| UniProt ID | AGE2_YEAST | |
|---|---|---|
| UniProt AC | P40529 | |
| Protein Name | ADP-ribosylation factor GTPase-activating protein effector protein 2 | |
| Gene Name | AGE2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 298 | |
| Subcellular Localization | Cytoplasm . Golgi apparatus . Associates with the Golgi complex. | |
| Protein Description | GTPase-activating protein for the ADP ribosylation factor family.. | |
| Protein Sequence | MSTSVPVKKALSALLRDPGNSHCADCKAQLHPRWASWSLGVFICIKCAGIHRSLGTHISKVKSVDLDTWKEEHLVKLIQFKNNLRANSYYEATLADELKQRKITDTSSLQNFIKNKYEYKKWIGDLSSIEGLNDSTEPVLHKPSANHSLPASNARLDQSSNSLQKTQTQPPSHLLSTSRSNTSLLNLQVSSLSKTTSNTSVTSSATSIGAANTKTGNRVGEFGQRNDLKKSILSLYSKPSAQTQSQNSFFTSTTPQPCNTPSPFVNTGITATNNNSMNSNSSSNISLDDNELFKNVWS | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSTSVPVKK ------CCCCHHHHH | 29.41 | 22814378 | |
| 4 | Phosphorylation | ----MSTSVPVKKAL ----CCCCHHHHHHH | 19.67 | 25533186 | |
| 59 | Phosphorylation | RSLGTHISKVKSVDL HHHCHHHHCCEECCC | 24.64 | 27017623 | |
| 63 | Phosphorylation | THISKVKSVDLDTWK HHHHCCEECCCCCCC | 24.69 | 24961812 | |
| 70 | Acetylation | SVDLDTWKEEHLVKL ECCCCCCCHHHHHHH | 56.15 | 24489116 | |
| 117 | Phosphorylation | QNFIKNKYEYKKWIG HHHHHCHHHHHHHHC | 33.61 | 27017623 | |
| 159 | Phosphorylation | SNARLDQSSNSLQKT CCCCCCCCCCCHHHH | 31.02 | 22369663 | |
| 160 | Phosphorylation | NARLDQSSNSLQKTQ CCCCCCCCCCHHHHC | 25.46 | 22369663 | |
| 162 | Phosphorylation | RLDQSSNSLQKTQTQ CCCCCCCCHHHHCCC | 33.84 | 22369663 | |
| 166 | Phosphorylation | SSNSLQKTQTQPPSH CCCCHHHHCCCCCHH | 24.72 | 22369663 | |
| 168 | Phosphorylation | NSLQKTQTQPPSHLL CCHHHHCCCCCHHHH | 48.55 | 22369663 | |
| 172 | Phosphorylation | KTQTQPPSHLLSTSR HHCCCCCHHHHCCCC | 33.19 | 20377248 | |
| 176 | Phosphorylation | QPPSHLLSTSRSNTS CCCHHHHCCCCCCCC | 30.60 | 22369663 | |
| 177 | Phosphorylation | PPSHLLSTSRSNTSL CCHHHHCCCCCCCCC | 28.29 | 20377248 | |
| 178 | Phosphorylation | PSHLLSTSRSNTSLL CHHHHCCCCCCCCCE | 30.27 | 22369663 | |
| 180 | Phosphorylation | HLLSTSRSNTSLLNL HHHCCCCCCCCCEEE | 44.20 | 22369663 | |
| 182 | Phosphorylation | LSTSRSNTSLLNLQV HCCCCCCCCCEEEEE | 23.23 | 22369663 | |
| 183 | Phosphorylation | STSRSNTSLLNLQVS CCCCCCCCCEEEEEE | 34.80 | 22369663 | |
| 190 | Phosphorylation | SLLNLQVSSLSKTTS CCEEEEEEECCCCCC | 16.76 | 22890988 | |
| 191 | Phosphorylation | LLNLQVSSLSKTTSN CEEEEEEECCCCCCC | 37.49 | 22890988 | |
| 193 | Phosphorylation | NLQVSSLSKTTSNTS EEEEEECCCCCCCCE | 29.88 | 22890988 | |
| 195 | Phosphorylation | QVSSLSKTTSNTSVT EEEECCCCCCCCEEC | 31.89 | 22890988 | |
| 196 | Phosphorylation | VSSLSKTTSNTSVTS EEECCCCCCCCEECC | 24.58 | 22890988 | |
| 197 | Phosphorylation | SSLSKTTSNTSVTSS EECCCCCCCCEECCC | 43.26 | 22369663 | |
| 199 | Phosphorylation | LSKTTSNTSVTSSAT CCCCCCCCEECCCCC | 25.09 | 22890988 | |
| 200 | Phosphorylation | SKTTSNTSVTSSATS CCCCCCCEECCCCCE | 27.87 | 22890988 | |
| 202 | Phosphorylation | TTSNTSVTSSATSIG CCCCCEECCCCCEEC | 19.41 | 22890988 | |
| 203 | Phosphorylation | TSNTSVTSSATSIGA CCCCEECCCCCEECC | 18.80 | 22890988 | |
| 204 | Phosphorylation | SNTSVTSSATSIGAA CCCEECCCCCEECCC | 26.63 | 22890988 | |
| 206 | Phosphorylation | TSVTSSATSIGAANT CEECCCCCEECCCCC | 23.87 | 22890988 | |
| 207 | Phosphorylation | SVTSSATSIGAANTK EECCCCCEECCCCCC | 20.81 | 22369663 | |
| 213 | Phosphorylation | TSIGAANTKTGNRVG CEECCCCCCCCCCCH | 25.84 | 22890988 | |
| 214 | Ubiquitination | SIGAANTKTGNRVGE EECCCCCCCCCCCHH | 55.00 | 23749301 | |
| 231 | Phosphorylation | QRNDLKKSILSLYSK CCCHHHHHHHHHHCC | 27.46 | 22369663 | |
| 234 | Phosphorylation | DLKKSILSLYSKPSA HHHHHHHHHHCCCCC | 24.48 | 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 AGE2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of AGE2_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 AGE2_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-178; SER-180; SER-183;THR-195 AND SER-197, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182, AND MASSSPECTROMETRY. | |