| UniProt ID | DEP1_YEAST | |
|---|---|---|
| UniProt AC | P31385 | |
| Protein Name | Transcriptional regulatory protein DEP1 | |
| Gene Name | DEP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 405 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.. | |
| Protein Sequence | MSQQTPQESEQTTAKEQDLDQESVLSNIDFNTDLNHNLNLSEYCISSDAGTEKMDSDEEKSLANLPELKYAPKLSSLVKQETLTESLKRPHEDEKEAIDEAKKMKVPGENEDESKEEEKSQELEEAIDSKEKSTDARDEQGDEGDNEEENNEEDNENENEHTAPPALVMPSPIEMEEQRMTALKEITDIEYKFAQLRQKLYDNQLVRLQTELQMCLEGSHPELQVYYSKIAAIRDYKLHRAYQRQKYELSCINTETIATRTFIHQDFHKKVTDLRARLLNRTTQTWYDINKERRDMDIVIPDVNYHVPIKLDNKTLSCITGYASAAQLCYPGEPVAEDLACESIEYRYRANPVDKLEVIVDRMRLNNEISDLEGLRKYFHSFPGAPELNPLRDSEINDDFHQWAQ | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSQQTPQES ------CCCCCCCCH | 30.88 | 22369663 | |
| 5 | Phosphorylation | ---MSQQTPQESEQT ---CCCCCCCCHHHC | 21.21 | 28889911 | |
| 56 | Phosphorylation | AGTEKMDSDEEKSLA CCCCCCCCHHHHHHH | 43.34 | 27214570 | |
| 61 | Phosphorylation | MDSDEEKSLANLPEL CCCHHHHHHHCCHHH | 35.67 | 22369663 | |
| 69 | Acetylation | LANLPELKYAPKLSS HHCCHHHHHHHHHHH | 37.39 | 24489116 | |
| 73 | Acetylation | PELKYAPKLSSLVKQ HHHHHHHHHHHHHCH | 53.48 | 24489116 | |
| 76 | Phosphorylation | KYAPKLSSLVKQETL HHHHHHHHHHCHHHH | 47.84 | 22369663 | |
| 79 | Acetylation | PKLSSLVKQETLTES HHHHHHHCHHHHHHH | 47.94 | 24489116 | |
| 82 | Phosphorylation | SSLVKQETLTESLKR HHHHCHHHHHHHHCC | 36.16 | 22369663 | |
| 84 | Phosphorylation | LVKQETLTESLKRPH HHCHHHHHHHHCCCC | 30.83 | 21440633 | |
| 86 | Phosphorylation | KQETLTESLKRPHED CHHHHHHHHCCCCHH | 33.67 | 22369663 | |
| 114 | Phosphorylation | PGENEDESKEEEKSQ CCCCCCCCHHHHHHH | 58.66 | 19823750 | |
| 120 | Phosphorylation | ESKEEEKSQELEEAI CCHHHHHHHHHHHHH | 31.97 | 22369663 | |
| 129 | Phosphorylation | ELEEAIDSKEKSTDA HHHHHHHHHHHCCCC | 36.28 | 22369663 | |
| 192 | Acetylation | EITDIEYKFAQLRQK HHHHHHHHHHHHHHH | 22.79 | 24489116 | |
| 199 | Acetylation | KFAQLRQKLYDNQLV HHHHHHHHHHHCHHH | 42.45 | 24489116 | |
| 310 | Acetylation | VNYHVPIKLDNKTLS CCEECEEEECCCEEC | 43.66 | 24489116 | |
| 355 | Acetylation | YRANPVDKLEVIVDR CCCCCCCCHHHHHHH | 46.94 | 24489116 | |
| 355 | Ubiquitination | YRANPVDKLEVIVDR CCCCCCCCHHHHHHH | 46.94 | 24961812 | |
| 370 | Phosphorylation | MRLNNEISDLEGLRK HHHCCCCCCHHHHHH | 29.93 | 28889911 | |
| 377 | Acetylation | SDLEGLRKYFHSFPG CCHHHHHHHHHHCCC | 58.26 | 24489116 | |
| 381 | Phosphorylation | GLRKYFHSFPGAPEL HHHHHHHHCCCCCCC | 24.20 | 30377154 | |
| 394 | Phosphorylation | ELNPLRDSEINDDFH CCCCCCCCCCCCCCH | 33.66 | 28889911 |
| 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 DEP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DEP1_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 DEP1_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-120 AND SER-370, ANDMASS SPECTROMETRY. | |
