HGNC approved symbol | MEAF6 |
HGNC ID | HGNC:25674 |
HGNC approved name | MYST/Esa1-associated factor 6 |
Entrez gene ID | GeneID:64769 (SSTAR profile) |
UniProt AC (human) | Q9HAF1 |
UniProt ID (human) | EAF6_HUMAN |
Pfam domains | NuA4 PF09340 (18-95) |
MGI symbol | Meaf6 |
MGI ID | MGI:1917338 |
UniProt AC (mouse) | Q2VPQ9 |
UniProt ID (mouse) | EAF6_MOUSE |
HGNC gene family tag | # |
HGNC gene family description | # |
Function | Histone modification write cofactor |
Modification | Histone acetylation |
PMID for information on function | PMID:18794358 |
Protein complex | HBO1, NuA4, MOZ/MORF |
Target molecule | histone |
Target entity | H2A, H3K14, H4K5, H4K8, H4K12 |
Product | H2Aac, H3K14ac, H4K5ac, H4K8ac, H4K12ac |
PMID for information on target | PMID:18794358 |
Comment | BRPF proteins bridge the association of MOZ and MORF with ING5 and EAF6=MEAF6. An N-terminal region of BRPF1 interacts with the acetyltransferases; the enhancer of polycomb (EPc) homology domain in the middle part binds to ING5 and EAF6. The association of BRPF1 with EAF6 is weak, but ING5 increases the affinity. These three proteins form a trimeric core that is conserved from Drosophila melanogaster to humans, although authentic orthologs of MOZ and MORF are absent in invertebrates. Deletion mapping studies revealed that the acetyltransferase domain of MOZ/MORF is sufficient for BRPF1 interaction. At the functional level, complex formation with BRPF1 and ING5 drastically stimulates the activity of the acetyltransferase domain in acetylation of nucleosomal histone H3 and free histones H3 and H4. |
Status of entry | # |