| UniProt ID | ESF1_YEAST | |
|---|---|---|
| UniProt AC | Q06344 | |
| Protein Name | Pre-rRNA-processing protein ESF1 | |
| Gene Name | ESF1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 628 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | Involved in the 18S rRNA synthesis. Required for the early cleavages at sites A0, A1 and A2.. | |
| Protein Sequence | MAGENPKKEGVDARFAGIYSDPKFKNTKTKDHKIKLDSRFSKKDLEVQHKSKVDKYGRKIKNAQNNRELEDFDKYFEKEAENDEDSEVNAKTVVDRARGEVPDDYVSSSDEFTSSDSESSGESEVESEEENEVEIENAKPESGDISKNLAVVNLDWDHVKSEDLMITFSSFVPKGGKIERVAIYPSEFGKERMQREEVEGPPKELFQKKNKNKTSKKKKTDDSDSDMDIGIKDLYEEGDADKDVDSRALRQYQLDRLRYYYAIVYCSDTTTSKAIYDNCDGTEYESTANMFDLRYVPDGMTFDDDVRDECSILPKNYRPHQFSTDALQHSSVKLTWDETPADRVEVAKRAFTQKEIDDMDFKAYLASDSDESDGQVDEEAKNKLKSLVGDFGFNSKKETPNDEDEEVDMEITFTPALEGGNEKSSEDKEETTIEKIRRKEKERRKARKQKVKELKQQSEKDKKSKLKSVNKKHTNDEEEIEKNAKSKAELELLMDDDDDTETQGTINNKAHFNMNEILRSEKEKHKKGRYQKKERIVEDTFTPDLEDPRFKEVFEDHDFAIDPTQPEFKGTQAMSKILKERSKRVKNKKRKLGGSENNMTNNADDNEDIGNLVNKLKKKSKSSKKVKV | |
| 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 | MAGENPKKEGVDARF CCCCCCCCCCCCCHH | 62.04 | 25381059 | |
| 23 | Acetylation | AGIYSDPKFKNTKTK HCCCCCCCCCCCCCC | 74.16 | 24489116 | |
| 43 | Acetylation | LDSRFSKKDLEVQHK CCCCCCHHHHHHHHH | 67.36 | 25381059 | |
| 50 | Acetylation | KDLEVQHKSKVDKYG HHHHHHHHHHHHHHH | 34.58 | 25381059 | |
| 55 | Acetylation | QHKSKVDKYGRKIKN HHHHHHHHHHHHHHC | 53.22 | 24489116 | |
| 86 | Phosphorylation | EAENDEDSEVNAKTV HHCCCCCCCCHHHHH | 41.20 | 22369663 | |
| 91 | Acetylation | EDSEVNAKTVVDRAR CCCCCHHHHHHHHHC | 36.33 | 24489116 | |
| 220 | Phosphorylation | KTSKKKKTDDSDSDM CCCCCCCCCCCCCCC | 54.65 | 22369663 | |
| 223 | Phosphorylation | KKKKTDDSDSDMDIG CCCCCCCCCCCCCCC | 41.65 | 22369663 | |
| 225 | Phosphorylation | KKTDDSDSDMDIGIK CCCCCCCCCCCCCHH | 38.49 | 22369663 | |
| 235 | Phosphorylation | DIGIKDLYEEGDADK CCCHHHHHHCCCCCC | 23.28 | 28889911 | |
| 276 | Phosphorylation | TTTSKAIYDNCDGTE CCCCCHHHCCCCCCC | 13.13 | 27017623 | |
| 282 | Phosphorylation | IYDNCDGTEYESTAN HHCCCCCCCEECCCC | 23.34 | 27017623 | |
| 284 | Phosphorylation | DNCDGTEYESTANMF CCCCCCCEECCCCCC | 18.28 | 27017623 | |
| 286 | Phosphorylation | CDGTEYESTANMFDL CCCCCEECCCCCCCE | 31.73 | 27017623 | |
| 287 | Phosphorylation | DGTEYESTANMFDLR CCCCEECCCCCCCEE | 15.31 | 27017623 | |
| 323 | Phosphorylation | NYRPHQFSTDALQHS CCCCCCCCCCCCCCC | 20.86 | 30377154 | |
| 324 | Phosphorylation | YRPHQFSTDALQHSS CCCCCCCCCCCCCCC | 26.95 | 28889911 | |
| 330 | Phosphorylation | STDALQHSSVKLTWD CCCCCCCCCCEEECC | 24.70 | 20377248 | |
| 331 | Phosphorylation | TDALQHSSVKLTWDE CCCCCCCCCEEECCC | 22.58 | 24961812 | |
| 352 | Phosphorylation | EVAKRAFTQKEIDDM HHHHHHHCHHHCCCC | 37.43 | 28889911 | |
| 354 | Acetylation | AKRAFTQKEIDDMDF HHHHHCHHHCCCCCH | 54.29 | 25381059 | |
| 364 | Phosphorylation | DDMDFKAYLASDSDE CCCCHHHHHCCCCCC | 11.91 | 22890988 | |
| 367 | Phosphorylation | DFKAYLASDSDESDG CHHHHHCCCCCCCCC | 34.74 | 22369663 | |
| 369 | Phosphorylation | KAYLASDSDESDGQV HHHHCCCCCCCCCCC | 40.56 | 22369663 | |
| 372 | Phosphorylation | LASDSDESDGQVDEE HCCCCCCCCCCCCHH | 52.62 | 22369663 | |
| 386 | Phosphorylation | EAKNKLKSLVGDFGF HHHHHHHHHHHHCCC | 38.43 | 21551504 | |
| 396 | Acetylation | GDFGFNSKKETPNDE HHCCCCCCCCCCCCC | 56.59 | 25381059 | |
| 399 | Phosphorylation | GFNSKKETPNDEDEE CCCCCCCCCCCCCCC | 35.95 | 27017623 | |
| 412 | Phosphorylation | EEVDMEITFTPALEG CCCCEEEEECCCCCC | 14.24 | 27017623 | |
| 414 | Phosphorylation | VDMEITFTPALEGGN CCEEEEECCCCCCCC | 10.05 | 27017623 | |
| 424 | Phosphorylation | LEGGNEKSSEDKEET CCCCCCCCCCCHHHH | 32.55 | 27214570 | |
| 425 | Phosphorylation | EGGNEKSSEDKEETT CCCCCCCCCCHHHHH | 61.96 | 19795423 | |
| 432 | Phosphorylation | SEDKEETTIEKIRRK CCCHHHHHHHHHHHH | 30.34 | 23749301 | |
| 435 | Acetylation | KEETTIEKIRRKEKE HHHHHHHHHHHHHHH | 37.35 | 25381059 | |
| 455 | Acetylation | KQKVKELKQQSEKDK HHHHHHHHHHCHHHH | 47.59 | 25381059 | |
| 472 | Acetylation | KLKSVNKKHTNDEEE HHHHHCHHCCCCHHH | 50.92 | 25381059 | |
| 482 | Acetylation | NDEEEIEKNAKSKAE CCHHHHHHHHCCHHH | 68.79 | 22865919 | |
| 500 | Phosphorylation | LMDDDDDTETQGTIN CCCCCCCCCCCCCCC | 48.18 | 21440633 | |
| 502 | Phosphorylation | DDDDDTETQGTINNK CCCCCCCCCCCCCCH | 34.10 | 28889911 | |
| 530 | Phosphorylation | EKHKKGRYQKKERIV HHHHCCCCCHHHHHH | 33.09 | 25533186 | |
| 540 | Phosphorylation | KERIVEDTFTPDLED HHHHHCCCCCCCCCC | 18.86 | 30377154 | |
| 542 | Phosphorylation | RIVEDTFTPDLEDPR HHHCCCCCCCCCCHH | 20.27 | 17330950 | |
| 576 | Acetylation | KGTQAMSKILKERSK CHHHHHHHHHHHHHH | 38.69 | 25381059 | |
| 591 | Acetylation | RVKNKKRKLGGSENN HHHHHCCCCCCCCCC | 61.43 | 24489116 | |
| 595 | Phosphorylation | KKRKLGGSENNMTNN HCCCCCCCCCCCCCC | 35.04 | 23749301 | |
| 600 | Phosphorylation | GGSENNMTNNADDNE CCCCCCCCCCCCCCH | 27.69 | 19795423 | |
| 615 | Acetylation | DIGNLVNKLKKKSKS HHHHHHHHHHHHCCC | 54.96 | 25381059 |
| 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 ESF1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ESF1_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 ESF1_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-86; SER-223; SER-225;SER-369; SER-372 AND THR-542, AND MASS 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 THR-220; SER-225 ANDSER-330, AND MASS 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-86; SER-223; SER-225;SER-367; SER-369; SER-372 AND THR-542, AND MASS SPECTROMETRY. | |
