BAIT

SNL1

L000004403, YIL016W
Ribosome-associated protein; proposed to act in protein synthesis and nuclear pore complex biogenesis and maintenance as well as protein folding; has similarity to the mammalian BAG-1 protein
GO Process (2)
GO Function (1)
GO Component (5)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RPL20A

RPL18A2, ribosomal 60S subunit protein L20A, L20e, L20A, L18A, L000004458, L000003149, YMR242C
Ribosomal 60S subunit protein L20A; homologous to mammalian ribosomal protein L18A, no bacterial homolog; RPL20A has a paralog, RPL20B, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
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

A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.

Verghese J, Morano KA

Heat shock protein (Hsp) 70 is a highly conserved molecular chaperone that assists in the folding of nascent chains and repair of unfolded proteins through iterative cycles of ATP binding, hydrolysis and nucleotide exchange tightly coupled to polypeptide binding and release. Co-chaperones, including nucleotide exchange factors (NEFs), modulate the rate of ADP/ATP exchange and serve to recruit Hsp70 to distinct ... [more]

Unknown May. 25, 2012; 0(0); [Pubmed: 22635919]

Throughput

  • High Throughput

Curated By

  • BioGRID