BAIT
ESYT1
FAM62A, MBC2
extended synaptotagmin-like protein 1
GO Process (0)
GO Function (2)
GO Component (3)
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
ATP2A2
ATP2B, DAR, DD, SERCA2
ATPase, Ca++ transporting, cardiac muscle, slow twitch 2
GO Process (17)
GO Function (7)
GO Component (10)
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]
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
ESYT1 tethers the ER to mitochondria and is required for mitochondrial lipid and calcium homeostasis.
Mitochondria interact with the ER at structurally and functionally specialized membrane contact sites known as mitochondria-ER contact sites (MERCs). Combining proximity labelling (BioID), co-immunoprecipitation, confocal microscopy and subcellular fractionation, we found that the ER resident SMP-domain protein ESYT1 was enriched at MERCs, where it forms a complex with the outer mitochondrial membrane protein SYNJ2BP. BioID analyses using ER-targeted, outer mitochondrial ... [more]
Life Sci Alliance Jan. 01, 2024; 7(1); [Pubmed: 37931956]
Throughput
- Low Throughput
Curated By
- BioGRID