| UniProt ID | SPT8_YEAST | |
|---|---|---|
| UniProt AC | P38915 | |
| Protein Name | Transcription factor SPT8 | |
| Gene Name | SPT8 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 602 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Required, directly or indirectly, for TATA-binding protein function at particular promoters. May promote a functional interaction between SPT3 and TATA-binding protein. Functions as a component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).. | |
| Protein Sequence | MDEVDDILINNQVVDDEEDDEEMLSGLENDSKQDLEGNDDGGEDEEDDDDDDEDDDDDEDEREDDDEQEDDDGEDDAARMDKTATPTNEHQHDEQKAAAAGAGGAGDSGDAVTKIGSEDVKLSDVDGGVGSREASSSTHEASANGEVYEYYKHMLNAAQIADSYNIYPTAAIPIQTHVNALAVSRGLKYLFLGGSDGYIRKYDLLNTLEGKLSLTILQKHSLAESIQNAGILQSYWENEIPQKKSEMKLSANKTDYEPKVSPVHSLEVQSECLFILSGLQNGGITMQGVRYMEGSIAHYFKGRNGHTQIVNILRLNGQEDRFLSGSWDKRLLEWDLQTGDIVNEFKKSRSELSSLEMRPLYSSVDVSGNVNSGKENENADDDMDSLFGDEDEDEKQDAGNEPVETGDGSNGEENKEQISEESLNIVYDESVFMTSGLNGSVHIWDRRMTQSPALSLERGAGVPPWCLSACWGVDGDHVYAGRRNACVEQFDLKMPSKPIHNLKLPSISGPVSCVKAMPNNKHLLCASRDNIRLYNVEIAVDASNSTTKSSKVPFLIVPGHHGGIISNLYLDPTSRFIISTSGNRGWQGNSTDTTLIYDIDLE | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 83 | Phosphorylation | DAARMDKTATPTNEH HHHHHCCCCCCCCCC | 31.34 | 19795423 | |
| 85 | Phosphorylation | ARMDKTATPTNEHQH HHHCCCCCCCCCCCH | 35.56 | 25521595 | |
| 87 | Phosphorylation | MDKTATPTNEHQHDE HCCCCCCCCCCCHHH | 49.21 | 21440633 | |
| 108 | Phosphorylation | GAGGAGDSGDAVTKI CCCCCCCCCCCCCCC | 37.34 | 22369663 | |
| 113 | Phosphorylation | GDSGDAVTKIGSEDV CCCCCCCCCCCCCCC | 20.75 | 24961812 | |
| 114 | Acetylation | DSGDAVTKIGSEDVK CCCCCCCCCCCCCCC | 38.17 | 22865919 | |
| 117 | Phosphorylation | DAVTKIGSEDVKLSD CCCCCCCCCCCCHHH | 33.81 | 22369663 | |
| 121 | Acetylation | KIGSEDVKLSDVDGG CCCCCCCCHHHCCCC | 55.37 | 24489116 | |
| 121 | Ubiquitination | KIGSEDVKLSDVDGG CCCCCCCCHHHCCCC | 55.37 | 23749301 | |
| 123 | Phosphorylation | GSEDVKLSDVDGGVG CCCCCCHHHCCCCCC | 29.85 | 22369663 | |
| 131 | Phosphorylation | DVDGGVGSREASSST HCCCCCCCCCCCCCC | 25.25 | 22369663 | |
| 135 | Phosphorylation | GVGSREASSSTHEAS CCCCCCCCCCCEEHH | 21.77 | 24961812 | |
| 136 | Phosphorylation | VGSREASSSTHEASA CCCCCCCCCCEEHHH | 46.43 | 24961812 | |
| 137 | Phosphorylation | GSREASSSTHEASAN CCCCCCCCCEEHHHC | 31.15 | 24961812 | |
| 138 | Phosphorylation | SREASSSTHEASANG CCCCCCCCEEHHHCC | 26.19 | 24961812 | |
| 195 | Phosphorylation | KYLFLGGSDGYIRKY CEEEECCCCCEEEHH | 26.51 | 28889911 | |
| 261 | Phosphorylation | TDYEPKVSPVHSLEV CCCCCCCCCCCCCHH | 27.60 | 28889911 | |
| 277 | Phosphorylation | SECLFILSGLQNGGI HHHEEHHHHHHHCCE | 32.42 | 28889911 | |
| 285 | Phosphorylation | GLQNGGITMQGVRYM HHHHCCEEECCEEEC | 13.50 | 28889911 | |
| 385 | Phosphorylation | NADDDMDSLFGDEDE CCCCCHHHHHCCCCH | 20.96 | 25521595 | |
| 405 | Phosphorylation | AGNEPVETGDGSNGE CCCCCCCCCCCCCCC | 40.58 | 21551504 | |
| 409 | Phosphorylation | PVETGDGSNGEENKE CCCCCCCCCCCCCHH | 46.53 | 29734811 | |
| 449 | Phosphorylation | HIWDRRMTQSPALSL EEECCCCCCCCCCHH | 24.88 | 22369663 | |
| 451 | Phosphorylation | WDRRMTQSPALSLER ECCCCCCCCCCHHHC | 11.72 | 22369663 | |
| 534 | Phosphorylation | SRDNIRLYNVEIAVD ECCCEEEEEEEEEEE | 13.81 | 30377154 | |
| 543 | Phosphorylation | VEIAVDASNSTTKSS EEEEEECCCCCCCCC | 27.18 | 30377154 |
| 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 SPT8_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT8_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 SPT8_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-108; SER-123; SER-131AND SER-451, 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-123, 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 THR-85, AND MASSSPECTROMETRY. | |
