| UniProt ID | ATG21_YEAST | |
|---|---|---|
| UniProt AC | Q02887 | |
| Protein Name | Autophagy-related protein 21 | |
| Gene Name | ATG21 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 496 | |
| Subcellular Localization | Cytoplasm. Vacuole. And perivacuolar punctate structures. | |
| Protein Description | Required for cytoplasm to vacuole transport (Cvt) vesicles formation and mitophagy. Involved in binding of phosphatidylethanolamine to ATG8 and in recruitment of ATG8 and ATG5 to the pre-autophagosomal structure. Protects ATG8 from ARG4-mediated cleavage. Essential for maturation of proaminopeptidase I.. | |
| Protein Sequence | MKVLQFNQDATCCVVAASSHQISIFNCDPFGKCFEIDTKNSKKKTSNNNGSASNSESRNNEESILITNGSRDRTDAEEEEDNEDNALVTGNILKEGEFVIEMLFSTSLIAIADRGQGLNKGKKLKIVNTKRKCTICEIVFPHEIVDVVMNRKRMCVLLESDQIFIYDISCMKPLETIDLWEDHYKRSQANSFSNASNTGTLEGDSANLNRVATNLLANATQKSVNGSNPSVRTRRNSLRSKIRPRMVLSNDDRSILCFTAYSSPKKNKPNSEALYDVVIYDTLNVTPVNYLNSVHKGNVACLAVSHDGKLLATASDKGTIIRVFHTGVDSDYMSSRSLFKEFRRGTRLCNLYQLAFDKSMTMIGCVGDTDTIHLFKLDDASNSLPGDNSSNGHWNEEEYILASNSNPSMGTPKEIPLSKPRIANYFSKKIKSSIPNQNLSRNFAYITVNESNRSCLGFPDEFPNQVYIASDDGTFSIYSIPSKPGECVLTKNNKFT | |
| 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 |
|---|---|---|---|---|---|
| 63 | Phosphorylation | ESRNNEESILITNGS CCCCCCCCEEEECCC | 19.27 | 22369663 | |
| 67 | Phosphorylation | NEESILITNGSRDRT CCCCEEEECCCCCCC | 30.04 | 22369663 | |
| 70 | Phosphorylation | SILITNGSRDRTDAE CEEEECCCCCCCCCC | 32.83 | 30377154 | |
| 187 | Phosphorylation | WEDHYKRSQANSFSN HHHHHHHHHHHCCCC | 29.50 | 22369663 | |
| 191 | Phosphorylation | YKRSQANSFSNASNT HHHHHHHCCCCCCCC | 32.82 | 22369663 | |
| 193 | Phosphorylation | RSQANSFSNASNTGT HHHHHCCCCCCCCCC | 31.16 | 22369663 | |
| 196 | Phosphorylation | ANSFSNASNTGTLEG HHCCCCCCCCCCCCC | 38.89 | 23749301 | |
| 198 | Phosphorylation | SFSNASNTGTLEGDS CCCCCCCCCCCCCCH | 29.11 | 22369663 | |
| 205 | Phosphorylation | TGTLEGDSANLNRVA CCCCCCCHHHHHHHH | 29.88 | 28889911 | |
| 213 | Phosphorylation | ANLNRVATNLLANAT HHHHHHHHHHHHHHH | 24.44 | 21440633 | |
| 222 | Ubiquitination | LLANATQKSVNGSNP HHHHHHHHHHCCCCC | 52.60 | 23749301 | |
| 223 | Phosphorylation | LANATQKSVNGSNPS HHHHHHHHHCCCCCC | 15.82 | 22369663 | |
| 230 | Phosphorylation | SVNGSNPSVRTRRNS HHCCCCCCHHHHHHH | 28.60 | 23749301 | |
| 233 | Phosphorylation | GSNPSVRTRRNSLRS CCCCCHHHHHHHHHH | 31.65 | 17563356 | |
| 237 | Phosphorylation | SVRTRRNSLRSKIRP CHHHHHHHHHHHCCC | 24.29 | 17287358 | |
| 317 | Acetylation | LLATASDKGTIIRVF EEEEECCCCCEEEEE | 56.30 | 24489116 | |
| 381 | Phosphorylation | LFKLDDASNSLPGDN EEEECCCCCCCCCCC | 33.67 | 21440633 | |
| 403 | Phosphorylation | EEEYILASNSNPSMG HHHEEEECCCCCCCC | 37.03 | 24961812 | |
| 405 | Phosphorylation | EYILASNSNPSMGTP HEEEECCCCCCCCCC | 47.85 | 24961812 | |
| 408 | Phosphorylation | LASNSNPSMGTPKEI EECCCCCCCCCCCCC | 33.81 | 24961812 | |
| 411 | Phosphorylation | NSNPSMGTPKEIPLS CCCCCCCCCCCCCCC | 23.65 | 24961812 |
| 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 ATG21_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATG21_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 ATG21_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-63; SER-191 AND THR-233,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-223 AND THR-233, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASSSPECTROMETRY. | |