| UniProt ID | INO80_YEAST | |
|---|---|---|
| UniProt AC | P53115 | |
| Protein Name | Chromatin-remodeling ATPase INO80 {ECO:0000305} | |
| Gene Name | INO80 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1489 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | ATPase component of the INO80 complex which remodels chromatin by shifting nucleosomes and is involved in DNA repair. [PubMed: 10952318] | |
| Protein Sequence | MSLAVLLNKEDKDISDFSKTTAGKSAKKNSRERVADVAPTRVLDKKQAYLSQLNSEFNRIKRRDSIEQLYQDWKFINLQEFELISEWNQQSKDWQFDNTNDSQDLHFKKLYRDMSMINKEWAEYQSFKNANLSDIINEKDADEDEEDDEDELEDGEEDMEEDEASTGRHTNGKSMRGNGIQKSRKKDAAAAAAIGKAIKDDQTHADTVVTVNGDENEDGNNGEDEDNDNDNENNNDNDNDNENENDNDSDNDDEEENGEEDEEEEEIEDLDEEDFAAFEEQDDNDDEDFNPDVEKRRKRSSSSSSSTKLSMNSLSLITSKKINKNITINSDRPKIVRELIKMCNKNKHQKIKKRRFTNCIVTDYNPIDSKLNIKITLKQYHVKRLKKLINDAKREREREEALKNNVGLDGNDLDNDEDGSESHKRRKLNNNTANGADDANKRKFNTRHGLPTYGMKMNAKEARAIQRHYDNTYTTIWKDMARKDSTKMSRLVQQIQSIRSTNFRKTSSLCAREAKKWQSKNFKQIKDFQTRARRGIREMSNFWKKNEREERDLKKKIEKEAMEQAKKEEEEKESKRQAKKLNFLLTQTELYSHFIGRKIKTNELEGNNVSSNDSESQKNIDISALAPNKNDFHAIDFDNENDEQLRLRAAENASNALAETRAKAKQFDDHANAHEEEEEEDELNFQNPTSLGEITIEQPKILACTLKEYQLKGLNWLANLYDQGINGILADEMGLGKTVQSISVLAHLAENHNIWGPFLVVTPASTLHNWVNEISKFLPQFKILPYWGNANDRKVLRKFWDRKNLRYNKNAPFHVMVTSYQMVVTDANYLQKMKWQYMILDEAQAIKSSQSSRWKNLLSFHCRNRLLLTGTPIQNSMQELWALLHFIMPSLFDSHDEFNEWFSKDIESHAEANTKLNQQQLRRLHMILKPFMLRRVKKNVQSELGDKIEIDVLCDLTQRQAKLYQVLKSQISTNYDAIENAATNDSTSNSASNSGSDQNLINAVMQFRKVCNHPDLFERADVDSPFSFTTFGKTTSMLTASVANNNSSVISNSNMNLSSMSSNNISNGKFTDLIYSSRNPIKYSLPRLIYEDLILPNYNNDVDIANKLKNVKFNIFNPSTNYELCLFLSKLTGEPSLNEFFRVSTTPLLKRVIERTNGPKNTDSLSFKTITQELLEVTRNAPSEGVMASLLNVEKHAYEREYLNCIQRGYHPNVSAPPVTIEVLGSSHVTNSINNELFDPLISQALSDIPAITQYNMHVKKGIPVEDFPKTGLFPEPLNKNFSSNISMPSMDRFITESAKLRKLDELLVKLKSEGHRVLIYFQMTKMMDLMEEYLTYRQYNHIRLDGSSKLEDRRDLVHDWQTNPEIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTIDSQAMDRAHRLGQTRQVTVYRLLVRGTIEERMRDRAKQKEQVQQVVMEGKTQEKNIKTIEVGENDSEVTREGSKSISQDGIKEAASALA | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSLAVLLNK ------CCCEECCCC | 36.02 | 24909858 | |
| 9 | Acetylation | SLAVLLNKEDKDISD CCEECCCCCCCCHHH | 68.23 | 22865919 | |
| 25 | Phosphorylation | SKTTAGKSAKKNSRE CCCCCCHHCCCCCHH | 44.39 | 28889911 | |
| 65 | Phosphorylation | NRIKRRDSIEQLYQD HHHHCHHHHHHHHHH | 26.64 | 17330950 | |
| 102 | Phosphorylation | QFDNTNDSQDLHFKK CCCCCCCHHHHHHHH | 27.88 | 20190278 | |
| 115 | Phosphorylation | KKLYRDMSMINKEWA HHHHHHHHHHCHHHH | 22.31 | 17287358 | |
| 133 | Phosphorylation | SFKNANLSDIINEKD HHHCCCHHHHHCCCC | 26.94 | 22369663 | |
| 165 | Phosphorylation | DMEEDEASTGRHTNG HHCCCHHHCCCCCCC | 29.37 | 21551504 | |
| 170 | Phosphorylation | EASTGRHTNGKSMRG HHHCCCCCCCCCCCC | 44.28 | 21551504 | |
| 300 | Phosphorylation | VEKRRKRSSSSSSST HHHHHHHCCCCCCCC | 37.29 | 21440633 | |
| 301 | Phosphorylation | EKRRKRSSSSSSSTK HHHHHHCCCCCCCCH | 37.97 | 21440633 | |
| 302 | Phosphorylation | KRRKRSSSSSSSTKL HHHHHCCCCCCCCHH | 35.17 | 23749301 | |
| 304 | Phosphorylation | RKRSSSSSSSTKLSM HHHCCCCCCCCHHHH | 30.20 | 23749301 | |
| 307 | Phosphorylation | SSSSSSSTKLSMNSL CCCCCCCCHHHHHHH | 37.64 | 28889911 | |
| 319 | Phosphorylation | NSLSLITSKKINKNI HHHHHHHCCCCCCCC | 25.59 | 21440633 | |
| 420 | Phosphorylation | LDNDEDGSESHKRRK CCCCCCCCHHHHHHH | 48.53 | 22369663 | |
| 422 | Phosphorylation | NDEDGSESHKRRKLN CCCCCCHHHHHHHCC | 35.69 | 21440633 | |
| 456 | Acetylation | GLPTYGMKMNAKEAR CCCCCCCCCCHHHHH | 25.33 | 25381059 | |
| 469 | Phosphorylation | ARAIQRHYDNTYTTI HHHHHHHHCCHHHHH | 17.05 | 19823750 | |
| 472 | Phosphorylation | IQRHYDNTYTTIWKD HHHHHCCHHHHHHHH | 21.24 | 19823750 | |
| 473 | Phosphorylation | QRHYDNTYTTIWKDM HHHHCCHHHHHHHHH | 14.24 | 19823750 | |
| 474 | Phosphorylation | RHYDNTYTTIWKDMA HHHCCHHHHHHHHHH | 15.12 | 19823750 | |
| 475 | Phosphorylation | HYDNTYTTIWKDMAR HHCCHHHHHHHHHHC | 17.90 | 19823750 | |
| 485 | Phosphorylation | KDMARKDSTKMSRLV HHHHCCCHHHHHHHH | 32.72 | 19823750 | |
| 486 | Phosphorylation | DMARKDSTKMSRLVQ HHHCCCHHHHHHHHH | 40.68 | 19823750 | |
| 489 | Phosphorylation | RKDSTKMSRLVQQIQ CCCHHHHHHHHHHHH | 24.82 | 28889911 | |
| 610 | Phosphorylation | ELEGNNVSSNDSESQ CCCCCCCCCCCCHHH | 26.08 | 28889911 | |
| 614 | Phosphorylation | NNVSSNDSESQKNID CCCCCCCCHHHCCCC | 43.32 | 19779198 | |
| 616 | Phosphorylation | VSSNDSESQKNIDIS CCCCCCHHHCCCCHH | 50.86 | 21551504 | |
| 618 | Acetylation | SNDSESQKNIDISAL CCCCHHHCCCCHHHC | 66.21 | 22865919 | |
| 929 | Acetylation | RRLHMILKPFMLRRV HHHHHHHHHHHHHHH | 25.86 | 25381059 | |
| 1145 | Phosphorylation | NEFFRVSTTPLLKRV HHHHHHCCHHHHHHH | 29.58 | 28889911 | |
| 1321 | Phosphorylation | EGHRVLIYFQMTKMM CCCEEEEEEEEHHHH | 5.43 | 19779198 | |
| 1334 | Phosphorylation | MMDLMEEYLTYRQYN HHHHHHHHHHHHHHC | 7.34 | 19779198 | |
| 1348 | Phosphorylation | NHIRLDGSSKLEDRR CCEECCCCCCCCCCH | 24.78 | 28889911 | |
| 1439 | Acetylation | MRDRAKQKEQVQQVV HHHHHHHHHHHHHHH | 49.78 | 17397211 | |
| 1466 | Phosphorylation | IEVGENDSEVTREGS EEECCCCHHCCCCCC | 45.61 | 22369663 | |
| 1469 | Phosphorylation | GENDSEVTREGSKSI CCCCHHCCCCCCCCC | 20.96 | 22369663 | |
| 1473 | Phosphorylation | SEVTREGSKSISQDG HHCCCCCCCCCCHHH | 20.62 | 22369663 | |
| 1475 | Phosphorylation | VTREGSKSISQDGIK CCCCCCCCCCHHHHH | 29.21 | 28889911 | |
| 1477 | Phosphorylation | REGSKSISQDGIKEA CCCCCCCCHHHHHHH | 29.34 | 27214570 | |
| 1486 | Phosphorylation | DGIKEAASALA---- HHHHHHHHHHC---- | 30.75 | 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 INO80_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of INO80_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 INO80_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-65; SER-115; SER-133;THR-1469 AND SER-1477, 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 SER-65 AND SER-115, 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-65, AND MASSSPECTROMETRY. | |
