UniProt ID | MED18_HUMAN | |
---|---|---|
UniProt AC | Q9BUE0 | |
Protein Name | Mediator of RNA polymerase II transcription subunit 18 | |
Gene Name | MED18 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 208 | |
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. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.. | |
Protein Sequence | MEAPPVTMMPVTGGTINMMEYLLQGSVLDHSLESLIHRLRGLCDNMEPETFLDHEMVFLLKGQQASPFVLRARRSMDRAGAPWHLRYLGQPEMGDKNRHALVRNCVDIATSENLTDFLMEMGFRMDHEFVAKGHLFRKGIMKIMVYKIFRILVPGNTDSTEALSLSYLVELSVVAPAGQDMVSDDMKNFAEQLKPLVHLEKIDPKRLM | |
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 |
---|---|---|---|---|---|
66 | Phosphorylation | LLKGQQASPFVLRAR HHHCCCCCHHHHHHH | 17.96 | 30266825 | |
78 | Methylation | RARRSMDRAGAPWHL HHHCCHHCCCCCCEE | 26.69 | 115483127 | |
93 | Sulfoxidation | RYLGQPEMGDKNRHA EECCCCCCCCCCHHH | 12.23 | 21406390 | |
96 | Ubiquitination | GQPEMGDKNRHALVR CCCCCCCCCHHHHHH | 50.59 | 33845483 | |
103 | Ubiquitination | KNRHALVRNCVDIAT CCHHHHHHHHHHHHC | 31.51 | 21906983 | |
125 | Sulfoxidation | LMEMGFRMDHEFVAK HHHCCCCCCHHHHHC | 6.03 | 30846556 | |
194 | Ubiquitination | KNFAEQLKPLVHLEK HHHHHHHHHHHHHHH | 35.68 | 29967540 | |
201 | Ubiquitination | KPLVHLEKIDPKRLM HHHHHHHHCCHHHCC | 59.79 | 29967540 |
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 MED18_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED18_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
66 | Phosphorylation | 74 (8) | R ⇒ C | rs139242087 |
| 28090653 |
78 | Methylation | 74 (4) | R ⇒ C | rs139242087 |
| 28090653 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY. | |
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY. |