| UniProt ID | SPL2_YEAST | |
|---|---|---|
| UniProt AC | P38839 | |
| Protein Name | Putative cyclin-dependent kinase inhibitor SPL2 | |
| Gene Name | SPL2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 148 | |
| Subcellular Localization | Cytoplasmic granule . Cytoplasm . | |
| Protein Description | Putative cyclin-dependent kinase (CDK) inhibitor necessary and sufficient for PHO pathway-dependent down-regulation of low-affinity phosphate transport.. | |
| Protein Sequence | MGTYTPLIYNIYNVHIWVFTESQGQIGQMSPRGKMETAVSQGQHKQLKDGHQHKGRKLSEEIASLLRLKECRRLNPASYYTPRRTSQSQSLSGSTFKEYNEYINEKDSSRAQRQNAAAVLSKLAHDFWENDCVIDEDIFEDSSDEEQS | |
| 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 |
|---|---|---|---|---|---|
| 59 | Phosphorylation | QHKGRKLSEEIASLL CCCCCHHHHHHHHHH | 35.90 | 17330950 | |
| 64 | Phosphorylation | KLSEEIASLLRLKEC HHHHHHHHHHHHHHH | 33.33 | 28152593 | |
| 78 | Phosphorylation | CRRLNPASYYTPRRT HHHCCCCHHCCCCCC | 21.67 | 19779198 | |
| 80 | Phosphorylation | RLNPASYYTPRRTSQ HCCCCHHCCCCCCCC | 14.05 | 19779198 | |
| 85 | Phosphorylation | SYYTPRRTSQSQSLS HHCCCCCCCCCCCCC | 32.19 | 22890988 | |
| 86 | Phosphorylation | YYTPRRTSQSQSLSG HCCCCCCCCCCCCCC | 26.48 | 17330950 | |
| 88 | Phosphorylation | TPRRTSQSQSLSGST CCCCCCCCCCCCCCC | 22.85 | 22890988 | |
| 90 | Phosphorylation | RRTSQSQSLSGSTFK CCCCCCCCCCCCCHH | 29.74 | 22890988 | |
| 92 | Phosphorylation | TSQSQSLSGSTFKEY CCCCCCCCCCCHHHH | 35.62 | 21082442 | |
| 106 | Ubiquitination | YNEYINEKDSSRAQR HHHHHCHHHCHHHHH | 59.42 | 22817900 |
| 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 SPL2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPL2_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 SPL2_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-86, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-86, AND MASSSPECTROMETRY. | |