| UniProt ID | SPT7_YEAST | |
|---|---|---|
| UniProt AC | P35177 | |
| Protein Name | Transcriptional activator SPT7 | |
| Gene Name | SPT7 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1332 | |
| 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. 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. SPT7 is transcriptional activator of TY elements and other genes.. | |
| Protein Sequence | MTERIPIKNYQRTNAKALLKLTEKLFNKNFFDLYLTSQQLVVLEYLLSISSEEDKLKAWDYFLKGNIALNVEKSFPLTQEEEHHGAVSPAVDTRSDDVSSQTIKDNNNTNTNTSISNENHVENEIEDKGDNAIANEDNFVNNDESDNVEEDLFKLDLEDLKQQISGTRFIGNLSLKIRYVLWQCAIDYIYCDRNEFGDENDTEYTLLDVEEKEEEEIGKNEKPQNKEGISKFAEDEDYDDEDENYDEDSTDVKNVDDPPKNLDSISSSNIEIDDERRLVLNISISKETLSKLKTNNVEEIMGNWNKIYHSFEYDKETMIKRLKLEESDKMIEKGKKKRSRSDLEAATDEQDRENTNDEPDTNQKLPTPEGSTFSDTGNKRPKQSNLDLTVNLGIENLSLKHLLSSIQQKKSQLGISDYELKHLIMDVRKNRSKWTSDERIGQEELYEACEKVVLELRNYTEHSTPFLNKVSKREAPNYHQIIKKSMDLNTVLKKLKSFQYDSKQEFVDDIMLIWKNCLTYNSDPSHFLRGHAIAMQKKSLQLIRMIPNITIRNRADLEKEIEDMEKDKDYELDEEEEVAGSGRKGLNMGAHMLAKENGKVSEKDSSKTVKDEAPTNDDKLTSVIPEGEKEKDKTASSTVTVHENVNKNEIKENGKNEEQDMVEESSKTEDSSKDADAAKKDTEDGLQDKTAENKEAGENNEEEEDDDDEDEDEDMVDSQSYLLEKDDDRDDLEISVWKTVTAKVRAEICLKRTEYFKNGKLNSDSEAFLKNPQRMKRFDQLFLEYKEQKALESYRQKIEQNSIMKNGFGTVLKQEDDDQLQFHNDHSLNGNEAFEKQPNDIELDDTRFLQEYDISNAIPDIVYEGVNTKTLDKMEDASVDRMLQNGINKQSRFLANKDLGLTPKMNQNITLIQQIRHICHKISLIRMLQSPLSAQNSRSNPNAFLNNHIYNYTIIDDSLDIDPVSQLPTHDYKNNRELIWKFMHKNISKVAMANGFETAHPSAINMLTEIAGDYLSNLIKTLKLHHETNSLNRGTNVEMLQTTLLENGINRPDDLFSYVESEFGKKTKKLQDIKQKLESFLRALLRPTLQELSERNFEDESQSFFTGDFASELTGEDFFGFRELGLEKEFGVLSSSVPLQLLTTQFQTVDGETKVQAKKIQPEESDSIVYKKITKGMLDAGSFWNTLLPLLQKDYERSKAYIAKQSKSSANDKTSMTSTEDNSFALLEEDQFVSKKTATKARLPPTGKISTTYKKKPIASAFILPEEDLENDVKADPTTTVNAKVGAENDGDSSLFLRTPQPLDPLDMDDAFDDTNMGSNSSFSLSLPRLNQ | |
| 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 |
|---|---|---|---|---|---|
| 45 | Phosphorylation | QQLVVLEYLLSISSE HHHHHHHHHHHCCCH | 14.58 | 27017623 | |
| 74 | Phosphorylation | IALNVEKSFPLTQEE EEEEEEECCCCCCCH | 20.70 | 29136822 | |
| 78 | Phosphorylation | VEKSFPLTQEEEHHG EEECCCCCCCHHCCC | 33.89 | 20190278 | |
| 88 | Phosphorylation | EEHHGAVSPAVDTRS HHCCCCCCCCCCCCC | 13.45 | 17330950 | |
| 93 | Phosphorylation | AVSPAVDTRSDDVSS CCCCCCCCCCCCCCC | 26.02 | 20377248 | |
| 95 | Phosphorylation | SPAVDTRSDDVSSQT CCCCCCCCCCCCCCE | 40.01 | 20377248 | |
| 99 | Phosphorylation | DTRSDDVSSQTIKDN CCCCCCCCCCEEECC | 24.59 | 22890988 | |
| 100 | Phosphorylation | TRSDDVSSQTIKDNN CCCCCCCCCEEECCC | 31.06 | 22890988 | |
| 102 | Phosphorylation | SDDVSSQTIKDNNNT CCCCCCCEEECCCCC | 31.76 | 22890988 | |
| 114 | Phosphorylation | NNTNTNTSISNENHV CCCCCCCCCCCCCHH | 26.53 | 28889911 | |
| 145 | Phosphorylation | NFVNNDESDNVEEDL CCCCCCCCCCHHHHH | 37.03 | 28889911 | |
| 174 | Phosphorylation | TRFIGNLSLKIRYVL CEEECHHHHHHHHHH | 31.45 | 15665377 | |
| 249 | Phosphorylation | DENYDEDSTDVKNVD CCCCCCCCCCCCCCC | 25.18 | 28889911 | |
| 250 | Phosphorylation | ENYDEDSTDVKNVDD CCCCCCCCCCCCCCC | 58.07 | 24961812 | |
| 266 | Phosphorylation | PKNLDSISSSNIEID CCCCHHCCCCCEEEC | 31.50 | 30377154 | |
| 310 | Phosphorylation | NWNKIYHSFEYDKET CHHHHHHHHCCCHHH | 11.64 | 30377154 | |
| 339 | Phosphorylation | EKGKKKRSRSDLEAA HHHCCCCCHHHHHHH | 45.04 | 19823750 | |
| 341 | Phosphorylation | GKKKRSRSDLEAATD HCCCCCHHHHHHHCC | 48.03 | 19823750 | |
| 347 | Phosphorylation | RSDLEAATDEQDREN HHHHHHHCCHHHHHC | 47.30 | 21551504 | |
| 355 | Phosphorylation | DEQDRENTNDEPDTN CHHHHHCCCCCCCCC | 39.02 | 28889911 | |
| 367 | Phosphorylation | DTNQKLPTPEGSTFS CCCCCCCCCCCCCCC | 44.39 | 28889911 | |
| 371 | Phosphorylation | KLPTPEGSTFSDTGN CCCCCCCCCCCCCCC | 25.31 | 21551504 | |
| 379 | Acetylation | TFSDTGNKRPKQSNL CCCCCCCCCCCCCCC | 72.00 | 24489116 | |
| 384 | Phosphorylation | GNKRPKQSNLDLTVN CCCCCCCCCCCEEEE | 45.55 | 19823750 | |
| 389 | Phosphorylation | KQSNLDLTVNLGIEN CCCCCCEEEEEECHH | 13.65 | 19823750 | |
| 398 | Phosphorylation | NLGIENLSLKHLLSS EEECHHHCHHHHHHH | 47.13 | 15665377 | |
| 400 | Acetylation | GIENLSLKHLLSSIQ ECHHHCHHHHHHHHH | 28.91 | 19731963 | |
| 404 | Phosphorylation | LSLKHLLSSIQQKKS HCHHHHHHHHHHHHH | 31.58 | 30377154 | |
| 405 | Phosphorylation | SLKHLLSSIQQKKSQ CHHHHHHHHHHHHHH | 25.12 | 30377154 | |
| 410 | Acetylation | LSSIQQKKSQLGISD HHHHHHHHHHCCCCH | 38.81 | 19731963 | |
| 411 | Phosphorylation | SSIQQKKSQLGISDY HHHHHHHHHCCCCHH | 37.36 | 30377154 | |
| 469 | Acetylation | HSTPFLNKVSKREAP CCCHHHHHCCCCCCC | 50.46 | 24489116 | |
| 584 | Acetylation | EVAGSGRKGLNMGAH HHCCCCCCCCHHHHH | 71.87 | 24489116 | |
| 595 | Acetylation | MGAHMLAKENGKVSE HHHHHHHHHCCCCCC | 47.99 | 24489116 | |
| 599 | Acetylation | MLAKENGKVSEKDSS HHHHHCCCCCCCCCC | 54.92 | 24489116 | |
| 603 | Acetylation | ENGKVSEKDSSKTVK HCCCCCCCCCCCCCC | 56.24 | 24489116 | |
| 607 | Acetylation | VSEKDSSKTVKDEAP CCCCCCCCCCCCCCC | 62.38 | 24489116 | |
| 610 | Acetylation | KDSSKTVKDEAPTND CCCCCCCCCCCCCCC | 55.90 | 19731963 | |
| 621 | Phosphorylation | PTNDDKLTSVIPEGE CCCCCCCCCCCCCCC | 27.04 | 21126336 | |
| 622 | Phosphorylation | TNDDKLTSVIPEGEK CCCCCCCCCCCCCCC | 28.61 | 24961812 | |
| 629 | Acetylation | SVIPEGEKEKDKTAS CCCCCCCCCCCCCCC | 79.50 | 24489116 | |
| 633 | Acetylation | EGEKEKDKTASSTVT CCCCCCCCCCCCEEE | 57.99 | 24489116 | |
| 647 | Acetylation | TVHENVNKNEIKENG EEECCCCHHHHHHCC | 52.23 | 24489116 | |
| 655 | Acetylation | NEIKENGKNEEQDMV HHHHHCCCCHHHHHH | 73.16 | 24489116 | |
| 667 | Acetylation | DMVEESSKTEDSSKD HHHHHHHCCCCCHHH | 66.27 | 24489116 | |
| 679 | Acetylation | SKDADAAKKDTEDGL HHHHHHHHHHCCCCH | 53.56 | 22865919 | |
| 680 | Acetylation | KDADAAKKDTEDGLQ HHHHHHHHHCCCCHH | 66.22 | 24489116 | |
| 682 | Phosphorylation | ADAAKKDTEDGLQDK HHHHHHHCCCCHHCH | 44.87 | 27214570 | |
| 718 | Phosphorylation | EDEDMVDSQSYLLEK CCCCHHHHHHHEEEC | 15.04 | 21551504 | |
| 760 | Acetylation | TEYFKNGKLNSDSEA CHHHHCCCCCCCCHH | 54.62 | 24489116 | |
| 827 | Phosphorylation | LQFHNDHSLNGNEAF EEECCCCCCCCCHHH | 26.79 | 20377248 | |
| 878 | Phosphorylation | LDKMEDASVDRMLQN HHHHHHHHHHHHHHC | 36.55 | 21440633 | |
| 897 | Acetylation | QSRFLANKDLGLTPK HHHHHHCCCCCCCCC | 49.04 | 24489116 | |
| 1174 | Phosphorylation | SIVYKKITKGMLDAG CHHHHHCCCCCCCHH | 30.35 | 21440633 | |
| 1217 | Phosphorylation | ANDKTSMTSTEDNSF CCCCCCCCCCCCCCE | 32.06 | 30377154 | |
| 1218 | Phosphorylation | NDKTSMTSTEDNSFA CCCCCCCCCCCCCEE | 22.58 | 30377154 | |
| 1219 | Phosphorylation | DKTSMTSTEDNSFAL CCCCCCCCCCCCEEE | 37.89 | 30377154 | |
| 1234 | Phosphorylation | LEEDQFVSKKTATKA ECCCCCCCHHCCCCC | 29.71 | 30377154 | |
| 1293 | Phosphorylation | GAENDGDSSLFLRTP CCCCCCCCCCEECCC | 34.17 | 23749301 | |
| 1294 | Phosphorylation | AENDGDSSLFLRTPQ CCCCCCCCCEECCCC | 28.07 | 25752575 | |
| 1319 | Phosphorylation | FDDTNMGSNSSFSLS CCCCCCCCCCCCEEC | 23.83 | 30377154 | |
| 1321 | Phosphorylation | DTNMGSNSSFSLSLP CCCCCCCCCCEECCC | 34.16 | 30377154 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 78 | T | Phosphorylation | Kinase | ATM | P38110 | Uniprot |
| 78 | T | Phosphorylation | Kinase | ATR | P38111 | Uniprot |
| 78 | T | Phosphorylation | Kinase | ATM/ATR | - | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | TOM1 | Q03280 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT7_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 SPT7_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 THR-78; SER-88 AND SER-1293,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 THR-78 AND SER-88, 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-88, AND MASSSPECTROMETRY. | |
