SCUBA

BRD8 — Bromodomain containing 8

BRD8 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

BRD8's module in each cell type

Cell typeModuleShares the module with
Gamma-delta T cellsmRNA Splicing
RNA processing & translation
ACTB, ACTG1, ACTL6A, ACTR3, AK2, CASP2, CCDC14, CCT5 +13 more
Mucosal-associated invariant T cellInnate Stress Activation
Stress
BATF, BCL2L1, DNAJA3, FAM13A, IL6ST, LRRN3, OXNAD1, PTGER2 +5 more

About the gene

Synonymsp120, SMAP
Chromosome5: 138139770-138178953
Predicted locationIntracellular
Essential geneYes
Protein classEssential proteins, Predicted intracellular proteins
Molecular functionChromatin regulator
Biological processGrowth regulation, Transcription, Transcription regulation

Function

May act as a coactivator during transcriptional activation by hormone-activated nuclear receptors (NR). Isoform 2 stimulates transcriptional activation by AR/DHTR, ESR1/NR3A1, RXRA/NR2B1 and THRB/ERBA2. At least isoform 1 and isoform 2 are components of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.