HDAC8
HDAC8 (Histone deacetylase 8) is a protein that switches other genes on and off. The public catalogues list it as a drug target, and an approved or late-stage drug is recorded against it. Tied to Non-Hodgkin lymphoma and Multiple myeloma.
Overview
Histone deacetylase that catalyses the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
Open Targets scores its association with cancer at 0.61 (direct and indirect evidence; datatypes literature 0.97, genetic association 0.00, clinical 0.95).
- Target · the protein and the cell it sits on
- Drug · antibody, small molecule, cell or radioligand
- Effect · signal, damage or kill
In plain words · HDAC8 (Histone deacetylase 8) is a protein that switches other genes on and off. The public catalogues list it as a drug target, and an approved or late-stage drug is recorded against it. Tied to Non-Hodgkin lymphoma and Multiple myeloma.
- 1 · What it is
HDAC8 (Histone deacetylase 8) is a protein that switches other genes on and off. The public catalogues list it as a drug target, and an approved or late-stage drug is recorded against it. Tied to Non-Hodgkin lymphoma and Multiple myeloma.
- 2 · What goes wrong in cancer
Histone deacetylase that catalyses the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4).
- 3 · How drugs use it
No product in this corpus aims at HDAC8 yet. Transcription factors have no pocket to plug, so drugs either degrade them or block the partner protein they need to dock on DNA.
External identifiers
Sources: HGNC HGNC:13315 (approved symbol, name, aliases, locus and cross-references (hgnc_complete_set.txt)); UniProt Q9BY41 (protein name, function text, keywords and locations (REST API)); Open Targets ENSG00000147099 (association with cancer (MONDO_0004992) 0.61; per-cancer scores at or above 0.5: plasma cell myeloma 0.55, non-Hodgkin lymphoma 0.57 (GraphQL API, CC0))
Biology
Histone deacetylase that catalyses the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility. In addition to protein deacetylase activity, also has protein-lysine deacylase activity: acts as a protein decrotonylase by mediating decrotonylation ((2E)-butenoyl) of histones. Location: Nucleus; Chromosome; Cytoplasm (UniProt). Locus Xq13.1 (HGNC).
- Non-Hodgkin lymphoma: Open Targets association 0.57 with non-Hodgkin lymphoma (MONDO_0018908)
- Multiple myeloma: Open Targets association 0.55 with plasma cell myeloma (MONDO_0009693)
Notes
top- Written by scripts/fetch-cancer-genes.ts from CIViC, Open Targets, IntOGen, HGNC and UniProt; the function text is UniProt's, condensed and in UK spelling. Roles: Open Targets known-drug datatype score 0.95. Evidence tier "approved-drug" is the strongest of those signals.
- Prevalence not recorded: none of the sources gives a positivity rate.
Latest papers
topQuery for this target: (TITLE:"HDAC8" OR ABSTRACT:"HDAC8" OR TITLE:"histone deacetylase 8" OR ABSTRACT:"histone deacetylase 8" OR TITLE:"Histone deacetylase 8" OR ABSTRACT:"Histone deacetylase 8" OR TITLE:"RPD3" OR ABSTRACT:"RPD3" OR TITLE:"KDAC8" OR ABSTRACT:"KDAC8" OR TITLE:"HDACL1" OR ABSTRACT:"HDACL1") AND (cancer OR tumor OR tumour OR oncology OR carcinoma OR lymphoma OR leukemia OR leukaemia OR myeloma OR sarcoma OR melanoma OR glioma). Results are unfiltered search hits about HDAC8, not a curated reading list.