| UniProt ID | CSN5_YEAST | |
|---|---|---|
| UniProt AC | Q12468 | |
| Protein Name | COP9 signalosome complex subunit 5 | |
| Gene Name | RRI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 440 | |
| Subcellular Localization | Cytoplasm. Nucleus. Nuclear localization requires the formation of the CSN complex. | |
| Protein Description | Catalytic component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex is involved in the regulation of the mating pheromone response.. | |
| Protein Sequence | MSLSNKTVKELRQLLKERYTVEDELTESIALSSMRFKPSQEPEFHALSQSSLLKTKLKQQSSTDIPSYTHVLISKLSCEKITHYAVRGGNIEIMGILMGFTLKDNIVVMDCFNLPVVGTETRVNAQLESYEYMVQYIDEMYNHNDGGDGRDYKGAKLNVVGWFHSHPGYDCWLSNIDIQTQDLNQRFQDPYVAIVVDPLKSLEDKILRMGAFRTIESKSDDNSATSYYELETIIFDSELNRALFETKLNLHCVIEDDESEQISLNRLIDSMKQYSYLMDSKNVRTRIKLATTSERVSNENKKNIDYQNRSTRSQFCLNTQRGDSTETSSFGSMFSGDNTSDVDMEDRNLTEFDSTDTSLCINGEPSIHVNRVERSSRSTDNFHNSKKRMNSNQERCHDEGNDMLQRNVLETDYARAKNRILASKIKQYERLRFYKDTFTL | |
| 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 | ------MSLSNKTVK ------CCCCHHHHH | 40.27 | 26447709 | |
| 4 | Phosphorylation | ----MSLSNKTVKEL ----CCCCHHHHHHH | 29.04 | 26447709 | |
| 7 | Phosphorylation | -MSLSNKTVKELRQL -CCCCHHHHHHHHHH | 40.85 | 26447709 | |
| 39 | Phosphorylation | SSMRFKPSQEPEFHA HHCCCCCCCCHHHHH | 48.00 | 25752575 | |
| 313 | Phosphorylation | YQNRSTRSQFCLNTQ CCCCCCCCEEECCCC | 27.91 | 28889911 | |
| 324 | Phosphorylation | LNTQRGDSTETSSFG CCCCCCCCCCCCCCC | 30.85 | 27017623 | |
| 328 | Phosphorylation | RGDSTETSSFGSMFS CCCCCCCCCCCCCCC | 19.89 | 28889911 | |
| 332 | Phosphorylation | TETSSFGSMFSGDNT CCCCCCCCCCCCCCC | 18.04 | 27017623 | |
| 335 | Phosphorylation | SSFGSMFSGDNTSDV CCCCCCCCCCCCCCC | 36.27 | 27017623 | |
| 339 | Phosphorylation | SMFSGDNTSDVDMED CCCCCCCCCCCCCCC | 30.92 | 30377154 | |
| 340 | Phosphorylation | MFSGDNTSDVDMEDR CCCCCCCCCCCCCCC | 41.72 | 28889911 | |
| 378 | Phosphorylation | RVERSSRSTDNFHNS EECCCCCCCCCCHHH | 41.90 | 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 CSN5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CSN5_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 CSN5_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-313, AND MASSSPECTROMETRY. | |
