BAIT
VTCN1
B7-H4, B7H4, B7S1, B7X, B7h.5, PRO1291, VCTN1, RP11-229A19.4
V-set domain containing T cell activation inhibitor 1
GO Process (0)
GO Function (0)
GO Component (0)
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
Pharmacologic Suppression of B7-H4 Glycosylation Restores Antitumor Immunity in Immune-Cold Breast Cancers.
Despite widespread utilization of immunotherapy, treating immune-cold tumors has proved to be a challenge. Here, we report that expression of the immune checkpoint molecule B7-H4 is prevalent among immune-cold triple-negative breast cancers (TNBC), where its expression inversely correlates with that of PD-L1. Glycosylation of B7-H4 interferes with its interaction/ubiquitination by AMFR, resulting in B7-H4 stabilization. B7-H4 expression inhibits doxorubicin-induced cell ... [more]
Cancer Discov Dec. 01, 2019; 10(12);1872-1893 [Pubmed: 32938586]
Throughput
- High Throughput
Curated By
- BioGRID