UniProt ID | ESF2_YEAST | |
---|---|---|
UniProt AC | P53743 | |
Protein Name | Pre-rRNA-processing protein ESF2 | |
Gene Name | ESF2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 316 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Involved in the small subunit (SSU) processome assembly and function, and in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2. Stimulates DBP8 RNA helicase ATPase activity.. | |
Protein Sequence | MSEKVNSDFEDFSSDEETDQHNVLIQTKKKISSKDDIFSKKVEDIESENESDIEEEQKQEEKEDVEQPDKENGEKLDREVEEQASSTTSLDLKTEKLRQLVKSKAAKKSKHKTGVVYFSSIPPYMKPAKMRQILTRFGEVDRLFLKKEDDQKYKQRVKGGGNKKNKYEEGWAEFIRKRDAKLCAETLNGNIIGGKKGTFYHDDILNVKYLPGFKWADLTEQIARENDIRQAKLEMEISQANKLNAEFIRNVEQSKMIQNIKNSRKRAGKEGESADSHPHREFKQRRVETSRANAPSDIKQQSSGSKDLGNVLTNLL | |
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 | ------MSEKVNSDF ------CCCCCCCCC | 46.23 | 19795423 | |
7 | Phosphorylation | -MSEKVNSDFEDFSS -CCCCCCCCCCCCCC | 46.82 | 22369663 | |
13 | Phosphorylation | NSDFEDFSSDEETDQ CCCCCCCCCCCCHHH | 49.56 | 22369663 | |
14 | Phosphorylation | SDFEDFSSDEETDQH CCCCCCCCCCCHHHH | 49.38 | 22369663 | |
18 | Phosphorylation | DFSSDEETDQHNVLI CCCCCCCHHHHCCHH | 38.62 | 22890988 | |
27 | Phosphorylation | QHNVLIQTKKKISSK HHCCHHHHCCCCCCC | 37.53 | 22890988 | |
32 | Phosphorylation | IQTKKKISSKDDIFS HHHCCCCCCCHHHHH | 39.97 | 30377154 | |
33 | Phosphorylation | QTKKKISSKDDIFSK HHCCCCCCCHHHHHH | 43.51 | 27214570 | |
34 | Succinylation | TKKKISSKDDIFSKK HCCCCCCCHHHHHHH | 53.26 | 23954790 | |
34 | Acetylation | TKKKISSKDDIFSKK HCCCCCCCHHHHHHH | 53.26 | 24489116 | |
47 | Phosphorylation | KKVEDIESENESDIE HHHHHHHCCCHHHHH | 46.16 | 22369663 | |
51 | Phosphorylation | DIESENESDIEEEQK HHHCCCHHHHHHHHH | 56.31 | 22369663 | |
85 | Phosphorylation | REVEEQASSTTSLDL HHHHHHHCCCCCHHH | 28.10 | 22369663 | |
86 | Phosphorylation | EVEEQASSTTSLDLK HHHHHHCCCCCHHHH | 38.43 | 22369663 | |
87 | Phosphorylation | VEEQASSTTSLDLKT HHHHHCCCCCHHHHH | 20.22 | 22369663 | |
88 | Phosphorylation | EEQASSTTSLDLKTE HHHHCCCCCHHHHHH | 29.28 | 22369663 | |
89 | Phosphorylation | EQASSTTSLDLKTEK HHHCCCCCHHHHHHH | 21.70 | 22369663 | |
166 | Acetylation | GGGNKKNKYEEGWAE CCCCCCCCHHHHHHH | 64.02 | 24489116 | |
195 | Acetylation | NGNIIGGKKGTFYHD CCCCCCCCCCCCCCC | 42.70 | 25381059 | |
214 | Acetylation | VKYLPGFKWADLTEQ CEECCCCCHHHHHHH | 47.60 | 24489116 | |
255 | Acetylation | IRNVEQSKMIQNIKN HHHHHHHHHHHHHHH | 39.45 | 25381059 | |
269 | Acetylation | NSRKRAGKEGESADS HHHHHCCCCCCCCCC | 62.65 | 25381059 | |
296 | Phosphorylation | TSRANAPSDIKQQSS HHCCCCCHHHHHCCC | 49.94 | 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 ESF2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ESF2_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 ESF2_YEAST !! |
Kegg Drug | ||||||
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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-33; SER-47; SER-51 ANDTHR-88, 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-47 AND SER-51, AND MASSSPECTROMETRY. | |
"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-7; SER-13 AND SER-14,AND MASS SPECTROMETRY. |