| UniProt ID | TFS2_YEAST | |
|---|---|---|
| UniProt AC | P07273 | |
| Protein Name | Transcription elongation factor S-II | |
| Gene Name | DST1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 309 | |
| Subcellular Localization | Nucleus. | |
| Protein Description | Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-II allows the resumption of elongation from the new 3'-terminus.; Can promote the transfer of one strand of a double-stranded DNA molecule to a homologous single strand and thus may be involved in recombination.. | |
| Protein Sequence | MDSKEVLVHVKNLEKNKSNDAAVLEILHVLDKEFVPTEKLLRETKVGVEVNKFKKSTNVEISKLVKKMISSWKDAINKNKRSRQAQQHHQDHAPGNAEDKTTVGESVNGVQQPASSQSDAMKQDKYVSTKPRNSKNDGVDTAIYHHKLRDQVLKALYDVLAKESEHPPQSILHTAKAIESEMNKVNNCDTNEAAYKARYRIIYSNVISKNNPDLKHKIANGDITPEFLATCDAKDLAPAPLKQKIEEIAKQNLYNAQGATIERSVTDRFTCGKCKEKKVSYYQLQTRSADEPLTTFCTCEACGNRWKFS | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MDSKEVLVHV -----CCHHHHEEEE | 29.44 | 30377154 | |
| 4 | Acetylation | ----MDSKEVLVHVK ----CCHHHHEEEEC | 47.80 | 24489116 | |
| 39 | Acetylation | KEFVPTEKLLRETKV CCCCCHHHHHHHHCC | 56.13 | 24489116 | |
| 63 | Acetylation | STNVEISKLVKKMIS CCCHHHHHHHHHHHH | 64.06 | 24489116 | |
| 73 | Acetylation | KKMISSWKDAINKNK HHHHHHHHHHHHHCH | 38.95 | 24489116 | |
| 100 | Acetylation | APGNAEDKTTVGESV CCCCCCCCCCCCCCC | 37.29 | 24489116 | |
| 101 | Phosphorylation | PGNAEDKTTVGESVN CCCCCCCCCCCCCCC | 38.75 | 21126336 | |
| 115 | Phosphorylation | NGVQQPASSQSDAMK CCCCCCCCCCHHHHH | 35.28 | 25521595 | |
| 116 | Phosphorylation | GVQQPASSQSDAMKQ CCCCCCCCCHHHHHH | 35.49 | 20190278 | |
| 118 | Phosphorylation | QQPASSQSDAMKQDK CCCCCCCHHHHHHHC | 29.32 | 19823750 | |
| 125 | Acetylation | SDAMKQDKYVSTKPR HHHHHHHCCCCCCCC | 45.09 | 25381059 | |
| 154 | Acetylation | KLRDQVLKALYDVLA HHHHHHHHHHHHHHH | 37.17 | 24489116 | |
| 176 | Acetylation | QSILHTAKAIESEMN CHHHHHHHHHHHHHH | 51.56 | 24489116 | |
| 184 | Ubiquitination | AIESEMNKVNNCDTN HHHHHHHHHCCCCCH | 45.06 | 23749301 | |
| 224 | Phosphorylation | KIANGDITPEFLATC HHCCCCCCHHHHHCC | 22.85 | 22369663 | |
| 234 | Acetylation | FLATCDAKDLAPAPL HHHCCCHHHCCCCCH | 39.77 | 24489116 | |
| 242 | Acetylation | DLAPAPLKQKIEEIA HCCCCCHHHHHHHHH | 48.78 | 25381059 | |
| 244 | Acetylation | APAPLKQKIEEIAKQ CCCCHHHHHHHHHHC | 50.96 | 24489116 | |
| 250 | Acetylation | QKIEEIAKQNLYNAQ HHHHHHHHCCCCCCC | 45.43 | 24489116 | |
| 266 | Phosphorylation | ATIERSVTDRFTCGK CEEEEECCCCCCCCC | 23.78 | 27017623 | |
| 278 | Ubiquitination | CGKCKEKKVSYYQLQ CCCCCCCEEEEEEEE | 37.19 | 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 TFS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TFS2_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 TFS2_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-115; SER-116 ANDSER-118, AND MASS SPECTROMETRY. | |
