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
PTPN1
PTP1B
protein tyrosine phosphatase, non-receptor type 1
GO Process (19)
GO Function (8)
GO Component (5)
Gene Ontology Biological Process
- JAK-STAT cascade involved in growth hormone signaling pathway [TAS]
- actin cytoskeleton reorganization [IMP]
- blood coagulation [TAS]
- cytokine-mediated signaling pathway [TAS]
- endoplasmic reticulum unfolded protein response [IDA]
- interferon-gamma-mediated signaling pathway [TAS]
- negative regulation of ERK1 and ERK2 cascade [ISS]
- negative regulation of insulin receptor signaling pathway [NAS]
- negative regulation of vascular endothelial growth factor receptor signaling pathway [ISS]
- peptidyl-tyrosine dephosphorylation [IDA, IMP]
- peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity [ISS]
- platelet activation [TAS]
- platelet-derived growth factor receptor-beta signaling pathway [IMP]
- regulation of endocytosis [IDA]
- regulation of hepatocyte growth factor receptor signaling pathway [IMP]
- regulation of interferon-gamma-mediated signaling pathway [TAS]
- regulation of signal transduction [IMP]
- regulation of type I interferon-mediated signaling pathway [TAS]
- type I interferon signaling pathway [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