BAIT

PPH21

phosphoprotein phosphatase 2A catalytic subunit PPH21, L000001472, YDL134C
Catalytic subunit of protein phosphatase 2A (PP2A); functionally redundant with Pph22p; methylated at C terminus; forms alternate complexes with several regulatory subunits; involved in signal transduction and regulation of mitosis; forms nuclear foci upon DNA replication stress; PPH21 has a paralog, PPH22, that arose from the whole genome duplication
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

PPE1

carboxylesterase-mitochondrial 37S ribosomal protein YmS2, YmS2, MRPS2, YHR075C
Protein with carboxyl methyl esterase activity; may have a role in demethylation of the phosphoprotein phosphatase catalytic subunit; also identified as a small subunit mitochondrial ribosomal protein
GO Process (2)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Publication

Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry.

Ho Y, Gruhler A, Heilbut A, Bader GD, Moore L, Adams SL, Millar A, Taylor P, Bennett K, Boutilier K, Yang L, Wolting C, Donaldson I, Schandorff S, Shewnarane J, Vo M, Taggart J, Goudreault M, Muskat B, Alfarano C, Dewar D, Lin Z, Michalickova K, Willems AR, Sassi H, Nielsen PA, Rasmussen KJ, Andersen JR, Johansen LE, Hansen LH, Jespersen H, Podtelejnikov A, Nielsen E, Crawford J, Poulsen V, Sorensen BD, Matthiesen J, Hendrickson RC, Gleeson F, Pawson T, Moran MF, Durocher D, Mann M, Hogue CW, Figeys D, Tyers M

The recent abundance of genome sequence data has brought an urgent need for systematic proteomics to decipher the encoded protein networks that dictate cellular function. To date, generation of large-scale protein-protein interaction maps has relied on the yeast two-hybrid system, which detects binary interactions through activation of reporter gene expression. With the advent of ultrasensitive mass spectrometric protein identification methods, ... [more]

Nature Jan. 10, 2002; 415(6868);180-3 [Pubmed: 11805837]

Throughput

  • High Throughput

Curated By

  • BioGRID