We developed a proteomics approach to examine the mammalian CTD-interactome. We used six synthetic peptides each consisting of four consensus CTD-repeats and with different combinations of serine and tyrosine phosphorylation as affinity-matrix to pull-down nuclear proteins from HeLa cells. The pull-down fractions were then analyzed by MUDPIT mass spectrometry. This approach identified a total of 100 CTD-interacting proteins pull-downed by the differentially phosphorylated CTD-peptides. Our analyses showed that the majority of proteins pulled-down by serine-phosphorylatd CTD are involved in RNA processing. Furthermore, this study identified proteins that were preferentially pulled-down by tyrosine/serine-doubly phosphorylated CTD.
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: ABL, Ionizing Radiation, MUDPIT, Phosphotyrosine, pY1-CTD antibodies, RPRD1B
Principal Investigators: (in alphabetical order) |
Jean Y. J. Wang |
Submitting User: | zhouxinshen |
Number of Files: | |
Total Size: | |
Spectra: | |
Subscribers: | |
Owner | Reanalyses | |
---|---|---|
Experimental Design | ||
Conditions:
|
||
Biological Replicates:
|
||
Technical Replicates:
|
||
Identification Results | ||
Proteins (Human, Remapped):
|
||
Proteins (Reported):
|
||
Peptides:
|
||
Variant Peptides:
|
||
PSMs:
|
||
Quantification Results | ||
Differential Proteins:
|
||
Quantified Proteins:
|
||
Browse Dataset Files | |
FTP Download Link (click to copy):
|