BAIT

CALR

CRT, HEL-S-99n, RO, SSA, cC1qR
calreticulin
GO Process (33)
GO Function (15)
GO Component (17)

Gene Ontology Biological Process

Homo sapiens
PREY

CALR

CRT, HEL-S-99n, RO, SSA, cC1qR
calreticulin
GO Process (33)
GO Function (15)
GO Component (17)

Gene Ontology Biological Process

Homo sapiens

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

A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region.

Rizvi SM, Mancino L, Thammavongsa V, Cantley RL, Raghavan M

It is widely believed that the chaperone activity of calreticulin is mediated by its ability to bind glycoproteins containing monoglucosylated oligosaccharides. However, calreticulin is also a polypeptide binding protein. Here we show that heat shock, calcium depletion, or deletion of the C-terminal acidic domain enhance binding of purified calreticulin to polypeptide substrates and enhance calreticulin's chaperone activity. These conditions also ... [more]

Mol. Cell Sep. 24, 2004; 15(6);913-23 [Pubmed: 15383281]

Throughput

  • Low Throughput

Curated By

  • BioGRID