KLF1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CSNK2A1
Gene Ontology Biological Process
- axon guidance [TAS]
- chaperone-mediated protein folding [TAS]
- mitotic cell cycle [TAS]
- mitotic spindle checkpoint [IMP]
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [IMP]
- positive regulation of Wnt signaling pathway [IMP]
- positive regulation of cell growth [IDA]
- positive regulation of cell proliferation [IDA]
- positive regulation of protein catabolic process [IDA]
- protein phosphorylation [IDA]
- signal transduction [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Regulation of erythroid Krueppel-like factor (EKLF) transcriptional activity by phosphorylation of a protein kinase casein kinase II site within its interaction domain.
Erythroid Krueppel-like factor (EKLF) is a red cell-specific activator whose presence is crucial for establishing high levels of adult beta-globin expression in definitive cells during erythroid ontogeny. However, its simple presence within the erythroid lineage is not sufficient to activate the beta-globin promoter. One explanation that may account for this is that post-translational modification of EKLF differs within erythroid cell ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CSNK2A1 KLF1 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 262806 |
Curated By
- BioGRID