PTPLAD1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ATP2A2
Gene Ontology Biological Process
- blood coagulation [TAS]
- calcium ion import into sarcoplasmic reticulum [IC, ISS]
- calcium ion transmembrane transport [IDA]
- calcium ion transport from cytosol to endoplasmic reticulum [IDA]
- cell adhesion [TAS]
- cellular calcium ion homeostasis [IDA]
- endoplasmic reticulum calcium ion homeostasis [IDA]
- epidermis development [TAS]
- ion transmembrane transport [TAS]
- positive regulation of endoplasmic reticulum calcium ion concentration [IDA]
- positive regulation of heart rate [TAS]
- regulation of cardiac muscle cell action potential involved in regulation of contraction [ISS]
- regulation of cardiac muscle cell membrane potential [IC, ISS, TAS]
- regulation of cardiac muscle contraction by calcium ion signaling [IDA]
- relaxation of cardiac muscle [IDA]
- sarcoplasmic reticulum calcium ion transport [TAS]
- transmembrane transport [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- calcium ion-transporting ATPase complex [IDA]
- endoplasmic reticulum [IDA]
- endoplasmic reticulum membrane [IDA, TAS]
- integral component of plasma membrane [TAS]
- intercalated disc [IDA]
- longitudinal sarcoplasmic reticulum [IDA]
- membrane [IDA]
- platelet dense tubular network membrane [TAS]
- sarcoplasmic reticulum [IDA]
- sarcoplasmic reticulum membrane [IC, TAS]
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.
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]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| PTPLAD1 ATP2A2 | 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