| UniProt ID | CTK3_YEAST | |
|---|---|---|
| UniProt AC | P46963 | |
| Protein Name | CTD kinase subunit gamma | |
| Gene Name | CTK3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 296 | |
| Subcellular Localization | Nucleus, nucleolus. Cytoplasm. | |
| Protein Description | Gamma subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase I transcription and RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK2, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.. | |
| Protein Sequence | MDSLEARLQFIQVLKNLQKTLHKTRDSITSSSTTTPPSSQQKLNNDPIQFYLRNYRHHYEDFHQCLFDTTMKMDPLDRLDVVIYYVRIIRNLYPHSHSNTNVTKVLNEVLLMDIDLVFELCLPCQDWKSLTNQATCKELFLDLSKLIHYDATSVTHTPSDTTLIDATTWYSVKTERTTKDYKESLQRTESLLKDRDLKKLAFFQQFNSDTTAINPDLQTQPTNANILLHRMEADRELHKRSKETSWYIERPSNDILDESEFKSLWTHFETTDSGFDKDDYKNIKALNDIAKASYIY | |
| 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 |
|---|---|---|---|---|---|
| 24 | Phosphorylation | LQKTLHKTRDSITSS HHHHHHHCHHCCCCC | 29.03 | 22369663 | |
| 27 | Phosphorylation | TLHKTRDSITSSSTT HHHHCHHCCCCCCCC | 25.19 | 22890988 | |
| 29 | Phosphorylation | HKTRDSITSSSTTTP HHCHHCCCCCCCCCC | 26.89 | 22890988 | |
| 30 | Phosphorylation | KTRDSITSSSTTTPP HCHHCCCCCCCCCCC | 22.18 | 22890988 | |
| 31 | Phosphorylation | TRDSITSSSTTTPPS CHHCCCCCCCCCCCC | 24.05 | 22369663 | |
| 32 | Phosphorylation | RDSITSSSTTTPPSS HHCCCCCCCCCCCCH | 29.55 | 22369663 | |
| 33 | Phosphorylation | DSITSSSTTTPPSSQ HCCCCCCCCCCCCHH | 36.32 | 22369663 | |
| 34 | Phosphorylation | SITSSSTTTPPSSQQ CCCCCCCCCCCCHHH | 38.97 | 22369663 | |
| 35 | Phosphorylation | ITSSSTTTPPSSQQK CCCCCCCCCCCHHHH | 33.04 | 22369663 | |
| 38 | Phosphorylation | SSTTTPPSSQQKLNN CCCCCCCCHHHHHCC | 41.82 | 22890988 | |
| 39 | Phosphorylation | STTTPPSSQQKLNND CCCCCCCHHHHHCCC | 42.26 | 22890988 | |
| 129 | Phosphorylation | LPCQDWKSLTNQATC CCCCCHHHHCCHHHH | 35.85 | 19823750 | |
| 131 | Phosphorylation | CQDWKSLTNQATCKE CCCHHHHCCHHHHHH | 32.16 | 19823750 | |
| 135 | Phosphorylation | KSLTNQATCKELFLD HHHCCHHHHHHHHHC | 17.85 | 19823750 | |
| 144 | Phosphorylation | KELFLDLSKLIHYDA HHHHHCHHHHHCCCC | 25.69 | 19823750 | |
| 244 | Phosphorylation | LHKRSKETSWYIERP HHHHHHHCCEEEECC | 28.44 | 24961812 | |
| 245 | Phosphorylation | HKRSKETSWYIERPS HHHHHHCCEEEECCC | 20.97 | 21440633 | |
| 247 | Phosphorylation | RSKETSWYIERPSND HHHHCCEEEECCCCC | 7.83 | 24961812 |
| 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 CTK3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CTK3_YEAST !! | ||||||
* 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 CTK3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND THR-35, AND MASSSPECTROMETRY. | |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; THR-34 AND THR-35,AND MASS SPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND THR-34, AND MASSSPECTROMETRY. | |
