BAIT
SALL1
HEL-S-89, HSAL1, Sal-1, TBS, ZNF794
spalt-like transcription factor 1
GO Process (25)
GO Function (5)
GO Component (5)
Gene Ontology Biological Process
- adrenal gland development [IEP]
- branching involved in ureteric bud morphogenesis [ISS]
- embryonic digestive tract development [IMP]
- embryonic digit morphogenesis [IMP]
- gonad development [IEP]
- heart development [IMP]
- histone deacetylation [ISS]
- inductive cell-cell signaling [ISS]
- kidney development [IMP]
- kidney epithelium development [ISS]
- limb development [IMP]
- mesenchymal to epithelial transition involved in metanephros morphogenesis [IEP]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- olfactory bulb interneuron differentiation [ISS]
- olfactory bulb mitral cell layer development [IMP]
- olfactory nerve development [ISS]
- outer ear morphogenesis [IMP]
- pituitary gland development [IEP]
- positive regulation of Wnt signaling pathway [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription, DNA-templated [IDA]
- ureteric bud development [ISS]
- ureteric bud invasion [ISS]
- ventricular septum development [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
MCCC1
MCC-B, MCCA
methylcrotonoyl-CoA carboxylase 1 (alpha)
GO Process (7)
GO Function (3)
GO Component (3)
Gene Ontology Biological Process
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
Identification of proximal SUMO-dependent interactors using SUMO-ID.
The fast dynamics and reversibility of posttranslational modifications by the ubiquitin family pose significant challenges for research. Here we present SUMO-ID, a technology that merges proximity biotinylation by TurboID and protein-fragment complementation to find SUMO-dependent interactors of proteins of interest. We develop an optimized split-TurboID version and show SUMO interaction-dependent labelling of proteins proximal to PML and RANGAP1. SUMO-dependent interactors ... [more]
Nat Commun Dec. 18, 2020; 12(1);6671 [Pubmed: 34795231]
Throughput
- High Throughput
Additional Notes
- Sumo-dependent interaction
Curated By
- BioGRID