MassIVE MSV000078867

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Proteomics Studies of the Interactome of RNA Polymerase II C-Terminal Repeated Domain

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Description

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

Contact

Principal Investigators:
(in alphabetical order) 		Jean Y. J. Wang
Submitting User: zhouxinshen
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Originally identified proteins that were automatically remapped by MassIVE to proteins in the SwissProt human reference database.

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Distinct protein accessions are counted across all files submitted in the "Statistical Analysis of Quantified Analytes" category having a "Protein" column in this dataset.

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