BAIT
FAM20C
DMP-4, DMP4, GEF-CK, RNS
family with sequence similarity 20, member C
GO Process (1)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
VCP
ALS14, HEL-220, HEL-S-70, IBMPFD, IBMPFD1, TERA, p97
valosin containing protein
GO Process (18)
GO Function (8)
GO Component (13)
Gene Ontology Biological Process
- DNA repair [NAS]
- ER-associated ubiquitin-dependent protein catabolic process [IDA, IMP, TAS]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [ISS]
- cellular response to DNA damage stimulus [IDA]
- double-strand break repair [IDA]
- endoplasmic reticulum unfolded protein response [TAS]
- establishment of protein localization [TAS]
- positive regulation of Lys63-specific deubiquitinase activity [IDA]
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of protein K63-linked deubiquitination [IDA]
- positive regulation of protein catabolic process [IDA]
- positive regulation of protein complex assembly [IDA]
- proteasome-mediated ubiquitin-dependent protein catabolic process [NAS]
- protein N-linked glycosylation via asparagine [IMP]
- protein ubiquitination [IDA, NAS]
- regulation of apoptotic process [TAS]
- retrograde protein transport, ER to cytosol [IDA]
- translesion synthesis [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- Hrd1p ubiquitin ligase complex [IDA]
- cytoplasm [IDA]
- cytosol [IDA]
- endoplasmic reticulum [IDA]
- endoplasmic reticulum membrane [IDA]
- extracellular vesicular exosome [IDA]
- intracellular membrane-bounded organelle [ISS]
- lipid particle [IDA]
- nucleoplasm [IDA]
- nucleus [IDA, TAS]
- perinuclear region of cytoplasm [IDA]
- proteasome complex [IDA]
- site of double-strand break [IDA]
Homo sapiens
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress.
Accumulated unfolded proteins in the endoplasmic reticulum (ER) trigger the unfolded protein response (UPR) to increase ER protein folding capacity. ER proteostasis and UPR signaling need to be regulated in a precise and timely manner. Here, we identify phosphorylation of protein disulfide isomerase (PDI), one of the most abundant and critical folding catalysts in the ER, as an early event ... [more]
EMBO J Dec. 18, 2019; 39(10);e103841 [Pubmed: 32149426]
Throughput
- High Throughput
Curated By
- BioGRID