Proteomics

Dataset Information

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Phosphorylation of CPSF6 RS-like domain


ABSTRACT: Cleavage factor I mammalian (CFIm) complex, composed of cleavage and polyadenylation specificity factor CPSF6, regulates alternative polyadenylation (APA). CPSF6 has a RS-like domain which plays role in protein -protein interactions. This interaction might have role in alternative polyadenylation site selection. The phosphorylation of RS- like domain might play role in protein -protein interaction and thus might have a role in alternative polyadenylation site selection. So we did mass specteroanalysis to analyse phosphorylation sites of RS-like domain of CPSF6.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Kidney

SUBMITTER: Parmit Singh  

LAB HEAD: Alan N. Engelman

PROVIDER: PXD012713 | Pride | 2019-04-01

REPOSITORIES: Pride

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Publications

Differential role for phosphorylation in alternative polyadenylation function versus nuclear import of SR-like protein CPSF6.

Jang Sooin S   Cook Nicola J NJ   Pye Valerie E VE   Bedwell Gregory J GJ   Dudek Amanda M AM   Singh Parmit K PK   Cherepanov Peter P   Engelman Alan N AN  

Nucleic acids research 20190501 9


Cleavage factor I mammalian (CFIm) complex, composed of cleavage and polyadenylation specificity factor 5 (CPSF5) and serine/arginine-like protein CPSF6, regulates alternative polyadenylation (APA). Loss of CFIm function results in proximal polyadenylation site usage, shortening mRNA 3' untranslated regions (UTRs). Although CPSF6 plays additional roles in human disease, its nuclear translocation mechanism remains unresolved. Two β-karyopherins, transportin (TNPO) 1 and TNPO3, can bind CPSF6 in v  ...[more]

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