BAIT
RNF11
SID1669, CGI-123
ring finger protein 11
GO Process (2)
GO Function (3)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
UBE2V1
CIR1, CROC-1, CROC1, UBE2V, UEV-1, UEV1, UEV1A, P/OKcl.19
ubiquitin-conjugating enzyme E2 variant 1
GO Process (23)
GO Function (4)
GO Component (8)
Gene Ontology Biological Process
- Fc-epsilon receptor signaling pathway [TAS]
- MyD88-dependent toll-like receptor signaling pathway [TAS]
- T cell receptor signaling pathway [TAS]
- cell differentiation [NAS]
- innate immune response [TAS]
- nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway [TAS]
- nucleotide-binding oligomerization domain containing signaling pathway [TAS]
- positive regulation of I-kappaB kinase/NF-kappaB signaling [IMP, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of transcription, DNA-templated [TAS]
- postreplication repair [IBA]
- protein K63-linked ubiquitination [IDA]
- protein polyubiquitination [TAS]
- regulation of DNA repair [TAS]
- regulation of transcription, DNA-templated [TAS]
- toll-like receptor 10 signaling pathway [TAS]
- toll-like receptor 2 signaling pathway [TAS]
- toll-like receptor 4 signaling pathway [TAS]
- toll-like receptor 5 signaling pathway [TAS]
- toll-like receptor 9 signaling pathway [TAS]
- toll-like receptor TLR1:TLR2 signaling pathway [TAS]
- toll-like receptor TLR6:TLR2 signaling pathway [TAS]
- toll-like receptor signaling pathway [TAS]
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
RNF11 sequestration of the E3 ligase SMURF2 on membranes antagonizes SMAD7 down-regulation of transforming growth factor β signaling.
The activity of the E3 ligase, SMURF2, is antagonized by an intramolecular, autoinhibitory interaction between its C2 and Hect domains. Relief of SMURF2 autoinhibition is induced by TGFβ and is mediated by the inhibitory SMAD, SMAD7. In a proteomic screen for endomembrane interactants of the RING-domain E3 ligase, RNF11, we identified SMURF2, among a cohort of Hect E3 ligases previously ... [more]
J. Biol. Chem. Dec. 05, 2016; 292(18);7435-7451 [Pubmed: 28292929]
Throughput
- Low Throughput
Curated By
- BioGRID