BAIT
TNKS
ARTD5, PARP-5a, PARP5A, PARPL, TIN1, TINF1, TNKS1, pART5
tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase
GO Process (14)
GO Function (3)
GO Component (6)
Gene Ontology Biological Process
- mitotic spindle organization [TAS]
- negative regulation of DNA binding [IDA]
- peptidyl-serine phosphorylation [IDA]
- peptidyl-threonine phosphorylation [IDA]
- positive regulation of canonical Wnt signaling pathway [IMP]
- positive regulation of telomere maintenance via telomerase [IDA, IMP]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- protein ADP-ribosylation [IDA]
- protein auto-ADP-ribosylation [IDA]
- protein localization to chromosome, telomeric region [IMP]
- protein poly-ADP-ribosylation [IDA]
- protein polyubiquitination [IDA]
- regulation of telomere maintenance via telomerase [IC]
- spindle assembly [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
DTNBP1
BLOC1S8, DBND, HPS7, My031, SDY, RP1-147M19.1
dystrobrevin binding protein 1
GO Process (12)
GO Function (1)
GO Component (12)
Gene Ontology Biological Process
- actin cytoskeleton reorganization [ISS]
- anterograde axon cargo transport [ISS]
- anterograde synaptic vesicle transport [ISS]
- melanosome organization [NAS]
- membrane organization [TAS]
- neuron projection development [IDA]
- neuron projection morphogenesis [ISS]
- positive regulation of gene expression [ISS]
- positive regulation of neurotransmitter secretion [ISS]
- post-Golgi vesicle-mediated transport [TAS]
- regulation of dopamine receptor signaling pathway [ISS]
- regulation of dopamine secretion [ISS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Protein-peptide
An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.
Publication
Proteome-scale mapping of binding sites in the unstructured regions of the human proteome.
Specific protein-protein interactions are central to all processes that underlie cell physiology. Numerous studies have together identified hundreds of thousands of human protein-protein interactions. However, many interactions remain to be discovered, and low affinity, conditional, and cell type-specific interactions are likely to be disproportionately underrepresented. Here, we describe an optimized proteomic peptide-phage display library that tiles all disordered regions of ... [more]
Mol Syst Biol Jan. 01, 2022; 18(1);e10584 [Pubmed: 35044719]
Throughput
- High Throughput
Curated By
- BioGRID