| UniProt ID | CTI6_YEAST | |
|---|---|---|
| UniProt AC | Q08923 | |
| Protein Name | Histone deacetylase complex subunit CTI6 | |
| Gene Name | CTI6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 506 | |
| Subcellular Localization | 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. CTI6 links the SAGA coactivator to the CYC8-TUP1 corepressor. Involved in transcription regulation of heme-regulated genes and required for GCN5 recruitment, histone H3 acetylation and SPT15/TBP binding to promoters.. | |
| Protein Sequence | MESTAIVPKGPVVGSEDMEKAEVIASGSTDIISTTSTATTTAAIGSVQEESVKQEDVPMEGGEGEVEEEEGETRCICGELDTPDDSGFFIQCEQCSSWQHGYCVSITQDNAPDKYWCEQCRPELHQLFTTDTGEARSIYKPVQEKRRQSRRKARSAAASKSHAANEAEKSPRNTSNTDDNVDDIGDEEDEVEDEASAVALAKDGNTRSSRRRRRNSMDDASTDQYSLDPGDSDKKLLDRKRATFMAREEKQYQRMLEKALKESRRTSHQEDPESYENDADIYQGDTDNHNGTTRLQTDVMLTEGKPDSVTNDDMKESLRPSKEQSMEKTNDVEKEASQEKESSTGSAQDTEKTDEPILPLTSISSSEDDSRKASSRGSKRVSKPARKGNRTRRSNTSSDTNQNRRSADIGTDKPVKPRLPPQRTSLNEMRRRVSAILEFISRTQWELSEDQSDREEFVRFVENQHFVEKVDTIYNGYNESLSMMDDLTRELLLWEKKYSNNTNAIQ | |
| 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 |
|---|---|---|---|---|---|
| 9 | Acetylation | ESTAIVPKGPVVGSE CCCEECCCCCCCCCH | 66.02 | 25381059 | |
| 9 | Ubiquitination | ESTAIVPKGPVVGSE CCCEECCCCCCCCCH | 66.02 | 19722269 | |
| 145 | Acetylation | IYKPVQEKRRQSRRK HHHHHHHHHHHHHHH | 35.47 | 24489116 | |
| 155 | Phosphorylation | QSRRKARSAAASKSH HHHHHHHHHHHHHHH | 27.41 | 28889911 | |
| 159 | Phosphorylation | KARSAAASKSHAANE HHHHHHHHHHHHHHH | 29.93 | 19684113 | |
| 161 | Phosphorylation | RSAAASKSHAANEAE HHHHHHHHHHHHHHH | 18.83 | 21440633 | |
| 169 | Acetylation | HAANEAEKSPRNTSN HHHHHHHHCCCCCCC | 73.19 | 24489116 | |
| 170 | Phosphorylation | AANEAEKSPRNTSNT HHHHHHHCCCCCCCC | 22.16 | 17563356 | |
| 174 | Phosphorylation | AEKSPRNTSNTDDNV HHHCCCCCCCCCCCC | 25.32 | 22369663 | |
| 175 | Phosphorylation | EKSPRNTSNTDDNVD HHCCCCCCCCCCCCH | 41.08 | 22369663 | |
| 177 | Phosphorylation | SPRNTSNTDDNVDDI CCCCCCCCCCCCHHC | 44.49 | 22369663 | |
| 202 | Acetylation | ASAVALAKDGNTRSS HHHHHHHHCCCCHHH | 68.00 | 24489116 | |
| 216 | Phosphorylation | SRRRRRNSMDDASTD HHHHHHHCCCCCCCC | 23.06 | 22369663 | |
| 221 | Phosphorylation | RNSMDDASTDQYSLD HHCCCCCCCCCCCCC | 39.24 | 22369663 | |
| 222 | Phosphorylation | NSMDDASTDQYSLDP HCCCCCCCCCCCCCC | 28.92 | 22369663 | |
| 225 | Phosphorylation | DDASTDQYSLDPGDS CCCCCCCCCCCCCCC | 17.63 | 19779198 | |
| 226 | Phosphorylation | DASTDQYSLDPGDSD CCCCCCCCCCCCCCC | 22.21 | 19795423 | |
| 232 | Phosphorylation | YSLDPGDSDKKLLDR CCCCCCCCCHHHHHH | 58.19 | 19795423 | |
| 243 | Phosphorylation | LLDRKRATFMAREEK HHHHHHHHHHHHHHH | 20.27 | 21551504 | |
| 250 | Acetylation | TFMAREEKQYQRMLE HHHHHHHHHHHHHHH | 49.94 | 24489116 | |
| 258 | Acetylation | QYQRMLEKALKESRR HHHHHHHHHHHHHHH | 55.87 | 22865919 | |
| 266 | Phosphorylation | ALKESRRTSHQEDPE HHHHHHHCCCCCCHH | 29.47 | 22369663 | |
| 267 | Phosphorylation | LKESRRTSHQEDPES HHHHHHCCCCCCHHH | 22.74 | 22369663 | |
| 274 | Phosphorylation | SHQEDPESYENDADI CCCCCHHHHCCCCCC | 43.04 | 22369663 | |
| 275 | Phosphorylation | HQEDPESYENDADIY CCCCHHHHCCCCCCC | 19.65 | 29136822 | |
| 282 | Phosphorylation | YENDADIYQGDTDNH HCCCCCCCCCCCCCC | 13.64 | 29136822 | |
| 297 | Phosphorylation | NGTTRLQTDVMLTEG CCCEEEEEEEEEECC | 34.84 | 19779198 | |
| 302 | Phosphorylation | LQTDVMLTEGKPDSV EEEEEEEECCCCCCC | 25.29 | 22369663 | |
| 308 | Phosphorylation | LTEGKPDSVTNDDMK EECCCCCCCCCHHHH | 39.09 | 22369663 | |
| 310 | Phosphorylation | EGKPDSVTNDDMKES CCCCCCCCCHHHHHH | 36.56 | 22369663 | |
| 317 | Phosphorylation | TNDDMKESLRPSKEQ CCHHHHHHHCCCHHH | 24.94 | 29136822 | |
| 321 | Phosphorylation | MKESLRPSKEQSMEK HHHHHCCCHHHHHHH | 42.25 | 24961812 | |
| 325 | Phosphorylation | LRPSKEQSMEKTNDV HCCCHHHHHHHHCHH | 29.96 | 29136822 | |
| 328 | Acetylation | SKEQSMEKTNDVEKE CHHHHHHHHCHHHHH | 43.94 | 22865919 | |
| 334 | Acetylation | EKTNDVEKEASQEKE HHHCHHHHHHHHHHH | 59.43 | 22865919 | |
| 343 | Phosphorylation | ASQEKESSTGSAQDT HHHHHHHCCCCCCCC | 37.57 | 28889911 | |
| 344 | Phosphorylation | SQEKESSTGSAQDTE HHHHHHCCCCCCCCC | 44.42 | 27717283 | |
| 346 | Phosphorylation | EKESSTGSAQDTEKT HHHHCCCCCCCCCCC | 23.89 | 28889911 | |
| 350 | Phosphorylation | STGSAQDTEKTDEPI CCCCCCCCCCCCCCC | 27.57 | 27717283 | |
| 352 | Acetylation | GSAQDTEKTDEPILP CCCCCCCCCCCCCEE | 64.47 | 24489116 | |
| 361 | Phosphorylation | DEPILPLTSISSSED CCCCEECCCCCCCCC | 23.29 | 22369663 | |
| 362 | Phosphorylation | EPILPLTSISSSEDD CCCEECCCCCCCCCH | 28.31 | 25521595 | |
| 364 | Phosphorylation | ILPLTSISSSEDDSR CEECCCCCCCCCHHH | 27.81 | 22369663 | |
| 365 | Phosphorylation | LPLTSISSSEDDSRK EECCCCCCCCCHHHH | 35.76 | 22369663 | |
| 366 | Phosphorylation | PLTSISSSEDDSRKA ECCCCCCCCCHHHHH | 37.95 | 20377248 | |
| 370 | Phosphorylation | ISSSEDDSRKASSRG CCCCCCHHHHHHHHC | 48.26 | 22369663 | |
| 396 | Phosphorylation | NRTRRSNTSSDTNQN CCCCCCCCCCCCCCC | 30.74 | 28889911 | |
| 398 | Phosphorylation | TRRSNTSSDTNQNRR CCCCCCCCCCCCCHH | 46.55 | 28889911 | |
| 406 | Phosphorylation | DTNQNRRSADIGTDK CCCCCHHHCCCCCCC | 27.36 | 29136822 | |
| 441 | Phosphorylation | SAILEFISRTQWELS HHHHHHHHHHCCCCC | 34.30 | 28889911 | |
| 448 | Phosphorylation | SRTQWELSEDQSDRE HHHCCCCCCCCCCHH | 27.84 | 30377154 | |
| 452 | Phosphorylation | WELSEDQSDREEFVR CCCCCCCCCHHHHHH | 51.46 | 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 CTI6_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CTI6_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 CTI6_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-216; SER-364 ANDSER-441, 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 SER-170 AND SER-216, ANDMASS SPECTROMETRY. | |
