| UniProt ID | MED19_HUMAN | |
|---|---|---|
| UniProt AC | A0JLT2 | |
| Protein Name | Mediator of RNA polymerase II transcription subunit 19 | |
| Gene Name | MED19 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 244 | |
| 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 | MENFTALFGAQADPPPPPTALGFGPGKPPPPPPPPAGGGPGTAPPPTAATAPPGADKSGAGCGPFYLMRELPGSTELTGSTNLITHYNLEQAYNKFCGKKVKEKLSNFLPDLPGMIDLPGSHDNSSLRSLIEKPPILSSSFNPITGTMLAGFRLHTGPLPEQCRLMHIQPPKKKNKHKHKQSRTQDPVPPETPSDSDHKKKKKKKEEDPDRKRKKKEKKKKKNRHSPDHPGMGSSQASSSSSLR | |
| 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 |
|---|---|---|---|---|---|
| 42 | Phosphorylation | PAGGGPGTAPPPTAA CCCCCCCCCCCCCCC | 38.84 | 20068231 | |
| 47 | Phosphorylation | PGTAPPPTAATAPPG CCCCCCCCCCCCCCC | 34.40 | 20068231 | |
| 50 | Phosphorylation | APPPTAATAPPGADK CCCCCCCCCCCCCCC | 36.91 | 20068231 | |
| 67 | Phosphorylation | AGCGPFYLMRELPGS CCCCCCEEEEECCCC | 2.39 | 20068231 | |
| 106 | Phosphorylation | KKVKEKLSNFLPDLP HHHHHHHHHHCCCCC | 36.28 | - | |
| 125 | Phosphorylation | LPGSHDNSSLRSLIE CCCCCCCHHHHHHHH | 36.49 | - | |
| 129 | Phosphorylation | HDNSSLRSLIEKPPI CCCHHHHHHHHCCCC | 38.70 | 24719451 | |
| 184 | Phosphorylation | HKHKQSRTQDPVPPE CCCCCCCCCCCCCCC | 42.44 | 23186163 | |
| 192 | Phosphorylation | QDPVPPETPSDSDHK CCCCCCCCCCCCHHH | 33.59 | 30266825 | |
| 194 | Phosphorylation | PVPPETPSDSDHKKK CCCCCCCCCCHHHHH | 58.11 | 23401153 | |
| 196 | Phosphorylation | PPETPSDSDHKKKKK CCCCCCCCHHHHHHH | 46.05 | 23401153 | |
| 209 | Phosphorylation | KKKKEEDPDRKRKKK HHHHCCCCHHHHHHH | 46.73 | - | |
| 211 | Phosphorylation | KKEEDPDRKRKKKEK HHCCCCHHHHHHHHH | 46.17 | - | |
| 213 | Phosphorylation | EEDPDRKRKKKEKKK CCCCHHHHHHHHHHH | 57.85 | - | |
| 226 | Phosphorylation | KKKKNRHSPDHPGMG HHHHCCCCCCCCCCC | 28.87 | 20201521 | |
| 234 | Phosphorylation | PDHPGMGSSQASSSS CCCCCCCCCCCCCCC | 15.47 | 30266825 | |
| 235 | Phosphorylation | DHPGMGSSQASSSSS CCCCCCCCCCCCCCC | 24.84 | 30266825 | |
| 238 | Phosphorylation | GMGSSQASSSSSLR- CCCCCCCCCCCCCC- | 24.10 | 30266825 | |
| 239 | Phosphorylation | MGSSQASSSSSLR-- CCCCCCCCCCCCC-- | 36.94 | 23927012 | |
| 240 | Phosphorylation | GSSQASSSSSLR--- CCCCCCCCCCCC--- | 22.81 | 23927012 | |
| 241 | Phosphorylation | SSQASSSSSLR---- CCCCCCCCCCC---- | 35.03 | 23927012 | |
| 242 | Phosphorylation | SQASSSSSLR----- CCCCCCCCCC----- | 30.06 | 25219547 | |
| 243 | Phosphorylation | QASSSSSLR------ CCCCCCCCC------ | 8.99 | 17081983 | |
| 251 | Phosphorylation | R-------------- C-------------- | - | ||
| 252 | Phosphorylation | --------------- --------------- | - |
| 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 MED19_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED19_HUMAN !! | ||||||
* 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 MED19_HUMAN !! | ||||||
| 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 |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-234 ANDSER-235, AND MASS SPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY. | |
| "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 THR-192, AND MASSSPECTROMETRY. | |
