BAIT
PRKACB
PKA C-beta, PKACB, RP11-82H13.1
protein kinase, cAMP-dependent, catalytic, beta
GO Process (22)
GO Function (5)
GO Component (5)
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
Homo sapiens
PREY
RANBP2
ADANE, ANE1, IIAE3, NUP358, TRP1, TRP2
RAN binding protein 2
GO Process (12)
GO Function (2)
GO Component (6)
Gene Ontology Biological Process
- carbohydrate metabolic process [TAS]
- cytokine-mediated signaling pathway [TAS]
- glucose transport [TAS]
- hexose transport [TAS]
- mitotic cell cycle [TAS]
- mitotic nuclear envelope disassembly [TAS]
- protein import into nucleus [TAS]
- protein sumoylation [IDA]
- regulation of glucose transport [TAS]
- small molecule metabolic process [TAS]
- transmembrane transport [TAS]
- viral process [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
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]
Nucleic Acids Res Dec. 20, 2020; 49(14);8145-8160 [Pubmed: 34244791]
Throughput
- High Throughput
Curated By
- BioGRID