UniProt ID | MED4_HUMAN | |
---|---|---|
UniProt AC | Q9NPJ6 | |
Protein Name | Mediator of RNA polymerase II transcription subunit 4 | |
Gene Name | MED4 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 270 | |
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 | MAASSSGEKEKERLGGGLGVAGGNSTRERLLSALEDLEVLSRELIEMLAISRNQKLLQAGEENQVLELLIHRDGEFQELMKLALNQGKIHHEMQVLEKEVEKRDSDIQQLQKQLKEAEQILATAVYQAKEKLKSIEKARKGAISSEEIIKYAHRISASNAVCAPLTWVPGDPRRPYPTDLEMRSGLLGQMNNPSTNGVNGHLPGDALAAGRLPDVLAPQYPWQSNDMSMNMLPPNHSSDFLLEPPGHNKENEDDVEIMSTDSSSSSSESD | |
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 | ------MAASSSGEK ------CCCCCCCHH | 18.95 | 22814378 | |
4 | Phosphorylation | ----MAASSSGEKEK ----CCCCCCCHHHH | 18.59 | 29083192 | |
5 | Phosphorylation | ---MAASSSGEKEKE ---CCCCCCCHHHHH | 37.32 | 29083192 | |
6 | Phosphorylation | --MAASSSGEKEKER --CCCCCCCHHHHHH | 48.77 | 29083192 | |
9 | Ubiquitination | AASSSGEKEKERLGG CCCCCCHHHHHHHCC | 77.07 | 21890473 | |
32 | Phosphorylation | STRERLLSALEDLEV HHHHHHHHHHHHHHH | 35.09 | 22617229 | |
35 | Ubiquitination | ERLLSALEDLEVLSR HHHHHHHHHHHHHHH | 61.33 | 21890473 | |
51 | Phosphorylation | LIEMLAISRNQKLLQ HHHHHHHHHCHHHHH | 21.41 | 24719451 | |
55 | Acetylation | LAISRNQKLLQAGEE HHHHHCHHHHHCCCH | 55.50 | 25953088 | |
55 | Ubiquitination | LAISRNQKLLQAGEE HHHHHCHHHHHCCCH | 55.50 | 21890473 | |
66 | Ubiquitination | AGEENQVLELLIHRD CCCHHHHHHHHHCCC | 2.50 | 21890473 | |
81 | Ubiquitination | GEFQELMKLALNQGK CHHHHHHHHHHHCCC | 43.14 | 21890473 | |
88 | Ubiquitination | KLALNQGKIHHEMQV HHHHHCCCCHHHHHH | 29.15 | - | |
98 | Ubiquitination | HEMQVLEKEVEKRDS HHHHHHHHHHHHCHH | 64.00 | - | |
104 | Ubiquitination | EKEVEKRDSDIQQLQ HHHHHHCHHHHHHHH | 62.83 | 21890473 | |
105 | Phosphorylation | KEVEKRDSDIQQLQK HHHHHCHHHHHHHHH | 40.42 | 25056879 | |
112 | Ubiquitination | SDIQQLQKQLKEAEQ HHHHHHHHHHHHHHH | 67.21 | 21890473 | |
115 | Ubiquitination | QQLQKQLKEAEQILA HHHHHHHHHHHHHHH | 53.00 | - | |
123 | Phosphorylation | EAEQILATAVYQAKE HHHHHHHHHHHHHHH | 17.14 | 29978859 | |
126 | Phosphorylation | QILATAVYQAKEKLK HHHHHHHHHHHHHHH | 10.57 | 29978859 | |
129 | Ubiquitination | ATAVYQAKEKLKSIE HHHHHHHHHHHHHHH | 39.60 | - | |
131 | Ubiquitination | AVYQAKEKLKSIEKA HHHHHHHHHHHHHHH | 61.58 | - | |
134 | Phosphorylation | QAKEKLKSIEKARKG HHHHHHHHHHHHHCC | 46.55 | 24719451 | |
140 | Ubiquitination | KSIEKARKGAISSEE HHHHHHHCCCCCHHH | 58.51 | - | |
150 | Ubiquitination | ISSEEIIKYAHRISA CCHHHHHHHHHHHCC | 41.88 | 21890473 | |
150 | Acetylation | ISSEEIIKYAHRISA CCHHHHHHHHHHHCC | 41.88 | 26051181 |
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 MED4_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED4_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 MED4_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 |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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 SER-32, AND MASSSPECTROMETRY. |