BAIT
RHBDD1
RRP4, HSD50
rhomboid domain containing 1
GO Process (12)
GO Function (3)
GO Component (3)
Gene Ontology Biological Process
- ER-associated ubiquitin-dependent protein catabolic process [ISS]
- cellular response to UV [ISS]
- cellular response to unfolded protein [ISS]
- membrane protein intracellular domain proteolysis [ISS]
- membrane protein proteolysis [IDA]
- negative regulation of apoptotic process [IDA, IMP, ISS]
- positive regulation of protein catabolic process [IDA, IMP]
- positive regulation of protein processing [ISS]
- positive regulation of secretion [IMP]
- post-translational protein modification [ISS]
- regulation of male germ cell proliferation [ISS]
- spermatid differentiation [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
PLA2G4A
PLA2G4, cPLA2-alpha
phospholipase A2, group IVA (cytosolic, calcium-dependent)
GO Process (15)
GO Function (4)
GO Component (4)
Gene Ontology Biological Process
- arachidonic acid metabolic process [TAS]
- blood coagulation [TAS]
- cardiolipin acyl-chain remodeling [TAS]
- glycerophospholipid biosynthetic process [TAS]
- icosanoid metabolic process [NAS]
- phosphatidic acid biosynthetic process [TAS]
- phosphatidylcholine acyl-chain remodeling [TAS]
- phosphatidylethanolamine acyl-chain remodeling [TAS]
- phosphatidylglycerol acyl-chain remodeling [TAS]
- phosphatidylinositol acyl-chain remodeling [TAS]
- phosphatidylserine acyl-chain remodeling [TAS]
- phospholipid metabolic process [TAS]
- platelet activating factor biosynthetic process [NAS]
- platelet activation [TAS]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Proximity Label-MS
An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.
Publication
Spatial proteomics reveal that the protein phosphatase PTP1B interacts with and may modify tyrosine phosphorylation of the rhomboid protease RHBDL4.
Rhomboid-like proteins are evolutionarily conserved, ubiquitous polytopic membrane proteins, including the canonical rhomboid intramembrane serine proteases and also others that have lost protease activity during evolution. We still have much to learn about their cellular roles, and evidence suggests that some may have more than one function. For example, RHBDL4 (rhomboid-like protein 4) is an endoplasmic reticulum (ER)-resident protease that ... [more]
J. Biol. Chem. Dec. 26, 2018; 294(30);11486-11497 [Pubmed: 31177093]
Throughput
- High Throughput
Curated By
- BioGRID