Matches in Ubergraph for { <https://frink.apps.renci.org/.well-known/genid/B730cfaeb813e3e05de2a8fd00a6ffbfc> ?p ?o ?g. }
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- B730cfaeb813e3e05de2a8fd00a6ffbfc hasDbXref "GOC:bf" @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc hasDbXref "GOC:ma" @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc hasDbXref "PMID:12055104" @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc hasDbXref "PMID:20300203" @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc type Axiom @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc annotatedProperty IAO_0000115 @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc annotatedSource GO_0008385 @default.
- B730cfaeb813e3e05de2a8fd00a6ffbfc annotatedTarget "A trimeric protein complex that phosphorylates inhibitory-kappaB (I-kappaB) proteins. The complex is composed of two kinase subunits (alpha and beta) and a regulatory gamma subunit (also called NEMO). In a resting state, NF-kappaB dimers are bound to inhibitory IKB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription." @default.