 | Acetylation | VDLSEILKHYSRYMR CCHHHHHHHHHHHHH | 46.27 | 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 ATG20_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATG20_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 ATG20_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-361; SER-363 ANDTHR-365, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; SER-363 ANDTHR-365, AND MASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-49, AND MASSSPECTROMETRY. |