UniProt ID | RPN6_YEAST | |
---|---|---|
UniProt AC | Q12377 | |
Protein Name | 26S proteasome regulatory subunit RPN6 | |
Gene Name | RPN6 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 434 | |
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. In the complex, RPN6 is required for proteasome assembly.. | |
Protein Sequence | MSLPGSKLEEARRLVNEKQYNEAEQVYLSLLDKDSSQSSAAAGASVDDKRRNEQETSILELGQLYVTMGAKDKLREFIPHSTEYMMQFAKSKTVKVLKTLIEKFEQVPDSLDDQIFVCEKSIEFAKREKRVFLKHSLSIKLATLHYQKKQYKDSLALINDLLREFKKLDDKPSLVDVHLLESKVYHKLRNLAKSKASLTAARTAANSIYCPTQTVAELDLMSGILHCEDKDYKTAFSYFFESFESYHNLTTHNSYEKACQVLKYMLLSKIMLNLIDDVKNILNAKYTKETYQSRGIDAMKAVAEAYNNRSLLDFNTALKQYEKELMGDELTRSHFNALYDTLLESNLCKIIEPFECVEISHISKIIGLDTQQVEGKLSQMILDKIFYGVLDQGNGWLYVYETPNQDATYDSALELVGQLNKVVDQLFEKASVLY | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSLPGSKLE ------CCCCCCHHH | 43.18 | 28152593 | |
2 | Acetylation | ------MSLPGSKLE ------CCCCCCHHH | 43.18 | 22814378 | |
7 | Acetylation | -MSLPGSKLEEARRL -CCCCCCHHHHHHHH | 66.87 | 25381059 | |
33 | Ubiquitination | VYLSLLDKDSSQSSA HHHHHHCCCCCCCHH | 60.52 | 17644757 | |
35 | Phosphorylation | LSLLDKDSSQSSAAA HHHHCCCCCCCHHHC | 35.70 | 22369663 | |
36 | Phosphorylation | SLLDKDSSQSSAAAG HHHCCCCCCCHHHCC | 44.19 | 22369663 | |
38 | Phosphorylation | LDKDSSQSSAAAGAS HCCCCCCCHHHCCCC | 24.72 | 20486117 | |
39 | Phosphorylation | DKDSSQSSAAAGASV CCCCCCCHHHCCCCC | 17.81 | 22369663 | |
45 | Phosphorylation | SSAAAGASVDDKRRN CHHHCCCCCCHHHHC | 25.76 | 22369663 | |
49 | Ubiquitination | AGASVDDKRRNEQET CCCCCCHHHHCHHHC | 49.12 | 23749301 | |
81 | Phosphorylation | LREFIPHSTEYMMQF HHHHCCCCHHHHHHH | 19.99 | 19823750 | |
82 | Phosphorylation | REFIPHSTEYMMQFA HHHCCCCHHHHHHHH | 28.27 | 19823750 | |
84 | Phosphorylation | FIPHSTEYMMQFAKS HCCCCHHHHHHHHHH | 9.66 | 19823750 | |
90 | Acetylation | EYMMQFAKSKTVKVL HHHHHHHHHHHHHHH | 54.49 | 24489116 | |
98 | Acetylation | SKTVKVLKTLIEKFE HHHHHHHHHHHHHHH | 44.25 | 22865919 | |
134 | Acetylation | REKRVFLKHSLSIKL HCCCHHHHHHHHHHH | 21.49 | 24489116 | |
140 | Ubiquitination | LKHSLSIKLATLHYQ HHHHHHHHHHHHHHC | 28.79 | 17644757 | |
148 | Ubiquitination | LATLHYQKKQYKDSL HHHHHHCHHHHHHHH | 34.38 | 17644757 | |
149 | Ubiquitination | ATLHYQKKQYKDSLA HHHHHCHHHHHHHHH | 43.25 | 17644757 | |
149 | Acetylation | ATLHYQKKQYKDSLA HHHHHCHHHHHHHHH | 43.25 | 24489116 | |
152 | Acetylation | HYQKKQYKDSLALIN HHCHHHHHHHHHHHH | 38.04 | 24489116 | |
152 | Ubiquitination | HYQKKQYKDSLALIN HHCHHHHHHHHHHHH | 38.04 | 17644757 | |
166 | Ubiquitination | NDLLREFKKLDDKPS HHHHHHHHCCCCCCC | 47.90 | 17644757 | |
167 | Ubiquitination | DLLREFKKLDDKPSL HHHHHHHCCCCCCCC | 63.57 | 17644757 | |
171 | Acetylation | EFKKLDDKPSLVDVH HHHCCCCCCCCEEHH | 35.85 | 24489116 | |
171 | Ubiquitination | EFKKLDDKPSLVDVH HHHCCCCCCCCEEHH | 35.85 | 17644757 | |
183 | Ubiquitination | DVHLLESKVYHKLRN EHHHHHHHHHHHHHH | 37.12 | 17644757 | |
199 | Phosphorylation | AKSKASLTAARTAAN HHCHHHHHHHHHHHH | 18.77 | 25704821 | |
233 | Ubiquitination | HCEDKDYKTAFSYFF ECCCCCHHHHHHHHH | 43.44 | 17644757 | |
257 | Ubiquitination | TTHNSYEKACQVLKY CCCCHHHHHHHHHHH | 46.35 | 17644757 | |
263 | Acetylation | EKACQVLKYMLLSKI HHHHHHHHHHHHHHH | 29.74 | 24489116 | |
279 | Ubiquitination | LNLIDDVKNILNAKY HHHHHHHHHHHCCCC | 45.31 | 24961812 | |
287 | Phosphorylation | NILNAKYTKETYQSR HHHCCCCCHHHHHHC | 23.00 | 17563356 | |
300 | Acetylation | SRGIDAMKAVAEAYN HCCHHHHHHHHHHHC | 41.24 | 24489116 | |
319 | Acetylation | LDFNTALKQYEKELM HHHHHHHHHHHHHHC | 48.66 | 24489116 | |
323 | Acetylation | TALKQYEKELMGDEL HHHHHHHHHHCCCHH | 51.73 | 24489116 | |
349 | Ubiquitination | LLESNLCKIIEPFEC HHHCCCCHHCCCEEE | 50.30 | 17644757 | |
364 | Ubiquitination | VEISHISKIIGLDTQ EEHHHHHHHHCCCHH | 37.43 | 17644757 | |
376 | Ubiquitination | DTQQVEGKLSQMILD CHHHHCHHHHHHHHH | 31.31 | 23749301 | |
429 | Ubiquitination | VVDQLFEKASVLY-- HHHHHHHHHCCCC-- | 38.33 | 23749301 |
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 RPN6_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN6_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 RPN6_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 2-9, AND ACETYLATION AT SER-2. | |
Phosphorylation | |
Reference | PubMed |
"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-287, AND MASSSPECTROMETRY. |