BAIT

CHORDC1

CHP1
cysteine and histidine-rich domain (CHORD) containing 1
GO Process (2)
GO Function (2)
GO Component (0)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Homo sapiens
PREY

TOMM34

HTOM34P, TOM34, URCC3
translocase of outer mitochondrial membrane 34
GO Process (1)
GO Function (1)
GO Component (6)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens

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 quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

Taipale M, Tucker G, Peng J, Krykbaeva I, Lin ZY, Larsen B, Choi H, Berger B, Gingras AC, Lindquist S

Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). In vivo, chaperones also associate with a large and diverse set of cofactors (cochaperones) that regulate their specificity and function. However, how these cochaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We combined mass spectrometry and quantitative high-throughput LUMIER ... [more]

Cell Jul. 17, 2014; 158(2);434-48 [Pubmed: 25036637]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CHORDC1 TOMM34
Affinity Capture-Luminescence
Affinity Capture-Luminescence

An interaction is inferred when a bait protein, tagged with luciferase, is enzymatically detected in immunoprecipitates of the prey protein as light emission. The prey protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag.

Low-BioGRID
-

Curated By

  • BioGRID