UniProt ID | SCS2_YEAST | |
---|---|---|
UniProt AC | P40075 | |
Protein Name | Vesicle-associated membrane protein-associated protein SCS2 | |
Gene Name | SCS2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 244 | |
Subcellular Localization |
Endoplasmic reticulum membrane Single-pass type IV membrane protein. Nucleus membrane Single-pass type IV membrane protein. |
|
Protein Description | Targets proteins containing a FFAT motif to endoplasmic reticulum membranes. Regulates phospholipid biosynthesis by modulating the subcellular localization of the transcriptional repressor OPI1.. | |
Protein Sequence | MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGETIQVQVIFLGLTEEPAADFKCRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKKIKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPAVVNEKEVPAEPETQPPVQVKKEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLGWFYR | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSAVEISPD ------CCCCEECCC | 40.81 | 28152593 | |
2 | Acetylation | ------MSAVEISPD ------CCCCEECCC | 40.81 | - | |
7 | Phosphorylation | -MSAVEISPDVLVYK -CCCCEECCCEEEEE | 11.09 | 30377154 | |
13 | Phosphorylation | ISPDVLVYKSPLTEQ ECCCEEEEECCCCCC | 11.11 | 28132839 | |
38 | Acetylation | SDQTIAFKVKTTAPK CCCEEEEEEECCCCC | 33.52 | 24489116 | |
84 | Acetylation | ADFKCRDKFLVITLP CCCCCCCCEEEEECC | 22.65 | 24489116 | |
106 | Phosphorylation | KAVADVWSDLEAEFK CHHHHHHHHHHHHHH | 31.97 | 22369663 | |
113 | Ubiquitination | SDLEAEFKQQAISKK HHHHHHHHHHHHHHC | 32.76 | 24961812 | |
113 | Acetylation | SDLEAEFKQQAISKK HHHHHHHHHHHHHHC | 32.76 | 24489116 | |
118 | Phosphorylation | EFKQQAISKKIKVKY HHHHHHHHHCCCEEE | 30.80 | 28889911 | |
124 | Acetylation | ISKKIKVKYLISPDV HHHCCCEEEEECCCC | 29.36 | 24489116 | |
125 | Phosphorylation | SKKIKVKYLISPDVH HHCCCEEEEECCCCC | 16.56 | 24961812 | |
128 | Phosphorylation | IKVKYLISPDVHPAQ CCEEEEECCCCCHHH | 16.68 | 21440633 | |
143 | Ubiquitination | NQNIQENKETVEPVV CCCHHHCCCCCCCCC | 54.75 | 23749301 | |
143 | Acetylation | NQNIQENKETVEPVV CCCHHHCCCCCCCCC | 54.75 | 24489116 | |
145 | Phosphorylation | NIQENKETVEPVVQD CHHHCCCCCCCCCCC | 31.60 | 28889911 | |
153 | Phosphorylation | VEPVVQDSEPKEVPA CCCCCCCCCCCCCCC | 38.41 | 21551504 | |
156 | Ubiquitination | VVQDSEPKEVPAVVN CCCCCCCCCCCCEEC | 68.26 | 23749301 | |
156 | Acetylation | VVQDSEPKEVPAVVN CCCCCCCCCCCCEEC | 68.26 | 24489116 | |
165 | Ubiquitination | VPAVVNEKEVPAEPE CCCEECCCCCCCCCC | 59.83 | 23749301 | |
165 | Succinylation | VPAVVNEKEVPAEPE CCCEECCCCCCCCCC | 59.83 | 23954790 | |
165 | Acetylation | VPAVVNEKEVPAEPE CCCEECCCCCCCCCC | 59.83 | 24489116 | |
180 | Acetylation | TQPPVQVKKEEVPPV CCCCCCCCHHHCCCE | 37.06 | 24489116 | |
180 | Sumoylation | TQPPVQVKKEEVPPV CCCCCCCCHHHCCCE | 37.06 | - | |
181 | Ubiquitination | QPPVQVKKEEVPPVV CCCCCCCHHHCCCEE | 61.32 | 23749301 | |
190 | Acetylation | EVPPVVQKTVPHENE HCCCEEEECCCCCCC | 39.62 | 24489116 | |
198 | Ubiquitination | TVPHENEKQTSNSTP CCCCCCCCCCCCCCC | 71.15 | 23749301 | |
200 | Phosphorylation | PHENEKQTSNSTPAP CCCCCCCCCCCCCCC | 40.73 | 22369663 | |
201 | Phosphorylation | HENEKQTSNSTPAPQ CCCCCCCCCCCCCCH | 26.70 | 22369663 | |
203 | Phosphorylation | NEKQTSNSTPAPQNQ CCCCCCCCCCCCHHH | 35.22 | 22890988 | |
204 | Phosphorylation | EKQTSNSTPAPQNQI CCCCCCCCCCCHHHH | 27.93 | 22369663 | |
212 | Ubiquitination | PAPQNQIKEAATVPA CCCHHHHHHHCCCCC | 31.38 | 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 SCS2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SCS2_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 SCS2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-153, AND MASSSPECTROMETRY. | |
"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 SER-106, AND MASSSPECTROMETRY. |