BAIT

GIN4

ERC47, protein kinase GIN4, L000002876, YDR507C
Protein kinase involved in bud growth and assembly of the septin ring; proposed to have kinase-dependent and kinase-independent activities; undergoes autophosphorylation; similar to Hsl1p; GIN4 has a paralog, KCC4, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (5)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

SEC13

ANU3, GTPase-activating protein SEC13, L000001838, YLR208W
Structural component of 3 distinct complexes; subunit of Nup84 nuclear pore sub-complex (NPC), COPII vesicle coat, and Seh1-associated (SEA) complex; COPII vesicle coat is required for ER to Golgi transport; the Nup84 subcomplex contributes to nucleocytoplasmic transport, NPC biogenesis and processes that may require localization of chromosomes at the nuclear periphery, including transcription; homologous to human SEC13; abundance increases under DNA replication stress
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes.

Fasolo J, Sboner A, Sun MG, Yu H, Chen R, Sharon D, Kim PM, Gerstein M, Snyder M

Protein kinases are key regulators of cellular processes. In spite of considerable effort, a full understanding of the pathways they participate in remains elusive. We globally investigated the proteins that interact with the majority of yeast protein kinases using protein microarrays. Eighty-five kinases were purified and used to probe yeast proteome microarrays. One-thousand-twenty-three interactions were identified, and the vast majority ... [more]

Genes Dev. Apr. 01, 2011; 25(7);767-78 [Pubmed: 21460040]

Throughput

  • High Throughput

Additional Notes

  • High Throughput: Proteome microarrays were used to identify proteins that interact with protein kinases.

Curated By

  • BioGRID