| UniProt ID | SLT11_YEAST | |
|---|---|---|
| UniProt AC | P38241 | |
| Protein Name | Pre-mRNA-splicing factor SLT11 | |
| Gene Name | ECM2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 364 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Involved in pre-mRNA splicing. Facilitates the cooperative formation of U2/U6 helix II in association with stem II in the spliceosome. Binds to RNA.. | |
| Protein Sequence | MNDEINEPPPNICEQCLGDEANIRMTKIPQGSECKICTLPFTLYHFKTSKRSNNIIKTLICVRCATQRNICQCCMLDSRWHIPIQLRDHLISLVNEENVMTEEAKNDMMKRFLSLKNVKLGGAQITSDPSEADNIVDKLKNILLRATSDGPSTPLIKNTTALYKNEKGANEVKNLEKYASVDISHILKKLPLNESFLKNPSTKSFFLYNIDASIPEWKITDTVSQLLGIKKWKDGNSLSLIVNHKAKCGGLRFQSSELGERFVSKISETLVTPKGLKRGVLLIDRFRIFIIPWSSGFSAASFGTNTAENIKLSLSLNKLIQLELGLSFPTKSTDNAKNDKKKTSKKVHKDRSKKSKPRANKLTI | |
| 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 |
|---|---|---|---|---|---|
| 147 | Phosphorylation | KNILLRATSDGPSTP HHHHHHHCCCCCCCC | 22.40 | 21126336 | |
| 148 | Phosphorylation | NILLRATSDGPSTPL HHHHHHCCCCCCCCC | 39.32 | 27017623 | |
| 153 | Phosphorylation | ATSDGPSTPLIKNTT HCCCCCCCCCCCCHH | 25.83 | 27214570 | |
| 160 | Phosphorylation | TPLIKNTTALYKNEK CCCCCCHHHHHCCCC | 24.86 | 27017623 | |
| 233 | Acetylation | LLGIKKWKDGNSLSL HHCCEECCCCCEEEE | 65.72 | 22865919 | |
| 352 | Phosphorylation | KKVHKDRSKKSKPRA HHHHHHHCCCCCCCC | 55.35 | 17287358 |
| 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 SLT11_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SLT11_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 SLT11_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-352, AND MASSSPECTROMETRY. | |
| "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 THR-153, AND MASSSPECTROMETRY. | |
