BAIT

CCT3

BIN2, TCP3, L000002270, YJL014W
Subunit of the cytosolic chaperonin Cct ring complex; related to Tcp1p, required for the assembly of actin and tubulins in vivo; capable of binding Q/N rich proteins and mediating their folding
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

PIF1

TST1, DNA helicase PIF1, L000001435, YML061C
DNA helicase, potent G-quadruplex DNA binder/unwinder; possesses strand annealing activity; promotes DNA synthesis during break-induced replication; important for crossover recombination; translation from different start sites produces mitochondrial and nuclear forms; nuclear form is a catalytic inhibitor of telomerase; mitochondrial form involved in DNA repair and recombination; mutations affect Zn, Fe homeostasis; regulated by Rad53p-dependent phosphorylation in rho0 cells
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

The interaction network of the chaperonin CCT.

Dekker C, Stirling PC, McCormack EA, Filmore H, Paul A, Brost RL, Costanzo M, Boone C, Leroux MR, Willison KR

The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an important function in maintaining cellular homoeostasis by assisting the folding of many proteins, including the cytoskeletal components actin and tubulin. Yet the nature of the proteins and cellular pathways dependent on CCT function has not been established globally. Here, we use proteomic and genomic approaches to define CCT interaction networks involving ... [more]

EMBO J. Jul. 09, 2008; 27(13);1827-39 [Pubmed: 18511909]

Throughput

  • High Throughput

Curated By

  • BioGRID