UniProt ID | SDS22_YEAST | |
---|---|---|
UniProt AC | P36047 | |
Protein Name | Protein phosphatase 1 regulatory subunit SDS22 | |
Gene Name | SDS22 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 338 | |
Subcellular Localization | Nucleus. | |
Protein Description | Regulator of the mitotic function of yeast type 1 protein phosphatase.. | |
Protein Sequence | MDKNSVNKDSEEKDERHKIEVVDDTNPDFITADSELTQDLPDDVEVIDLVHLKIKSLEDLNLYRFKNLKQLCLRQNLIESISEVEVLPHDKIVDLDFYDNKIKHISSNVNKLTKLTSLDLSFNKIKHIKNLENLTDLENLYFVQNSISKIENLSTLKSLKNLELGGNKVHSIEPDSFEGLSNLEEIWLGKNSIPRLINLHPLKNLKILSIQSNKLKKIENLEELTNLEELYLSHNFITKIEGLEKNLKLTTLDVTSNKITSLENLNHLSNLTDIWASFNKIDQSFESLGENLSALSRLETIYLEGNPIQLENKTSYRRKLTMNLPPSLQKIDATYIRG | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MDKNSVNKDSEE ---CCCCCCCCCCHH | 32.57 | 22369663 | |
8 | Acetylation | MDKNSVNKDSEEKDE CCCCCCCCCCHHHHH | 61.55 | 25381059 | |
10 | Phosphorylation | KNSVNKDSEEKDERH CCCCCCCCHHHHHHH | 49.63 | 22369663 | |
55 | Acetylation | DLVHLKIKSLEDLNL EEEEEEECCHHHCCC | 47.61 | 24489116 | |
56 | Phosphorylation | LVHLKIKSLEDLNLY EEEEEECCHHHCCCH | 40.23 | 22369663 | |
63 | Phosphorylation | SLEDLNLYRFKNLKQ CHHHCCCHHCCCHHH | 16.96 | 24930733 | |
80 | Phosphorylation | LRQNLIESISEVEVL HHHHHHHHHHEEECC | 25.15 | 28889911 | |
107 | Phosphorylation | NKIKHISSNVNKLTK CHHHHHHHCHHHHHH | 44.16 | 27017623 | |
113 | Phosphorylation | SSNVNKLTKLTSLDL HHCHHHHHHHHHCCC | 26.14 | 27017623 | |
116 | Phosphorylation | VNKLTKLTSLDLSFN HHHHHHHHHCCCCHH | 28.88 | 27017623 | |
124 | Acetylation | SLDLSFNKIKHIKNL HCCCCHHHHHHCCCC | 51.63 | 24489116 | |
126 | Acetylation | DLSFNKIKHIKNLEN CCCHHHHHHCCCCCC | 40.67 | 24489116 | |
129 | Acetylation | FNKIKHIKNLENLTD HHHHHHCCCCCCCCC | 56.02 | 24489116 | |
158 | Phosphorylation | ENLSTLKSLKNLELG CCHHHHHHHCCCEEC | 47.92 | 29688323 | |
214 | Acetylation | ILSIQSNKLKKIENL EEEECCCCCHHCCCH | 67.92 | 24489116 | |
248 | 2-Hydroxyisobutyrylation | EGLEKNLKLTTLDVT HHHHHCCCEEEEECC | 53.86 | - | |
293 | Phosphorylation | ESLGENLSALSRLET HHHHHHHHHHHHHEE | 38.45 | 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 SDS22_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SDS22_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 SDS22_YEAST !! |
Kegg Drug | ||||||
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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-56, AND MASSSPECTROMETRY. |