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
RAB3GAP2
RAB3-GAP150, RAB3GAP150, SPG69, WARBM2, p150, RP11-568G11.1
RAB3 GTPase activating protein subunit 2 (non-catalytic)
GO Process (7)
GO Function (5)
GO Component (3)
Gene Ontology Biological Process
- establishment of protein localization to endoplasmic reticulum membrane [IMP]
- intracellular protein transport [TAS]
- positive regulation of GTPase activity [TAS]
- positive regulation of Rab GTPase activity [IMP]
- positive regulation of catalytic activity [TAS]
- positive regulation of endoplasmic reticulum tubular network organization [IMP]
- regulation of GTPase activity [ISS]
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