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Target intelligence / Profile preview
RB binding protein 5, histone lysine methyltransferase complex subunit (RBBP5)
- Target
- RBBP5
- Molecular classification
- Histone modification, Enzyme (Histone lysine methyltransferase complex component), Transcription regulator (complex subunit)
01
Overview
RBBP5 is a nuclear WD-repeat protein, highly conserved evolutionarily, involved in the control of transcription via its role in histone lysine methyltransferase complexes (notably the MLL/SET1 family complexes). This protein binds retinoblastoma protein and cooperates with other subunits (WDR5, ASH2L, DPY30) to facilitate methylation of histone H3 at lysine 4 (H3K4), a marker for transcriptional activation. Its alteration is linked to cancer and developmental syndromes, underscoring its therapeutic relevance for epigenetic modulation.
- Other names
- Retinoblastoma-binding protein 5RBBP5_HUMANRB binding protein 5
02
Mechanism of action
Inhibitors targeting histone methyltransferase complex subunits lead to reduced histone H3K4 methylation, thus altering chromatin accessibility and transcription of disease-relevant genes.
03
Biological functions
Regulation of transcriptionChromatin remodelingEpigenetic gene activation (through H3K4 methylation)Cell proliferationNeurodevelopment (differentiation of embryonic stem cells along neural lineage)
04
Disease associations
Cancer (misregulation implicated in oncogenesis through transcriptional dysregulation)Developmental disorders (Kleefstra syndrome, Kabuki syndrome 1)
05
Safety considerations
Targeting components of chromatin-modifying complexes can affect global gene expression, posing potential risks for off-target effects, developmental toxicity, and disruption of essential cellular processes
06
Interacting drugs
No approved drugs are directly listed as targeting RBBP5 specifically, but histone methyltransferase inhibitors (e.g., targeting the MLL complex) may functionally impact RBBP5-containing complexes
07
Biomarkers
H3K4 methylation status (as readout for effective targeting)altered RBBP5 complex integrity in cancers and certain syndromes
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