| UniProt ID | IES2_YEAST | |
|---|---|---|
| UniProt AC | P40154 | |
| Protein Name | Ino eighty subunit 2 | |
| Gene Name | IES2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 320 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair.. | |
| Protein Sequence | MDSEASDIEAELSDSVSAGGEEYIDDDDYTEDIDDQIVTAKSSRRTARRSVPKGVRTSKRIRDKELSVEVDEDYDEEEDVLSPSKKRHLHTRSMDKRQVAATASEKSDIGDSKGNDGEIEDGILEEEESLEKELNRGGGKEVEKSEESYYAQNDVGQKGEEEQDGESGGYEDNEPSISKESDELVSVVNGNGNEEDDEVEATKENTTDSTRSTTTRSKMLLDLLEDGGSKKKLTDEEIQLRRAENARKRKNLSEKRLEEEKQDTINKLLKKRAGKSRSHLPNDDEKNDGSSSFVKPRRPYNSEGMTRILRRYEEDLFCTF | |
| 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 |
|---|---|---|---|---|---|
| 67 | Phosphorylation | RIRDKELSVEVDEDY CCCCCCCCEEECCCC | 19.81 | 28889911 | |
| 82 | Phosphorylation | DEEEDVLSPSKKRHL CCCCCCCCHHHHCCC | 27.29 | 28132839 | |
| 84 | Phosphorylation | EEDVLSPSKKRHLHT CCCCCCHHHHCCCCC | 47.65 | 28132839 | |
| 102 | Phosphorylation | DKRQVAATASEKSDI CHHHHHHHHHCCCCC | 22.45 | 24961812 | |
| 104 | Phosphorylation | RQVAATASEKSDIGD HHHHHHHHCCCCCCC | 41.00 | 28889911 | |
| 107 | Phosphorylation | AATASEKSDIGDSKG HHHHHCCCCCCCCCC | 30.34 | 29136822 | |
| 112 | Phosphorylation | EKSDIGDSKGNDGEI CCCCCCCCCCCCCCC | 36.93 | 27214570 | |
| 129 | Phosphorylation | GILEEEESLEKELNR CCCCCHHHHHHHHHC | 45.14 | 22369663 | |
| 140 | Acetylation | ELNRGGGKEVEKSEE HHHCCCCCCCHHHHH | 62.96 | 25381059 | |
| 145 | Phosphorylation | GGKEVEKSEESYYAQ CCCCCHHHHHHHCCC | 32.84 | 28889911 | |
| 149 | Phosphorylation | VEKSEESYYAQNDVG CHHHHHHHCCCCCCC | 13.19 | 21126336 | |
| 167 | Phosphorylation | EEEQDGESGGYEDNE CCCCCCCCCCCCCCC | 42.94 | 22369663 | |
| 170 | Phosphorylation | QDGESGGYEDNEPSI CCCCCCCCCCCCCCC | 24.51 | 21440633 | |
| 176 | Phosphorylation | GYEDNEPSISKESDE CCCCCCCCCCCCCCC | 33.06 | 24909858 | |
| 178 | Phosphorylation | EDNEPSISKESDELV CCCCCCCCCCCCCCE | 34.41 | 27717283 | |
| 186 | Phosphorylation | KESDELVSVVNGNGN CCCCCCEEEECCCCC | 32.73 | 24961812 | |
| 202 | Phosphorylation | EDDEVEATKENTTDS CCCCCEECHHCCCCC | 25.94 | 19779198 | |
| 206 | Phosphorylation | VEATKENTTDSTRST CEECHHCCCCCCCCC | 32.83 | 19779198 | |
| 207 | Phosphorylation | EATKENTTDSTRSTT EECHHCCCCCCCCCH | 39.26 | 27017623 | |
| 209 | Phosphorylation | TKENTTDSTRSTTTR CHHCCCCCCCCCHHH | 24.51 | 19779198 | |
| 210 | Phosphorylation | KENTTDSTRSTTTRS HHCCCCCCCCCHHHH | 31.30 | 19779198 | |
| 212 | Phosphorylation | NTTDSTRSTTTRSKM CCCCCCCCCHHHHHH | 30.14 | 27017623 | |
| 213 | Phosphorylation | TTDSTRSTTTRSKML CCCCCCCCHHHHHHH | 28.97 | 27717283 | |
| 214 | Phosphorylation | TDSTRSTTTRSKMLL CCCCCCCHHHHHHHH | 22.81 | 27717283 | |
| 215 | Phosphorylation | DSTRSTTTRSKMLLD CCCCCCHHHHHHHHH | 32.79 | 27717283 | |
| 217 | Phosphorylation | TRSTTTRSKMLLDLL CCCCHHHHHHHHHHH | 21.96 | 27017623 | |
| 218 | Acetylation | RSTTTRSKMLLDLLE CCCHHHHHHHHHHHH | 30.21 | 24489116 | |
| 230 | Acetylation | LLEDGGSKKKLTDEE HHHHCCCCCCCCHHH | 58.14 | 25381059 | |
| 255 | Acetylation | KRKNLSEKRLEEEKQ HHCCHHHHHHHHHHH | 59.93 | 22865919 | |
| 264 | Phosphorylation | LEEEKQDTINKLLKK HHHHHHHHHHHHHHH | 24.77 | 28889911 | |
| 278 | Phosphorylation | KRAGKSRSHLPNDDE HHHCCCCCCCCCCCC | 36.14 | 17287358 |
| 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 IES2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IES2_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 IES2_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-67 AND SER-167, AND MASSSPECTROMETRY. | |
| "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-129, AND MASSSPECTROMETRY. | |
| "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-278, AND MASSSPECTROMETRY. | |
