UniProt ID | ATG2_YEAST | |
---|---|---|
UniProt AC | P53855 | |
Protein Name | Autophagy-related protein 2 | |
Gene Name | ATG2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1592 | |
Subcellular Localization |
Preautophagosomal structure membrane Peripheral membrane protein . ATG1 and ATG9 are required for the proper localization the PAS. |
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Protein Description | Required for cytoplasm to vacuole transport (Cvt) vesicle and autophagosome completion. Necessary for the localization of ATG18 to the preautophagosomal structure (PAS) and the binding of ATG18 to ATG9. Involved in correct ATG9 trafficking through the preautophagosomal structure and in peroxisome degradation. ATG2 is the most downstream ATG protein in the preautophagosomal structure organization process. Plays a significant role in life span extension.. | |
Protein Sequence | MAFWLPQNIQKRLLLYVLQQISLFSNIDLSNLDVSIGSKSHFSFHDVNLSLDDLNIPNVQINEGIVDELVLKLTVSGGVEIDGSGLRFIMTPLYSSGSQELHSDFLVKSIQDLTNSMLQFSDPLTTYNRYKEDDISSSDSSSDLNSNIEASKPAANGSYTLQNMRNKALNVALAKLKIALKDVTIRFIVNDRDPSDNIVEVHLESIQLITTDANLRHINIENITISSIQKQAVPDSPVHPFNNDDLSQSVYLSKMEATSLYMSAMEEQSNEDPSEPQVTQEEQENDKCKESLMEINNLNIAFKGLSSVNDLRMSNIVIDIQDVHLAIHKIVEIKNSTLKNIIDIIVTHLDANESFSCQDSQSPSPDKQEPSALSSVDIKCIYLNLGQDITVILKSFKLEQKENNSLAFSLGSFYSNSSPLTISHKTKPLLTGEQTPQSIALNMGDELDIIISHDGIAHFFKIFQFVSKCMSFYQNKSKGMMPQIASDTKRTVQLTSKAVKLSLKFPYFLLCFQVSPFIYDSNRELYIELVDVFKKLPSRCTKILTMSSITISNLQSPLQLGSYDDTLKEALIYSSVHAIIKEVIFNEEYSGIVQLVEDISAFGKLFTDSKNSECTGKSKSKRGSFLQRSVRVLNSSRFVYKQSLSANFSLKIDSMKLKVSEIIGPQFGSVEALLSNNFFAITDDSQIVYFTKNLKVERKTPSLLEPQEIMSVVLNKAVNEPVLYVHRRANGKLKVIFNNIRIHYYARWLEILKKNIGPDNASSKDEPVSQKLSKKQPTSGFPWELKCLDCSLILHPFRLKSVMVIVLDNLTTGGSSFIPQAKLLSKANTLFLIDDYQNFKIQKDKNWPSLINFYAGQGFSAIGKIDTLNFLINKSDGALLLDCKIEQVGLSLCADSFQTFCQLCIDLKYPQTFPDEEKFRTQLKNPIDVFKDIDCDLFNSAFIRENNHQNDYDSVHLVDSFLDKTHEFNNGARSKLSSQGSYEMDSSSGTATGGILLPHESYLDSAQPKEEDTPPIASKEQERDVDIRGSIDVEKVVIKLFDGYDWKYTRKFIANTVEKLDKELSKAEASSSKSNVPQSEANIFDSIYISANKNNVTDLRRNLDGEIQGVQNSFSDVSKVNLRPSKHYKALIQLNKVHVNLKNYRVDEPDESNSDNSTDVLNRCVVSIYEFEIIDNVPTSTWNKFVTLLKHEPWPHSSPMFLLDLEFIRPIDFLQAVELVMQLNVAPLRLHVDQDTLEFLIRFLGFKDKRFELIDEYPDIVFIQKFSTNSIKLRLDYKPKKVDYAGLRSGQTSELMNFFTLDGSKIILKSVVLYGLNGFDELNNKLKAIWTPDITKKQLPGVLEGLAPVRSFMAIGSGVKTLVTVLMSEYRQEGHLGRSLKKGGNVFLKTTTGDFVKLGVKLTSGTQAILENTEELFGGVGSNGRVYDASKFGSADGADSDTAAVLDLDTLFEEDQLVGSKYSRIRDHEPTAVVIDMSSPGDHNEPTIVSLYADQPLDLPTGLKEAYSSLEKHMHIAYDAVWRAKGQMKDDKRGGPSAAAVYVARAAPVAIIRPLIGATEAVSKTLQGIANQVDKTHNEQINDKYKSNRTDS | |
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 |
---|---|---|---|---|---|
11 | Acetylation | WLPQNIQKRLLLYVL CCCHHHHHHHHHHHH | 41.01 | 25381059 | |
137 | Phosphorylation | YKEDDISSSDSSSDL CCCCCCCCCCCCCCC | 38.20 | 28889911 | |
140 | Phosphorylation | DDISSSDSSSDLNSN CCCCCCCCCCCCHHC | 33.42 | 21551504 | |
142 | Phosphorylation | ISSSDSSSDLNSNIE CCCCCCCCCCHHCCC | 50.50 | 21551504 | |
236 | Phosphorylation | QKQAVPDSPVHPFNN HHCCCCCCCCCCCCC | 23.81 | 22369663 | |
247 | Phosphorylation | PFNNDDLSQSVYLSK CCCCCCCCHHHHHHH | 27.66 | 22369663 | |
249 | Phosphorylation | NNDDLSQSVYLSKME CCCCCCHHHHHHHHH | 14.89 | 24961812 | |
253 | Phosphorylation | LSQSVYLSKMEATSL CCHHHHHHHHHHHHH | 16.57 | 24961812 | |
334 | Acetylation | IHKIVEIKNSTLKNI HHHHHHCCCCHHHHH | 31.19 | 24489116 | |
496 | Phosphorylation | KRTVQLTSKAVKLSL CHHHHHCCHHHHHHH | 27.49 | 28889911 | |
515 | Phosphorylation | FLLCFQVSPFIYDSN HHHEEECCEEEECCC | 11.87 | 27017623 | |
519 | Phosphorylation | FQVSPFIYDSNRELY EECCEEEECCCCCEE | 17.44 | 27017623 | |
521 | Phosphorylation | VSPFIYDSNRELYIE CCEEEECCCCCEEEE | 22.33 | 27017623 | |
645 | Phosphorylation | FVYKQSLSANFSLKI CEEEEECCCCEEEEE | 26.81 | 27017623 | |
762 | Phosphorylation | NIGPDNASSKDEPVS HCCCCCCCCCCCCHH | 44.14 | 30377154 | |
940 | Phosphorylation | IDCDLFNSAFIRENN CCCCHHCCCHHCCCC | 19.74 | 27214570 | |
954 | Phosphorylation | NHQNDYDSVHLVDSF CCCCCCCEEHHHHHH | 12.76 | 25704821 | |
990 | Phosphorylation | EMDSSSGTATGGILL EECCCCCCCCCCEEE | 24.00 | 21440633 | |
1047 | Acetylation | LFDGYDWKYTRKFIA ECCCCCHHHHHHHHH | 33.57 | 24489116 | |
1056 | Phosphorylation | TRKFIANTVEKLDKE HHHHHHHHHHHHHHH | 22.48 | 30377154 | |
1113 | Phosphorylation | EIQGVQNSFSDVSKV CEEHHHCCCCCHHCC | 14.72 | 28889911 | |
1115 | Phosphorylation | QGVQNSFSDVSKVNL EHHHCCCCCHHCCCC | 36.60 | 28889911 | |
1118 | Phosphorylation | QNSFSDVSKVNLRPS HCCCCCHHCCCCCCC | 35.56 | 26447709 | |
1154 | Phosphorylation | DEPDESNSDNSTDVL CCCCCCCCCCHHHHH | 47.66 | 23749301 | |
1277 | Phosphorylation | SIKLRLDYKPKKVDY CEEEEEECCCCCCCC | 33.51 | 28889911 | |
1351 | Phosphorylation | EGLAPVRSFMAIGSG CCCCCHHHHHHHCCC | 21.43 | 21440633 |
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 ATG2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of ATG2_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of ATG2_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-236 AND SER-1113, ANDMASS 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-236, AND MASSSPECTROMETRY. |