| UniProt ID | RPD3_YEAST | |
|---|---|---|
| UniProt AC | P32561 | |
| Protein Name | Histone deacetylase RPD3 | |
| Gene Name | RPD3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 433 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing.. | |
| Protein Sequence | MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRDAEDLGDVEEDSAEAKDTKGGSQYARDLHVEHDNEFY | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MVYEATPFDP -----CCCCCCCCCC | 9.88 | 28132839 | |
| 6 | Phosphorylation | --MVYEATPFDPITV --CCCCCCCCCCEEC | 16.73 | 28152593 | |
| 12 | Phosphorylation | ATPFDPITVKPSDKR CCCCCCEECCCCCCC | 28.06 | 23607784 | |
| 16 | Phosphorylation | DPITVKPSDKRRVAY CCEECCCCCCCCEEE | 50.47 | 23607784 | |
| 50 | Phosphorylation | HRIRMAHSLIMNYGL HHHHHHHHHHHHHCH | 15.28 | 27017623 | |
| 55 | Phosphorylation | AHSLIMNYGLYKKME HHHHHHHHCHHHHHE | 7.36 | 27017623 | |
| 58 | Phosphorylation | LIMNYGLYKKMEIYR HHHHHCHHHHHEEEE | 12.28 | 27017623 | |
| 336 | Ubiquitination | LNNVVLDKDLPYNEY CCCEECCCCCCCCCC | 57.93 | 17644757 | |
| 352 | Ubiquitination | EYYGPDYKLSVRPSN HHHCCCCEECCCHHH | 41.48 | 17644757 | |
| 365 | Phosphorylation | SNMFNVNTPEYLDKV HHCCCCCCHHHHHHH | 17.14 | 22369663 | |
| 368 | Phosphorylation | FNVNTPEYLDKVMTN CCCCCHHHHHHHHHH | 22.77 | 21440633 | |
| 371 | Ubiquitination | NTPEYLDKVMTNIFA CCHHHHHHHHHHHHH | 31.17 | 17644757 | |
| 384 | Ubiquitination | FANLENTKYAPSVQL HHCCCCCCCCCCEEC | 51.50 | 17644757 | |
| 385 | Phosphorylation | ANLENTKYAPSVQLN HCCCCCCCCCCEECC | 23.00 | 22369663 | |
| 388 | Phosphorylation | ENTKYAPSVQLNHTP CCCCCCCCEECCCCC | 17.83 | 22369663 | |
| 394 | Phosphorylation | PSVQLNHTPRDAEDL CCEECCCCCCCHHHH | 20.95 | 22369663 | |
| 408 | Phosphorylation | LGDVEEDSAEAKDTK HCCCCCCCCCCCCCC | 31.15 | 19823750 | |
| 412 | Ubiquitination | EEDSAEAKDTKGGSQ CCCCCCCCCCCCCCH | 58.39 | 23749301 | |
| 412 | Acetylation | EEDSAEAKDTKGGSQ CCCCCCCCCCCCCCH | 58.39 | 24489116 | |
| 414 | Phosphorylation | DSAEAKDTKGGSQYA CCCCCCCCCCCCHHC | 30.77 | 30377154 | |
| 415 | Acetylation | SAEAKDTKGGSQYAR CCCCCCCCCCCHHCC | 71.99 | 24489116 | |
| 418 | Phosphorylation | AKDTKGGSQYARDLH CCCCCCCCHHCCCEE | 28.78 | 25752575 | |
| 420 | Phosphorylation | DTKGGSQYARDLHVE CCCCCCHHCCCEECC | 12.80 | 21440633 | |
| 433 | Phosphorylation | VEHDNEFY------- CCCCCCCC------- | 16.09 | 19823750 |
| 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 RPD3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPD3_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 RPD3_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 THR-6; SER-388; THR-394 ANDSER-408, 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 THR-394 AND SER-408, ANDMASS SPECTROMETRY. | |
| "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 THR-394, AND MASSSPECTROMETRY. | |
