Detailed gene information

Genes [306]

TAIR: AT5G44200


Hugouvieux V et al., 2001, Cell
Kmieciak M et al., 2002, Gene
Papp I et al., 2004, Plant Mol. Biol.
Kim S et al., 2008, Plant Cell Physiol.
Geraldo N et al., 2009, Plant Physiol.
Jäger K et al., 2011, Plant Biol (Stuttg)
Kong X et al., 2014, J. Proteome Res.
Raczynska K D et al., 2014, Nucleic Acids Res.

Appears in the following schemes

microRNA biosynthesis
FLC regulation through protein complexes
General processes & autonomous pathway

Protein function

Encodes a component of the cap-binding complex (CBC) that binds to the 5-cap of pre-miRNAs.


cbp20 single mutant has reduced miRNA levels and increased pri-miRNA levels. [Kim et al., 2008]

Single mutant:
cbp20 single mutant is early flowering under LD conditions in Col-0 and Col FRI backgrounds. (No data available under SD conditions. The whole plant development seems to be delayed.) [Geraldo et al., 2009][Papp et al., 2004]

CBP20 is required for FRI activity. Loss of CBP20 results in reduced mature FLC mRNA levels and an increase of unspliced FLC transcripts. [Geraldo et al., 2009]

Component of the cap-binding complex (CBC), which binds co-transcriptionally to the 5 cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi) by microRNAs (miRNAs). The CBC complex is involved in miRNA-mediated RNA interference and is required for primary miRNA processing. In the CBC complex, CBP20 recognizes and binds capped RNAs (m7GpppG-capped RNA) but requires ABH1/CBP80 to stabilize the movement of its N-terminal loop and lock the CBC into a high affinity cap-binding state with the cap structure. CBP20 also plays a role in stabilization of ABH1/CBP80 and ABH1/CBP80 localization to the nucleus. Involved in flowering regulation via its interaction with FRIGIDA. [Data from UniProt]

Regulators, targets and interactors

Downstream actors

Upstream actors

Protein-protein interactions

CBP20 interaction network

Downstream and upstream flowering-related genes

Physical interactions with other flowering-related proteins