| UniProt ID | RPN13_YEAST | |
|---|---|---|
| UniProt AC | O13563 | |
| Protein Name | 26S proteasome regulatory subunit RPN13 | |
| Gene Name | RPN13 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 156 | |
| Subcellular Localization | Cytoplasm . Nucleus . | |
| Protein Description | Component of the 19S cap proteasome complex which acts as a regulatory subunit of the 26S proteasome, involved in the ATP-dependent degradation of ubiquitinated proteins.. | |
| Protein Sequence | MSMSSTVIKFRAGVCEYNEDSRLCTPIPVQGEIEIKPNEEEELGFWDFEWRPTEKPVGRELDPISLILIPGETMWVPIKSSKSGRIFALVFSSNERYFFWLQEKNSGNLPLNELSAKDKEIYNKMIGVLNNSSESDEEESNDEKQKAQDVDVSMQD | |
| 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 | Acetylation | ------MSMSSTVIK ------CCCCCCEEE | 27.63 | 22814378 | |
| 2 (in isoform 2) | Acetylation | - | 27.63 | 22814378 | |
| 2 | Phosphorylation | ------MSMSSTVIK ------CCCCCCEEE | 27.63 | 30377154 | |
| 4 | Phosphorylation | ----MSMSSTVIKFR ----CCCCCCEEEEE | 18.62 | 30377154 | |
| 6 | Phosphorylation | --MSMSSTVIKFRAG --CCCCCCEEEEEEE | 20.95 | 30377154 | |
| 97 | Phosphorylation | VFSSNERYFFWLQEK EEECCCEEEEEEECC | 9.28 | 23749301 | |
| 106 | Phosphorylation | FWLQEKNSGNLPLNE EEEECCCCCCCCHHH | 39.88 | 23749301 | |
| 115 | Phosphorylation | NLPLNELSAKDKEIY CCCHHHCCHHHHHHH | 27.39 | 23749301 | |
| 117 | Succinylation | PLNELSAKDKEIYNK CHHHCCHHHHHHHHH | 66.99 | 23954790 | |
| 117 | Acetylation | PLNELSAKDKEIYNK CHHHCCHHHHHHHHH | 66.99 | 24489116 | |
| 132 | Phosphorylation | MIGVLNNSSESDEEE HHHHHCCCCCCCHHH | 34.12 | 25521595 | |
| 133 | Phosphorylation | IGVLNNSSESDEEES HHHHCCCCCCCHHHC | 43.15 | 22369663 | |
| 135 | Phosphorylation | VLNNSSESDEEESND HHCCCCCCCHHHCCH | 52.88 | 22369663 | |
| 140 | Phosphorylation | SESDEEESNDEKQKA CCCCHHHCCHHHHHH | 53.51 | 22369663 | |
| 144 | Ubiquitination | EEESNDEKQKAQDVD HHHCCHHHHHHHHCC | 61.02 | 23749301 | |
| 146 | Ubiquitination | ESNDEKQKAQDVDVS HCCHHHHHHHHCCCC | 60.11 | 23749301 | |
| 153 | Phosphorylation | KAQDVDVSMQD---- HHHHCCCCCCC---- | 13.28 | 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 RPN13_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPN13_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 RPN13_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-132; SER-133; SER-135AND SER-140, AND MASS SPECTROMETRY. | |
| "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 SER-132 AND SER-135, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-140, ANDMASS SPECTROMETRY. | |