| UniProt ID | RHC31_YEAST | |
|---|---|---|
| UniProt AC | Q06624 | |
| Protein Name | DNA damage tolerance protein RHC31 | |
| Gene Name | AOS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 347 | |
| Subcellular Localization | ||
| Protein Description | Could be involved in a ubiquitin-related process important for DNA damage tolerance.. | |
| Protein Sequence | MDMKVEKLSEDEIALYDRQIRLWGMTAQANMRSAKVLLINLGAIGSEITKSIVLSGIGHLTILDGHMVTEEDLGSQFFIGSEDVGQWKIDATKERIQDLNPRIELNFDKQDLQEKDEEFFQQFDLVVATEMQIDEAIKINTLTRKLNIPLYVAGSNGLFAYVFIDLIEFISEDEKLQSVRPTTVGPISSNRSIIEVTTRKDEEDEKKTYERIKTKNCYRPLNEVLSTATLKEKMTQRQLKRVTSILPLTLSLLQYGLNQKGKAISFEQMKRDAAVWCENLGVPATVVKDDYIQQFIKQKGIEFAPVAAIIGGAVAQDVINILGKRLSPLNNFIVFDGITLDMPLFEF | |
| 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 |
|---|---|---|---|---|---|
| 9 | Phosphorylation | DMKVEKLSEDEIALY CCCCEECCHHHHHHH | 54.81 | 22369663 | |
| 35 | Sumoylation | QANMRSAKVLLINLG HHHHHHCEEEEEECC | 34.36 | - | |
| 35 | Sumoylation | QANMRSAKVLLINLG HHHHHHCEEEEEECC | 34.36 | 15166219 | |
| 218 | Phosphorylation | RIKTKNCYRPLNEVL HHHCCCCCHHHHHHH | 25.34 | 19823750 | |
| 226 | Phosphorylation | RPLNEVLSTATLKEK HHHHHHHCHHHHHHH | 22.60 | 19823750 | |
| 227 | Phosphorylation | PLNEVLSTATLKEKM HHHHHHCHHHHHHHC | 21.35 | 19823750 | |
| 229 | Phosphorylation | NEVLSTATLKEKMTQ HHHHCHHHHHHHCCH | 38.15 | 19823750 | |
| 235 | Phosphorylation | ATLKEKMTQRQLKRV HHHHHHCCHHHHHHH | 31.50 | 19823750 |
| 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 RHC31_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RHC31_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 RHC31_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-9, AND MASSSPECTROMETRY. | |
| Sumoylation | |
| Reference | PubMed |
| "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.Induction of protein sumoylation by cellular stresses."; Zhou W., Ryan J.J., Zhou H.; J. Biol. Chem. 279:32262-32268(2004). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND MASS SPECTROMETRY. | |
