An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.

Publication

Comprehensive interactome profiling of the human Hsp70 network highlights functional differentiation of J domains.

Piette BL, Alerasool N, Lin ZY, Lacoste J, Lam MHY, Qian WW, Tran S, Larsen B, Campos E, Peng J, Gingras AC, Taipale M

Hsp70s comprise a deeply conserved chaperone family that has a central role in maintaining protein homeostasis. In humans, Hsp70 client specificity is provided by 49 different co-factors known as J domain proteins (JDPs). However, the cellular function and client specificity of JDPs have largely remained elusive. We have combined affinity purification-mass spectrometry (AP-MS) and proximity-dependent biotinylation (BioID) to characterize the ... [more]

Mol Cell Apr. 27, 2021; (); [Pubmed: 33957083]

Quantitative Score

65.0 [FoldChange]

Throughput

High Throughput

Additional Notes

BioID
High confidence proximal protein interactions had an average probability of the identified interaction (AvgP) >= 0.98. The associated score represents the fold change of spectral counts (or intensities) for each individual interaction.

Curated By

BioGRID

Interaction Summary

DNAJB1

Gene Ontology Biological Process

Gene Ontology Molecular Function

ATPase activator activity [IDA]ATPase binding [IPI]Hsp70 protein binding [IPI]chaperone binding [IPI]protein binding [IPI]unfolded protein binding [IDA]

Gene Ontology Cellular Component

PRCC