| UniProt ID | CSL4_YEAST | |
|---|---|---|
| UniProt AC | P53859 | |
| Protein Name | Exosome complex component CSL4 | |
| Gene Name | CSL4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 292 | |
| Subcellular Localization | Cytoplasm . Nucleus, nucleolus . | |
| Protein Description | Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.. | |
| Protein Sequence | MACNFQFPEIAYPGKLICPQYGTENKDGEDIIFNYVPGPGTKLIQYEHNGRTLEAITATLVGTVRCEEEKKTDQEEEREGTDQSTEEEKSVDASPNDVTRRTVKNILVSVLPGTEKGRKTNKYANNDFANNLPKEGDIVLTRVTRLSLQRANVEILAVEDKPSPIDSGIGSNGSGIVAAGGGSGAATFSVSQASSDLGETFRGIIRSQDVRSTDRDRVKVIECFKPGDIVRAQVLSLGDGTNYYLTTARNDLGVVFARAANGAGGLMYATDWQMMTSPVTGATEKRKCAKPF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 46 | Phosphorylation | PGTKLIQYEHNGRTL CCCEEEEEEECCEEE | 16.50 | 30377154 | |
| 57 | Phosphorylation | GRTLEAITATLVGTV CEEEEEEEEEEEEEE | 22.19 | 30377154 | |
| 59 | Phosphorylation | TLEAITATLVGTVRC EEEEEEEEEEEEEEC | 17.21 | 30377154 | |
| 63 | Phosphorylation | ITATLVGTVRCEEEK EEEEEEEEEECCHHH | 9.41 | 30377154 | |
| 81 | Phosphorylation | QEEEREGTDQSTEEE HHHHHCCCCCCHHHH | 26.55 | 28889911 | |
| 84 | Phosphorylation | EREGTDQSTEEEKSV HHCCCCCCHHHHHHC | 40.36 | 28889911 | |
| 85 | Phosphorylation | REGTDQSTEEEKSVD HCCCCCCHHHHHHCC | 41.61 | 28889911 | |
| 90 | Phosphorylation | QSTEEEKSVDASPND CCHHHHHHCCCCCCC | 28.63 | 22369663 | |
| 94 | Phosphorylation | EEKSVDASPNDVTRR HHHHCCCCCCCHHHH | 21.55 | 22369663 | |
| 99 | Phosphorylation | DASPNDVTRRTVKNI CCCCCCHHHHHHHHH | 19.80 | 22369663 | |
| 102 | Phosphorylation | PNDVTRRTVKNILVS CCCHHHHHHHHHEEE | 32.32 | 24961812 | |
| 114 | Phosphorylation | LVSVLPGTEKGRKTN EEEECCCCCHHCCCC | 32.36 | 27017623 | |
| 116 | Acetylation | SVLPGTEKGRKTNKY EECCCCCHHCCCCCC | 64.95 | 24489116 | |
| 270 | Phosphorylation | AGGLMYATDWQMMTS CCCEEEEECCEEECC | 21.93 | 27017623 | |
| 277 | Phosphorylation | TDWQMMTSPVTGATE ECCEEECCCCCCCCC | 10.24 | 28889911 | |
| 280 | Phosphorylation | QMMTSPVTGATEKRK EEECCCCCCCCCCCC | 25.20 | 27017623 | |
| 283 | Phosphorylation | TSPVTGATEKRKCAK CCCCCCCCCCCCCCC | 43.30 | 27017623 |
| 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 CSL4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSL4_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 CSL4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-94 AND SER-277, AND MASSSPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY. | |
