BAIT

HRR25

KTI14, serine/threonine protein kinase HRR25, L000000810, YPL204W
Protein kinase; involved in regulating diverse events including vesicular trafficking, DNA repair, and chromosome segregation; binds the CTD of RNA pol II; phosphorylates the COPII coat; phosphorylates Tif6p which plays a critical role in 60S ribosomal subunit biogenesis; interacts with Sit4p phosphatase; homolog of mammalian casein kinase 1delta (CK1delta)
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

ABP1

L000000013, YCR088W
Actin-binding protein of the cortical actin cytoskeleton; important for activation of the Arp2/3 complex that plays a key role actin in cytoskeleton organization; inhibits barbed-end actin filament elongation; phosphorylation within its Proline-Rich Regio, mediated by Cdc28p and Pho85p, protects Abp1p from proteolysis mediated by its own PEST sequences; mammalian homologue of HIP-55 (hematopoietic progenitor kinase 1 [HPK1]-interacting protein of 55 kDa)
GO Process (3)
GO Function (1)
GO Component (4)

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