| UniProt ID | SGF73_YEAST | |
|---|---|---|
| UniProt AC | P53165 | |
| Protein Name | SAGA-associated factor 73 | |
| Gene Name | SGF73 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 657 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Functions as 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 | MRSGDAEIKGIKPKVIEEYSLSQGSGPSNDSWKSLMSSAKDTPLQYDHMNRESLKKYFNPNAQLIEDPLDKPIQYRVCEKCGKPLALTAIVDHLENHCAGASGKSSTDPRDESTRETIRNGVESTGRNNNDDDNSNDNNNDDDDDDDNDDNEDDDDADDDDDNSNGANYKKNDSSFNPLKRSTSMESANTPNMDTKRSKTGTPQTFSSSIKKQKKVKQRNPTEKHLIDFNKQCGVELPEGGYCARSLTCKSHSMGAKRAVSGRSKPYDVLLADYHREHQTKIGAAAEKRAKQQELQKLQKQIQKEQKKHTQQQKQGQRSKQRNVNGGKSAKNGGKSTVHNGNNINEIGHVNLTPEEETTQVLNGVSRSFPLPLESTVLSSVRYRTKYFRMREMFASSFSVKPGYTSPGYGAIHSRVGCLDLDRTTDYKFRVRTPQPINHLTNQNLNPKQIQRLQQQRALQAQLLSQQQQQQQQQQQHHSPQAQAQASTQQPTQGMVPNHFPGGATNSSFNANVSSKQIQQQQQQQQHKSQDTGLTPLEIQSQQQKLRQQQLQQQKFEAAASYLANATKLMQESNQDSHLSGTHNNNSSKNGNNNLMTMKASISSPNTSVNSIQSPPSVNSVNGSGQGVSTGINVSGNNGRIEVGIGNSVNPYNGRIN | |
| 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 |
|---|---|---|---|---|---|
| 9 | Ubiquitination | RSGDAEIKGIKPKVI CCCCCCCCCCCHHHE | 46.20 | 22817900 | |
| 12 | Ubiquitination | DAEIKGIKPKVIEEY CCCCCCCCHHHEEEE | 47.67 | 23749301 | |
| 14 | Ubiquitination | EIKGIKPKVIEEYSL CCCCCCHHHEEEEEC | 51.33 | 22817900 | |
| 20 | Phosphorylation | PKVIEEYSLSQGSGP HHHEEEEECCCCCCC | 25.48 | 30377154 | |
| 22 | Phosphorylation | VIEEYSLSQGSGPSN HEEEEECCCCCCCCC | 26.93 | 25752575 | |
| 25 | Phosphorylation | EYSLSQGSGPSNDSW EEECCCCCCCCCHHH | 39.63 | 27214570 | |
| 33 | Acetylation | GPSNDSWKSLMSSAK CCCCHHHHHHHHHCC | 37.35 | 24489116 | |
| 40 | Acetylation | KSLMSSAKDTPLQYD HHHHHHCCCCCCCCC | 65.17 | 24489116 | |
| 171 | Acetylation | SNGANYKKNDSSFNP CCCCCCCCCCCCCCC | 56.48 | 25381059 | |
| 174 | Phosphorylation | ANYKKNDSSFNPLKR CCCCCCCCCCCCCCC | 46.34 | 23749301 | |
| 175 | Phosphorylation | NYKKNDSSFNPLKRS CCCCCCCCCCCCCCC | 31.72 | 23749301 | |
| 180 | Acetylation | DSSFNPLKRSTSMES CCCCCCCCCCCCCCC | 45.63 | 24489116 | |
| 182 | Phosphorylation | SFNPLKRSTSMESAN CCCCCCCCCCCCCCC | 24.21 | 22369663 | |
| 183 | Phosphorylation | FNPLKRSTSMESANT CCCCCCCCCCCCCCC | 35.80 | 25521595 | |
| 184 | Phosphorylation | NPLKRSTSMESANTP CCCCCCCCCCCCCCC | 23.07 | 22369663 | |
| 187 | Phosphorylation | KRSTSMESANTPNMD CCCCCCCCCCCCCCC | 20.41 | 22369663 | |
| 190 | Phosphorylation | TSMESANTPNMDTKR CCCCCCCCCCCCCCC | 18.76 | 22369663 | |
| 195 | Phosphorylation | ANTPNMDTKRSKTGT CCCCCCCCCCCCCCC | 20.00 | 23749301 | |
| 196 | Acetylation | NTPNMDTKRSKTGTP CCCCCCCCCCCCCCC | 50.87 | 25381059 | |
| 198 | Phosphorylation | PNMDTKRSKTGTPQT CCCCCCCCCCCCCCC | 35.80 | 21440633 | |
| 199 | Acetylation | NMDTKRSKTGTPQTF CCCCCCCCCCCCCCC | 55.81 | 24489116 | |
| 200 | Phosphorylation | MDTKRSKTGTPQTFS CCCCCCCCCCCCCCC | 47.75 | 22369663 | |
| 202 | Phosphorylation | TKRSKTGTPQTFSSS CCCCCCCCCCCCCHH | 19.91 | 22369663 | |
| 205 | Phosphorylation | SKTGTPQTFSSSIKK CCCCCCCCCCHHHHH | 27.04 | 29734811 | |
| 207 | Phosphorylation | TGTPQTFSSSIKKQK CCCCCCCCHHHHHHH | 26.94 | 22369663 | |
| 208 | Phosphorylation | GTPQTFSSSIKKQKK CCCCCCCHHHHHHHH | 31.71 | 22369663 | |
| 209 | Phosphorylation | TPQTFSSSIKKQKKV CCCCCCHHHHHHHHH | 36.91 | 22369663 | |
| 211 | Acetylation | QTFSSSIKKQKKVKQ CCCCHHHHHHHHHHC | 51.61 | 24489116 | |
| 212 | Acetylation | TFSSSIKKQKKVKQR CCCHHHHHHHHHHCC | 66.72 | 23572591 | |
| 224 | Acetylation | KQRNPTEKHLIDFNK HCCCCCHHHHHCHHH | 46.30 | 24489116 | |
| 257 | Acetylation | KSHSMGAKRAVSGRS CCCCCCCCCCCCCCC | 34.85 | 25381059 | |
| 265 | Acetylation | RAVSGRSKPYDVLLA CCCCCCCCCCCEEEE | 46.35 | 24489116 | |
| 281 | Acetylation | YHREHQTKIGAAAEK HHHHHHHHHHHHHHH | 32.35 | 22865919 | |
| 288 | Acetylation | KIGAAAEKRAKQQEL HHHHHHHHHHHHHHH | 53.59 | 24489116 | |
| 297 | Acetylation | AKQQELQKLQKQIQK HHHHHHHHHHHHHHH | 66.56 | 25381059 | |
| 300 | Acetylation | QELQKLQKQIQKEQK HHHHHHHHHHHHHHH | 60.86 | 19731963 | |
| 555 | Acetylation | QQQLQQQKFEAAASY HHHHHHHHHHHHHHH | 40.61 | 24489116 | |
| 607 | Phosphorylation | ASISSPNTSVNSIQS EEECCCCCCCCCCCC | 37.12 | 23749301 | |
| 614 | Phosphorylation | TSVNSIQSPPSVNSV CCCCCCCCCCCCCCC | 36.79 | 23749301 | |
| 648 | Phosphorylation | IEVGIGNSVNPYNGR EEEECCCCCCCCCCC | 20.32 | 28889911 | |
| 652 | Phosphorylation | IGNSVNPYNGRIN-- CCCCCCCCCCCCC-- | 25.66 | 19779198 |
| 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 SGF73_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SGF73_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 SGF73_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-22; SER-182; SER-184 ANDSER-187, 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-182 AND SER-184, ANDMASS SPECTROMETRY. | |
