UniProt ID | MED29_HUMAN | |
---|---|---|
UniProt AC | Q9NX70 | |
Protein Name | Mediator of RNA polymerase II transcription subunit 29 | |
Gene Name | MED29 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 200 | |
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 | MAASQQQASAASSAAGVSGPSSAGGPGPQQQPQPPAQLVGPAQSGLLQQQQQDFDPVQRYKMLIPQLKESLQTLMKVAAQNLIQNTNIDNGQKSSDGPIQRFDKCLEEFYALCDQLELCLRLAHECLSQSCDSAKHSPTLVPTATKPDAVQPDSLPYPQYLAVIKAQISCAKDIHTALLDCANKVTGKTPAPPAGPGGTL | |
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 | ------MAASQQQAS ------CCHHHHHHH | 18.80 | 19413330 | |
60 | Phosphorylation | DFDPVQRYKMLIPQL CCCHHHHHHHHHHHH | 5.44 | - | |
61 | Ubiquitination | FDPVQRYKMLIPQLK CCHHHHHHHHHHHHH | 29.44 | 21890473 | |
61 | Ubiquitination | FDPVQRYKMLIPQLK CCHHHHHHHHHHHHH | 29.44 | 21890473 | |
70 | Phosphorylation | LIPQLKESLQTLMKV HHHHHHHHHHHHHHH | 24.96 | - | |
76 | Ubiquitination | ESLQTLMKVAAQNLI HHHHHHHHHHHHHHH | 31.66 | 21890473 | |
76 | Ubiquitination | ESLQTLMKVAAQNLI HHHHHHHHHHHHHHH | 31.66 | 21890473 | |
82 | Ubiquitination | MKVAAQNLIQNTNID HHHHHHHHHHCCCCC | 2.57 | 21890473 | |
93 | Ubiquitination | TNIDNGQKSSDGPIQ CCCCCCCCCCCCCHH | 54.01 | 2190698 | |
97 | Ubiquitination | NGQKSSDGPIQRFDK CCCCCCCCCHHHHHH | 24.13 | 21890473 | |
110 | Phosphorylation | DKCLEEFYALCDQLE HHHHHHHHHHHHHHH | 11.27 | - | |
114 | Ubiquitination | EEFYALCDQLELCLR HHHHHHHHHHHHHHH | 57.88 | 21890473 | |
128 | Phosphorylation | RLAHECLSQSCDSAK HHHHHHHHHHCHHCC | 31.54 | 26074081 | |
130 | Phosphorylation | AHECLSQSCDSAKHS HHHHHHHHCHHCCCC | 19.26 | 26074081 | |
133 | Phosphorylation | CLSQSCDSAKHSPTL HHHHHCHHCCCCCCC | 43.47 | 26074081 | |
137 | Phosphorylation | SCDSAKHSPTLVPTA HCHHCCCCCCCCCCC | 20.90 | 30576142 | |
139 | Phosphorylation | DSAKHSPTLVPTATK HHCCCCCCCCCCCCC | 43.32 | 30576142 | |
143 | Phosphorylation | HSPTLVPTATKPDAV CCCCCCCCCCCCCCC | 39.21 | 26074081 | |
145 | Phosphorylation | PTLVPTATKPDAVQP CCCCCCCCCCCCCCC | 45.66 | 30576142 | |
154 | Phosphorylation | PDAVQPDSLPYPQYL CCCCCCCCCCCHHHH | 37.62 | 27080861 | |
157 | Phosphorylation | VQPDSLPYPQYLAVI CCCCCCCCHHHHHHH | 14.30 | 26074081 | |
158 | Phosphorylation | QPDSLPYPQYLAVIK CCCCCCCHHHHHHHH | 17.88 | - | |
160 | Phosphorylation | DSLPYPQYLAVIKAQ CCCCCHHHHHHHHHH | 7.66 | 26074081 | |
167 | Ubiquitination | YLAVIKAQISCAKDI HHHHHHHHHHHHHHH | 24.11 | - | |
176 | Phosphorylation | SCAKDIHTALLDCAN HHHHHHHHHHHHHHH | 21.23 | - | |
184 | Ubiquitination | ALLDCANKVTGKTPA HHHHHHHHHCCCCCC | 23.73 | - | |
184 | Malonylation | ALLDCANKVTGKTPA HHHHHHHHHCCCCCC | 23.73 | 32601280 | |
184 | Acetylation | ALLDCANKVTGKTPA HHHHHHHHHCCCCCC | 23.73 | 26051181 | |
186 | Phosphorylation | LDCANKVTGKTPAPP HHHHHHHCCCCCCCC | 34.27 | - | |
188 | Ubiquitination | CANKVTGKTPAPPAG HHHHHCCCCCCCCCC | 41.80 | - | |
193 | Ubiquitination | TGKTPAPPAGPGGTL CCCCCCCCCCCCCCC | 52.54 | - | |
199 | Phosphorylation | PPAGPGGTL------ CCCCCCCCC------ | 34.90 | 25159151 | |
205 | Ubiquitination | GTL------------ CCC------------ | - | ||
209 | Ubiquitination | ---------------- ---------------- | - | ||
220 | 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 MED29_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MED29_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 MED29_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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Acetylation | |
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. |