| UniProt ID | MED15_YEAST | |
|---|---|---|
| UniProt AC | P19659 | |
| Protein Name | Mediator of RNA polymerase II transcription subunit 15 | |
| Gene Name | GAL11 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1081 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins. It has an important role in the negative regulation of Ty transcription.. | |
| Protein Sequence | MSAAPVQDKDTLSNAERAKNVNGLLQVLMDINTLNGGSSDTADKIRIHAKNFEAALFAKSSSKKEYMDSMNEKVAVMRNTYNTRKNAVTAAAANNNIKPVEQHHINNLKNSGNSANNMNVNMNLNPQMFLNQQAQARQQVAQQLRNQQQQQQQQQQQQRRQLTPQQQQLVNQMKVAPIPKQLLQRIPNIPPNINTWQQVTALAQQKLLTPQDMEAAKEVYKIHQQLLFKARLQQQQAQAQAQANNNNNGLPQNGNINNNINIPQQQQMQPPNSSANNNPLQQQSSQNTVPNVLNQINQIFSPEEQRSLLQEAIETCKNFEKTQLGSTMTEPVKQSFIRKYINQKALRKIQALRDVKNNNNANNNGSNLQRAQNVPMNIIQQQQQQNTNNNDTIATSATPNAAAFSQQQNASSKLYQMQQQQQAQAQAQAQAQAQAQAQAQAQAAQAAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAHAQHQPSQQPQQAQQQPNPLHGLTPTAKDVEVIKQLSLDASKTNLRLTDVTNSLSNEEKEKIKMKLKQGQKLFVQVSNFAPQVYIITKNENFLKEVFQLRIFVKEILEKCAEGIFVVKLDTVDRLIIKYQKYWESMRIQILRRQAILRQQQQMANNNGNPGTTSTGNNNNIATQQNMQQSLQQMQHLQQLKMQQQQQQQQQQQQQQQQQQQQQQQHIYPSSTPGVANYSAMANAPGNNIPYMNHKNTSSMDFLNSMENTPKVPVSAAATPSLNKTINGKVNGRTKSNTIPVTSIPSTNKKLSISNAASQQPTPRSASNTAKSTPNTNPSPLKTQTKNGTPNPNNMKTVQSPMGAQPSYNSAIIENAFRKEELLLKDLEIRKLEISSRFKHRQEIFKDSPMDLFMSTLGDCLGIKDEEMLTSCTIPKAVVDHINGSGKRKPTKAAQRARDQDSIDISIKDNKLVMKSKFNKSNRSYSIALSNVAAIFKGIGGNFKDLSTLVHSSSPSTSSNMDVGNPRKRKASVLEISPQDSIASVLSPDSNIMSDSKKIKVDSPDDPFMTKSGATTSEKQEVTNEAPFLTSGTSSEQFNVWDWNNWTSAT | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MSAAPVQDK ------CCCCCCCCH | 44.43 | 22814378 | |
| 2 | Phosphorylation | ------MSAAPVQDK ------CCCCCCCCH | 44.43 | 30377154 | |
| 13 | Phosphorylation | VQDKDTLSNAERAKN CCCHHHCCHHHHHHC | 35.77 | 24961812 | |
| 33 | Phosphorylation | QVLMDINTLNGGSSD HHHHHHCCCCCCCCC | 23.18 | 24909858 | |
| 80 | Phosphorylation | KVAVMRNTYNTRKNA HHHHHHHCHHHHHHH | 14.05 | 28889911 | |
| 163 | Phosphorylation | QQQRRQLTPQQQQLV HHHHHCCCHHHHHHH | 15.65 | 22369663 | |
| 335 | Phosphorylation | MTEPVKQSFIRKYIN CCHHHHHHHHHHHCC | 19.54 | 28889911 | |
| 366 | Phosphorylation | NNANNNGSNLQRAQN CCCCCCCHHHHHHHH | 36.17 | 30377154 | |
| 518 | Phosphorylation | VEVIKQLSLDASKTN HHHHHHHCCCCCHHC | 23.01 | 25533186 | |
| 522 | Phosphorylation | KQLSLDASKTNLRLT HHHCCCCCHHCCCHH | 39.41 | 25533186 | |
| 590 | Ubiquitination | FVKEILEKCAEGIFV HHHHHHHHHCCCCEE | 34.99 | 19722269 | |
| 599 | Ubiquitination | AEGIFVVKLDTVDRL CCCCEEEEEHHCHHH | 35.03 | 19722269 | |
| 728 | Phosphorylation | PYMNHKNTSSMDFLN CCCCCCCCCCHHHHH | 27.29 | 22369663 | |
| 729 | Phosphorylation | YMNHKNTSSMDFLNS CCCCCCCCCHHHHHH | 32.81 | 22369663 | |
| 730 | Phosphorylation | MNHKNTSSMDFLNSM CCCCCCCCHHHHHHC | 21.97 | 22369663 | |
| 736 | Phosphorylation | SSMDFLNSMENTPKV CCHHHHHHCCCCCCC | 29.62 | 22369663 | |
| 740 | Phosphorylation | FLNSMENTPKVPVSA HHHHCCCCCCCCCCC | 15.92 | 22369663 | |
| 746 | Phosphorylation | NTPKVPVSAAATPSL CCCCCCCCCCCCCCC | 13.20 | 22369663 | |
| 750 | Phosphorylation | VPVSAAATPSLNKTI CCCCCCCCCCCCCCC | 14.53 | 22369663 | |
| 752 | Phosphorylation | VSAAATPSLNKTING CCCCCCCCCCCCCCC | 39.97 | 22369663 | |
| 755 | Acetylation | AATPSLNKTINGKVN CCCCCCCCCCCCEEC | 56.95 | 24489116 | |
| 765 | Phosphorylation | NGKVNGRTKSNTIPV CCEECCCCCCCEEEC | 39.98 | 29136822 | |
| 767 | Phosphorylation | KVNGRTKSNTIPVTS EECCCCCCCEEECCC | 38.30 | 22369663 | |
| 769 | Phosphorylation | NGRTKSNTIPVTSIP CCCCCCCEEECCCCC | 33.48 | 22369663 | |
| 773 | Phosphorylation | KSNTIPVTSIPSTNK CCCEEECCCCCCCCC | 18.65 | 19779198 | |
| 774 | Phosphorylation | SNTIPVTSIPSTNKK CCEEECCCCCCCCCE | 32.51 | 29136822 | |
| 777 | Phosphorylation | IPVTSIPSTNKKLSI EECCCCCCCCCEEEC | 42.83 | 29136822 | |
| 778 | Phosphorylation | PVTSIPSTNKKLSIS ECCCCCCCCCEEECC | 45.78 | 29136822 | |
| 783 | Phosphorylation | PSTNKKLSISNAASQ CCCCCEEECCCHHHC | 32.61 | 22369663 | |
| 785 | Phosphorylation | TNKKLSISNAASQQP CCCEEECCCHHHCCC | 19.62 | 22369663 | |
| 789 | Phosphorylation | LSISNAASQQPTPRS EECCCHHHCCCCCCC | 27.26 | 22369663 | |
| 793 | Phosphorylation | NAASQQPTPRSASNT CHHHCCCCCCCCCCC | 27.31 | 22369663 | |
| 796 | Phosphorylation | SQQPTPRSASNTAKS HCCCCCCCCCCCCCC | 36.93 | 22369663 | |
| 798 | Phosphorylation | QPTPRSASNTAKSTP CCCCCCCCCCCCCCC | 35.64 | 20377248 | |
| 800 | Phosphorylation | TPRSASNTAKSTPNT CCCCCCCCCCCCCCC | 32.73 | 20377248 | |
| 803 | Phosphorylation | SASNTAKSTPNTNPS CCCCCCCCCCCCCCC | 46.78 | 22369663 | |
| 804 | Phosphorylation | ASNTAKSTPNTNPSP CCCCCCCCCCCCCCC | 21.61 | 22369663 | |
| 807 | Phosphorylation | TAKSTPNTNPSPLKT CCCCCCCCCCCCCCC | 50.11 | 22369663 | |
| 810 | Phosphorylation | STPNTNPSPLKTQTK CCCCCCCCCCCCCCC | 44.96 | 22369663 | |
| 820 | Phosphorylation | KTQTKNGTPNPNNMK CCCCCCCCCCCCCCC | 29.32 | 22369663 | |
| 828 | Phosphorylation | PNPNNMKTVQSPMGA CCCCCCCCCCCCCCC | 17.01 | 22369663 | |
| 831 | Phosphorylation | NNMKTVQSPMGAQPS CCCCCCCCCCCCCCC | 16.71 | 22369663 | |
| 838 | Phosphorylation | SPMGAQPSYNSAIIE CCCCCCCCCHHHHHH | 25.51 | 23749301 | |
| 839 | Phosphorylation | PMGAQPSYNSAIIEN CCCCCCCCHHHHHHH | 21.59 | 22369663 | |
| 841 | Phosphorylation | GAQPSYNSAIIENAF CCCCCCHHHHHHHCC | 16.77 | 22369663 | |
| 866 | Phosphorylation | EIRKLEISSRFKHRQ CHHHHHHHHHHHHHH | 13.19 | 24961812 | |
| 867 | Phosphorylation | IRKLEISSRFKHRQE HHHHHHHHHHHHHHH | 47.61 | 24961812 | |
| 901 | Phosphorylation | IKDEEMLTSCTIPKA CCCHHHHHCCCCCHH | 22.05 | 28889911 | |
| 902 | Phosphorylation | KDEEMLTSCTIPKAV CCHHHHHCCCCCHHH | 12.80 | 28889911 | |
| 904 | Phosphorylation | EEMLTSCTIPKAVVD HHHHHCCCCCHHHHH | 39.83 | 28889911 | |
| 952 | Phosphorylation | MKSKFNKSNRSYSIA EECCCCCCCCCHHHH | 38.28 | 24961812 | |
| 955 | Phosphorylation | KFNKSNRSYSIALSN CCCCCCCCHHHHHHH | 27.73 | 24961812 | |
| 956 | Phosphorylation | FNKSNRSYSIALSNV CCCCCCCHHHHHHHH | 10.81 | 24961812 | |
| 957 | Phosphorylation | NKSNRSYSIALSNVA CCCCCCHHHHHHHHH | 11.57 | 21440633 | |
| 961 | Phosphorylation | RSYSIALSNVAAIFK CCHHHHHHHHHHHHC | 21.89 | 24961812 | |
| 978 | Phosphorylation | GGNFKDLSTLVHSSS CCCHHCHHHHHHCCC | 29.81 | 22890988 | |
| 979 | Phosphorylation | GNFKDLSTLVHSSSP CCHHCHHHHHHCCCC | 39.85 | 19823750 | |
| 983 | Phosphorylation | DLSTLVHSSSPSTSS CHHHHHHCCCCCCCC | 25.65 | 19823750 | |
| 984 | Phosphorylation | LSTLVHSSSPSTSSN HHHHHHCCCCCCCCC | 31.24 | 19823750 | |
| 985 | Phosphorylation | STLVHSSSPSTSSNM HHHHHCCCCCCCCCC | 26.36 | 19823750 | |
| 987 | Phosphorylation | LVHSSSPSTSSNMDV HHHCCCCCCCCCCCC | 42.75 | 19823750 | |
| 988 | Phosphorylation | VHSSSPSTSSNMDVG HHCCCCCCCCCCCCC | 39.29 | 22890988 | |
| 989 | Phosphorylation | HSSSPSTSSNMDVGN HCCCCCCCCCCCCCC | 24.85 | 22890988 | |
| 990 | Phosphorylation | SSSPSTSSNMDVGNP CCCCCCCCCCCCCCC | 35.94 | 22890988 | |
| 1003 | Phosphorylation | NPRKRKASVLEISPQ CCCCCCCEEEEECCC | 30.21 | 19823750 | |
| 1008 | Phosphorylation | KASVLEISPQDSIAS CCEEEEECCCCCHHH | 13.72 | 21440633 | |
| 1012 | Phosphorylation | LEISPQDSIASVLSP EEECCCCCHHHHHCC | 18.14 | 20377248 | |
| 1015 | Phosphorylation | SPQDSIASVLSPDSN CCCCCHHHHHCCCCC | 23.17 | 22369663 | |
| 1018 | Phosphorylation | DSIASVLSPDSNIMS CCHHHHHCCCCCCCC | 25.22 | 22369663 | |
| 1021 | Phosphorylation | ASVLSPDSNIMSDSK HHHHCCCCCCCCCCC | 31.47 | 22369663 | |
| 1025 | Phosphorylation | SPDSNIMSDSKKIKV CCCCCCCCCCCCCCC | 34.63 | 22369663 | |
| 1027 | Phosphorylation | DSNIMSDSKKIKVDS CCCCCCCCCCCCCCC | 28.65 | 22369663 | |
| 1034 | Phosphorylation | SKKIKVDSPDDPFMT CCCCCCCCCCCCCCC | 32.96 | 22369663 | |
| 1041 | Phosphorylation | SPDDPFMTKSGATTS CCCCCCCCCCCCCCC | 23.57 | 22890988 | |
| 1043 | Phosphorylation | DDPFMTKSGATTSEK CCCCCCCCCCCCCCC | 25.21 | 21440633 | |
| 1046 | Phosphorylation | FMTKSGATTSEKQEV CCCCCCCCCCCCCCC | 34.09 | 27017623 | |
| 1048 | Phosphorylation | TKSGATTSEKQEVTN CCCCCCCCCCCCCCC | 38.14 | 21440633 |
| 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 MED15_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED15_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 MED15_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 THR-163; SER-335; SER-730;SER-736; SER-746; THR-750; SER-752; SER-783; SER-785; THR-793;SER-803; THR-804; SER-810; THR-828; SER-831; THR-979; SER-983;SER-984; SER-985; SER-987; SER-1003; SER-1018 AND SER-1034, AND MASSSPECTROMETRY. | |
| "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-785; SER-985; SER-1003;SER-1018 AND SER-1034, AND MASS SPECTROMETRY. | |
| "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 SER-1034, 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-1034, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783 AND SER-985, ANDMASS SPECTROMETRY. | |
