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
MTDH
3D3, AEG-1, AEG1, LYRIC, LYRIC/3D3
metadherin
GO Process (8)
GO Function (6)
GO Component (10)
Gene Ontology Biological Process
- lipopolysaccharide-mediated signaling pathway [IMP]
- negative regulation of apoptotic process [IDA]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- positive regulation of NF-kappaB transcription factor activity [IDA]
- positive regulation of angiogenesis [IDA]
- positive regulation of autophagy [IDA]
- positive regulation of protein kinase B signaling [IDA]
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