PRKACB
Gene Ontology Biological Process
- activation of phospholipase C activity [TAS]
- activation of protein kinase A activity [TAS]
- adenylate cyclase-modulating G-protein coupled receptor signaling pathway [TAS]
- blood coagulation [TAS]
- carbohydrate metabolic process [TAS]
- cellular response to glucagon stimulus [TAS]
- energy reserve metabolic process [TAS]
- epidermal growth factor receptor signaling pathway [TAS]
- fibroblast growth factor receptor signaling pathway [TAS]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- innate immune response [TAS]
- intracellular signal transduction [TAS]
- neurotrophin TRK receptor signaling pathway [TAS]
- protein phosphorylation [IDA]
- regulation of insulin secretion [TAS]
- signal transduction [TAS]
- small molecule metabolic process [TAS]
- synaptic transmission [TAS]
- transmembrane transport [TAS]
- triglyceride catabolic process [TAS]
- water transport [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HIST1H1C
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
The conserved Tpk1 regulates non-homologous end joining double-strand break repair by phosphorylation of Nej1, a homolog of the human XLF.
The yeast cyclic AMP-dependent protein kinase A (PKA) is a ubiquitous serine-threonine kinase, encompassing three catalytic (Tpk1-3) and one regulatory (Bcy1) subunits. Evidence suggests PKA involvement in DNA damage checkpoint response, but how DNA repair pathways are regulated by PKA subunits remains inconclusive. Here, we report that deleting the tpk1 catalytic subunit reduces non-homologous end joining (NHEJ) efficiency, whereas tpk2-3 ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HIST1H1C PRKACB | Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods. | High | 11.1303 | BioGRID | 2952460 | |
| HIST1H1C PRKACB | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3680149 |
Curated By
- BioGRID