| UniProt ID | YPT1_YEAST | |
|---|---|---|
| UniProt AC | P01123 | |
| Protein Name | GTP-binding protein YPT1 | |
| Gene Name | YPT1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 206 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Peripheral membrane protein . Golgi apparatus membrane Peripheral membrane protein . Cytoplasm . Preautophagosomal structure membrane Lipid-anchor Cytoplasmic side . ER and Golgi when GTP-bound. Cytoplasmic when |
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| Protein Description | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. YPT1 regulates the trafficking of secretory vesicles from the endoplasmic reticulum (ER) to the Golgi. Vesicular transport depends on shuttling of YPT1 between membrane and cytosol by GDI1, probably by recycling it to its membrane of origin after a vesicle fusion event. Plays a role in the initial events of the autophagic vacuole development which take place at specialized regions of the endoplasmic reticulum. Also involved in the recycling of membrane proteins.. | |
| Protein Sequence | MNSEYDYLFKLLLIGNSGVGKSCLLLRFSDDTYTNDYISTIGVDFKIKTVELDGKTVKLQIWDTAGQERFRTITSSYYRGSHGIIIVYDVTDQESFNGVKMWLQEIDRYATSTVLKLLVGNKCDLKDKRVVEYDVAKEFADANKMPFLETSALDSTNVEDAFLTMARQIKESMSQQNLNETTQKKEDKGNVNLKGQSLTNTGGGCC | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MNSEYDYL -------CCCHHHHH | 12.89 | - | |
| 3 | Phosphorylation | -----MNSEYDYLFK -----CCCHHHHHHH | 35.91 | 28152593 | |
| 5 | Phosphorylation | ---MNSEYDYLFKLL ---CCCHHHHHHHHH | 15.09 | 27214570 | |
| 7 | Phosphorylation | -MNSEYDYLFKLLLI -CCCHHHHHHHHHHH | 17.09 | 30377154 | |
| 17 | Phosphorylation | KLLLIGNSGVGKSCL HHHHHCCCCCCCCEE | 29.64 | 28889911 | |
| 21 | Acetylation | IGNSGVGKSCLLLRF HCCCCCCCCEEEEEE | 35.27 | 24489116 | |
| 23 | S-palmitoylation | NSGVGKSCLLLRFSD CCCCCCCEEEEEECC | 3.37 | - | |
| 29 | Phosphorylation | SCLLLRFSDDTYTND CEEEEEECCCCCCCC | 28.30 | 21126336 | |
| 39 | Phosphorylation | TYTNDYISTIGVDFK CCCCCEEEEEECCEE | 14.03 | 30377154 | |
| 48 | 2-Hydroxyisobutyrylation | IGVDFKIKTVELDGK EECCEEEEEEEECCE | 47.29 | - | |
| 48 | Ubiquitination | IGVDFKIKTVELDGK EECCEEEEEEEECCE | 47.29 | 23749301 | |
| 55 | 2-Hydroxyisobutyrylation | KTVELDGKTVKLQIW EEEEECCEEEEEEEE | 50.22 | - | |
| 55 | Ubiquitination | KTVELDGKTVKLQIW EEEEECCEEEEEEEE | 50.22 | 23749301 | |
| 58 | Ubiquitination | ELDGKTVKLQIWDTA EECCEEEEEEEECCC | 39.65 | 17644757 | |
| 58 | Acetylation | ELDGKTVKLQIWDTA EECCEEEEEEEECCC | 39.65 | 24489116 | |
| 100 | Ubiquitination | QESFNGVKMWLQEID CHHCCCHHHHHHHHH | 26.25 | 17644757 | |
| 122 | Ubiquitination | LKLLVGNKCDLKDKR HHHHHCCCCCCCCCE | 24.17 | 23749301 | |
| 123 | S-palmitoylation | KLLVGNKCDLKDKRV HHHHCCCCCCCCCEE | 9.57 | - | |
| 126 | Ubiquitination | VGNKCDLKDKRVVEY HCCCCCCCCCEEEEH | 48.21 | 22817900 | |
| 128 | Ubiquitination | NKCDLKDKRVVEYDV CCCCCCCCEEEEHHH | 45.57 | 22817900 | |
| 137 | Acetylation | VVEYDVAKEFADANK EEEHHHHHHHHHHCC | 53.89 | 24489116 | |
| 137 | Ubiquitination | VVEYDVAKEFADANK EEEHHHHHHHHHHCC | 53.89 | 23749301 | |
| 144 | Ubiquitination | KEFADANKMPFLETS HHHHHHCCCCCCCCC | 50.07 | 23749301 | |
| 170 | Ubiquitination | LTMARQIKESMSQQN HHHHHHHHHHHHHCC | 35.08 | 23749301 | |
| 172 | Phosphorylation | MARQIKESMSQQNLN HHHHHHHHHHHCCCC | 20.80 | 22369663 | |
| 174 | Phosphorylation | RQIKESMSQQNLNET HHHHHHHHHCCCCHH | 37.58 | 22369663 | |
| 181 | Phosphorylation | SQQNLNETTQKKEDK HHCCCCHHHHCHHHC | 33.19 | 22369663 | |
| 184 | Ubiquitination | NLNETTQKKEDKGNV CCCHHHHCHHHCCCC | 56.91 | 23749301 | |
| 185 | Ubiquitination | LNETTQKKEDKGNVN CCHHHHCHHHCCCCC | 62.42 | 22817900 | |
| 188 | Ubiquitination | TTQKKEDKGNVNLKG HHHCHHHCCCCCCCC | 54.17 | 23749301 | |
| 197 | Phosphorylation | NVNLKGQSLTNTGGG CCCCCCCCCCCCCCC | 45.92 | 21551504 | |
| 199 | Phosphorylation | NLKGQSLTNTGGGCC CCCCCCCCCCCCCCC | 35.66 | 21551504 | |
| 205 | Geranylgeranylation | LTNTGGGCC------ CCCCCCCCC------ | 2.55 | 16395334 | |
| 205 | Geranylgeranylation | LTNTGGGCC------ CCCCCCCCC------ | 2.55 | 10071213 | |
| 206 | Geranylgeranylation | TNTGGGCC------- CCCCCCCC------- | 7.65 | 14576435 | |
| 206 | Geranylgeranylation | TNTGGGCC------- CCCCCCCC------- | 7.65 | 10071213 |
| 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 YPT1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YPT1_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 YPT1_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-17; SER-172 AND SER-174,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-174, AND MASSSPECTROMETRY. | |
