| UniProt ID | 2ABA_YEAST | |
|---|---|---|
| UniProt AC | Q00362 | |
| Protein Name | Protein phosphatase PP2A regulatory subunit B | |
| Gene Name | CDC55 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 526 | |
| Subcellular Localization | ||
| Protein Description | Phosphatase 2A affects a variety of biological processes in the cell such as transcription, cell cycle progression and cellular morphogenesis, and provides an initial identification of critical substrates for this phosphatase. The regulatory subunit may direct the catalytic subunit to distinct, albeit overlapping, subsets of substrates.. | |
| Protein Sequence | MAQNNFDFKFSQCFGDKADIVVTEADLITAVEFDYTGNYLATGDKGGRVVLFERSNSRHCEYKFLTEFQSHDAEFDYLKSLEIEEKINEIKWLRPTQRSHFLLSTNDKTIKLWKVYEKNIKLVSQNNLTEGVTFAKKGKPDNHNSRGGSVRAVLSLQSLKLPQLSQHDKIIAATPKRIYSNAHTYHINSISLNSDQETFLSADDLRINLWNLDIPDQSFNIVDIKPTNMEELTEVITSAEFHPQECNLFMYSSSKGTIKLCDMRQNSLCDNKTKTFEEYLDPINHNFFTEITSSISDIKFSPNGRYIASRDYLTVKIWDVNMDNKPLKTINIHEQLKERLSDTYENDAIFDKFEVNFSGDSSSVMTGSYNNNFMIYPNVVTSGDNDNGIVKTFDEHNAPNSNSNKNIHNSIQNKDSSSSGNSHKRRSNGRNTGMVGSSNSSRSSIAGGEGANSEDSGTEMNEIVLQADKTAFRNKRYGSLAQRSARNKDWGDDIDFKKNILHFSWHPRENSIAVAATNNLFIFSAL | |
| 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 |
|---|---|---|---|---|---|
| 104 | Phosphorylation | QRSHFLLSTNDKTIK CCCCEEEECCCCEEE | 27.58 | 27017623 | |
| 105 | Phosphorylation | RSHFLLSTNDKTIKL CCCEEEECCCCEEEE | 47.62 | 27017623 | |
| 108 | Acetylation | FLLSTNDKTIKLWKV EEEECCCCEEEEEEE | 54.97 | 24489116 | |
| 114 | Acetylation | DKTIKLWKVYEKNIK CCEEEEEEEHHHHCE | 45.43 | 24489116 | |
| 124 | Phosphorylation | EKNIKLVSQNNLTEG HHHCEEEECCCCCCC | 37.31 | 25752575 | |
| 136 | Acetylation | TEGVTFAKKGKPDNH CCCCEEECCCCCCCC | 58.84 | 22865919 | |
| 155 | Phosphorylation | GSVRAVLSLQSLKLP CCHHHHHEECCCCCC | 20.12 | 22369663 | |
| 160 | Acetylation | VLSLQSLKLPQLSQH HHEECCCCCCCCCCC | 64.47 | 24489116 | |
| 169 | Acetylation | PQLSQHDKIIAATPK CCCCCCCCEEEECCC | 33.61 | 24489116 | |
| 325 | Acetylation | WDVNMDNKPLKTINI EEECCCCCCCEEECH | 47.68 | 24489116 | |
| 341 | Phosphorylation | EQLKERLSDTYENDA HHHHHHHHCCCCCCC | 33.84 | 28889911 | |
| 401 | Phosphorylation | DEHNAPNSNSNKNIH CCCCCCCCCCCCCHH | 40.34 | 28889911 | |
| 403 | Phosphorylation | HNAPNSNSNKNIHNS CCCCCCCCCCCHHHH | 49.34 | 21440633 | |
| 405 | Acetylation | APNSNSNKNIHNSIQ CCCCCCCCCHHHHHC | 58.04 | 25381059 | |
| 410 | Phosphorylation | SNKNIHNSIQNKDSS CCCCHHHHHCCCCCC | 16.05 | 23749301 | |
| 427 | Phosphorylation | GNSHKRRSNGRNTGM CCCCCCCCCCCCCCC | 47.90 | 21440633 | |
| 437 | Phosphorylation | RNTGMVGSSNSSRSS CCCCCCCCCCCCCCC | 18.22 | 28889911 | |
| 438 | Phosphorylation | NTGMVGSSNSSRSSI CCCCCCCCCCCCCCC | 34.50 | 25752575 | |
| 440 | Phosphorylation | GMVGSSNSSRSSIAG CCCCCCCCCCCCCCC | 29.13 | 23749301 | |
| 441 | Phosphorylation | MVGSSNSSRSSIAGG CCCCCCCCCCCCCCC | 40.19 | 25752575 | |
| 443 | Phosphorylation | GSSNSSRSSIAGGEG CCCCCCCCCCCCCCC | 28.22 | 30377154 | |
| 444 | Phosphorylation | SSNSSRSSIAGGEGA CCCCCCCCCCCCCCC | 18.49 | 28889911 | |
| 453 | Phosphorylation | AGGEGANSEDSGTEM CCCCCCCCCCCCCCH | 42.10 | 28889911 | |
| 479 | Phosphorylation | FRNKRYGSLAQRSAR HHCHHHHHHHHHHHH | 16.17 | 25752575 | |
| 488 | Acetylation | AQRSARNKDWGDDID HHHHHHCCCCCCCCC | 49.67 | 24489116 | |
| 497 | Acetylation | WGDDIDFKKNILHFS CCCCCCCCCCEEEEE | 40.96 | 24489116 |
| 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 2ABA_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of 2ABA_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 2ABA_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-124; SER-155 ANDSER-440, AND MASS SPECTROMETRY. | |
