BAIT
RHBDF2
RHBDL5, RHBDL6, TEC, TOC, TOCG, iRhom2
rhomboid 5 homolog 2 (Drosophila)
GO Process (1)
GO Function (0)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Cellular Component
Homo sapiens
PREY
HGS
HRS
hepatocyte growth factor-regulated tyrosine kinase substrate
GO Process (13)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
- endosomal transport [NAS, TAS]
- epidermal growth factor receptor signaling pathway [TAS]
- membrane invagination [IMP]
- membrane organization [TAS]
- negative regulation of JAK-STAT cascade [IDA]
- negative regulation of cell proliferation [TAS]
- negative regulation of epidermal growth factor receptor signaling pathway [TAS]
- positive regulation of exosomal secretion [IMP]
- positive regulation of gene expression [IMP]
- protein localization to membrane [IMP]
- protein targeting to lysosome [IMP]
- regulation of protein catabolic process [TAS]
- signal transduction [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