UniProt ID | MED31_HUMAN | |
---|---|---|
UniProt AC | Q9Y3C7 | |
Protein Name | Mediator of RNA polymerase II transcription subunit 31 | |
Gene Name | MED31 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 131 | |
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 | MAAAVAMETDDAGNRLRFQLELEFVQCLANPNYLNFLAQRGYFKDKAFVNYLKYLLYWKDPEYAKYLKYPQCLHMLELLQYEHFRKELVNAQCAKFIDEQQILHWQHYSRKRMRLQQALAEQQQQNNTSGK | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAAAVAMET ------CCCEEEEEC | 12.25 | 22814378 | |
9 | Phosphorylation | AAAVAMETDDAGNRL CCEEEEECCCCCCCE | 26.54 | - | |
65 | Ubiquitination | WKDPEYAKYLKYPQC CCCHHHHHHCCCHHH | 50.65 | 29967540 | |
69 | Phosphorylation | EYAKYLKYPQCLHML HHHHHCCCHHHHHHH | 8.92 | - | |
95 | Ubiquitination | LVNAQCAKFIDEQQI HHHHHHHHHCCHHHH | 50.94 | 29967540 | |
128 | Phosphorylation | EQQQQNNTSGK---- HHHHHHCCCCC---- | 46.54 | 28555341 | |
129 | Phosphorylation | QQQQNNTSGK----- HHHHHCCCCC----- | 46.86 | 17192257 | |
131 | Acetylation | QQNNTSGK------- HHHCCCCC------- | 57.86 | 30590379 | |
131 | Ubiquitination | QQNNTSGK------- HHHCCCCC------- | 57.86 | 24816145 |
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 MED31_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED31_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 MED31_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MED19_HUMAN | MED19 | physical | 12584197 | |
ZSCA1_HUMAN | ZSCAN1 | physical | 20211142 | |
HD_HUMAN | HTT | physical | 15383276 |
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-129, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASSSPECTROMETRY. |