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]
ATP2A3
Gene Ontology Biological Process
Gene Ontology Cellular Component
Cross-Linking-MS (XL-MS)
An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).
Publication
Exploring an Alternative Cysteine-Reactive Chemistry to Enable Proteome-Wide PPI Analysis by Cross-Linking Mass Spectrometry.
The development of MS-cleavable cross-linking mass spectrometry (XL-MS) has enabled the effective capture and identification of endogenous protein-protein interactions (PPIs) and their residue contacts at the global scale without cell engineering. So far, only lysine-reactive cross-linkers have been successfully applied for proteome-wide PPI profiling. However, lysine cross-linkers alone cannot uncover the complete PPI map in cells. Previously, we have developed ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ATP2A3 ATP2A2 | Affinity Capture-MS 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. | High | 0.9942 | BioGRID | 3073627 | |
| ATP2A2 ATP2A3 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3720750 |
Curated By
- BioGRID