| UniProt ID | CCR4_YEAST | |
|---|---|---|
| UniProt AC | P31384 | |
| Protein Name | Glucose-repressible alcohol dehydrogenase transcriptional effector | |
| Gene Name | CCR4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 837 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. CCR4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA. Discovered because of its role in the control of ADH2 gene expression. It is required for the expression of genes involved in non-fermentative growth and it mediates or is required for the action of the SPT6 and SPT10 genes.. | |
| Protein Sequence | MNDPSLLGYPNVGPQQQQQQQQQQHAGLLGKGTPNALQQQLHMNQLTGIPPPGLMNNSDVHTSSNNNSRQLLDQLANGNANMLNMNMDNNNNNNNNNNNNNNNGGGSGVMMNASTAAVNSIGMVPTVGTPVNINVNASNPLLHPHLDDPSLLNNPIWKLQLHLAAVSAQSLGQPNIYARQNAMKKYLATQQAQQAQQQAQQQAQQQVPGPFGPGPQAAPPALQPTDFQQSHIAEASKSLVDCTKQALMEMADTLTDSKTAKKQQPTGDSTPSGTATNSAVSTPLTPKIELFANGKDEANQALLQHKKLSQYSIDEDDDIENRMVMPKDSKYDDQLWHALDLSNLQIFNISANIFKYDFLTRLYLNGNSLTELPAEIKNLSNLRVLDLSHNRLTSLPAELGSCFQLKYFYFFDNMVTTLPWEFGNLCNLQFLGVEGNPLEKQFLKILTEKSVTGLIFYLRDNRPEIPLPHERRFIEINTDGEPQREYDSLQQSTEHLATDLAKRTFTVLSYNTLCQHYATPKMYRYTPSWALSWDYRRNKLKEQILSYDSDLLCLQEVESKTFEEYWVPLLDKHGYTGIFHAKARAKTMHSKDSKKVDGCCIFFKRDQFKLITKDAMDFSGAWMKHKKFQRTEDYLNRAMNKDNVALFLKLQHIPSGDTIWAVTTHLHWDPKFNDVKTFQVGVLLDHLETLLKEETSHNFRQDIKKFPVLICGDFNSYINSAVYELINTGRVQIHQEGNGRDFGYMSEKNFSHNLALKSSYNCIGELPFTNFTPSFTDVIDYIWFSTHALRVRGLLGEVDPEYVSKFIGFPNDKFPSDHIPLLARFEFMKTNTGSKKV | |
| 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 |
|---|---|---|---|---|---|
| 33 | Phosphorylation | AGLLGKGTPNALQQQ HHHHCCCCHHHHHHH | 19.49 | 28889911 | |
| 47 | Phosphorylation | QLHMNQLTGIPPPGL HHHHHHCCCCCCCCC | 24.25 | 19779198 | |
| 238 | Phosphorylation | HIAEASKSLVDCTKQ HHHHHHHHHHHHHHH | 31.00 | 28889911 | |
| 262 | Ubiquitination | TDSKTAKKQQPTGDS CCCCCCCCCCCCCCC | 52.26 | 23749301 | |
| 266 | Phosphorylation | TAKKQQPTGDSTPSG CCCCCCCCCCCCCCC | 49.65 | 22369663 | |
| 269 | Phosphorylation | KQQPTGDSTPSGTAT CCCCCCCCCCCCCCC | 43.49 | 22369663 | |
| 270 | Phosphorylation | QQPTGDSTPSGTATN CCCCCCCCCCCCCCC | 26.64 | 22369663 | |
| 272 | Phosphorylation | PTGDSTPSGTATNSA CCCCCCCCCCCCCCC | 49.19 | 22369663 | |
| 274 | Phosphorylation | GDSTPSGTATNSAVS CCCCCCCCCCCCCCC | 34.35 | 22369663 | |
| 276 | Phosphorylation | STPSGTATNSAVSTP CCCCCCCCCCCCCCC | 29.55 | 22369663 | |
| 278 | Phosphorylation | PSGTATNSAVSTPLT CCCCCCCCCCCCCCC | 26.20 | 22369663 | |
| 281 | Phosphorylation | TATNSAVSTPLTPKI CCCCCCCCCCCCCCE | 24.83 | 22369663 | |
| 282 | Phosphorylation | ATNSAVSTPLTPKIE CCCCCCCCCCCCCEE | 18.73 | 22369663 | |
| 285 | Phosphorylation | SAVSTPLTPKIELFA CCCCCCCCCCEEEEE | 24.60 | 22369663 | |
| 295 | Acetylation | IELFANGKDEANQAL EEEEECCCHHHHHHH | 52.80 | 24489116 | |
| 307 | Ubiquitination | QALLQHKKLSQYSID HHHHHHHCHHHCCCC | 51.77 | 23749301 | |
| 309 | Phosphorylation | LLQHKKLSQYSIDED HHHHHCHHHCCCCCC | 35.63 | 22369663 | |
| 311 | Phosphorylation | QHKKLSQYSIDEDDD HHHCHHHCCCCCCCC | 12.29 | 21440633 | |
| 312 | Phosphorylation | HKKLSQYSIDEDDDI HHCHHHCCCCCCCCC | 18.87 | 22369663 | |
| 449 | Ubiquitination | FLKILTEKSVTGLIF HHHHHHHHCCCEEEE | 45.02 | 17644757 | |
| 504 | Phosphorylation | ATDLAKRTFTVLSYN HHHHHHHHEEEEECC | 23.97 | 28889911 | |
| 506 | Phosphorylation | DLAKRTFTVLSYNTL HHHHHHEEEEECCHH | 21.66 | 28889911 | |
| 509 | Phosphorylation | KRTFTVLSYNTLCQH HHHEEEEECCHHHHH | 16.41 | 30377154 | |
| 510 | Phosphorylation | RTFTVLSYNTLCQHY HHEEEEECCHHHHHC | 14.17 | 28889911 | |
| 512 | Phosphorylation | FTVLSYNTLCQHYAT EEEEECCHHHHHCCC | 22.22 | 28889911 | |
| 517 | Phosphorylation | YNTLCQHYATPKMYR CCHHHHHCCCCCCCC | 6.06 | 30377154 | |
| 521 | Acetylation | CQHYATPKMYRYTPS HHHCCCCCCCCCCCH | 44.18 | 24489116 | |
| 613 | Ubiquitination | DQFKLITKDAMDFSG HHEEEEECCCCCCCC | 36.17 | 23749301 | |
| 613 | Acetylation | DQFKLITKDAMDFSG HHEEEEECCCCCCCC | 36.17 | 24489116 | |
| 624 | Acetylation | DFSGAWMKHKKFQRT CCCCCHHHCCCHHHC | 41.38 | 24489116 | |
| 641 | Acetylation | YLNRAMNKDNVALFL HHHHHCCCCCEEEEE | 37.28 | 24489116 | |
| 748 | Acetylation | DFGYMSEKNFSHNLA CCCCCCCCCCCCCEE | 56.86 | 24489116 | |
| 805 | Ubiquitination | VDPEYVSKFIGFPND CCHHHHHHHCCCCCC | 30.84 | 17644757 | |
| 813 | Ubiquitination | FIGFPNDKFPSDHIP HCCCCCCCCCCCCHH | 66.85 | 24961812 | |
| 829 | Acetylation | LARFEFMKTNTGSKK HHHEEEECCCCCCCC | 43.90 | 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 CCR4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CCR4_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 CCR4_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-278, AND MASSSPECTROMETRY. | |
| "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-266; THR-276; SER-278;SER-281; THR-282 AND THR-285, AND MASS 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-285, AND MASSSPECTROMETRY. | |
