| UniProt ID | MED4_YEAST | |
|---|---|---|
| UniProt AC | Q12343 | |
| Protein Name | Mediator of RNA polymerase II transcription subunit 4 | |
| Gene Name | MED4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 284 | |
| 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.. | |
| Protein Sequence | MSVQDTKAVEFSMGHIRSSSVSLVAEATSNTNSEDKLSKVQLYEDLCRYEDTLSKLVESVDRFKPNLDIAKDLIRTDEALFENVKLLAEYDNIYRNLQKIDKDSEELDSKTRKILEILNECHDELKALPMLEQVEFEKNTILQQRSKINSTELLDYATKLSKFTKIPPTFDKGAVGPNNFIWPAEDALRRGMLAMASLHSKELTRIPGEEVEETEVPTVPPSQSEEQKGQMAKKEGTPKTDSFIFDGTAKEVGDEADNTKDKEKEENNDDALDLDLDLFDPDDF | |
| 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 | ------MSVQDTKAV ------CCHHHHHHE | 28.61 | 22814378 | |
| 18 | Phosphorylation | FSMGHIRSSSVSLVA EECCCCCCCCEEEEE | 26.76 | 22369663 | |
| 19 | Phosphorylation | SMGHIRSSSVSLVAE ECCCCCCCCEEEEEE | 25.55 | 22369663 | |
| 20 | Phosphorylation | MGHIRSSSVSLVAEA CCCCCCCCEEEEEEE | 19.57 | 22369663 | |
| 22 | Phosphorylation | HIRSSSVSLVAEATS CCCCCCEEEEEEECC | 21.05 | 22369663 | |
| 64 | Acetylation | VESVDRFKPNLDIAK HHHHHHHCCCCHHHH | 33.61 | 24489116 | |
| 218 | Phosphorylation | VEETEVPTVPPSQSE CEECCCCCCCCCCCH | 51.31 | 21440633 | |
| 222 | Phosphorylation | EVPTVPPSQSEEQKG CCCCCCCCCCHHHHC | 40.02 | 25752575 | |
| 224 | Phosphorylation | PTVPPSQSEEQKGQM CCCCCCCCHHHHCCC | 47.65 | 21440633 | |
| 237 | Phosphorylation | QMAKKEGTPKTDSFI CCCCCCCCCCCCCEE | 23.78 | 22369663 | |
| 240 | Phosphorylation | KKEGTPKTDSFIFDG CCCCCCCCCCEEEEC | 37.77 | 22369663 | |
| 242 | Phosphorylation | EGTPKTDSFIFDGTA CCCCCCCCEEEECCH | 26.02 | 22369663 | |
| 248 | Phosphorylation | DSFIFDGTAKEVGDE CCEEEECCHHHHCCC | 36.08 | 22369663 | |
| 259 | Phosphorylation | VGDEADNTKDKEKEE HCCCCCCCCHHHHHH | 40.96 | 28889911 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 237 | T | Phosphorylation | Kinase | KIN28 | P06242 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED4_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 MED4_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-222; THR-237 ANDSER-242, 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-237 AND SER-242, ANDMASS 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 THR-237 AND SER-242, ANDMASS SPECTROMETRY. | |
| "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 THR-237, AND MASSSPECTROMETRY. | |
| "Mutual targeting of mediator and the TFIIH kinase Kin28."; Guidi B.W., Bjornsdottir G., Hopkins D.C., Lacomis L.,Erdjument-Bromage H., Tempst P., Myers L.C.; J. Biol. Chem. 279:29114-29120(2004). Cited for: PHOSPHORYLATION AT THR-237. | |
