| UniProt ID | SECU_YEAST | |
|---|---|---|
| UniProt AC | P40316 | |
| Protein Name | Securin | |
| Gene Name | PDS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 373 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | Regulatory protein, which plays a central role in chromosome stability. Probably acts by blocking the action of key proteins. During the mitosis, it blocks Separase/ESP1 function, preventing the proteolysis of the cohesin complex and the subsequent segregation of the chromosomes. At the onset of anaphase, it is ubiquitinated, conducting to its destruction and to the liberation of ESP1.. | |
| Protein Sequence | MMPANEDKENNIVYTGNESSGINFPQTPAHLLKRSHSNILKPPVRLDQLKRDANSNNGNTLKYIQGGKEVSPTKRLHTHAQQQGRLPLAAKDNNRSKSFIFPETSNQSKDADLPQLQNTLSIRKNDQLRKLSQISRSRSRANHNDLLSNSRKLQKYGSVLGYNALPKMKSLVLKDLADSGKNEESSDDDEGNEDSESKLGKKLQSALLKQDSSDGENELNGGLGLFNEQGGLQQLIKNSTKNEQKTKNDKSDKTDDYDIEIAPQRQEPLPYVPEGYSPFQQDDIEKLKTFNSPYKLDLEDEDDTPDKVDLLPLEQIDEEGEKDETECITRNQEEGAALPLLSKNFKEVAAVPTMELVYSEEGLDPEELEDLVT | |
| 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 |
|---|---|---|---|---|---|
| 35 | Phosphorylation | PAHLLKRSHSNILKP HHHHHHHCCCCCCCC | 29.67 | 28889911 | |
| 37 | Phosphorylation | HLLKRSHSNILKPPV HHHHHCCCCCCCCCC | 27.15 | 11390356 | |
| 68 | Acetylation | LKYIQGGKEVSPTKR EEEEECCCCCCCCCC | 62.86 | 25381059 | |
| 71 | Phosphorylation | IQGGKEVSPTKRLHT EECCCCCCCCCCCCC | 28.13 | 28152593 | |
| 73 | Phosphorylation | GGKEVSPTKRLHTHA CCCCCCCCCCCCCHH | 22.69 | 21082442 | |
| 91 | Acetylation | GRLPLAAKDNNRSKS CCCCEEECCCCCCCC | 56.21 | 25381059 | |
| 96 | Phosphorylation | AAKDNNRSKSFIFPE EECCCCCCCCCCCCC | 34.47 | 23749301 | |
| 98 | Phosphorylation | KDNNRSKSFIFPETS CCCCCCCCCCCCCCC | 25.48 | 24909858 | |
| 119 | Phosphorylation | DLPQLQNTLSIRKND CCHHHHHHHHHHHHH | 14.66 | 21440633 | |
| 121 | Phosphorylation | PQLQNTLSIRKNDQL HHHHHHHHHHHHHHH | 20.50 | 23749301 | |
| 132 | Phosphorylation | NDQLRKLSQISRSRS HHHHHHHHHHHHHHH | 28.62 | 23749301 | |
| 139 | Phosphorylation | SQISRSRSRANHNDL HHHHHHHHHCCHHHH | 36.67 | 17287358 | |
| 148 | Phosphorylation | ANHNDLLSNSRKLQK CCHHHHHHHHHHHHH | 39.80 | 30377154 | |
| 155 | Acetylation | SNSRKLQKYGSVLGY HHHHHHHHHCHHHCC | 63.11 | 22865919 | |
| 156 | Phosphorylation | NSRKLQKYGSVLGYN HHHHHHHHCHHHCCC | 11.15 | 21440633 | |
| 158 | Phosphorylation | RKLQKYGSVLGYNAL HHHHHHCHHHCCCCC | 15.87 | 28152593 | |
| 170 | Phosphorylation | NALPKMKSLVLKDLA CCCHHHHHHHHHHHH | 21.88 | 21440633 | |
| 179 | Phosphorylation | VLKDLADSGKNEESS HHHHHHHCCCCCCCC | 46.16 | 28889911 | |
| 185 | Phosphorylation | DSGKNEESSDDDEGN HCCCCCCCCCCCCCC | 32.65 | 21551504 | |
| 186 | Phosphorylation | SGKNEESSDDDEGNE CCCCCCCCCCCCCCC | 48.62 | 21551504 | |
| 195 | Phosphorylation | DDEGNEDSESKLGKK CCCCCCCHHHHHHHH | 37.28 | 26447709 | |
| 197 | Phosphorylation | EGNEDSESKLGKKLQ CCCCCHHHHHHHHHH | 36.81 | 26447709 | |
| 205 | Phosphorylation | KLGKKLQSALLKQDS HHHHHHHHHHHHCCC | 31.18 | 21440633 | |
| 212 | Phosphorylation | SALLKQDSSDGENEL HHHHHCCCCCCCCCC | 28.03 | 11390356 | |
| 213 | Phosphorylation | ALLKQDSSDGENELN HHHHCCCCCCCCCCC | 58.90 | 11390356 | |
| 276 | Phosphorylation | LPYVPEGYSPFQQDD CCCCCCCCCCCCHHH | 16.12 | 27017623 | |
| 277 | Phosphorylation | PYVPEGYSPFQQDDI CCCCCCCCCCCHHHH | 30.05 | 20377248 | |
| 289 | Phosphorylation | DDIEKLKTFNSPYKL HHHHHHHCCCCCCCC | 38.19 | 28889911 | |
| 292 | Phosphorylation | EKLKTFNSPYKLDLE HHHHCCCCCCCCCCC | 25.97 | 12050115 | |
| 343 | Acetylation | AALPLLSKNFKEVAA CHHHHHCCCHHHHCC | 67.39 | 24489116 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 292 | S | Phosphorylation | Kinase | CDC28 | P00546 | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | AMA1 | P50082 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | CDC20 | P26309 | PMID:22199232 |
| - | K | Ubiquitination | E3 ubiquitin ligase | CDH1 | P53197 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SECU_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 SECU_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-179; SER-185; SER-186;SER-212 AND SER-213, 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-185; SER-186 ANDSER-277, AND MASS SPECTROMETRY. | |
| "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 SER-37 AND SER-139, AND MASSSPECTROMETRY. | |
