| UniProt ID | YPT52_YEAST | |
|---|---|---|
| UniProt AC | P36018 | |
| Protein Name | GTP-binding protein YPT52 | |
| Gene Name | YPT52 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 234 | |
| Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side . Endoplasmic reticulum . Also found in association with endoplasmic reticulum vesicles having SED5 on their surface. |
|
| Protein Description | Required for transport in the endocytic pathway and for correct sorting of the vacuolar hydrolases suggesting a possible intersection of the endocytic with the vacuolar sorting pathway.. | |
| Protein Sequence | MLQFKLVLLGDSSVGKSSIVHRFVKDTFDELRESTIGAAFLSQSITIHPNDGNETKDVVIKFEIWDTAGQERYKSLAPMYYRNANAALVVYDITQEDSLQKARNWVDELKNKVGDDDLVIYLLGNKVDLCQETPSTETSPDSNEGGDEEQKVRAISTEEAKQYAQEQGLLFREVSAKTGEGVKEIFQDIGEKLYDLKKDEILSKQNRQIGGGNNGQVDINLQRPSTNDPTSCCS | |
| 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 |
|---|---|---|---|---|---|
| 12 | Phosphorylation | KLVLLGDSSVGKSSI EEEEECCCCCCCHHH | 25.73 | 22369663 | |
| 13 | Phosphorylation | LVLLGDSSVGKSSIV EEEECCCCCCCHHHH | 39.36 | 22369663 | |
| 16 | Ubiquitination | LGDSSVGKSSIVHRF ECCCCCCCHHHHHHH | 38.58 | 24961812 | |
| 17 | Phosphorylation | GDSSVGKSSIVHRFV CCCCCCCHHHHHHHH | 21.26 | 30377154 | |
| 18 | Phosphorylation | DSSVGKSSIVHRFVK CCCCCCHHHHHHHHH | 31.92 | 30377154 | |
| 25 | Acetylation | SIVHRFVKDTFDELR HHHHHHHHHHHHHHH | 48.62 | 24489116 | |
| 46 | Phosphorylation | AFLSQSITIHPNDGN HHHCCCEEECCCCCC | 20.62 | 28889911 | |
| 101 | Ubiquitination | TQEDSLQKARNWVDE CCHHHHHHHHHHHHH | 55.39 | 24961812 | |
| 133 | Phosphorylation | KVDLCQETPSTETSP CCCCCCCCCCCCCCC | 9.17 | 29136822 | |
| 135 | Phosphorylation | DLCQETPSTETSPDS CCCCCCCCCCCCCCC | 46.42 | 20377248 | |
| 136 | Phosphorylation | LCQETPSTETSPDSN CCCCCCCCCCCCCCC | 44.48 | 29136822 | |
| 138 | Phosphorylation | QETPSTETSPDSNEG CCCCCCCCCCCCCCC | 45.72 | 20377248 | |
| 139 | Phosphorylation | ETPSTETSPDSNEGG CCCCCCCCCCCCCCC | 22.07 | 20377248 | |
| 142 | Phosphorylation | STETSPDSNEGGDEE CCCCCCCCCCCCCHH | 39.92 | 20377248 | |
| 151 | Ubiquitination | EGGDEEQKVRAISTE CCCCHHHHHHEECHH | 36.65 | 23749301 | |
| 161 | Acetylation | AISTEEAKQYAQEQG EECHHHHHHHHHHHC | 47.31 | 24489116 | |
| 183 | Acetylation | AKTGEGVKEIFQDIG HCCCCCHHHHHHHHH | 56.82 | 24489116 | |
| 192 | Acetylation | IFQDIGEKLYDLKKD HHHHHHHHHHHCCHH | 47.32 | 24489116 | |
| 197 | Acetylation | GEKLYDLKKDEILSK HHHHHHCCHHHHHHH | 56.11 | 24489116 | |
| 203 | Phosphorylation | LKKDEILSKQNRQIG CCHHHHHHHCCCCCC | 37.55 | 24909858 | |
| 232 | Geranylgeranylation | STNDPTSCCS----- CCCCCCCCCC----- | 2.65 | - | |
| 233 | Geranylgeranylation | TNDPTSCCS------ CCCCCCCCC------ | 5.61 | - |
| 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 YPT52_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YPT52_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 YPT52_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 THR-46 AND SER-135, AND MASSSPECTROMETRY. | |