| UniProt ID | CCNC_HUMAN | |
|---|---|---|
| UniProt AC | P24863 | |
| Protein Name | Cyclin-C | |
| Gene Name | CCNC | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 283 | |
| 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. Binds to and activates cyclin-dependent kinase CDK8 that 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.. | |
| Protein Sequence | MAGNFWQSSHYLQWILDKQDLLKERQKDLKFLSEEEYWKLQIFFTNVIQALGEHLKLRQQVIATATVYFKRFYARYSLKSIDPVLMAPTCVFLASKVEEFGVVSNTRLIAAATSVLKTRFSYAFPKEFPYRMNHILECEFYLLELMDCCLIVYHPYRPLLQYVQDMGQEDMLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQKDARQWFAELSVDMEKILEIIRVILKLYEQWKNFDERKEMATILSKMPKPKPPPNSEGEQGPNGSQNSSYSQS | |
| 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 |
|---|---|---|---|---|---|
| 30 | Ubiquitination | KERQKDLKFLSEEEY HHHHHHHHCCCHHHH | 55.16 | 21890473 | |
| 33 | Phosphorylation | QKDLKFLSEEEYWKL HHHHHCCCHHHHHHH | 46.20 | - | |
| 37 | Phosphorylation | KFLSEEEYWKLQIFF HCCCHHHHHHHHHHH | 15.89 | 17924679 | |
| 41 | Ubiquitination | EEEYWKLQIFFTNVI HHHHHHHHHHHHHHH | 27.07 | 21890473 | |
| 73 | Phosphorylation | TVYFKRFYARYSLKS HHHHHHHHHHHCCCC | 8.32 | - | |
| 77 | Phosphorylation | KRFYARYSLKSIDPV HHHHHHHCCCCCCCC | 24.62 | 24719451 | |
| 104 | Phosphorylation | VEEFGVVSNTRLIAA HHHHCCCCHHHHHHH | 30.03 | 19060867 | |
| 113 | Phosphorylation | TRLIAAATSVLKTRF HHHHHHHHHHHHHHH | 18.03 | 20071362 | |
| 117 | Ubiquitination | AAATSVLKTRFSYAF HHHHHHHHHHHCCCC | 35.18 | 21906983 | |
| 121 | Phosphorylation | SVLKTRFSYAFPKEF HHHHHHHCCCCCCCC | 16.56 | 17924679 | |
| 122 | Phosphorylation | VLKTRFSYAFPKEFP HHHHHHCCCCCCCCC | 15.00 | 17924679 | |
| 126 | Ubiquitination | RFSYAFPKEFPYRMN HHCCCCCCCCCCCCC | 66.58 | 21890473 | |
| 238 | Phosphorylation | IRVILKLYEQWKNFD HHHHHHHHHHHCCHH | 12.42 | 28509920 | |
| 248 | Ubiquitination | WKNFDERKEMATILS HCCHHHHHHHHHHHH | 50.20 | - | |
| 252 | Phosphorylation | DERKEMATILSKMPK HHHHHHHHHHHCCCC | 22.57 | 20068231 | |
| 255 | Phosphorylation | KEMATILSKMPKPKP HHHHHHHHCCCCCCC | 24.06 | 20068231 | |
| 275 | Phosphorylation | GEQGPNGSQNSSYSQ CCCCCCCCCCCCCCC | 32.59 | 17525332 | |
| 278 | Phosphorylation | GPNGSQNSSYSQS-- CCCCCCCCCCCCC-- | 24.02 | 18077418 | |
| 279 | Phosphorylation | PNGSQNSSYSQS--- CCCCCCCCCCCC--- | 36.03 | 17525332 | |
| 280 | Phosphorylation | NGSQNSSYSQS---- CCCCCCCCCCC---- | 15.56 | - | |
| 281 | Phosphorylation | GSQNSSYSQS----- CCCCCCCCCC----- | 26.37 | 17525332 | |
| 283 | Phosphorylation | QNSSYSQS------- CCCCCCCC------- | 35.93 | 28348404 | |
| 295 | Phosphorylation | ------------------- ------------------- | 17525332 | ||
| 299 | Phosphorylation | ----------------------- ----------------------- | 17525332 | ||
| 301 | Phosphorylation | ------------------------- ------------------------- | 17525332 |
| 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 CCNC_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CCNC_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 CCNC_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 |
| "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-104, AND MASSSPECTROMETRY. | |
| "ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279 ANDSER-281, AND MASS SPECTROMETRY. | |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND TYR-122, ANDMASS SPECTROMETRY. | |
