BAIT
BIRC3
AIP1, API2, CIAP2, HAIP1, HIAP1, MALT2, MIHC, RNF49, c-IAP2
baculoviral IAP repeat containing 3
GO Process (23)
GO Function (3)
GO Component (5)
Gene Ontology Biological Process
- MyD88-independent toll-like receptor signaling pathway [TAS]
- NIK/NF-kappaB signaling [TAS]
- TRIF-dependent toll-like receptor signaling pathway [TAS]
- cell surface receptor signaling pathway [TAS]
- inhibition of cysteine-type endopeptidase activity involved in apoptotic process [IBA]
- innate immune response [TAS]
- negative regulation of apoptotic process [TAS]
- negative regulation of necroptotic process [IBA]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [TAS]
- positive regulation of protein ubiquitination [IDA]
- protein ubiquitination [IDA]
- regulation of RIG-I signaling pathway [TAS]
- regulation of apoptotic process [IMP]
- regulation of cysteine-type endopeptidase activity [TAS]
- regulation of inflammatory response [TAS]
- regulation of innate immune response [TAS]
- regulation of necroptotic process [IMP]
- regulation of nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- regulation of toll-like receptor signaling pathway [TAS]
- spindle assembly involved in mitosis [IBA]
- toll-like receptor 3 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
UBR4
RBAF600, ZUBR1, p600, RP5-1126H10.1
ubiquitin protein ligase E3 component n-recognin 4
GO Process (1)
GO Function (2)
GO Component (4)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
OTUB1 modulates c-IAP1 stability to regulate signalling pathways.
The cellular inhibitor of apoptosis (c-IAP) proteins are E3 ubiquitin ligases that are critical regulators of tumour necrosis factor (TNF) receptor (TNFR)-mediated signalling. Through their E3 ligase activity c-IAP proteins promote ubiquitination of receptor-interaction protein 1 (RIP1), NF-κB-inducing kinase (NIK) and themselves, and regulate the assembly of TNFR signalling complexes. Consequently, in the absence of c-IAP proteins, TNFR-mediated activation of ... [more]
EMBO J. Apr. 17, 2013; 32(8);1103-14 [Pubmed: 23524849]
Throughput
- Low Throughput
Curated By
- BioGRID