Proteomics

Dataset Information

0

Phosphorylation of Asc1p and Asc1p-dependent phospho-proteome


ABSTRACT: Phosphorylation of Asc1p and Asc1p-dependent phospho-proteome We determined 1) the phosphorylation sites within the Asc1 protein purified from Saccharomyces cerevisiae via its Strep-tag and 2) the Asc1p-dependent phospho-proteome. 1) Phospho-sites within tryptic peptides of Asc1p were identified using the Proteome Discoverer 1.4 software with the SequestHT and Mascot search engines and phosphorylation site localization was evaluated with the phosphoRS tool. 2) Quantitative triple SILAC-based phospho-proteome comparison of an ASC1 wild-type strain with asc1 mutant strains. MS data were analyzed with MaxQuant and Perseus.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Oliver Valerius  

LAB HEAD: Dr. Oliver Valerius

PROVIDER: PXD003031 | Pride | 2016-12-13

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Asc1p-phospho.msf Msf
KS081.raw Raw
KS082.raw Raw
KS083.raw Raw
KS084.raw Raw
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Publications

Asc1p/RACK1 Connects Ribosomes to Eukaryotic Phosphosignaling.

Schmitt Kerstin K   Smolinski Nadine N   Neumann Piotr P   Schmaul Samantha S   Hofer-Pretz Verena V   Braus Gerhard H GH   Valerius Oliver O  

Molecular and cellular biology 20170119 3


WD40 repeat proteins fold into characteristic β-propeller structures and control signaling circuits during cellular adaptation processes within eukaryotes. The RACK1 protein of Saccharomyces cerevisiae, Asc1p, consists exclusively of a single seven-bladed β-propeller that operates from the ribosomal base at the head region of the 40S subunit. Here we show that the R38D K40E ribosomal binding-compromised variant (Asc1DEp) is severely destabilized through mutation of phosphosite T143 to a dephosph  ...[more]

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