CPL1
Gene Ontology Biological Process
Gene Ontology Molecular Function
SE
Gene Ontology Biological Process
- RNA splicing [IMP]
- chromatin modification [TAS]
- primary miRNA processing [IMP]
- production of ta-siRNAs involved in RNA interference [IMP]
- regulation of adaxial/abaxial pattern formation [IMP]
- regulation of meristem development [IMP]
- regulation of transcription, DNA-templated [TAS]
- shoot system development [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Fast-forward genetics identifies plant CPL phosphatases as regulators of miRNA processing factor HYL1.
MicroRNAs (miRNAs) are processed from primary transcripts that contain partially self-complementary foldbacks. As in animals, the core microprocessor in plants is a Dicer protein, DICER-LIKE1 (DCL1). Processing accuracy and strand selection is greatly enhanced through the RNA binding protein HYPONASTIC LEAVES 1 (HYL1) and the zinc finger protein SERRATE (SE). We have combined a luciferase-based genetic screen with whole-genome sequencing ... [more]
Throughput
- Low Throughput
Additional Notes
- Figure 4
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CPL1 SE | PCA 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. | Low | - | BioGRID | 1112578 |
Curated By
- BioGRID