| UniProt ID | SPT3_YEAST | |
|---|---|---|
| UniProt AC | P06844 | |
| Protein Name | Protein SPT3 | |
| Gene Name | SPT3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 337 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. 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). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SPT3 is required for recruitment of TATA-binding protein (TBP) to SAGA-dependent promoters. During SAGA-mediated transcriptional inhibition, SPT3 and SPT8 prevent binding of TBP to the TATA box. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus. SPT factors 3, 7 and 8 are required for the initiation of Ty transcription from the delta promoter. SPT3 regulates Ty1 as well as the mating factor genes.. | |
| Protein Sequence | MMDKHKYRVEIQQMMFVSGEINDPPVETTSLIEDIVRGQVIEILLQSNKTAHLRGSRSILPEDVIFLIRHDKAKVNRLRTYLSWKDLRKNAKDQDASAGVASGTGNPGAGGEDDLKKAGGGEKDEKDGGNMMKVKKSQIKLPWELQFMFNEHPLENNDDNDDMDEDEREANIVTLKRLKMADDRTRNMTKEEYVHWSDCRQASFTFRKNKRFKDWSGISQLTEGKPHDDVIDILGFLTFEIVCSLTETALKIKQREQVLQTQKDKSQQSSQDNTNFEFASSTLHRKKRLFDGPENVINPLKPRHIEEAWRVLQTIDMRHRALTNFKGGRLSSKPIIM | |
| 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 |
|---|---|---|---|---|---|
| 97 | Phosphorylation | NAKDQDASAGVASGT HCCCCCCCCCCCCCC | 33.57 | 28889911 | |
| 102 | Phosphorylation | DASAGVASGTGNPGA CCCCCCCCCCCCCCC | 34.19 | 28889911 | |
| 104 | Phosphorylation | SAGVASGTGNPGAGG CCCCCCCCCCCCCCC | 31.15 | 28889911 | |
| 222 | Phosphorylation | WSGISQLTEGKPHDD CCCCHHHCCCCCCCH | 34.75 | 27017623 | |
| 261 | Phosphorylation | QREQVLQTQKDKSQQ HHHHHHHHHHCHHHH | 33.16 | 28889911 | |
| 269 | Phosphorylation | QKDKSQQSSQDNTNF HHCHHHHCCCCCCCC | 23.48 | 27017623 | |
| 270 | Phosphorylation | KDKSQQSSQDNTNFE HCHHHHCCCCCCCCH | 36.90 | 23749301 | |
| 274 | Phosphorylation | QQSSQDNTNFEFASS HHCCCCCCCCHHHHH | 49.96 | 28889911 | |
| 280 | Phosphorylation | NTNFEFASSTLHRKK CCCCHHHHHHHHHCC | 29.22 | 28889911 | |
| 301 | Acetylation | ENVINPLKPRHIEEA CCCCCCCCHHHHHHH | 41.06 | 24489116 | |
| 323 | Phosphorylation | DMRHRALTNFKGGRL HHHHHHHHCCCCCCC | 37.31 | 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 SPT3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT3_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 SPT3_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-270, AND MASSSPECTROMETRY. | |
