UniProt ID | CDK8_HUMAN | |
---|---|---|
UniProt AC | P49336 | |
Protein Name | Cyclin-dependent kinase 8 | |
Gene Name | CDK8 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 464 | |
Subcellular Localization | Nucleus . | |
Protein Description | Component of the Mediator complex, a coactivator involved in regulated gene 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. Phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex. Phosphorylates CCNH leading to down-regulation of the TFIIH complex and transcriptional repression. Recruited through interaction with MAML1 to hyperphosphorylate the intracellular domain of NOTCH, leading to its degradation.. | |
Protein Sequence | MDYDFKVKLSSERERVEDLFEYEGCKVGRGTYGHVYKAKRKDGKDDKDYALKQIEGTGISMSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKHKVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYFLEDPLPTSDVFAGCQIPYPKREFLTEEEPDDKGDKKNQQQQQGNNHTNGTGHPGNQDSSHTQGPPLKKVRVVPPTTTSGGLIMTSDYQRSNPHAAYPNPGPSTSQPQSSMGYSATSQQPPQYSHQTHRY | |
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 |
---|---|---|---|---|---|
11 | Phosphorylation | DFKVKLSSERERVED CCEEECCCHHHHHHH | 51.62 | - | |
26 | Ubiquitination | LFEYEGCKVGRGTYG HHHCCCCEECCCCCC | 59.59 | - | |
31 | Phosphorylation | GCKVGRGTYGHVYKA CCEECCCCCCEEEEC | 25.60 | - | |
52 | Ubiquitination | DDKDYALKQIEGTGI CCHHHHHHHHCCCCC | 40.85 | - | |
62 | Phosphorylation | EGTGISMSACREIAL CCCCCCHHHHHHHHH | 19.89 | 24043423 | |
74 | Ubiquitination | IALLRELKHPNVISL HHHHHHCCCCCEEEE | 52.87 | 29967540 | |
80 | Phosphorylation | LKHPNVISLQKVFLS CCCCCEEEEEEHHHH | 22.06 | 24719451 | |
119 | Ubiquitination | RASKANKKPVQLPRG HCHHCCCCCCCCCHH | 50.67 | 29967540 | |
130 | Phosphorylation | LPRGMVKSLLYQILD CCHHHHHHHHHHHHH | 16.52 | - | |
133 | Phosphorylation | GMVKSLLYQILDGIH HHHHHHHHHHHHHHH | 9.98 | - | |
141 | Phosphorylation | QILDGIHYLHANWVL HHHHHHHHHCCCEEE | 9.77 | - | |
272 | Ubiquitination | KDWEDIKKMPEHSTL CCHHHHHHCCCCCHH | 61.08 | 29967540 | |
292 | Phosphorylation | RNTYTNCSLIKYMEK HHCCCCHHHHHHHHH | 34.89 | 24719451 | |
295 | Acetylation | YTNCSLIKYMEKHKV CCCHHHHHHHHHCCC | 43.78 | 26051181 | |
322 | Ubiquitination | LLTMDPIKRITSEQA HHCCCHHHHCCCHHH | 43.04 | 29967540 | |
360 | Phosphorylation | YPKREFLTEEEPDDK CCCCCCCCCCCCCCC | 46.82 | - | |
367 | Acetylation | TEEEPDDKGDKKNQQ CCCCCCCCCCHHHHH | 76.12 | 23236377 | |
402 | Acetylation | HTQGPPLKKVRVVPP CCCCCCCCEEEEECC | 55.80 | 24180087 | |
410 | Phosphorylation | KVRVVPPTTTSGGLI EEEEECCCCCCCCEE | 36.31 | 19369195 | |
411 | Phosphorylation | VRVVPPTTTSGGLIM EEEECCCCCCCCEEE | 25.41 | 24275569 | |
411 | O-linked_Glycosylation | VRVVPPTTTSGGLIM EEEECCCCCCCCEEE | 25.41 | 30059200 | |
412 | O-linked_Glycosylation | RVVPPTTTSGGLIMT EEECCCCCCCCEEEC | 28.05 | 30059200 | |
413 | Phosphorylation | VVPPTTTSGGLIMTS EECCCCCCCCEEECC | 28.86 | 22817900 | |
413 | O-linked_Glycosylation | VVPPTTTSGGLIMTS EECCCCCCCCEEECC | 28.86 | 30059200 | |
419 | Phosphorylation | TSGGLIMTSDYQRSN CCCCEEECCCCCCCC | 16.08 | 24275569 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDK8_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 CDK8_HUMAN !! |
Kegg Disease | ||||||
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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 THR-410 AND SER-413, ANDMASS SPECTROMETRY. |