BAIT
PTK6
BRK
protein tyrosine kinase 6
GO Process (14)
GO Function (4)
GO Component (5)
Gene Ontology Biological Process
- actin cytoskeleton organization [IBA]
- cell migration [IDA]
- cellular response to retinoic acid [IMP]
- innate immune response [IBA]
- intestinal epithelial cell differentiation [IBA]
- negative regulation of protein tyrosine kinase activity [IDA]
- peptidyl-tyrosine autophosphorylation [IBA]
- positive regulation of neuron projection development [IMP]
- protein autophosphorylation [IMP]
- protein phosphorylation [TAS]
- regulation of cell proliferation [IBA]
- transmembrane receptor protein tyrosine kinase signaling pathway [IBA]
- tyrosine phosphorylation of Stat3 protein [IDA]
- tyrosine phosphorylation of Stat5 protein [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
PREY
DDX5
G17P1, HLR1, HUMP68, p68
DEAD (Asp-Glu-Ala-Asp) box helicase 5
GO Process (11)
GO Function (7)
GO Component (7)
Gene Ontology Biological Process
- cell growth [NAS]
- intrinsic apoptotic signaling pathway by p53 class mediator [IMP]
- mRNA splicing, via spliceosome [IC]
- negative regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of DNA damage response, signal transduction by p53 class mediator [IMP]
- positive regulation of intracellular estrogen receptor signaling pathway [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- regulation of alternative mRNA splicing, via spliceosome [IDA]
- regulation of androgen receptor signaling pathway [IMP]
- regulation of osteoblast differentiation [ISS]
- regulation of skeletal muscle cell differentiation [ISS]
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
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRASG13D.
Protein-protein-interaction networks (PPINs) organize fundamental biological processes, but how oncogenic mutations impact these interactions and their functions at a network-level scale is poorly understood. Here, we analyze how a common oncogenic KRAS mutation (KRASG13D) affects PPIN structure and function of the Epidermal Growth Factor Receptor (EGFR) network in colorectal cancer (CRC) cells. Mapping >6000 PPIs shows that this network is ... [more]
Nat Commun Dec. 24, 2019; 11(1);499 [Pubmed: 31980649]
Throughput
- High Throughput
Curated By
- BioGRID