| UniProt ID | TOP1_YEAST | |
|---|---|---|
| UniProt AC | P04786 | |
| Protein Name | DNA topoisomerase 1 | |
| Gene Name | TOP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 769 | |
| Subcellular Localization | Nucleus, nucleolus. Nucleus, nucleoplasm. Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli (By similarity).. | |
| Protein Description | Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity).. | |
| Protein Sequence | MTIADASKVNHELSSDDDDDVPLSQTLKKRKVASMNSASLQDEAEPYDSDEAISKISKKKTKKIKTEPVQSSSLPSPPAKKSATSKPKKIKKEDGDVKVKTTKKEEQENEKKKREEEEEEDKKAKEEEEEYKWWEKENEDDTIKWVTLKHNGVIFPPPYQPLPSHIKLYYDGKPVDLPPQAEEVAGFFAALLESDHAKNPVFQKNFFNDFLQVLKESGGPLNGIEIKEFSRCDFTKMFDYFQLQKEQKKQLTSQEKKQIRLEREKFEEDYKFCELDGRREQVGNFKVEPPDLFRGRGAHPKTGKLKRRVNPEDIVLNLSKDAPVPPAPEGHKWGEIRHDNTVQWLAMWRENIFNSFKYVRLAANSSLKGQSDYKKFEKARQLKSYIDAIRRDYTRNLKSKVMLERQKAVAIYLIDVFALRAGGEKSEDEADTVGCCSLRYEHVTLKPPNTVIFDFLGKDSIRFYQEVEVDKQVFKNLTIFKRPPKQPGHQLFDRLDPSILNKYLQNYMPGLTAKVFRTYNASKTMQDQLDLIPNKGSVAEKILKYNAANRTVAILCNHQRTVTKGHAQTVEKANNRIQELEWQKIRCKRAILQLDKDLLKKEPKYFEEIDDLTKEDEATIHKRIIDREIEKYQRKFVRENDKRKFEKEELLPESQLKEWLEKVDEKKQEFEKELKTGEVELKSSWNSVEKIKAQVEKLEQRIQTSSIQLKDKEENSQVSLGTSKINYIDPRLSVVFCKKYDVPIEKIFTKTLREKFKWAIESVDENWRF | |
| 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 | ------MTIADASKV ------CCCCCHHHC | 25.52 | 28889911 | |
| 7 | Phosphorylation | -MTIADASKVNHELS -CCCCCHHHCCCCCC | 37.37 | 28889911 | |
| 14 | Phosphorylation | SKVNHELSSDDDDDV HHCCCCCCCCCCCCC | 28.83 | 22369663 | |
| 15 | Phosphorylation | KVNHELSSDDDDDVP HCCCCCCCCCCCCCC | 58.65 | 22369663 | |
| 24 | Phosphorylation | DDDDVPLSQTLKKRK CCCCCCHHHHHHHHC | 18.30 | 22369663 | |
| 26 | Phosphorylation | DDVPLSQTLKKRKVA CCCCHHHHHHHHCCC | 36.85 | 22890988 | |
| 34 | Phosphorylation | LKKRKVASMNSASLQ HHHHCCCCCCCHHCC | 22.83 | 22890988 | |
| 37 | Phosphorylation | RKVASMNSASLQDEA HCCCCCCCHHCCCCC | 15.59 | 22890988 | |
| 39 | Phosphorylation | VASMNSASLQDEAEP CCCCCCHHCCCCCCC | 26.78 | 22890988 | |
| 47 | Phosphorylation | LQDEAEPYDSDEAIS CCCCCCCCCCHHHHH | 21.42 | 25521595 | |
| 49 | Phosphorylation | DEAEPYDSDEAISKI CCCCCCCCHHHHHHH | 31.35 | 22369663 | |
| 54 | Phosphorylation | YDSDEAISKISKKKT CCCHHHHHHHCCCCC | 30.86 | 22369663 | |
| 65 | Sumoylation | KKKTKKIKTEPVQSS CCCCCCCCCCCCCCC | 56.57 | - | |
| 66 | Phosphorylation | KKTKKIKTEPVQSSS CCCCCCCCCCCCCCC | 49.33 | 22369663 | |
| 71 | Phosphorylation | IKTEPVQSSSLPSPP CCCCCCCCCCCCCCC | 23.33 | 22890988 | |
| 72 | Phosphorylation | KTEPVQSSSLPSPPA CCCCCCCCCCCCCCC | 20.85 | 22890988 | |
| 73 | Phosphorylation | TEPVQSSSLPSPPAK CCCCCCCCCCCCCCC | 49.93 | 22890988 | |
| 76 | Phosphorylation | VQSSSLPSPPAKKSA CCCCCCCCCCCCCCC | 49.13 | 22369663 | |
| 91 | Sumoylation | TSKPKKIKKEDGDVK CCCCCCCCCCCCCCC | 60.02 | - | |
| 92 | Sumoylation | SKPKKIKKEDGDVKV CCCCCCCCCCCCCCC | 65.59 | - | |
| 142 | Phosphorylation | EKENEDDTIKWVTLK HHHCCCCCEEEEEEE | 36.46 | 21440633 | |
| 332 | Acetylation | PPAPEGHKWGEIRHD CCCCCCCCCCCCCCC | 68.68 | 24489116 | |
| 355 | Phosphorylation | WRENIFNSFKYVRLA HHHHCHHHHHHHHHH | 16.62 | 30377154 | |
| 426 | Phosphorylation | LRAGGEKSEDEADTV HHCCCCCCCCCCCCC | 46.08 | 23749301 | |
| 596 | Acetylation | RAILQLDKDLLKKEP HHHHHHCHHHHHCCC | 59.89 | 24489116 | |
| 705 | Phosphorylation | LEQRIQTSSIQLKDK HHHHHHHCCEECCCH | 14.74 | 26447709 | |
| 706 | Phosphorylation | EQRIQTSSIQLKDKE HHHHHHCCEECCCHH | 20.10 | 30377154 | |
| 746 | Acetylation | KYDVPIEKIFTKTLR CCCCCHHHHHHHHHH | 43.79 | 24489116 |
| 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 TOP1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TOP1_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 TOP1_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-14; SER-15; SER-24;SER-49; SER-54 AND SER-76, 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-14; SER-15 AND SER-49,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-14; SER-15 AND SER-76,AND MASS SPECTROMETRY. | |
