| UniProt ID | SA155_YEAST | |
|---|---|---|
| UniProt AC | P43612 | |
| Protein Name | SIT4-associating protein SAP155 | |
| Gene Name | SAP155 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1002 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Positive regulator of protein phosphatase SIT4. Involved in directing expression of TOR-repressed genes and in dephosphorylation of NPR1 in response to nutrient starvation. Negatively modulates K(+) efflux of the cell by the Na(+)-K(+)/H(+) antiporter NHA1.. | |
| Protein Sequence | MSFWPFGQNLNHSNINKILDEYFHVLHELERINPSVGKAIPAIFNNVQERGTSDSLDSIPEEYSHGDEVKTARGDQKSRFEKDDQQERYEKEEEERSMNSSESSTTSFSSGSTSKTDLDEEDISNATAPMMVTTKNLDNSFIERMLVETELLNELSRQNKTLLDFICFGFFFDKKTNKKVNNMEYLVDQLMECISKIKTATTVDLNNLIDYQEQQQLDDSSQEDVYVESDTEQEEEKEDDNNSNNKKRRKRGSSSFGNDDINNNDDDDDANEDDESAYLTKATIISEIFSLDIWLISESLVKNQSYLNKIWSIINQPNFNSENSPLVPIFLKINQNLLLTRQDQYLNFIRTERSFVDDMLKHVDISLLMDFFLKIISTDKIESPTGIIELVYDQNLISKCLSFLNNKESPADIQACVGDFLKALIAISANAPLDDISIGPNSLTRQLASPESIAKLVDIMINQRGAALNTTVSIVIELIRKNNSDYDQVNLLTTTIKTHPPSNRDPIYLGYLLRKFSNHLSDFFQIILDIENDANIPLHENQLHEKFKPLGFERFKVVELIAELLHCSNMGLMNSKRAERIARRRDKVRSQLSHHLQDALNDLSIEEKEQLKTKHSPTRDTDHDLKNNNGKIDNDNNDNDDESDYGDEIDESFEIPYINMKQNIKLRTDPTVGDLFKIKLYDTRIVSKIMELFLTHPWNNFWHNVIFDIIQQIFNGRMDFSYNSFLVLSLFNLKSSYQFMTDIVISDEKGTDVSRFSPVIRDPNFDFKITTDFILRGYQDSYKFYELRKMNLGYMGHIVLIAEEVVKFSKLYKVELISPDIQVILQTEEWQYYSEEVLNETRMMYSKILGGGSYIDDGNGNIIPQLPDNTTVLTPNGDASNNNEILDSDTGSSNGTSGGGQLINVESLEEQLSLSTESDLHNKLREMLINRAQEDVDNKNTENGVFILGPPEDKNSNSNINNTNHNSNNSNNNDNNDNNDNDNDNTRNYNEDADNDNDYDHE | |
| 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 | Phosphorylation | ------MSFWPFGQN ------CCCCCCCCC | 47.53 | 30377154 | |
| 13 | Phosphorylation | FGQNLNHSNINKILD CCCCCCCHHHHHHHH | 38.03 | 30377154 | |
| 38 | Ubiquitination | RINPSVGKAIPAIFN HHCCCHHHHHHHHHH | 40.77 | 23749301 | |
| 52 | Phosphorylation | NNVQERGTSDSLDSI HCHHHCCCCCCHHCC | 35.27 | 22369663 | |
| 53 | Phosphorylation | NVQERGTSDSLDSIP CHHHCCCCCCHHCCC | 28.20 | 22369663 | |
| 55 | Phosphorylation | QERGTSDSLDSIPEE HHCCCCCCHHCCCHH | 33.57 | 22369663 | |
| 58 | Phosphorylation | GTSDSLDSIPEEYSH CCCCCHHCCCHHHCC | 45.39 | 22369663 | |
| 63 | Phosphorylation | LDSIPEEYSHGDEVK HHCCCHHHCCCCHHC | 12.33 | 22369663 | |
| 64 | Phosphorylation | DSIPEEYSHGDEVKT HCCCHHHCCCCHHCC | 25.03 | 22369663 | |
| 70 | Ubiquitination | YSHGDEVKTARGDQK HCCCCHHCCCCCCCC | 34.13 | 23749301 | |
| 97 | Phosphorylation | EKEEEERSMNSSESS HHHHHHHHCCCCCCC | 26.12 | 21551504 | |
| 103 | Phosphorylation | RSMNSSESSTTSFSS HHCCCCCCCCCCCCC | 34.63 | 30377154 | |
| 106 | Phosphorylation | NSSESSTTSFSSGST CCCCCCCCCCCCCCC | 29.71 | 30377154 | |
| 107 | Phosphorylation | SSESSTTSFSSGSTS CCCCCCCCCCCCCCC | 24.18 | 27017623 | |
| 113 | Phosphorylation | TSFSSGSTSKTDLDE CCCCCCCCCCCCCCH | 37.46 | 28889911 | |
| 253 | Phosphorylation | KKRRKRGSSSFGNDD HHHHHHCCCCCCCCC | 27.17 | 23749301 | |
| 254 | Phosphorylation | KRRKRGSSSFGNDDI HHHHHCCCCCCCCCC | 32.29 | 21440633 | |
| 255 | Phosphorylation | RRKRGSSSFGNDDIN HHHHCCCCCCCCCCC | 38.58 | 23749301 | |
| 604 | Phosphorylation | QDALNDLSIEEKEQL HHHHHCCCHHHHHHH | 30.71 | 24961812 | |
| 613 | Phosphorylation | EEKEQLKTKHSPTRD HHHHHHCCCCCCCCC | 42.45 | 17287358 | |
| 616 | Phosphorylation | EQLKTKHSPTRDTDH HHHCCCCCCCCCCCC | 29.53 | 17287358 | |
| 618 | Phosphorylation | LKTKHSPTRDTDHDL HCCCCCCCCCCCCCC | 44.16 | 17287358 | |
| 643 | Phosphorylation | NNDNDDESDYGDEID CCCCCCCCCCCCCCC | 43.03 | 21440633 | |
| 645 | Phosphorylation | DNDDESDYGDEIDES CCCCCCCCCCCCCCC | 35.44 | 19795423 | |
| 652 | Phosphorylation | YGDEIDESFEIPYIN CCCCCCCCCCCCCCC | 25.16 | 19823750 | |
| 679 | 2-Hydroxyisobutyrylation | VGDLFKIKLYDTRIV HHHHEEEEEECHHHH | 41.40 | - | |
| 751 | Phosphorylation | VISDEKGTDVSRFSP EEECCCCCCHHHCCC | 44.27 | 21440633 | |
| 770 | Phosphorylation | PNFDFKITTDFILRG CCCCEEEECHHHHHC | 22.39 | 27017623 | |
| 781 | Phosphorylation | ILRGYQDSYKFYELR HHHCCCCCCCHHHHH | 18.07 | 27017623 | |
| 782 | Phosphorylation | LRGYQDSYKFYELRK HHCCCCCCCHHHHHH | 17.26 | 27017623 |
| 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 SA155_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SA155_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 SA155_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-55 AND SER-58, AND MASSSPECTROMETRY. | |
| "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-58, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-613; SER-616 ANDTHR-618, AND MASS SPECTROMETRY. | |