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 | ||||||
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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. |