SUMO2
Gene Ontology Biological Process
Gene Ontology Molecular Function
SALL1
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
PCA
A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay.
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]
Throughput
- Low Throughput
Additional Notes
- #LPPI Likely protein-protein interaction and
- #LPTM Likely post-translational modification
- TurboID
Curated By
- BioGRID