BAIT

PTPLAD1

B-IND1, BIND1, HACD3, HSPC121
protein tyrosine phosphatase-like A domain containing 1
GO Process (4)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Homo sapiens
PREY

ATP2B1

PMCA1, PMCA1kb
ATPase, Ca++ transporting, plasma membrane 1
GO Process (4)
GO Function (1)
GO Component (5)

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
PTPLAD1 ATP2B1
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