| UniProt ID | RPN11_YEAST | |
|---|---|---|
| UniProt AC | P43588 | |
| Protein Name | Ubiquitin carboxyl-terminal hydrolase RPN11 | |
| Gene Name | RPN11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 306 | |
| Subcellular Localization | ||
| Protein Description | Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. RPN11 is the only catalytically active member of the lid and serves as the essential deubiquitinase of the proteasome.. | |
| Protein Sequence | MERLQRLMMNSKVGSADTGRDDTKETVYISSIALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVNVVDVFAMPQSGTGVSVEAVDDVFQAKMMDMLKQTGRDQMVVGWYHSHPGFGCWLSSVDVNTQKSFEQLNSRAVAVVVDPIQSVKGKVVIDAFRLIDTGALINNLEPRQTTSNTGLLNKANIQALIHGLNRHYYSLNIDYHKTAKETKMLMNLHKEQWQSGLKMYDYEEKEESNLAATKSMVKIAEQYSKRIEEEKELTEEELKTRYVGRQDPKKHLSETADETLENNIVSVLTAGVNSVAIK | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MERLQRLM -------CHHHHHHH | 6.45 | 12504901 | |
| 12 | Ubiquitination | QRLMMNSKVGSADTG HHHHHCCCCCCCCCC | 45.68 | 23749301 | |
| 15 | Phosphorylation | MMNSKVGSADTGRDD HHCCCCCCCCCCCCC | 26.42 | 27214570 | |
| 146 | Phosphorylation | VVVDPIQSVKGKVVI EEECCHHHCCCEEEE | 26.90 | 22369663 | |
| 148 | 2-Hydroxyisobutyrylation | VDPIQSVKGKVVIDA ECCHHHCCCEEEEEE | 59.26 | - | |
| 148 | Ubiquitination | VDPIQSVKGKVVIDA ECCHHHCCCEEEEEE | 59.26 | 17644757 | |
| 182 | Ubiquitination | SNTGLLNKANIQALI CCCCCCCHHHHHHHH | 42.66 | 17644757 | |
| 182 | Acetylation | SNTGLLNKANIQALI CCCCCCCHHHHHHHH | 42.66 | 24489116 | |
| 205 | Ubiquitination | SLNIDYHKTAKETKM ECCCCHHHCHHHHHH | 43.90 | 23749301 | |
| 208 | Ubiquitination | IDYHKTAKETKMLMN CCHHHCHHHHHHHHH | 71.76 | 22817900 | |
| 218 | Acetylation | KMLMNLHKEQWQSGL HHHHHHCHHHHHHCC | 55.56 | 24489116 | |
| 233 | Ubiquitination | KMYDYEEKEESNLAA CCCCCCHHHHHCHHH | 55.64 | 23749301 | |
| 233 | Acetylation | KMYDYEEKEESNLAA CCCCCCHHHHHCHHH | 55.64 | 24489116 | |
| 241 | Phosphorylation | EESNLAATKSMVKIA HHHCHHHHHHHHHHH | 20.32 | 29136822 | |
| 243 | Phosphorylation | SNLAATKSMVKIAEQ HCHHHHHHHHHHHHH | 25.18 | 20486117 | |
| 246 | Acetylation | AATKSMVKIAEQYSK HHHHHHHHHHHHHHH | 27.79 | 24489116 | |
| 262 | Phosphorylation | IEEEKELTEEELKTR HHHHHHCCHHHHHHH | 42.30 | 28889911 | |
| 267 | Acetylation | ELTEEELKTRYVGRQ HCCHHHHHHHHCCCC | 33.95 | 24489116 | |
| 281 | Phosphorylation | QDPKKHLSETADETL CCHHHCHHHHHHHHH | 32.40 | 22369663 | |
| 283 | Phosphorylation | PKKHLSETADETLEN HHHCHHHHHHHHHHH | 35.71 | 22369663 | |
| 287 | Phosphorylation | LSETADETLENNIVS HHHHHHHHHHHCHHH | 39.66 | 21551504 | |
| 294 | Phosphorylation | TLENNIVSVLTAGVN HHHHCHHHHHCCCCC | 13.96 | 22369663 | |
| 297 | Phosphorylation | NNIVSVLTAGVNSVA HCHHHHHCCCCCCEE | 21.14 | 22369663 | |
| 302 | Phosphorylation | VLTAGVNSVAIK--- HHCCCCCCEEEC--- | 15.54 | 22369663 |
| 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 RPN11_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN11_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 RPN11_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "N-terminal modifications of the 19S regulatory particle subunits ofthe yeast proteasome."; Kimura Y., Saeki Y., Yokosawa H., Polevoda B., Sherman F., Hirano H.; Arch. Biochem. Biophys. 409:341-348(2003). Cited for: PROTEIN SEQUENCE OF 1-8, AND ACETYLATION AT MET-1. | |
| 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 THR-262, AND MASSSPECTROMETRY. | |