| UniProt ID | EBP2_YEAST | |
|---|---|---|
| UniProt AC | P36049 | |
| Protein Name | rRNA-processing protein EBP2 | |
| Gene Name | EBP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 427 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | Required for the processing of the 27S pre-rRNA. Probably involved in the step of the processing of the 27 SA precursor into the 27 SB intermediate.. | |
| Protein Sequence | MAKGFKLKELLSHQKEIEKAEKLENDLKKKKSQELKKEEPTIVTASNLKKLEKKEKKADVKKEVAADTEEYQSQALSKKEKRKLKKELKKMQEQDATEAQKHMSGDEDESGDDREEEEEEEEEEEGRLDLEKLAKSDSESEDDSESENDSEEDEDVVAKEESEEKEEQEEEQDVPLSDVEFDSDADVVPHHKLTVNNTKAMKHALERVQLPWKKHSFQEHQSVTSETNTDEHIKDIYDDTERELAFYKQSLDAVLVARDELKRLKVPFKRPLDYFAEMVKSDEHMDKIKGKLIEEASDKKAREEARRQRQLKKFGKQVQNATLQKRQLEKRETLEKIKSLKNKRKHNEIDHSEFNVGVEEEVEGKRFDRGRPNGKRAAKNAKYGQGGMKRFKRKNDATSSADVSGFSSRKMKGKTNRPGKSRRARRF | |
| 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 |
|---|---|---|---|---|---|
| 8 | Acetylation | MAKGFKLKELLSHQK CCCCCCHHHHHHCHH | 47.08 | 25381059 | |
| 19 | Acetylation | SHQKEIEKAEKLEND HCHHHHHHHHHHHHH | 68.46 | 25381059 | |
| 22 | Acetylation | KEIEKAEKLENDLKK HHHHHHHHHHHHHHH | 66.99 | 25381059 | |
| 32 | Phosphorylation | NDLKKKKSQELKKEE HHHHHHHHHHHHHHC | 37.45 | 21440633 | |
| 36 | Acetylation | KKKSQELKKEEPTIV HHHHHHHHHHCCCEE | 58.34 | 24489116 | |
| 36 | Sumoylation | KKKSQELKKEEPTIV HHHHHHHHHHCCCEE | 58.34 | - | |
| 37 | Acetylation | KKSQELKKEEPTIVT HHHHHHHHHCCCEEE | 78.80 | 24489116 | |
| 61 | Sumoylation | KEKKADVKKEVAADT HHHHHHHHHHHHCCH | 43.70 | - | |
| 68 | Phosphorylation | KKEVAADTEEYQSQA HHHHHCCHHHHHHHH | 26.45 | 22369663 | |
| 71 | Phosphorylation | VAADTEEYQSQALSK HHCCHHHHHHHHCCH | 13.77 | 22369663 | |
| 73 | Phosphorylation | ADTEEYQSQALSKKE CCHHHHHHHHCCHHH | 19.27 | 22369663 | |
| 77 | Phosphorylation | EYQSQALSKKEKRKL HHHHHHCCHHHHHHH | 44.70 | 22369663 | |
| 104 | Phosphorylation | TEAQKHMSGDEDESG HHHHHHHCCCCCCCC | 42.69 | 17330950 | |
| 110 | Phosphorylation | MSGDEDESGDDREEE HCCCCCCCCCCHHHH | 60.90 | 17330950 | |
| 136 | Phosphorylation | DLEKLAKSDSESEDD CHHHHHCCCCCCCCC | 40.54 | 19795423 | |
| 138 | Phosphorylation | EKLAKSDSESEDDSE HHHHCCCCCCCCCCC | 50.54 | 19795423 | |
| 140 | Phosphorylation | LAKSDSESEDDSESE HHCCCCCCCCCCCCC | 50.72 | 19795423 | |
| 144 | Phosphorylation | DSESEDDSESENDSE CCCCCCCCCCCCCCH | 56.17 | 19795423 | |
| 146 | Phosphorylation | ESEDDSESENDSEED CCCCCCCCCCCCHHH | 45.73 | 19795423 | |
| 150 | Phosphorylation | DSESENDSEEDEDVV CCCCCCCCHHHHHHH | 55.24 | 19795423 | |
| 162 | Phosphorylation | DVVAKEESEEKEEQE HHHHHHHHHHHHHHH | 52.74 | 25704821 | |
| 177 | Phosphorylation | EEQDVPLSDVEFDSD HHCCCCHHHCCCCCC | 33.27 | 22369663 | |
| 183 | Phosphorylation | LSDVEFDSDADVVPH HHHCCCCCCCCCCCC | 39.76 | 22369663 | |
| 198 | Phosphorylation | HKLTVNNTKAMKHAL CCCCCCCHHHHHHHH | 18.25 | 24909858 | |
| 202 | Acetylation | VNNTKAMKHALERVQ CCCHHHHHHHHHHCC | 30.50 | 25381059 | |
| 281 | Phosphorylation | YFAEMVKSDEHMDKI HHHHHHHCHHHHHHH | 36.50 | 28889911 | |
| 297 | Phosphorylation | GKLIEEASDKKAREE HHHHHHHCHHHHHHH | 53.92 | 28152593 | |
| 322 | Phosphorylation | GKQVQNATLQKRQLE HHHHHHHHHHHHHHH | 36.95 | 30377154 | |
| 325 | Acetylation | VQNATLQKRQLEKRE HHHHHHHHHHHHHHH | 45.27 | 25381059 | |
| 382 | Acetylation | KRAAKNAKYGQGGMK HHHHHHCCCCCCCHH | 60.34 | 25381059 | |
| 389 | Acetylation | KYGQGGMKRFKRKND CCCCCCHHHHHCCCC | 58.94 | 25381059 | |
| 398 | Phosphorylation | FKRKNDATSSADVSG HHCCCCCCCCCCCCC | 26.52 | 28889911 | |
| 399 | Phosphorylation | KRKNDATSSADVSGF HCCCCCCCCCCCCCC | 25.83 | 23749301 | |
| 400 | Phosphorylation | RKNDATSSADVSGFS CCCCCCCCCCCCCCC | 24.92 | 21551504 | |
| 404 | Phosphorylation | ATSSADVSGFSSRKM CCCCCCCCCCCCCCC | 34.37 | 21551504 | |
| 407 | Phosphorylation | SADVSGFSSRKMKGK CCCCCCCCCCCCCCC | 32.53 | 28889911 | |
| 408 | Phosphorylation | ADVSGFSSRKMKGKT CCCCCCCCCCCCCCC | 33.39 | 28889911 |
| 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 EBP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EBP2_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 EBP2_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-104 AND SER-110, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-183, 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-104; SER-110; SER-177AND SER-183, AND MASS SPECTROMETRY. | |
